PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
33360835-2	2021	Here, we investigated the potential for SUMO-1 protein to modulate the function of the CaV2.2 (N-type) voltage-gated calcium channel (VGCC), a protein vital for presynaptic neurotransmitter release.	Calcium	117-124	small ubiquitin like modifier 1	Homo sapiens	40-46
33360835-7	2021	Mutagenesis of selected individual lysine residues identified K394, but not K951, as a key residue for SUMO-1-mediated increase in CaV2.2 Ca2+ current density.	Lysine	35-41	small ubiquitin like modifier 1	Homo sapiens	103-109
32900482-4	2020	In this study, we found IDH2 is modified by small ubiquitin-like modifier 1 (SUMO1) at lysine 45.	Lysine	87-93	small ubiquitin like modifier 1	Homo sapiens	44-75
32592588-9	2020	Disruption of SUMO1-sumoylation by Pin1 silencing with shRNAs or inhibition with its inhibitor Juglone markedly abrogated GSC maintenance and mitigated GSC-driven tumor growth.	juglone	95-102	small ubiquitin like modifier 1	Homo sapiens	14-19
32900482-4	2020	In this study, we found IDH2 is modified by small ubiquitin-like modifier 1 (SUMO1) at lysine 45.	Lysine	87-93	small ubiquitin like modifier 1	Homo sapiens	77-82
32061854-0	2020	Characterization of Cu2+ and Zn2+ binding sites in SUMO1 and its impact on protein stability.	Copper	20-24	small ubiquitin like modifier 1	Homo sapiens	51-56
30426790-3	2020	In SPR studies, only endosulfan showed binding to SUMO1 (Kd1.313 x 10-4 M).	Endosulfan	21-31	small ubiquitin like modifier 1	Homo sapiens	50-55
30426790-7	2020	In HePG2 cells, endosulfan treatment resulted in elevated mRNA levels of SUMO1, 3 and UBC9, whereas, treatment with bisphenol A resulted in increased mRNA of SUMO2, 3 and UBC9.	Endosulfan	16-26	small ubiquitin like modifier 1	Homo sapiens	73-78
30426790-9	2020	Apart from influencing the gene expression, endosulfan caused decrease in SUMO1-Sumoylation of few proteins.	Endosulfan	44-54	small ubiquitin like modifier 1	Homo sapiens	74-79
32474020-7	2020	In addition, we also found that hypoxia promotes sumoylation in keloids and that HIF-1alpha is covalently modified by SUMO1 at Lys 391 and Lys 477 in HKFs.	Lysine	127-130	small ubiquitin like modifier 1	Homo sapiens	118-123
32796599-7	2020	The final yield of rebadioside A (Reb A) and rebadioside M (Reb M) reached 4.8 g/L and 1.8 g/L, respectively, when catalyzed by Smt3-UGT76G1 in the practical UDP-glucose regeneration transformation system in vitro.	rebadioside a	19-32	small ubiquitin like modifier 1	Homo sapiens	128-132
32796599-7	2020	The final yield of rebadioside A (Reb A) and rebadioside M (Reb M) reached 4.8 g/L and 1.8 g/L, respectively, when catalyzed by Smt3-UGT76G1 in the practical UDP-glucose regeneration transformation system in vitro.	rebadioside	19-30	small ubiquitin like modifier 1	Homo sapiens	128-132
32796599-7	2020	The final yield of rebadioside A (Reb A) and rebadioside M (Reb M) reached 4.8 g/L and 1.8 g/L, respectively, when catalyzed by Smt3-UGT76G1 in the practical UDP-glucose regeneration transformation system in vitro.	Glucose	162-169	small ubiquitin like modifier 1	Homo sapiens	128-132
32243901-7	2020	PML is sumoylated and contains a Sumo-interacting motif, and a significant fraction of Sumo1 and Sumo2/3 co-localizes with PML NBs.	Bromosuccinimide	127-130	small ubiquitin like modifier 1	Homo sapiens	87-92
32502496-0	2020	The pivotal role of SUMO-1-JNK-Tau axis in an in vitro model of oxidative stress counteracted by the protective effect of curcumin.	Curcumin	122-130	small ubiquitin like modifier 1	Homo sapiens	20-26
32502496-3	2020	In this study, we showed a strong interaction among SUMO-1-JNK-Tau proteins and their molecular targets in an in vitro model (SHSY5Y cell line) of oxidative stress in which a significant reduction of cell viability and an augmented cell death was induced by increased doses of H2O2.	Hydrogen Peroxide	277-281	small ubiquitin like modifier 1	Homo sapiens	52-58
32502496-5	2020	Curcumin, a natural compound with anti-oxidant and anti-inflammatory effects, demonstrated to tackle oxidative stress re-equilibrating SUMO-1, JNK and Tau functions.	Curcumin	0-8	small ubiquitin like modifier 1	Homo sapiens	135-141
32502496-7	2020	Interestingly, we found that H2O2 treatment induced a strong co-localization of SUMO-1-p-JNK-Tau proteins in nuclear bodies (NBs) and that curcumin was able to reduce these nuclear aggregates.	Hydrogen Peroxide	29-33	small ubiquitin like modifier 1	Homo sapiens	80-86
32502496-7	2020	Interestingly, we found that H2O2 treatment induced a strong co-localization of SUMO-1-p-JNK-Tau proteins in nuclear bodies (NBs) and that curcumin was able to reduce these nuclear aggregates.	Curcumin	139-147	small ubiquitin like modifier 1	Homo sapiens	80-86
32502496-8	2020	These results highlight the SUMO-1-JNK-Tau axis key role in oxidative stress and the protective effect of curcumin against this pathological event, focusing on the importance of SUMO/deSUMOylation balance to regulate essential cellular processes.	Curcumin	106-114	small ubiquitin like modifier 1	Homo sapiens	28-34
32483381-3	2020	We show here that in addition to phosphorylation, Olig2 is also conjugated by small ubiquitin-like modifier-1 (SUMO1) at three lysine residues K27, K76, and K112.	Lysine	127-133	small ubiquitin like modifier 1	Homo sapiens	78-109
32483381-3	2020	We show here that in addition to phosphorylation, Olig2 is also conjugated by small ubiquitin-like modifier-1 (SUMO1) at three lysine residues K27, K76, and K112.	Lysine	127-133	small ubiquitin like modifier 1	Homo sapiens	111-116
33192289-7	2020	Analysis of the polar contacts and hydrogen bonds, and the root mean square derivation results showed that R726 and R727 of CaMBD formed polar contacts or high occupancy hydrogen bonds with SUMO1.	Hydrogen	170-178	small ubiquitin like modifier 1	Homo sapiens	190-195
32530958-0	2020	Dietary flavonoid fisetin binds human SUMO1 and blocks sumoylation of p53.	flavonoid fisetin	8-25	small ubiquitin like modifier 1	Homo sapiens	38-43
32530958-4	2020	Using a combination of surface plasmon resonance, differential scanning fluorimetry and fluorescence quenching studies, we provide evidence for direct binding of the dietary flavonoid fisetin to human SUMO1.	Flavonoids	174-183	small ubiquitin like modifier 1	Homo sapiens	201-206
32530958-7	2020	A series of differential scanning fluorimetry experiments suggest that high concentrations of fisetin result in destabilization and unfolding of SUMO1, presenting a molecular mechanism by which flavonoid binding affects its activity.	Flavonoids	194-203	small ubiquitin like modifier 1	Homo sapiens	145-150
32061854-0	2020	Characterization of Cu2+ and Zn2+ binding sites in SUMO1 and its impact on protein stability.	Zinc	29-33	small ubiquitin like modifier 1	Homo sapiens	51-56
32061854-4	2020	Between Cu2+ and Zn2+, the former binds more strongly with SUMO1 as determined using fluorescence spectroscopy.	Copper	8-12	small ubiquitin like modifier 1	Homo sapiens	59-64
32061854-4	2020	Between Cu2+ and Zn2+, the former binds more strongly with SUMO1 as determined using fluorescence spectroscopy.	Zinc	17-21	small ubiquitin like modifier 1	Homo sapiens	59-64
32061854-5	2020	SUMO1 aggregates, forming trimer and higher oligomers in presence of Cu2+ ions which were characterized using gel electrophoresis, Bradford assay, and transmission electron microscopy.	Copper	69-73	small ubiquitin like modifier 1	Homo sapiens	0-5
32061854-7	2020	Cu2+ induced paramagnetic quenching and Zn2+ induced chemical shift perturbation of 15N-1H cross-peaks were used to identify their respective binding sites in SUMO1.	Copper	0-4	small ubiquitin like modifier 1	Homo sapiens	159-164
32061854-7	2020	Cu2+ induced paramagnetic quenching and Zn2+ induced chemical shift perturbation of 15N-1H cross-peaks were used to identify their respective binding sites in SUMO1.	Zinc	40-43	small ubiquitin like modifier 1	Homo sapiens	159-164
32061854-9	2020	Our findings provide structural insights into the SUMO1-Cu2+/Zn2+ interaction, and its impact on aggregation of SUMO1 which might affect its ability to modify functions of target proteins.	Copper	56-60	small ubiquitin like modifier 1	Homo sapiens	50-55
32061854-9	2020	Our findings provide structural insights into the SUMO1-Cu2+/Zn2+ interaction, and its impact on aggregation of SUMO1 which might affect its ability to modify functions of target proteins.	Copper	56-60	small ubiquitin like modifier 1	Homo sapiens	112-117
32061854-9	2020	Our findings provide structural insights into the SUMO1-Cu2+/Zn2+ interaction, and its impact on aggregation of SUMO1 which might affect its ability to modify functions of target proteins.	Zinc	61-64	small ubiquitin like modifier 1	Homo sapiens	50-55
32115503-10	2020	In addition, we provided evidence that resveratrol inhibited SUMO1 and beta-catenin expression and their nuclear localization in human colonic epithelial cell line (FHC).	Resveratrol	39-50	small ubiquitin like modifier 1	Homo sapiens	61-66
31960982-4	2020	The utility of gamma-selenolysine is demonstrated with the traceless ligation of the small ubiquitin-like modifier protein, SUMO-1, to a peptide segment of human glucokinase.	gamma-selenolysine	15-33	small ubiquitin like modifier 1	Homo sapiens	124-130
31964975-4	2020	In this study, by combining in silico analysis and sgRNA library based drug resistance screening assay, we identified SENP2 (Sentrin/SUMO-specific proteases-2) as a bortezomib sensitive gene and found its expression highly downregulated in bortezomib resistant multiple myeloma patient"s samples.	bortezomib	165-175	small ubiquitin like modifier 1	Homo sapiens	125-132
31964975-4	2020	In this study, by combining in silico analysis and sgRNA library based drug resistance screening assay, we identified SENP2 (Sentrin/SUMO-specific proteases-2) as a bortezomib sensitive gene and found its expression highly downregulated in bortezomib resistant multiple myeloma patient"s samples.	bortezomib	240-250	small ubiquitin like modifier 1	Homo sapiens	125-132
31642335-3	2020	RESULTS: We showed that N-methyl-D-aspartate receptors (NMDARs)-dependent neuronal activity enhancement induced the attachment of small ubiquitin-like modifier 1 (SUMO1) to nNOS.	N-Methylaspartate	24-44	small ubiquitin like modifier 1	Homo sapiens	130-161
31642335-3	2020	RESULTS: We showed that N-methyl-D-aspartate receptors (NMDARs)-dependent neuronal activity enhancement induced the attachment of small ubiquitin-like modifier 1 (SUMO1) to nNOS.	N-Methylaspartate	24-44	small ubiquitin like modifier 1	Homo sapiens	163-168
32115503-12	2020	In conclusions, resveratrol alleviates DSS-induced IBD by modulating SUMO1 through Wnt/beta-catenin pathway.	Resveratrol	16-27	small ubiquitin like modifier 1	Homo sapiens	69-74
32115503-12	2020	In conclusions, resveratrol alleviates DSS-induced IBD by modulating SUMO1 through Wnt/beta-catenin pathway.	dss	39-42	small ubiquitin like modifier 1	Homo sapiens	69-74
31891617-10	2019	CONCLUSIONS: Several of the sarcosine PIC1 variant substitutions synthesized yielded improved solubility as well as a number of unanticipated structure-function findings that provide new insights.	Sarcosine	28-37	small ubiquitin like modifier 1	Homo sapiens	38-42
31839606-3	2020	Recently, we have shown that GMP-1, a 2-(methoxymethyl)pyrimido [1, 2-a] benzimidazol-4-ol, protects mitochondrial function in drosophila and mice models of AD, and improved memory and behavior indicating neuroprotective effect of GMP-1 treatment.	3-(methoxymethyl)indole	38-63	small ubiquitin like modifier 1	Homo sapiens	29-34
31839606-3	2020	Recently, we have shown that GMP-1, a 2-(methoxymethyl)pyrimido [1, 2-a] benzimidazol-4-ol, protects mitochondrial function in drosophila and mice models of AD, and improved memory and behavior indicating neuroprotective effect of GMP-1 treatment.	benzimidazol-2-one	73-90	small ubiquitin like modifier 1	Homo sapiens	29-34
31839606-4	2020	Here, we have found that GMP-1 specifically binds to copper and zinc, metals that are dysregulated in AD brain.	Copper	53-59	small ubiquitin like modifier 1	Homo sapiens	25-30
31839606-6	2020	Also, binding of Zn(II) and Cu(II) by GMP-1 is weaker than the 8-hydroxyquinoline scaffold compound clioquinol previously tested in AD clinical trials.	Zinc	17-23	small ubiquitin like modifier 1	Homo sapiens	38-43
31839606-6	2020	Also, binding of Zn(II) and Cu(II) by GMP-1 is weaker than the 8-hydroxyquinoline scaffold compound clioquinol previously tested in AD clinical trials.	Copper	28-34	small ubiquitin like modifier 1	Homo sapiens	38-43
31839606-6	2020	Also, binding of Zn(II) and Cu(II) by GMP-1 is weaker than the 8-hydroxyquinoline scaffold compound clioquinol previously tested in AD clinical trials.	Oxyquinoline	63-81	small ubiquitin like modifier 1	Homo sapiens	38-43
31839606-7	2020	However, GMP-1 affects Cu(II)-dependent Abeta fibrillization as well as oxidative damage and viability of SH-SY5Y cells upon addition of Cu(II) and Abeta.	Copper	23-29	small ubiquitin like modifier 1	Homo sapiens	9-14
31839606-8	2020	Our data provide new insight on GMP-1 as a Zn(II) and Cu(II) specific metal chelator of moderate affinity that can be responsible for some of its neuroprotective effects observed in AD animal models.	Zinc	43-49	small ubiquitin like modifier 1	Homo sapiens	32-37
31839606-8	2020	Our data provide new insight on GMP-1 as a Zn(II) and Cu(II) specific metal chelator of moderate affinity that can be responsible for some of its neuroprotective effects observed in AD animal models.	Copper	54-60	small ubiquitin like modifier 1	Homo sapiens	32-37
31891617-1	2019	BACKGROUND: A product of rational molecular design, PA-dPEG24 is the lead derivative of the PIC1 family of peptides with multiple functional abilities including classical complement pathway inhibition, myeloperoxidase inhibition, NET inhibition and antioxidant activity.	pentaerythritol poly(ethylene glycol) ether tetrasuccinimidyl glutarate	55-61	small ubiquitin like modifier 1	Homo sapiens	92-96
31544029-11	2019	SUMO1 or SIRT1 overexpression and MG132 or RSV treatment affected the nuclear expression and activity of IkappaBalpha and NF-kappaB p65 under high glucose condition.	Glucose	147-154	small ubiquitin like modifier 1	Homo sapiens	0-5
31502464-5	2019	Modified forms of SUMO1 or SUMO2, with a histidine tag and a Thr to Lys mutation preceding the carboxyl-terminal di-gly motif, were expressed in mpkCCD14 cells, allowing SUMO-conjugated proteins to be purified and identified.	Histidine	41-50	small ubiquitin like modifier 1	Homo sapiens	18-23
31502464-5	2019	Modified forms of SUMO1 or SUMO2, with a histidine tag and a Thr to Lys mutation preceding the carboxyl-terminal di-gly motif, were expressed in mpkCCD14 cells, allowing SUMO-conjugated proteins to be purified and identified.	Threonine	61-64	small ubiquitin like modifier 1	Homo sapiens	18-23
31502464-5	2019	Modified forms of SUMO1 or SUMO2, with a histidine tag and a Thr to Lys mutation preceding the carboxyl-terminal di-gly motif, were expressed in mpkCCD14 cells, allowing SUMO-conjugated proteins to be purified and identified.	Lysine	68-71	small ubiquitin like modifier 1	Homo sapiens	18-23
31502464-5	2019	Modified forms of SUMO1 or SUMO2, with a histidine tag and a Thr to Lys mutation preceding the carboxyl-terminal di-gly motif, were expressed in mpkCCD14 cells, allowing SUMO-conjugated proteins to be purified and identified.	di-gly	113-119	small ubiquitin like modifier 1	Homo sapiens	18-23
31546024-3	2019	Our results indicated that the SUMO1 acceptor site of NRF2 is the conserved lysine residue 110 (K110), and that NRF2 SUMOylation deficiency inhibited tumorigenesis in hepatocellular carcinoma (HCC).	Lysine	76-82	small ubiquitin like modifier 1	Homo sapiens	31-36
31546024-3	2019	Our results indicated that the SUMO1 acceptor site of NRF2 is the conserved lysine residue 110 (K110), and that NRF2 SUMOylation deficiency inhibited tumorigenesis in hepatocellular carcinoma (HCC).	Fmoc-Cys(tBu)-OH	96-100	small ubiquitin like modifier 1	Homo sapiens	31-36
31654699-5	2019	Cells pre-treated with either GA or the related compound, anacardic acid, revealed a significant decrease in intracytoplasmic aggregates immunopositive for alpha-syn and SUMO-1.	ginkgolic acid	30-32	small ubiquitin like modifier 1	Homo sapiens	170-176
31654699-5	2019	Cells pre-treated with either GA or the related compound, anacardic acid, revealed a significant decrease in intracytoplasmic aggregates immunopositive for alpha-syn and SUMO-1.	Anacardic Acids	58-72	small ubiquitin like modifier 1	Homo sapiens	170-176
31544029-5	2019	With NAC, DTT, MG132 or Resveratrol (RSV) treatment, SUMO1 and SIRT1 expressions were detected by WB.	dithiothreitol tetraacetate	10-13	small ubiquitin like modifier 1	Homo sapiens	53-58
30975281-11	2019	Conclusion C/EBPalpha can be modified by SUMO1 and the site of its modification is the 161st lysine in human AECII.	Lysine	93-99	small ubiquitin like modifier 1	Homo sapiens	41-46
31544029-5	2019	With NAC, DTT, MG132 or Resveratrol (RSV) treatment, SUMO1 and SIRT1 expressions were detected by WB.	resveratrol	37-40	small ubiquitin like modifier 1	Homo sapiens	53-58
31544029-8	2019	RESULTS: SUMO1 and SIRT1 expressions were influenced by high glucose in mRNA and protein levels, which could be blocked by NAC or DTT.	Glucose	61-68	small ubiquitin like modifier 1	Homo sapiens	9-14
31544029-8	2019	RESULTS: SUMO1 and SIRT1 expressions were influenced by high glucose in mRNA and protein levels, which could be blocked by NAC or DTT.	dithiothreitol tetraacetate	130-133	small ubiquitin like modifier 1	Homo sapiens	9-14
31544029-9	2019	SUMO1 was down-regulated by using MG132, and SIRT1 was up-regulated under RSV treatment.	resveratrol	74-77	small ubiquitin like modifier 1	Homo sapiens	0-5
31125786-4	2019	Here we report that Csk is covalently modified by SUMO1 at lysine 53 (K53) both in vitro and in vivo.	Lysine	59-65	small ubiquitin like modifier 1	Homo sapiens	50-55
30873037-8	2019	S-CMC inhibited CSE-induced SUMO1 modification of HDAC2 in the presence of thiol/GSH, increased HDAC activity, and decreased IL-8 expression.	Sulfhydryl Compounds	75-80	small ubiquitin like modifier 1	Homo sapiens	28-33
30873037-8	2019	S-CMC inhibited CSE-induced SUMO1 modification of HDAC2 in the presence of thiol/GSH, increased HDAC activity, and decreased IL-8 expression.	Glutathione	81-84	small ubiquitin like modifier 1	Homo sapiens	28-33
30828290-13	2019	For that reason, the SUMO pathway including SUMO1, SUMO2, Ubc9, and DAT SUMOylation, can be critical therapeutic targets in regulating DAT stability and dopamine clearance in health and pathological states.	Dopamine	153-161	small ubiquitin like modifier 1	Homo sapiens	44-49
31616295-9	2019	Finally, we found that Ssd could reverse the effects promoted by hypoxia, specifically active sentrin/small ubiquitin-like modifier (SUMO)-specific protease 5 (SENP5), a SUMO-specific protease, in a time- and dose-dependent manner while inhibiting the expression of SUMO1 and GLI proteins.	saikosaponin D	23-26	small ubiquitin like modifier 1	Homo sapiens	94-101
31616295-9	2019	Finally, we found that Ssd could reverse the effects promoted by hypoxia, specifically active sentrin/small ubiquitin-like modifier (SUMO)-specific protease 5 (SENP5), a SUMO-specific protease, in a time- and dose-dependent manner while inhibiting the expression of SUMO1 and GLI proteins.	saikosaponin D	23-26	small ubiquitin like modifier 1	Homo sapiens	266-271
30407877-4	2019	When the mAChR was activated by the agonist carbachol, the colocalization of the M1 mAChR and SUMO-1 protein markedly decreased in immunoprecipitation and immunofluorescence assays.	Carbachol	44-53	small ubiquitin like modifier 1	Homo sapiens	94-100
30516430-4	2019	Here, we show that periplakin is SUMOylated at a conserved lysine in its linker domain (K1646) preferentially by small ubiquitin-like modifier 1 (SUMO1).	Lysine	59-65	small ubiquitin like modifier 1	Homo sapiens	113-144
30516430-4	2019	Here, we show that periplakin is SUMOylated at a conserved lysine in its linker domain (K1646) preferentially by small ubiquitin-like modifier 1 (SUMO1).	Lysine	59-65	small ubiquitin like modifier 1	Homo sapiens	146-151
30838143-0	2019	Ceftriaxone-Induced Immune Hemolytic Anemia: In Vitro Reversal with Peptide Inhibitor of Complement C1 (PIC1).	Ceftriaxone	0-11	small ubiquitin like modifier 1	Homo sapiens	104-108
30838143-6	2019	We confirmed that ceftriaxone initiated a classical complement pathway-mediated hemolysis by in vitro reversal with peptide inhibitor of complement C1 (PIC1).	Ceftriaxone	18-29	small ubiquitin like modifier 1	Homo sapiens	152-156
29654697-7	2018	Interestingly, melatonin attenuated small ubiquitin-related modifier-1 (SUMO-1) more than SUMO-2 or SUMO-3 and disturbed nuclear translocation of nestin for direct binding to c-Myc by SUMOylation of SUMO-1 protein by immunofluorescence and immunoprecipitation.	Melatonin	15-24	small ubiquitin like modifier 1	Homo sapiens	72-78
30184152-5	2018	Here, we report that FEN1 undergoes SUMOylation by SUMO-1 in response to DNA replication fork-stalling agents, such as UV irradiation, hydroxyurea, and mitomycin C.	Hydroxyurea	135-146	small ubiquitin like modifier 1	Homo sapiens	51-57
30184152-5	2018	Here, we report that FEN1 undergoes SUMOylation by SUMO-1 in response to DNA replication fork-stalling agents, such as UV irradiation, hydroxyurea, and mitomycin C.	Mitomycin	152-163	small ubiquitin like modifier 1	Homo sapiens	51-57
29654697-7	2018	Interestingly, melatonin attenuated small ubiquitin-related modifier-1 (SUMO-1) more than SUMO-2 or SUMO-3 and disturbed nuclear translocation of nestin for direct binding to c-Myc by SUMOylation of SUMO-1 protein by immunofluorescence and immunoprecipitation.	Melatonin	15-24	small ubiquitin like modifier 1	Homo sapiens	36-70
29654697-7	2018	Interestingly, melatonin attenuated small ubiquitin-related modifier-1 (SUMO-1) more than SUMO-2 or SUMO-3 and disturbed nuclear translocation of nestin for direct binding to c-Myc by SUMOylation of SUMO-1 protein by immunofluorescence and immunoprecipitation.	Melatonin	15-24	small ubiquitin like modifier 1	Homo sapiens	199-205
29506078-3	2018	Here we find that METTL3 is modified by SUMO1 mainly at lysine residues K177, K211, K212 and K215, which can be reduced by an SUMO1-specific protease SENP1.	Lysine	56-62	small ubiquitin like modifier 1	Homo sapiens	40-45
30197588-4	2018	In this study, exposure to high METH doses increased the expression of alpha-syn and the small ubiquitin-related modifier 1 (SUMO-1).	Methamphetamine	32-36	small ubiquitin like modifier 1	Homo sapiens	89-123
30197588-4	2018	In this study, exposure to high METH doses increased the expression of alpha-syn and the small ubiquitin-related modifier 1 (SUMO-1).	Methamphetamine	32-36	small ubiquitin like modifier 1	Homo sapiens	125-131
30197588-10	2018	The results showed that METH exposure decreases the SUMOylation level of alpha-syn, although the expression of alpha-syn and SUMO-1 are increased.	Methamphetamine	24-28	small ubiquitin like modifier 1	Homo sapiens	125-131
29506078-3	2018	Here we find that METTL3 is modified by SUMO1 mainly at lysine residues K177, K211, K212 and K215, which can be reduced by an SUMO1-specific protease SENP1.	Lysine	56-62	small ubiquitin like modifier 1	Homo sapiens	126-131
29599708-4	2018	We report that the DJ-1M26I mutant influences DJ-1 interactions with SUMO-1, in turn enhancing removal of mitochondria and conferring increased cellular susceptibility to dopamine toxicity.	Dopamine	171-179	small ubiquitin like modifier 1	Homo sapiens	69-75
29713182-16	2018	PKM2 could be covalently modified by SUMO1 at K336 (Lys336) site.	1,3-dimethylbarbituric acid	46-50	small ubiquitin like modifier 1	Homo sapiens	37-42
29713182-17	2018	SUMO1 modification of PKM2 at Lys-336 site increased glycolysis and promoted its cofactor functions.	Lysine	30-33	small ubiquitin like modifier 1	Homo sapiens	0-5
29632531-3	2018	The lead PIC1 derivative, PA-dPEG24, was able to dose-dependently inhibit complement activation initiated by multiple types of immune complexes (IC), including C1-anti-C1q IC, limiting the generation of pro-inflammatory complement effectors, including C5a and membrane attack complex (sC5b-9).	Protactinium	26-28	small ubiquitin like modifier 1	Homo sapiens	9-13
29481054-6	2018	NMR studies identified that streptonigrin binds to SENP1 on the surface where SUMO binds and disrupts SENP1-SUMO1 interaction.	Streptonigrin	28-41	small ubiquitin like modifier 1	Homo sapiens	108-113
29499069-0	2018	Peptide Inhibitor of Complement C1 (PIC1) demonstrates antioxidant activity via single electron transport (SET) and hydrogen atom transfer (HAT).	Hydrogen	116-124	small ubiquitin like modifier 1	Homo sapiens	0-34
29499069-0	2018	Peptide Inhibitor of Complement C1 (PIC1) demonstrates antioxidant activity via single electron transport (SET) and hydrogen atom transfer (HAT).	Hydrogen	116-124	small ubiquitin like modifier 1	Homo sapiens	36-40
29499069-3	2018	We have recently demonstrated that Peptide Inhibitor of Complement C1 (PIC1) mitigates peroxidase activity of the heme bearing proteins myeloperoxidase, hemoglobin, and myoglobin through a reversible process.	Heme	114-118	small ubiquitin like modifier 1	Homo sapiens	35-69
29499069-3	2018	We have recently demonstrated that Peptide Inhibitor of Complement C1 (PIC1) mitigates peroxidase activity of the heme bearing proteins myeloperoxidase, hemoglobin, and myoglobin through a reversible process.	Heme	114-118	small ubiquitin like modifier 1	Homo sapiens	71-75
29499069-5	2018	PIC1 showed dose-dependent antioxidant activity in a total antioxidant (TAC) assay, hydroxyl radical antioxidant capacity (HORAC) assay, oxygen radical antioxidant capacity (ORAC) assay as well as the thiobarbituric acid reactive substances (TBARS) assay to screen for PIC1 antioxidant activity in human plasma.	Hydroxyl Radical	84-92	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-5	2018	PIC1 showed dose-dependent antioxidant activity in a total antioxidant (TAC) assay, hydroxyl radical antioxidant capacity (HORAC) assay, oxygen radical antioxidant capacity (ORAC) assay as well as the thiobarbituric acid reactive substances (TBARS) assay to screen for PIC1 antioxidant activity in human plasma.	Oxygen	137-143	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-5	2018	PIC1 showed dose-dependent antioxidant activity in a total antioxidant (TAC) assay, hydroxyl radical antioxidant capacity (HORAC) assay, oxygen radical antioxidant capacity (ORAC) assay as well as the thiobarbituric acid reactive substances (TBARS) assay to screen for PIC1 antioxidant activity in human plasma.	Thiobarbituric Acid Reactive Substances	201-240	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-5	2018	PIC1 showed dose-dependent antioxidant activity in a total antioxidant (TAC) assay, hydroxyl radical antioxidant capacity (HORAC) assay, oxygen radical antioxidant capacity (ORAC) assay as well as the thiobarbituric acid reactive substances (TBARS) assay to screen for PIC1 antioxidant activity in human plasma.	Thiobarbituric Acid Reactive Substances	242-247	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-8	2018	PIC1 contains two vicinal cysteine residues and displayed similar antioxidant activity to the well characterized cysteine-containing tripeptide antioxidant molecule glutathione (GSH).	Cysteine	26-34	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-8	2018	PIC1 contains two vicinal cysteine residues and displayed similar antioxidant activity to the well characterized cysteine-containing tripeptide antioxidant molecule glutathione (GSH).	Cysteine	113-121	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-8	2018	PIC1 contains two vicinal cysteine residues and displayed similar antioxidant activity to the well characterized cysteine-containing tripeptide antioxidant molecule glutathione (GSH).	Glutathione	178-181	small ubiquitin like modifier 1	Homo sapiens	0-4
29499069-9	2018	Consistent with the role of the cysteine residues in the antioxidant activity of PIC1, oxidation of these residues significantly abrogated antioxidant activity.	Cysteine	32-40	small ubiquitin like modifier 1	Homo sapiens	81-85
29393359-4	2018	Further experiments confirmed that the conjugated site of Cx43 by SUMO1 was located in Lys-144 and Lys-237, both of which are highly conserved among species.	Lysine	87-90	small ubiquitin like modifier 1	Homo sapiens	66-71
29393359-4	2018	Further experiments confirmed that the conjugated site of Cx43 by SUMO1 was located in Lys-144 and Lys-237, both of which are highly conserved among species.	Lysine	99-102	small ubiquitin like modifier 1	Homo sapiens	66-71
29221668-5	2018	The SMAD4 was markedly reduced in both mRNA and protein levels in the H2O2 -treated hFOB1.19 cells, along with the reduction of Small ubiquitin-related modifier 1 (SUMO 1) and SUMO 2/3.	Hydrogen Peroxide	70-74	small ubiquitin like modifier 1	Homo sapiens	128-162
29221668-5	2018	The SMAD4 was markedly reduced in both mRNA and protein levels in the H2O2 -treated hFOB1.19 cells, along with the reduction of Small ubiquitin-related modifier 1 (SUMO 1) and SUMO 2/3.	Hydrogen Peroxide	70-74	small ubiquitin like modifier 1	Homo sapiens	164-170
29242151-8	2018	Inhibition of nuclear accumulation by the COX-2 specific inhibitor, NS-398, inhibited co-localization of nuclear COX-2 and SUMO-1.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	68-74	small ubiquitin like modifier 1	Homo sapiens	123-129
29242151-10	2018	Finally, inhibition of SUMO-1 expression also reduced resveratrol-induced expression of pro-apoptotic genes but increased the expression of proliferative genes.	Resveratrol	54-65	small ubiquitin like modifier 1	Homo sapiens	23-29
29242151-11	2018	In summary, these results demonstrate that inducible COX-2 associates with phosphorylated ERK1/2 to induce the phosphorylation of Ser-15 in p53 and then complexes with p53 and SUMO-1 which binds to p53-responsive pro-apoptotic genes to enhance their expression.	Serine	130-133	small ubiquitin like modifier 1	Homo sapiens	176-182
30277836-0	2018	Sorafenib inhibits caspase-1 expression through suppressing TLR4/stat3/SUMO1 pathway in hepatocellular carcinoma.	Sorafenib	0-9	small ubiquitin like modifier 1	Homo sapiens	71-76
30277836-6	2018	Co-immunoprecipitation (Co-IP) experiments and immunoblot analysis indicated that sorafenib treatment decreased the SUMOylation of p65 via inhibiting TLR4/stat3/SUMO1 signaling cascades.	Sorafenib	82-91	small ubiquitin like modifier 1	Homo sapiens	161-166
29018572-3	2017	Here we found that HOXA10 was modified by small ubiquitin like-modifier 1 (SUMO1) at the evolutionarily conserved lysine 164 residue.	Lysine	114-120	small ubiquitin like modifier 1	Homo sapiens	42-73
29115559-5	2018	Expression levels of SUMO1 and SUMO2/3 proteins in the normoxia group were significantly lower than those in the medium- or high-oxygen groups (P<0.01), but were comparable to those in the low-oxygen group.	Oxygen	129-135	small ubiquitin like modifier 1	Homo sapiens	21-26
29115559-5	2018	Expression levels of SUMO1 and SUMO2/3 proteins in the normoxia group were significantly lower than those in the medium- or high-oxygen groups (P<0.01), but were comparable to those in the low-oxygen group.	Oxygen	196-202	small ubiquitin like modifier 1	Homo sapiens	21-26
29115559-8	2018	Supplemental oxygen with FiO2>=30% was associated with upregulation of SUMO1 and SUMO2/3 expression and downregulation of SIRT1 expression.	Oxygen	13-19	small ubiquitin like modifier 1	Homo sapiens	74-79
29018572-5	2017	SUMO1-modified HOXA10 expression was decreased in estradiol- and progesterone-treated Ishikawa cells.	Progesterone	65-77	small ubiquitin like modifier 1	Homo sapiens	0-5
29018572-3	2017	Here we found that HOXA10 was modified by small ubiquitin like-modifier 1 (SUMO1) at the evolutionarily conserved lysine 164 residue.	Lysine	114-120	small ubiquitin like modifier 1	Homo sapiens	75-80
29018572-5	2017	SUMO1-modified HOXA10 expression was decreased in estradiol- and progesterone-treated Ishikawa cells.	Estradiol	50-59	small ubiquitin like modifier 1	Homo sapiens	0-5
28055018-3	2017	We identified lysines (K) 122 and 142 as the major Sumo1 conjugation sites in Prdx6.	Lysine	14-21	small ubiquitin like modifier 1	Homo sapiens	51-56
28135312-4	2017	Using TMB as the oxidizing substrate, PIC1 inhibited myeloperoxidase activity in cystic fibrosis sputum soluble fractions by an average of a 3.4-fold decrease (P = 0.02).	3,3',5,5'-tetramethylbenzidine	6-9	small ubiquitin like modifier 1	Homo sapiens	38-42
28135312-6	2017	PIC1 inhibited myeloperoxidase activity similarly, on a molar basis, as the specific myeloperoxidase inhibitor 4-Aminobenzoic acid hydrazide (ABAH) for various oxidizing substrates.	4-aminobenzhydrazide	111-140	small ubiquitin like modifier 1	Homo sapiens	0-4
28135312-6	2017	PIC1 inhibited myeloperoxidase activity similarly, on a molar basis, as the specific myeloperoxidase inhibitor 4-Aminobenzoic acid hydrazide (ABAH) for various oxidizing substrates.	4-aminobenzhydrazide	142-146	small ubiquitin like modifier 1	Homo sapiens	0-4
28135312-7	2017	PIC1 was able to protect the heme ring of myeloperoxidase from destruction by NaOCl, assayed by spectral analysis.	Sodium Hypochlorite	78-83	small ubiquitin like modifier 1	Homo sapiens	0-4
28135312-8	2017	PIC1 incubated with oxidized TMB reversed the oxidation state of TMB, as measured by absorbance at 450 nm, with a 20-fold reduction in oxidized TMB (P = 0.02).	3,3',5,5'-tetramethylbenzidine	29-32	small ubiquitin like modifier 1	Homo sapiens	0-4
28135312-8	2017	PIC1 incubated with oxidized TMB reversed the oxidation state of TMB, as measured by absorbance at 450 nm, with a 20-fold reduction in oxidized TMB (P = 0.02).	3,3',5,5'-tetramethylbenzidine	65-68	small ubiquitin like modifier 1	Homo sapiens	0-4
28135312-8	2017	PIC1 incubated with oxidized TMB reversed the oxidation state of TMB, as measured by absorbance at 450 nm, with a 20-fold reduction in oxidized TMB (P = 0.02).	3,3',5,5'-tetramethylbenzidine	65-68	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-5	2017	PIC1 reversibly and dose-dependently prevented TMB oxidation to tetramethylbenzidine diimine by RBC lysates, methemoglobin, and myoglobin, having comparable activity to the inhibitor 4-aminobenzoic acid hydrazide.	3,3',5,5'-tetramethylbenzidine	47-50	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-7	2017	PIC1 also inhibited heme destruction by NaOCl for RBC lysates, hemoglobin, and myoglobin as assayed by preservation of the Soret absorbance peak in the presence of NaOCl and reduction in free iron release.	Sodium Hypochlorite	40-45	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-5	2017	PIC1 reversibly and dose-dependently prevented TMB oxidation to tetramethylbenzidine diimine by RBC lysates, methemoglobin, and myoglobin, having comparable activity to the inhibitor 4-aminobenzoic acid hydrazide.	tetramethylbenzidine diimine	64-92	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-7	2017	PIC1 also inhibited heme destruction by NaOCl for RBC lysates, hemoglobin, and myoglobin as assayed by preservation of the Soret absorbance peak in the presence of NaOCl and reduction in free iron release.	Sodium Hypochlorite	164-169	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-7	2017	PIC1 also inhibited heme destruction by NaOCl for RBC lysates, hemoglobin, and myoglobin as assayed by preservation of the Soret absorbance peak in the presence of NaOCl and reduction in free iron release.	Iron	192-196	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-5	2017	PIC1 reversibly and dose-dependently prevented TMB oxidation to tetramethylbenzidine diimine by RBC lysates, methemoglobin, and myoglobin, having comparable activity to the inhibitor 4-aminobenzoic acid hydrazide.	4-aminobenzhydrazide	183-212	small ubiquitin like modifier 1	Homo sapiens	0-4
29081812-6	2017	PIC1 inhibited TMB oxidation of RBC lysates similar to L-cysteine suggesting that the two cysteine residues contained in PIC1 may mediate peroxidase activity.	3,3',5,5'-tetramethylbenzidine	15-18	small ubiquitin like modifier 1	Homo sapiens	0-4
26582473-5	2016	We found also that F508del CFTR could be modified by SUMO-1, a paralog that does not support SUMO polychain formation.	f508del	19-26	small ubiquitin like modifier 1	Homo sapiens	53-59
27150054-6	2016	Moreover, co-immunoprecipitation showed that rigosertib induced sequestration of c-Myb and TRAF6 in the cytoplasm by stimulating their sumoylation through the RanGAP1*SUMO1/Ubc9 pathway.	ON 01910	45-55	small ubiquitin like modifier 1	Homo sapiens	167-172
27181354-2	2016	Here, we found that as expected puromycin induced SUMO-1/2/3 accumulation with ubiquitin at multiple nuclear foci in HeLa cells when co-exposed to MG132.	Puromycin	32-41	small ubiquitin like modifier 1	Homo sapiens	50-60
27181354-2	2016	Here, we found that as expected puromycin induced SUMO-1/2/3 accumulation with ubiquitin at multiple nuclear foci in HeLa cells when co-exposed to MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	147-152	small ubiquitin like modifier 1	Homo sapiens	50-60
27023496-5	2016	A fraction named GMP-1 was obtained after isolation and purification by DEAE-52 and Sephadex G-100 gel chromatography, respectively.	deae-52	72-79	small ubiquitin like modifier 1	Homo sapiens	17-22
27023496-5	2016	A fraction named GMP-1 was obtained after isolation and purification by DEAE-52 and Sephadex G-100 gel chromatography, respectively.	sephadex	84-98	small ubiquitin like modifier 1	Homo sapiens	17-22
27023496-6	2016	GMP-1, with a molecular weight of 401 kDa, mainly consisted of galacturonic acid (GalA), xylose (Xyl), glucose (Glu).	galacturonic acid	63-80	small ubiquitin like modifier 1	Homo sapiens	0-5
27023496-6	2016	GMP-1, with a molecular weight of 401 kDa, mainly consisted of galacturonic acid (GalA), xylose (Xyl), glucose (Glu).	galacturonic acid	82-86	small ubiquitin like modifier 1	Homo sapiens	0-5
27023496-6	2016	GMP-1, with a molecular weight of 401 kDa, mainly consisted of galacturonic acid (GalA), xylose (Xyl), glucose (Glu).	Xylose	89-95	small ubiquitin like modifier 1	Homo sapiens	0-5
27023496-6	2016	GMP-1, with a molecular weight of 401 kDa, mainly consisted of galacturonic acid (GalA), xylose (Xyl), glucose (Glu).	Xylose	97-100	small ubiquitin like modifier 1	Homo sapiens	0-5
27023496-6	2016	GMP-1, with a molecular weight of 401 kDa, mainly consisted of galacturonic acid (GalA), xylose (Xyl), glucose (Glu).	Glucose	103-110	small ubiquitin like modifier 1	Homo sapiens	0-5
27023496-6	2016	GMP-1, with a molecular weight of 401 kDa, mainly consisted of galacturonic acid (GalA), xylose (Xyl), glucose (Glu).	Glucose	112-115	small ubiquitin like modifier 1	Homo sapiens	0-5
27023496-7	2016	Infrared spectroscopy was used to characterize the major functional groups of GMP-1 and the results indicated that it was an acidic polysaccharide.	Polysaccharides	132-146	small ubiquitin like modifier 1	Homo sapiens	78-83
27230680-0	2016	Prostaglandin E2 (PGE2) promotes proliferation and invasion by enhancing SUMO-1 activity via EP4 receptor in endometrial cancer.	Dinoprostone	0-16	small ubiquitin like modifier 1	Homo sapiens	73-79
27230680-0	2016	Prostaglandin E2 (PGE2) promotes proliferation and invasion by enhancing SUMO-1 activity via EP4 receptor in endometrial cancer.	Dinoprostone	18-22	small ubiquitin like modifier 1	Homo sapiens	73-79
27230680-7	2016	PGE2 stimulation enhanced the expression of SUMO-1, via PGE2 receptor subtype 4 (EP4).	Dinoprostone	0-4	small ubiquitin like modifier 1	Homo sapiens	44-50
27507651-1	2016	Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic.	Lysine	85-88	small ubiquitin like modifier 1	Homo sapiens	64-69
27507651-1	2016	Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic.	Arsenic	149-156	small ubiquitin like modifier 1	Homo sapiens	64-69
27507651-1	2016	Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic.	Arsenic	225-232	small ubiquitin like modifier 1	Homo sapiens	64-69
27195426-0	2016	A Central Cysteine Residue Is Essential for the Thermal Stability and Function of SUMO-1 Protein and SUMO-1 Peptide-Protein Conjugates.	Cysteine	10-18	small ubiquitin like modifier 1	Homo sapiens	82-88
27195426-0	2016	A Central Cysteine Residue Is Essential for the Thermal Stability and Function of SUMO-1 Protein and SUMO-1 Peptide-Protein Conjugates.	Cysteine	10-18	small ubiquitin like modifier 1	Homo sapiens	101-107
27195426-2	2016	The small ubiquitin-like modifier-1 (SUMO-1) features a central and conserved cysteine residue (Cys52) that is located in the hydrophobic core of the protein and in tight contact with Phe65, suggesting the occurrence of an S/pi interaction.	Cysteine	78-86	small ubiquitin like modifier 1	Homo sapiens	4-35
27195426-2	2016	The small ubiquitin-like modifier-1 (SUMO-1) features a central and conserved cysteine residue (Cys52) that is located in the hydrophobic core of the protein and in tight contact with Phe65, suggesting the occurrence of an S/pi interaction.	Cysteine	78-86	small ubiquitin like modifier 1	Homo sapiens	37-43
27284413-6	2016	Furthermore, small ubiquitin-related modifier 1 and several other ubiquitin proteasome pathway (UPP)-related proteins expressed higher levels in TRAIL-resistant cells U266 compared to the RPMI-8226 cells prior and subsequent to rmhTRAIL treatment.	rpmi	188-192	small ubiquitin like modifier 1	Homo sapiens	13-47
26549688-11	2016	Substitution of all its four putative lysine residues along with NDSM abolished the effect of SUMO-1-mediated transactivation function of PXR.	Lysine	38-44	small ubiquitin like modifier 1	Homo sapiens	94-100
26450989-6	2016	Using different p27(Kip1) point mutants, we identified lysine 134 (K134) as the residue modified by small ubiquitin-like modifier 1 (SUMO1) in response to TGFbeta treatment.	Lysine	55-61	small ubiquitin like modifier 1	Homo sapiens	100-131
26450989-6	2016	Using different p27(Kip1) point mutants, we identified lysine 134 (K134) as the residue modified by small ubiquitin-like modifier 1 (SUMO1) in response to TGFbeta treatment.	Lysine	55-61	small ubiquitin like modifier 1	Homo sapiens	133-138
26450989-6	2016	Using different p27(Kip1) point mutants, we identified lysine 134 (K134) as the residue modified by small ubiquitin-like modifier 1 (SUMO1) in response to TGFbeta treatment.	K-134	67-71	small ubiquitin like modifier 1	Homo sapiens	100-131
26450989-6	2016	Using different p27(Kip1) point mutants, we identified lysine 134 (K134) as the residue modified by small ubiquitin-like modifier 1 (SUMO1) in response to TGFbeta treatment.	K-134	67-71	small ubiquitin like modifier 1	Homo sapiens	133-138
26837744-1	2016	SUMOylation is a ubiquitin-related transient posttranslational modification pathway catalyzing the conjugation of small ubiquitin-like modifier (SUMO) proteins (SUMO1, SUMO2, and SUMO3) to lysine residues of proteins.	Lysine	189-195	small ubiquitin like modifier 1	Homo sapiens	161-166
25877955-9	2015	RESULTS: High glucose treatment induced SUMO1-4 expression and enhanced the expression of Cbx4 and PIASy.	Glucose	14-21	small ubiquitin like modifier 1	Homo sapiens	40-45
27246205-3	2016	HDAC2 has been shown to be modified by SUMO1 at lysine 462.	Lysine	48-54	small ubiquitin like modifier 1	Homo sapiens	39-44
26212320-3	2015	During metabolic stress, SUMO1 modification of LKB1 lysine 178 is essential in promoting its interaction with AMPK via a SUMO-interacting motif (SIM) essential for AMPK activation.	Lysine	52-58	small ubiquitin like modifier 1	Homo sapiens	25-30
26268556-5	2015	The solution structure of Usp28 UBR was obtained, and the key residues responsible for ubiquitin and SUMO1/2 recognition were identified.	ubr	32-35	small ubiquitin like modifier 1	Homo sapiens	101-106
26157143-3	2015	We have shown previously that the nuclear form of phosphatidylinositol-4-phosphate 5-kinase 1alpha (PIP5K), the enzyme responsible for phosphatidylinositol 4,5-bisphosphate synthesis, is modified by small ubiquitin-like modifier (SUMO)-1.	Phosphatidylinositols	50-70	small ubiquitin like modifier 1	Homo sapiens	199-237
26157143-3	2015	We have shown previously that the nuclear form of phosphatidylinositol-4-phosphate 5-kinase 1alpha (PIP5K), the enzyme responsible for phosphatidylinositol 4,5-bisphosphate synthesis, is modified by small ubiquitin-like modifier (SUMO)-1.	Phosphatidylinositol 4,5-Diphosphate	135-172	small ubiquitin like modifier 1	Homo sapiens	199-237
25917782-3	2015	Here we explored a stable chemical conjugate of the E2 enzyme from the SUMO pathway, Ubc9, with its modifier SUMO1 as a structural analogue of the Ubc9~SUMO1 thioester intermediate, by introducing a triazole linkage by biorthogonal click chemistry.	Triazoles	199-207	small ubiquitin like modifier 1	Homo sapiens	109-114
26060329-5	2015	We hypothesized that constitutive SUMO2 conjugation and deconjugation occurred basally and that arsenic trioxide treatment caused the exchange of SUMO2 for SUMO1 on a fraction of Lys(65) in PML.	Arsenic Trioxide	96-112	small ubiquitin like modifier 1	Homo sapiens	156-161
26060329-5	2015	We hypothesized that constitutive SUMO2 conjugation and deconjugation occurred basally and that arsenic trioxide treatment caused the exchange of SUMO2 for SUMO1 on a fraction of Lys(65) in PML.	Lysine	179-182	small ubiquitin like modifier 1	Homo sapiens	156-161
26090800-4	2015	Here, we report the covalent modification of delta-lactoferrin with the small ubiquitin-like modifier SUMO-1.	delta-lactoferrin	45-62	small ubiquitin like modifier 1	Homo sapiens	102-108
26090800-6	2015	The SUMOylation deficient M5S mutant displayed enhanced transactivation capacity on a delta-lactoferrin responsive promoter, suggesting that SUMO-1 negatively regulates the transactivation function of delta-lactoferrin.	delta-lactoferrin	86-103	small ubiquitin like modifier 1	Homo sapiens	141-147
26090800-6	2015	The SUMOylation deficient M5S mutant displayed enhanced transactivation capacity on a delta-lactoferrin responsive promoter, suggesting that SUMO-1 negatively regulates the transactivation function of delta-lactoferrin.	delta-lactoferrin	201-218	small ubiquitin like modifier 1	Homo sapiens	141-147
25917782-3	2015	Here we explored a stable chemical conjugate of the E2 enzyme from the SUMO pathway, Ubc9, with its modifier SUMO1 as a structural analogue of the Ubc9~SUMO1 thioester intermediate, by introducing a triazole linkage by biorthogonal click chemistry.	Triazoles	199-207	small ubiquitin like modifier 1	Homo sapiens	152-157
25917782-5	2015	Triazole-linked Ubc9-SUMO1 bound specifically to the preassembled E3 ligase complex RanBP2/RanGAP1*SUMO1/Ubc9, thus suggesting that it is a suitable thioester mimic.	Triazoles	0-8	small ubiquitin like modifier 1	Homo sapiens	21-26
25917782-5	2015	Triazole-linked Ubc9-SUMO1 bound specifically to the preassembled E3 ligase complex RanBP2/RanGAP1*SUMO1/Ubc9, thus suggesting that it is a suitable thioester mimic.	Triazoles	0-8	small ubiquitin like modifier 1	Homo sapiens	99-104
25823821-2	2015	Here we report that Shp2 is modified by SUMO1 at lysine residue 590 (K590) in its C-terminus, which is reduced by SUMO1-specific protease SENP1.	Lysine	49-55	small ubiquitin like modifier 1	Homo sapiens	40-45
25823821-2	2015	Here we report that Shp2 is modified by SUMO1 at lysine residue 590 (K590) in its C-terminus, which is reduced by SUMO1-specific protease SENP1.	Lysine	49-55	small ubiquitin like modifier 1	Homo sapiens	114-119
25823821-2	2015	Here we report that Shp2 is modified by SUMO1 at lysine residue 590 (K590) in its C-terminus, which is reduced by SUMO1-specific protease SENP1.	Salmeterol Xinafoate	69-73	small ubiquitin like modifier 1	Homo sapiens	40-45
25118297-10	2014	When SDF was induced by stressful conditions (freezing and thawing and oxidative stress), SUMO1-ylation increased.	[(R)-(2,4-dichlorophenyl)(sulfanyl)methyl]phosphonic acid	5-8	small ubiquitin like modifier 1	Homo sapiens	90-95
25823821-2	2015	Here we report that Shp2 is modified by SUMO1 at lysine residue 590 (K590) in its C-terminus, which is reduced by SUMO1-specific protease SENP1.	Salmeterol Xinafoate	69-73	small ubiquitin like modifier 1	Homo sapiens	114-119
25236368-1	2015	Small ubiquitin-like modifier (SUMO1-3) conjugation is a posttranslational protein modification whereby SUMOs are conjugated to lysine residues of target proteins.	Lysine	128-134	small ubiquitin like modifier 1	Homo sapiens	31-38
25497731-3	2015	The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SIM peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1.	Phosphoserine	119-133	small ubiquitin like modifier 1	Homo sapiens	26-31
25497731-3	2015	The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SIM peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1.	Phosphoserine	119-133	small ubiquitin like modifier 1	Homo sapiens	191-196
25447205-5	2015	The interaction of MxA with Small-Ubiquitin MOdifier 1 (SUMO1) and Ubiquitin conjugating enzyme 9 (Ubc9) was confirmed by co-immunoprecipitation and co-localization by confocal microscopy.	piritrexim	19-22	small ubiquitin like modifier 1	Homo sapiens	28-54
25447205-5	2015	The interaction of MxA with Small-Ubiquitin MOdifier 1 (SUMO1) and Ubiquitin conjugating enzyme 9 (Ubc9) was confirmed by co-immunoprecipitation and co-localization by confocal microscopy.	piritrexim	19-22	small ubiquitin like modifier 1	Homo sapiens	56-61
25447205-7	2015	We showed that MxA interacts with the EIL loop of SUMO1 in a SIM-independent manner via its CID-GED domain.	piritrexim	15-18	small ubiquitin like modifier 1	Homo sapiens	50-55
25220405-2	2014	In the heart, enhancement of lysine acetylation or SUMOylation using histone deacetylase (HDAC) inhibitors or SUMO-1 gene transfer, respectively, has been shown to be cardioprotective.	Lysine	29-35	small ubiquitin like modifier 1	Homo sapiens	110-116
25220405-9	2014	These findings reveal a novel role for reversible lysine acetylation in the control of SUMOylation in the heart, and suggest that cardioprotective actions of HDAC inhibitors are in part due to stimulation of protein SUMO-1-ylation in myocytes and fibroblasts.	Lysine	50-56	small ubiquitin like modifier 1	Homo sapiens	216-222
24819975-0	2014	Small ubiquitin-related modifier-1 modification regulates all-trans-retinoic acid-induced differentiation via stabilization of retinoic acid receptor alpha.	Tretinoin	68-81	small ubiquitin like modifier 1	Homo sapiens	0-34
24907310-0	2014	SUMO1 enhances cAMP-dependent exocytosis and glucagon secretion from pancreatic alpha-cells.	Cyclic AMP	15-19	small ubiquitin like modifier 1	Homo sapiens	0-5
24907310-7	2014	The ability of SUMO1 to enhance alpha-cell exocytosis was cAMP-dependent and resulted from an increased L-type Ca(2+) current and a shift away from exocytosis dependent on non-L-type channels, an effect that was mimicked by knockdown of the deSUMOylating enzyme sentrin/SUMO-specific protease-1 (SENP1).	Cyclic AMP	58-62	small ubiquitin like modifier 1	Homo sapiens	15-20
24907310-9	2014	Consistent with its cAMP dependence, however, SUMO1 enhanced alpha-cell exocytosis and glucagon secretion stimulated by adrenaline.	Cyclic AMP	20-24	small ubiquitin like modifier 1	Homo sapiens	46-51
24907310-9	2014	Consistent with its cAMP dependence, however, SUMO1 enhanced alpha-cell exocytosis and glucagon secretion stimulated by adrenaline.	Epinephrine	120-130	small ubiquitin like modifier 1	Homo sapiens	46-51
24991007-3	2014	We show that either a catalytically inactive form of Ubc9 (Ubc9-C93S) or Ubc9 small interfering RNA (siRNA) dramatically reduces Tax conjugation to endogenous SUMO-1 or SUMO-2/3, demonstrating that as expected, Tax SUMOylation is under the control of the catalytic activity of Ubc9.	ubc9	53-57	small ubiquitin like modifier 1	Homo sapiens	159-165
24991007-3	2014	We show that either a catalytically inactive form of Ubc9 (Ubc9-C93S) or Ubc9 small interfering RNA (siRNA) dramatically reduces Tax conjugation to endogenous SUMO-1 or SUMO-2/3, demonstrating that as expected, Tax SUMOylation is under the control of the catalytic activity of Ubc9.	ubc9	59-63	small ubiquitin like modifier 1	Homo sapiens	159-165
24975507-9	2014	Finally, we found that alpha-LA treatment leads to an increase in SUMO-1, but not in SUMO-2 or SUMO-3.	Thioctic Acid	23-31	small ubiquitin like modifier 1	Homo sapiens	66-72
24907310-10	2014	Thus, by contrast with its inhibitory role in beta-cell exocytosis, SUMO1 is a positive regulator of alpha-cell exocytosis and glucagon secretion under conditions of elevated cAMP.	Cyclic AMP	175-179	small ubiquitin like modifier 1	Homo sapiens	68-73
24910119-6	2014	LECs overexpressing Sumo1 showed reduced expression and activity of Prdx6 and its transactivator specificity protein 1 (Sp1), mRNA and protein with increased levels of reactive oxygen species; those cells were vulnerable to oxidative stress-induced cell death.	Reactive Oxygen Species	168-191	small ubiquitin like modifier 1	Homo sapiens	20-25
24819975-1	2014	Small ubiquitin-related modifier-1 (SUMO-1) modification has been implicated in many important cellular processes, including cell cycle progression, apoptosis, cellular proliferation, and development, but its role in all-trans-retinoic acid (ATRA)-induced differentiation processes of cancer cells remains unclear.	Tretinoin	221-240	small ubiquitin like modifier 1	Homo sapiens	0-34
24819975-1	2014	Small ubiquitin-related modifier-1 (SUMO-1) modification has been implicated in many important cellular processes, including cell cycle progression, apoptosis, cellular proliferation, and development, but its role in all-trans-retinoic acid (ATRA)-induced differentiation processes of cancer cells remains unclear.	Tretinoin	221-240	small ubiquitin like modifier 1	Homo sapiens	36-42
24819975-1	2014	Small ubiquitin-related modifier-1 (SUMO-1) modification has been implicated in many important cellular processes, including cell cycle progression, apoptosis, cellular proliferation, and development, but its role in all-trans-retinoic acid (ATRA)-induced differentiation processes of cancer cells remains unclear.	Tretinoin	242-246	small ubiquitin like modifier 1	Homo sapiens	0-34
24819975-1	2014	Small ubiquitin-related modifier-1 (SUMO-1) modification has been implicated in many important cellular processes, including cell cycle progression, apoptosis, cellular proliferation, and development, but its role in all-trans-retinoic acid (ATRA)-induced differentiation processes of cancer cells remains unclear.	Tretinoin	242-246	small ubiquitin like modifier 1	Homo sapiens	36-42
24819975-2	2014	Here, we report for the first time that ATRA-induced differentiation of leukemia and osteosarcoma is accompanied by a decrease in the level of SUMO-1 protein.	Tretinoin	40-44	small ubiquitin like modifier 1	Homo sapiens	143-149
24819975-3	2014	Our results also demonstrated that depletion or inhibition of SUMO-1 blocks ATRA-induced differentiation, suggesting that SUMO-1 is critical for the differentiation effect of ATRA.	Tretinoin	76-80	small ubiquitin like modifier 1	Homo sapiens	62-68
24819975-3	2014	Our results also demonstrated that depletion or inhibition of SUMO-1 blocks ATRA-induced differentiation, suggesting that SUMO-1 is critical for the differentiation effect of ATRA.	Tretinoin	76-80	small ubiquitin like modifier 1	Homo sapiens	122-128
24819975-3	2014	Our results also demonstrated that depletion or inhibition of SUMO-1 blocks ATRA-induced differentiation, suggesting that SUMO-1 is critical for the differentiation effect of ATRA.	Tretinoin	175-179	small ubiquitin like modifier 1	Homo sapiens	62-68
24819975-3	2014	Our results also demonstrated that depletion or inhibition of SUMO-1 blocks ATRA-induced differentiation, suggesting that SUMO-1 is critical for the differentiation effect of ATRA.	Tretinoin	175-179	small ubiquitin like modifier 1	Homo sapiens	122-128
24819975-8	2014	SUMO-1 modification may thus serve an important role in controlling ATRA-induced cell differentiation in cancers.	Tretinoin	68-72	small ubiquitin like modifier 1	Homo sapiens	0-6
24971881-3	2014	In these cells, SUMO1 modification occurred on both lysine 75 and lysine 9 of SOD1, and modification of ALS-linked SOD1 mutant proteins by SUMO3, rather than by SUMO1, significantly increased the stability of the proteins and accelerated intracellular aggregate formation.	Lysine	52-58	small ubiquitin like modifier 1	Homo sapiens	16-21
24971881-3	2014	In these cells, SUMO1 modification occurred on both lysine 75 and lysine 9 of SOD1, and modification of ALS-linked SOD1 mutant proteins by SUMO3, rather than by SUMO1, significantly increased the stability of the proteins and accelerated intracellular aggregate formation.	Lysine	66-72	small ubiquitin like modifier 1	Homo sapiens	16-21
24971881-2	2014	We report that both small ubiquitin-like modifier (SUMO) 1 and SUMO2/3 modify ALS-linked SOD1 mutant proteins at lysine 75 in a motoneuronal cell line, the cell type affected in ALS.	Lysine	113-119	small ubiquitin like modifier 1	Homo sapiens	20-58
24286314-0	2014	Characterization of a novel posttranslational modification in polypyrimidine tract-binding proteins by SUMO1.	polypyrimidine	62-76	small ubiquitin like modifier 1	Homo sapiens	103-108
24589211-8	2014	Bioinformatics analysis suggests that the genes ANKRD17, SMC1A, SUMO1, GTF2H1, and TP73, which are involved in DNA damage signaling pathways, are potential targets of miRNAs in promoting cisplatin resistance.	Cisplatin	187-196	small ubiquitin like modifier 1	Homo sapiens	64-69
23770046-0	2013	SUMO1 negatively regulates the transcriptional activity of EVI1 and significantly increases its co-localization with EVI1 after treatment with arsenic trioxide.	Arsenic Trioxide	143-159	small ubiquitin like modifier 1	Homo sapiens	0-5
24309115-4	2014	We find that the lysine 1766 residue is the primary NuMA acceptor site for SUMO-1 conjugation.	Lysine	17-23	small ubiquitin like modifier 1	Homo sapiens	75-81
23770046-3	2013	Here we demonstrated that EVI1 is post-translationally modified by SUMO1 at lysine residues 533, 698 and 874.	Lysine	76-82	small ubiquitin like modifier 1	Homo sapiens	67-72
24338848-8	2014	The triazole-linked SUMO1**RanGAP1 conjugate could be obtained in good yields, purified, and was shown to specifically interact with RanBP2/Ubc9.	Triazoles	4-12	small ubiquitin like modifier 1	Homo sapiens	20-25
23770046-8	2013	Arsenic trioxide (ATO) known to act as an antileukemic agent for acute promyelocytic leukemia (APL) not only enhanced EVI1 sumoylation but also enhanced the co-localization of EVI1 and SUMO1 in nuclear bodies distinct from PML nuclear bodies.	Arsenic Trioxide	0-16	small ubiquitin like modifier 1	Homo sapiens	185-190
23727357-6	2013	A structural analysis of ANXA1 revealed that K257 is located in a hot spot where Ca(2+) and SUMO-1 bind and where a nuclear export signal and a polyubiquitination site are also present.	k257	45-49	small ubiquitin like modifier 1	Homo sapiens	92-98
23770046-8	2013	Arsenic trioxide (ATO) known to act as an antileukemic agent for acute promyelocytic leukemia (APL) not only enhanced EVI1 sumoylation but also enhanced the co-localization of EVI1 and SUMO1 in nuclear bodies distinct from PML nuclear bodies.	Arsenic Trioxide	18-21	small ubiquitin like modifier 1	Homo sapiens	185-190
23651519-5	2013	Moreover, the levels of SUMO-1 conjugated proteins, as well as the conjugating enzyme, Ubc9, were decreased, with concomitant treatment with curcumin preventing these effects.	Curcumin	141-149	small ubiquitin like modifier 1	Homo sapiens	24-30
23686912-5	2013	Further study showed that ZHX1 is SUMOylated by Ubc9 with SUMO1 at the sites K159, K454, and K626.	k454	83-87	small ubiquitin like modifier 1	Homo sapiens	58-63
23930863-6	2013	After that, the nucleophilic sulfur anion of Cys603 in SENP1 attacked the carbonyl carbon of Gly97 of SUMO1 to trigger the reaction, and then a tetrahedral intermediate and an acyl-enzyme intermediate were generated in turn, leading to the final release of enzyme SENP1 and two products, free SUMO1 and RanGAP1.	Sulfur anion	29-41	small ubiquitin like modifier 1	Homo sapiens	102-107
23930863-6	2013	After that, the nucleophilic sulfur anion of Cys603 in SENP1 attacked the carbonyl carbon of Gly97 of SUMO1 to trigger the reaction, and then a tetrahedral intermediate and an acyl-enzyme intermediate were generated in turn, leading to the final release of enzyme SENP1 and two products, free SUMO1 and RanGAP1.	Sulfur anion	29-41	small ubiquitin like modifier 1	Homo sapiens	293-298
23930863-6	2013	After that, the nucleophilic sulfur anion of Cys603 in SENP1 attacked the carbonyl carbon of Gly97 of SUMO1 to trigger the reaction, and then a tetrahedral intermediate and an acyl-enzyme intermediate were generated in turn, leading to the final release of enzyme SENP1 and two products, free SUMO1 and RanGAP1.	Carbon	74-80	small ubiquitin like modifier 1	Homo sapiens	102-107
23930863-6	2013	After that, the nucleophilic sulfur anion of Cys603 in SENP1 attacked the carbonyl carbon of Gly97 of SUMO1 to trigger the reaction, and then a tetrahedral intermediate and an acyl-enzyme intermediate were generated in turn, leading to the final release of enzyme SENP1 and two products, free SUMO1 and RanGAP1.	Carbon	74-80	small ubiquitin like modifier 1	Homo sapiens	293-298
23470489-1	2013	Small ubiquitin-like modifier (SUMO1-3) is a small group of proteins that are ligated to lysine residues in target proteins.	Lysine	89-95	small ubiquitin like modifier 1	Homo sapiens	31-38
23007842-2	2013	Later, it turned out that the homologous mammalian proteins SUMO1 to SUMO4 are reversible protein modifiers that can form isopeptide bonds with lysine residues of respective target proteins (Mahajan et al.	Lysine	144-150	small ubiquitin like modifier 1	Homo sapiens	60-65
23375957-7	2013	MG132 caused a large increase in steady-state levels of SUMO-1 and of sumoylated proteins, and this was especially true for detergent-insoluble proteins.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	small ubiquitin like modifier 1	Homo sapiens	56-62
23544417-9	2013	These compounds share a common phenyl urea scaffold and have been confirmed to inhibit SUMO E1 by in vitro SUMO-1 thioester bond formation assay.	Urea	38-42	small ubiquitin like modifier 1	Homo sapiens	107-113
23375957-8	2013	The conjugation-incompetent GG-to-AA SUMO-1 mutant, which did not form nuclear foci, was only present in the detergent-soluble lysate fraction and was insensitive to BH3I-2", implying that BH3I-2" specifically affects SUMO in its conjugated form.	BH3I-2'	189-195	small ubiquitin like modifier 1	Homo sapiens	37-43
23359867-4	2013	Lysine 591 of menin was covalently modified by SUMO1 and K591R mutation in menin blocked SUMOylation of the C-terminal part of menin in transfected cells.	Lysine	0-6	small ubiquitin like modifier 1	Homo sapiens	47-52
23078246-1	2013	Small ubiquitin-like modifier (SUMO1-3) constitutes a group of proteins that conjugate to lysine residues of target proteins thereby modifying their activity, stability, and subcellular localization.	Lysine	90-96	small ubiquitin like modifier 1	Homo sapiens	31-38
23229893-13	2013	SUMO-1 labelling of lysosomes showed a major increase between 24 and 48 h post-incubation of 1321N1 cells with MG132 resulting in an increase in a 90 kDa SUMO-1-positive band that was immunopositive for Hsp90 and immunoprecipitated with an anti-SUMO-1 antibody.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	111-116	small ubiquitin like modifier 1	Homo sapiens	0-6
23229893-13	2013	SUMO-1 labelling of lysosomes showed a major increase between 24 and 48 h post-incubation of 1321N1 cells with MG132 resulting in an increase in a 90 kDa SUMO-1-positive band that was immunopositive for Hsp90 and immunoprecipitated with an anti-SUMO-1 antibody.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	111-116	small ubiquitin like modifier 1	Homo sapiens	154-160
23229893-13	2013	SUMO-1 labelling of lysosomes showed a major increase between 24 and 48 h post-incubation of 1321N1 cells with MG132 resulting in an increase in a 90 kDa SUMO-1-positive band that was immunopositive for Hsp90 and immunoprecipitated with an anti-SUMO-1 antibody.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	111-116	small ubiquitin like modifier 1	Homo sapiens	154-160
22930759-11	2012	SUMO1 was required for T3-mediated recruitment of NCoR and release of CBP from the TSHbeta-negative TRE.	Thyrotropin, beta Subunit	83-90	small ubiquitin like modifier 1	Homo sapiens	0-5
23020131-3	2013	Based on screening results, five unique genes (GNPAT, SUMO1, SPINT2, FLI1, and SSX1) significantly potentiated the growth inhibitory effects of CDDO-Me and induced apoptosis in A375, a BRAF mutated melanoma line (P < 0.001).	bardoxolone methyl	144-151	small ubiquitin like modifier 1	Homo sapiens	54-59
23382880-0	2013	SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity.	polyglutamine	31-36	small ubiquitin like modifier 1	Homo sapiens	0-6
23382880-4	2013	Here we identified that the major SUMO-1 binding site was located on lysine 166.	Lysine	69-75	small ubiquitin like modifier 1	Homo sapiens	34-40
23152501-3	2012	Surprisingly, DPP9 binds to SUMO1 independent of the well known SUMO interacting motif, but instead interacts with a loop involving Glu(67) of SUMO1.	Glutamic Acid	132-135	small ubiquitin like modifier 1	Homo sapiens	143-148
22586270-3	2012	ERbeta SUMO-1 modification occurs on a unique nonconsensus sumoylation motif which becomes fully competent upon phosphorylation of its contained serine residue, which provides the essential negative charge for sumoylation.	Serine	145-151	small ubiquitin like modifier 1	Homo sapiens	7-13
22651256-6	2012	Pioglitazone increased SUMO-1 expression by 23% (P<0.002) in adipose tissue and an adipocyte cell line (P<0.05), but not in macrophages.	Pioglitazone	0-12	small ubiquitin like modifier 1	Homo sapiens	23-29
22651256-8	2012	CONCLUSIONS: These results suggest that the coordinate regulation of SUMO-1, PPARgamma1/2, HDAC3, and NCoR may be more tightly controlled in macrophages than in adipocytes in human adipose and that these modulators of PPARgamma activity may be particularly important in the negative regulation of macrophage-mediated adipose inflammation by pioglitazone.	Pioglitazone	341-353	small ubiquitin like modifier 1	Homo sapiens	69-75
21989481-1	2012	Here, we show that oxygen and glucose deprivation (OGD) causes increased small ubiquitin-like modifier (SUMO)-1 and SUMO-2/3 conjugation to substrate proteins in cultured hippocampal neurones.	Oxygen	19-25	small ubiquitin like modifier 1	Homo sapiens	73-111
22555612-2	2012	Here we show that Blimp-1 is covalently modified by SUMO1 at lysine 816, a modification mediated by SUMO E3 ligase PIAS1.	Lysine	61-67	small ubiquitin like modifier 1	Homo sapiens	52-57
22649771-1	2011	Small ubiquitin-like modifier-1/2/3 (SUMO-1/2/3) and ubiquitin share similar structure and utilize analogous machinery for protein lysine conjugation.	Lysine	131-137	small ubiquitin like modifier 1	Homo sapiens	0-35
22649771-1	2011	Small ubiquitin-like modifier-1/2/3 (SUMO-1/2/3) and ubiquitin share similar structure and utilize analogous machinery for protein lysine conjugation.	Lysine	131-137	small ubiquitin like modifier 1	Homo sapiens	37-47
21383010-10	2011	Importantly, this interaction did not involve any direct contacts between DAXX and Ets1, but rather was derived from the non-covalent binding of SIM-C to SUMO-1, which in turn was covalently linked to the unstructured N-terminal segment of Ets1.	sim-c	145-150	small ubiquitin like modifier 1	Homo sapiens	154-160
22665316-5	2012	To identify SUMO acceptor sites in endogenous SUMO1 conjugated protein, the SUMO1 conjugates are purified by immunoprecipitation with anti-SUMO1 antibodies followed by SDS-PAGE separation and in-gel tryptic digestion.	Sodium Dodecyl Sulfate	168-171	small ubiquitin like modifier 1	Homo sapiens	46-51
22665316-5	2012	To identify SUMO acceptor sites in endogenous SUMO1 conjugated protein, the SUMO1 conjugates are purified by immunoprecipitation with anti-SUMO1 antibodies followed by SDS-PAGE separation and in-gel tryptic digestion.	Sodium Dodecyl Sulfate	168-171	small ubiquitin like modifier 1	Homo sapiens	76-81
22665316-5	2012	To identify SUMO acceptor sites in endogenous SUMO1 conjugated protein, the SUMO1 conjugates are purified by immunoprecipitation with anti-SUMO1 antibodies followed by SDS-PAGE separation and in-gel tryptic digestion.	Sodium Dodecyl Sulfate	168-171	small ubiquitin like modifier 1	Homo sapiens	76-81
21527745-0	2011	SUMO1 negatively regulates reactive oxygen species production from NADPH oxidases.	Reactive Oxygen Species	27-50	small ubiquitin like modifier 1	Homo sapiens	0-5
21527745-4	2011	In contrast, inhibition of endogenous SUMOylation with small interfering RNA to SUMO1 or ubiquitin conjugating enzyme 9 or with the inhibitor anacardic acid increased ROS production from human embryonic kidney-Nox5 cells, human vascular smooth muscle cells, and neutrophils.	Reactive Oxygen Species	167-170	small ubiquitin like modifier 1	Homo sapiens	80-85
21527745-5	2011	The suppression of ROS production was unique to SUMO1, and it required a C-terminal diglycine and the SUMO-specific conjugating enzyme ubiquitin conjugating enzyme 9.	Reactive Oxygen Species	19-22	small ubiquitin like modifier 1	Homo sapiens	48-53
21527745-5	2011	The suppression of ROS production was unique to SUMO1, and it required a C-terminal diglycine and the SUMO-specific conjugating enzyme ubiquitin conjugating enzyme 9.	Glycylglycine	84-93	small ubiquitin like modifier 1	Homo sapiens	48-53
21527745-6	2011	SUMO1 did not modify intracellular calcium or Nox5 phosphorylation but reduced ROS output in an isolated enzyme assay, suggesting direct effects of SUMOylation on enzyme activity.	Reactive Oxygen Species	79-82	small ubiquitin like modifier 1	Homo sapiens	0-5
22539995-7	2012	PIAS1 promoted SUMO-1 modification of GATA4 on lysine 366.	Lysine	47-53	small ubiquitin like modifier 1	Homo sapiens	15-21
21683690-0	2011	SUMO1 attenuates stress-induced ROS generation by inhibiting NADPH oxidase 2.	ros	32-35	small ubiquitin like modifier 1	Homo sapiens	0-5
21683690-4	2011	Intriguingly, SUMO1 conjugation resulted in decrease of intracellular ROS generation and protection cells from death under heat-shock stress.	ros	70-73	small ubiquitin like modifier 1	Homo sapiens	14-19
21683690-7	2011	These results suggested that SUMO1 plays an important role in modulation of NOX activity required for ROS generation.	ros	102-105	small ubiquitin like modifier 1	Homo sapiens	29-34
21288202-7	2011	Co-mutating a second lysine residue (Lys903) located in the mGluR8b isoform-specific C-terminus largely prevented SUMO1 conjugation by Ubc9.	Lysine	21-27	small ubiquitin like modifier 1	Homo sapiens	114-119
21527249-3	2011	Here we show that SAFB1 is modified by both the SUMO1 and SUMO2/3 family of proteins, on lysine"s K231 and K294.	Lysine	89-95	small ubiquitin like modifier 1	Homo sapiens	48-53
21490953-9	2011	Mutation of lysines at a potential site of SUMOylation in the CA region of the Gag gene reduced the SUMO-1 block and the TRIM5alpha restriction of N-MLV.	Lysine	12-19	small ubiquitin like modifier 1	Homo sapiens	100-106
21490953-9	2011	Mutation of lysines at a potential site of SUMOylation in the CA region of the Gag gene reduced the SUMO-1 block and the TRIM5alpha restriction of N-MLV.	Glycosaminoglycans	79-82	small ubiquitin like modifier 1	Homo sapiens	100-106
20676127-3	2010	In this study we report for the first time that ING2 can be sumoylated by small ubiquitin-like modifier 1 (SUMO1) on lysine 195 both in vitro and in vivo.	Lysine	117-123	small ubiquitin like modifier 1	Homo sapiens	74-105
20725866-0	2011	Membrane lipid modification by docosahexaenoic acid (DHA) promotes the formation of alpha-synuclein inclusion bodies immunopositive for SUMO-1 in oligodendroglial cells after oxidative stress.	Docosahexaenoic Acids	31-51	small ubiquitin like modifier 1	Homo sapiens	136-142
20725866-0	2011	Membrane lipid modification by docosahexaenoic acid (DHA) promotes the formation of alpha-synuclein inclusion bodies immunopositive for SUMO-1 in oligodendroglial cells after oxidative stress.	Docosahexaenoic Acids	53-56	small ubiquitin like modifier 1	Homo sapiens	136-142
21187340-7	2011	Sumoylation is important to stabilization of p53 and a COX-2-SUMO-1 interaction suggests sumoylation of COX-2 in resveratrol-treated cells and (iv) chromatin immunoprecipitation studies showed binding of induced nuclear COX-2 to the promoter region of PIG3 and Bax, pro-apoptotic gene targets of transcriptionally active p53.	Resveratrol	113-124	small ubiquitin like modifier 1	Homo sapiens	61-67
21047957-4	2011	Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites.	Lysine	17-23	small ubiquitin like modifier 1	Homo sapiens	77-82
21796528-4	2011	We have shown that AR is modified by SUMO-1 at two conserved lysine residues in its N-terminal domain.	Lysine	61-67	small ubiquitin like modifier 1	Homo sapiens	37-43
21120624-5	2011	Furthermore, we identified the five lysine residues of the Pellino-1 protein where SUMO-1 covalently attaches.	Lysine	36-42	small ubiquitin like modifier 1	Homo sapiens	83-89
21156324-2	2011	In this study, we found that MDA5 undergoes inducible SUMOylation by small ubiquitin-like modifier-1 (SUMO-1) in response to polyI:C stimulation.	Poly I-C	125-132	small ubiquitin like modifier 1	Homo sapiens	69-100
21156324-2	2011	In this study, we found that MDA5 undergoes inducible SUMOylation by small ubiquitin-like modifier-1 (SUMO-1) in response to polyI:C stimulation.	Poly I-C	125-132	small ubiquitin like modifier 1	Homo sapiens	102-108
21266332-6	2011	RESULTS: SUMO1 impairs glucose-stimulated insulin secretion by blunting the beta-cell exocytotic response to Ca(2+).	Glucose	23-30	small ubiquitin like modifier 1	Homo sapiens	9-14
21266332-8	2011	SUMO1 coimmunoprecipitates with the Ca(2+) sensor synaptotagmin VII, and this is transiently lost upon glucose stimulation.	Glucose	103-110	small ubiquitin like modifier 1	Homo sapiens	0-5
20502916-6	2011	SUMO-1 siRNA notably inhibited SMMC-7721 cells proliferation in vitro and increased the ratios of G2 phase and S phase in the cells.	smmc	31-35	small ubiquitin like modifier 1	Homo sapiens	0-6
21123177-5	2011	Overexpression of SUMO-1 in mammalian cancer cells resulted in increased hypoxia-induced glycolysis and resistance to hypoxia-dependent ATP depletion.	Adenosine Triphosphate	136-139	small ubiquitin like modifier 1	Homo sapiens	18-24
21123177-6	2011	Supporting this, non-transformed cells also demonstrated increased glucose uptake upon SUMO-1 overexpression.	Glucose	67-74	small ubiquitin like modifier 1	Homo sapiens	87-93
20676127-3	2010	In this study we report for the first time that ING2 can be sumoylated by small ubiquitin-like modifier 1 (SUMO1) on lysine 195 both in vitro and in vivo.	Lysine	117-123	small ubiquitin like modifier 1	Homo sapiens	107-112
20637912-6	2010	Conserved lysine residue 167 that is located in the NET inhibitory domain of ELK4 was identified as the main site of SUMO-1 conjugation.	Lysine	10-16	small ubiquitin like modifier 1	Homo sapiens	117-123
19859084-0	2010	Association of SUMO1 and UBC9 genotypes with tumor response in non-small-cell lung cancer treated with irinotecan-based chemotherapy.	Irinotecan	103-113	small ubiquitin like modifier 1	Homo sapiens	15-20
20516063-3	2010	Here we found that BZLF1 is conjugated at lysine 12 not only by SUMO-1 but also by SUMO-2 and 3.	Lysine	42-48	small ubiquitin like modifier 1	Homo sapiens	64-70
19859084-1	2010	Irinotecan induces small ubiquitin-like modifier (SUMO)-1 conjugation to topoisomerase-I, leading to enhanced sensitivity to irinotecan.	Irinotecan	0-10	small ubiquitin like modifier 1	Homo sapiens	19-57
19859084-1	2010	Irinotecan induces small ubiquitin-like modifier (SUMO)-1 conjugation to topoisomerase-I, leading to enhanced sensitivity to irinotecan.	Irinotecan	125-135	small ubiquitin like modifier 1	Homo sapiens	19-57
19859084-7	2010	This finding suggests that the UBC9 10920CG genotype enhances sensitivity to irinotecan chemotherapy in advanced NSCLC through upregulation of SUMO1 in tumor cells.	Irinotecan	77-87	small ubiquitin like modifier 1	Homo sapiens	143-148
19565496-1	2009	OBJECTIVE: To study the expression of small ubiquitin-like modifier 1 (SUMO-1) in aseptic loosening of prosthesis implants and to investigate its role in regulating the susceptibility of prosthesis-loosening fibroblast-like synoviocytes (FLS) to Fas-induced apoptosis.	ammonium ferrous sulfate	246-249	small ubiquitin like modifier 1	Homo sapiens	38-69
19955185-4	2010	In this report, we demonstrate that hPPARalpha is SUMOylated by SUMO-1 on lysine 185 in the hinge region.	Lysine	74-80	small ubiquitin like modifier 1	Homo sapiens	64-70
20006587-4	2010	Deletion of a short lysine-rich domain that contains the major SUMO acceptor sites of CBP abrogated its ability to be SUMO modified, and prevented its association with endogenous SUMO-1/PML speckles in vivo.	Lysine	20-26	small ubiquitin like modifier 1	Homo sapiens	179-185
20622442-1	2010	We found that the small ubiquitin-related modifier (SUMO) conjugation reaction can be visualized simply by incubating green fluorescent protein (GFP)-SUMO-1 with permeabilized cells in the presence of ATP for 15 min.	Adenosine Triphosphate	201-204	small ubiquitin like modifier 1	Homo sapiens	150-156
19889771-5	2010	Mapping data showed that multiple lysine residues are SUMO1 acceptors within S-HDAg.	Lysine	34-40	small ubiquitin like modifier 1	Homo sapiens	54-59
19565496-1	2009	OBJECTIVE: To study the expression of small ubiquitin-like modifier 1 (SUMO-1) in aseptic loosening of prosthesis implants and to investigate its role in regulating the susceptibility of prosthesis-loosening fibroblast-like synoviocytes (FLS) to Fas-induced apoptosis.	ammonium ferrous sulfate	246-249	small ubiquitin like modifier 1	Homo sapiens	71-77
19565496-5	2009	The functional role of SUMO-1 in Fas-induced apoptosis of prosthesis-loosening FLS was investigated by small interfering RNA-mediated knockdown of SUMO-1 and by gene transfer of the nuclear SUMO-specific protease SENP1.	ammonium ferrous sulfate	33-36	small ubiquitin like modifier 1	Homo sapiens	23-29
19565496-5	2009	The functional role of SUMO-1 in Fas-induced apoptosis of prosthesis-loosening FLS was investigated by small interfering RNA-mediated knockdown of SUMO-1 and by gene transfer of the nuclear SUMO-specific protease SENP1.	ammonium ferrous sulfate	33-36	small ubiquitin like modifier 1	Homo sapiens	147-153
19565496-8	2009	Knockdown of SUMO-1 had no effect on spontaneous apoptosis but significantly increased the susceptibility of prosthesis-loosening FLS to Fas-induced apoptosis.	ammonium ferrous sulfate	137-140	small ubiquitin like modifier 1	Homo sapiens	13-19
19217413-5	2009	We provide evidence that the phosphorylated residues contact lysine 39 and 35 in SUMO1 and SUMO2, respectively.	Lysine	61-67	small ubiquitin like modifier 1	Homo sapiens	81-86
19409099-3	2009	RESULTS: In the current study, we have identified a reactive oxygen species (ROS) dependent aggregation of PML, small ubiquitin-like modifier 1 (SUMO-1), heat shock protein 70 (HSP70) and 20S proteasomes in human cell lines that have been transiently transfected with vectors expressing the puromycin resistance gene, puromycin n-acetyl transferase (pac).	Puromycin	291-300	small ubiquitin like modifier 1	Homo sapiens	112-143
19409099-4	2009	Immunofluorescent studies demonstrated that PML, SUMO-1, HSP70 and 20S proteasomes aggregated to form nuclear inclusions in multiple cell lines transfected with vectors expressing puromycin (puro) resistance in regions distinct from nucleoli.	Puromycin	180-189	small ubiquitin like modifier 1	Homo sapiens	49-55
19409099-4	2009	Immunofluorescent studies demonstrated that PML, SUMO-1, HSP70 and 20S proteasomes aggregated to form nuclear inclusions in multiple cell lines transfected with vectors expressing puromycin (puro) resistance in regions distinct from nucleoli.	Puromycin	180-184	small ubiquitin like modifier 1	Homo sapiens	49-55
19251700-3	2009	Here, we report that AhRR has three evolutionarily conserved SUMOylation consensus sequences within its C-terminal repression domain and that Lys-542, Lys-583, and Lys-660 at the SUMOylation sites are modified by SUMO-1 in vivo.	Lysine	142-145	small ubiquitin like modifier 1	Homo sapiens	213-219
19344328-4	2009	Increasing protein SUMOylation by entrapping recombinant SUMO-1 in synaptosomes decreased glutamate release evoked by KCl whereas decreasing SUMOylation with the SUMO-specific protease SENP-1 enhanced KCl-evoked release.	Glutamic Acid	90-99	small ubiquitin like modifier 1	Homo sapiens	57-63
19344328-4	2009	Increasing protein SUMOylation by entrapping recombinant SUMO-1 in synaptosomes decreased glutamate release evoked by KCl whereas decreasing SUMOylation with the SUMO-specific protease SENP-1 enhanced KCl-evoked release.	Potassium Chloride	118-121	small ubiquitin like modifier 1	Homo sapiens	57-63
19344328-4	2009	Increasing protein SUMOylation by entrapping recombinant SUMO-1 in synaptosomes decreased glutamate release evoked by KCl whereas decreasing SUMOylation with the SUMO-specific protease SENP-1 enhanced KCl-evoked release.	Potassium Chloride	201-204	small ubiquitin like modifier 1	Homo sapiens	57-63
19409099-3	2009	RESULTS: In the current study, we have identified a reactive oxygen species (ROS) dependent aggregation of PML, small ubiquitin-like modifier 1 (SUMO-1), heat shock protein 70 (HSP70) and 20S proteasomes in human cell lines that have been transiently transfected with vectors expressing the puromycin resistance gene, puromycin n-acetyl transferase (pac).	Reactive Oxygen Species	52-75	small ubiquitin like modifier 1	Homo sapiens	112-143
19409099-3	2009	RESULTS: In the current study, we have identified a reactive oxygen species (ROS) dependent aggregation of PML, small ubiquitin-like modifier 1 (SUMO-1), heat shock protein 70 (HSP70) and 20S proteasomes in human cell lines that have been transiently transfected with vectors expressing the puromycin resistance gene, puromycin n-acetyl transferase (pac).	Reactive Oxygen Species	52-75	small ubiquitin like modifier 1	Homo sapiens	145-151
19409099-3	2009	RESULTS: In the current study, we have identified a reactive oxygen species (ROS) dependent aggregation of PML, small ubiquitin-like modifier 1 (SUMO-1), heat shock protein 70 (HSP70) and 20S proteasomes in human cell lines that have been transiently transfected with vectors expressing the puromycin resistance gene, puromycin n-acetyl transferase (pac).	Reactive Oxygen Species	77-80	small ubiquitin like modifier 1	Homo sapiens	112-143
19409099-3	2009	RESULTS: In the current study, we have identified a reactive oxygen species (ROS) dependent aggregation of PML, small ubiquitin-like modifier 1 (SUMO-1), heat shock protein 70 (HSP70) and 20S proteasomes in human cell lines that have been transiently transfected with vectors expressing the puromycin resistance gene, puromycin n-acetyl transferase (pac).	Reactive Oxygen Species	77-80	small ubiquitin like modifier 1	Homo sapiens	145-151
19211567-5	2009	However, paradoxically, cellular overexpression of SUMO-1 increases PR transcriptional activity even if Lys-388 is mutated, suggesting that the receptors are activated indirectly by other SUMOylated proteins.	Lysine	104-107	small ubiquitin like modifier 1	Homo sapiens	51-57
18854179-3	2008	We showed that CoREST can be modified by SUMO-1 at lysine 294.	Lysine	51-57	small ubiquitin like modifier 1	Homo sapiens	41-47
18403372-4	2008	When Ser(455), a phosphorylation site in SREBP-2, was substituted with Ala, this SREBP-2 mutant was more efficiently modified by SUMO-1.	Serine	5-8	small ubiquitin like modifier 1	Homo sapiens	129-135
18707152-5	2008	Here, we unambiguously show that serine 2 of the endogenous SUMO-1 N-terminal protrusion is phosphorylated in vivo using very high mass accuracy mass spectrometry at both the MS and the MS/MS level and complementary fragmentation techniques.	Serine	33-39	small ubiquitin like modifier 1	Homo sapiens	60-66
19053687-9	2008	Moreover, ZnTM2,3PyPz formed stable complexes with GMP with a binding constant of K(GMP) = 1.0 x 10(3) M(-1).	zntm2	10-15	small ubiquitin like modifier 1	Homo sapiens	82-92
19053687-9	2008	Moreover, ZnTM2,3PyPz formed stable complexes with GMP with a binding constant of K(GMP) = 1.0 x 10(3) M(-1).	Guanosine Monophosphate	51-54	small ubiquitin like modifier 1	Homo sapiens	82-92
18403372-4	2008	When Ser(455), a phosphorylation site in SREBP-2, was substituted with Ala, this SREBP-2 mutant was more efficiently modified by SUMO-1.	Alanine	71-74	small ubiquitin like modifier 1	Homo sapiens	129-135
17360386-0	2007	Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts.	ammonium ferrous sulfate	56-59	small ubiquitin like modifier 1	Homo sapiens	39-45
18211901-6	2008	We show that two conserved lysines, Lys(756) and Lys(1154), located in RD3 and RD4, respectively, are subject to reversible SUMOylation, with SUMO-1 being more efficiently conjugated than SUMO-2.	Lysine	27-34	small ubiquitin like modifier 1	Homo sapiens	142-148
18211901-6	2008	We show that two conserved lysines, Lys(756) and Lys(1154), located in RD3 and RD4, respectively, are subject to reversible SUMOylation, with SUMO-1 being more efficiently conjugated than SUMO-2.	Lysine	36-39	small ubiquitin like modifier 1	Homo sapiens	142-148
18211901-6	2008	We show that two conserved lysines, Lys(756) and Lys(1154), located in RD3 and RD4, respectively, are subject to reversible SUMOylation, with SUMO-1 being more efficiently conjugated than SUMO-2.	Lysine	49-52	small ubiquitin like modifier 1	Homo sapiens	142-148
18404132-7	2008	RESULTS: We found that estradiol could elevate CRH promoter activity to a much higher level in cells co-transfected with ER and SUMO1 than that with ER alone, and that the enhancement was blocked by the ER inhibitor, ICI182,780.	Estradiol	23-32	small ubiquitin like modifier 1	Homo sapiens	128-133
18404132-7	2008	RESULTS: We found that estradiol could elevate CRH promoter activity to a much higher level in cells co-transfected with ER and SUMO1 than that with ER alone, and that the enhancement was blocked by the ER inhibitor, ICI182,780.	ici182	217-223	small ubiquitin like modifier 1	Homo sapiens	128-133
18239466-4	2008	The first 7 amino acid residues of Sp1 enhance the accessibility of Lysine-16 to the homologous modifiers SUMO-1 and ubiquitin; and Serine-7 specifically enhances ubiquitinylation.	Lysine	68-74	small ubiquitin like modifier 1	Homo sapiens	106-112
18312666-4	2008	Considering these positive results and other data from the literature, we further tested the ability of ubiquitin or SUMO-1 linked to various PTD at their N-terminus to deliver within cells proteins or peptides fused downstream of their diglycine motif.	Glycylglycine	237-246	small ubiquitin like modifier 1	Homo sapiens	117-123
18312666-12	2008	CONCLUSION: Our observations indicate that fusion of SUMO-1 to a peptide-PTD module allows generation of a stable hybrid protein that is easily produced in bacteria and which efficiently enters into cells but this property necessitates mutation of the diglycine motif at the end of SUMO-1, thereby impairing delivery of the peptide alone.	Glycylglycine	252-261	small ubiquitin like modifier 1	Homo sapiens	53-59
18312666-12	2008	CONCLUSION: Our observations indicate that fusion of SUMO-1 to a peptide-PTD module allows generation of a stable hybrid protein that is easily produced in bacteria and which efficiently enters into cells but this property necessitates mutation of the diglycine motif at the end of SUMO-1, thereby impairing delivery of the peptide alone.	Glycylglycine	252-261	small ubiquitin like modifier 1	Homo sapiens	282-288
17671677-4	2007	Transfection of the anti-SUMO-1 antisense oligonucleotide to oral SCC cells significantly reduced proliferation of the cells.	Oligonucleotides	42-57	small ubiquitin like modifier 1	Homo sapiens	25-31
17284251-4	2007	While by the treatment with a tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA), GFP-SUMO-1 located homogeneously in nuclei.	Tetradecanoylphorbol Acetate	45-81	small ubiquitin like modifier 1	Homo sapiens	93-99
17284251-5	2007	When K562/GFP-SUMO-1 cells were treated with TPA plus MIT, GFP-SUMO-1 foci became larger and apoptosis was induced more than with MIT alone.	Tetradecanoylphorbol Acetate	45-48	small ubiquitin like modifier 1	Homo sapiens	14-20
17284251-5	2007	When K562/GFP-SUMO-1 cells were treated with TPA plus MIT, GFP-SUMO-1 foci became larger and apoptosis was induced more than with MIT alone.	Tetradecanoylphorbol Acetate	45-48	small ubiquitin like modifier 1	Homo sapiens	63-69
17284251-6	2007	The apoptosis induced by TPA plus MIT was prevented by blockage of GFP-SUMO-1 foci by small interfering RNA (siRNA) against SUMO-1.	Tetradecanoylphorbol Acetate	25-28	small ubiquitin like modifier 1	Homo sapiens	71-77
17284251-6	2007	The apoptosis induced by TPA plus MIT was prevented by blockage of GFP-SUMO-1 foci by small interfering RNA (siRNA) against SUMO-1.	Tetradecanoylphorbol Acetate	25-28	small ubiquitin like modifier 1	Homo sapiens	124-130
17284251-7	2007	The formation of GFP-SUMO-1 foci was reduced by a MEK inhibitor U0126 or a nuclear export inhibitor leptomycin B, and endogenous SUMO-1 foci were reduced in K562 cells expressing the dominant-negative MEK1 mutant.	U 0126	64-69	small ubiquitin like modifier 1	Homo sapiens	21-27
17284251-7	2007	The formation of GFP-SUMO-1 foci was reduced by a MEK inhibitor U0126 or a nuclear export inhibitor leptomycin B, and endogenous SUMO-1 foci were reduced in K562 cells expressing the dominant-negative MEK1 mutant.	U 0126	64-69	small ubiquitin like modifier 1	Homo sapiens	129-135
17284251-7	2007	The formation of GFP-SUMO-1 foci was reduced by a MEK inhibitor U0126 or a nuclear export inhibitor leptomycin B, and endogenous SUMO-1 foci were reduced in K562 cells expressing the dominant-negative MEK1 mutant.	leptomycin B	100-112	small ubiquitin like modifier 1	Homo sapiens	21-27
17610843-2	2007	Here, we show that HIF-1alpha undergoes post-translational modification by the three isoforms of the small ubiquitin-related modifier (SUMO-1, -2 and -3) in vitro in proximity to and within the oxygen-dependent degradation domain (ODDD).	Oxygen	194-200	small ubiquitin like modifier 1	Homo sapiens	135-152
17548468-4	2007	Here we report that the small ubiquitin-like protein SUMO-1 can modify MafB in vitro and in vivo on lysines 32 and 297.	Lysine	100-107	small ubiquitin like modifier 1	Homo sapiens	53-59
17320104-3	2007	In this context, we used here non-linear dependence of amide proton chemical shifts on temperature to identify residues accessing alternative conformations in SUMO-1 in the native state as well as in the near-native states created by sub-denaturing concentrations of urea.	Amides	55-60	small ubiquitin like modifier 1	Homo sapiens	159-165
17360386-3	2007	Here, we show that the increased expression of SUMO-1 in rheumatoid arthritis (RA) synovial fibroblasts (SFs) contributes to the resistance of these cells against Fas-induced apoptosis through increased SUMOylation of nuclear PML protein and increased recruitment of the transcriptional repressor DAXX to PML NBs.	ammonium ferrous sulfate	163-166	small ubiquitin like modifier 1	Homo sapiens	47-53
17360386-3	2007	Here, we show that the increased expression of SUMO-1 in rheumatoid arthritis (RA) synovial fibroblasts (SFs) contributes to the resistance of these cells against Fas-induced apoptosis through increased SUMOylation of nuclear PML protein and increased recruitment of the transcriptional repressor DAXX to PML NBs.	Bromosuccinimide	309-312	small ubiquitin like modifier 1	Homo sapiens	47-53
17079232-5	2007	Moreover, the KAP1 sumoylation level was transiently decreased upon Dox exposure, and transfection with the KAP1 sumoylation mimetic, SUMO-1-KAP1, desensitizes breast cancer MCF-7 cells to Dox-elicited cell death.	Doxorubicin	68-71	small ubiquitin like modifier 1	Homo sapiens	134-140
17079232-5	2007	Moreover, the KAP1 sumoylation level was transiently decreased upon Dox exposure, and transfection with the KAP1 sumoylation mimetic, SUMO-1-KAP1, desensitizes breast cancer MCF-7 cells to Dox-elicited cell death.	Doxorubicin	189-192	small ubiquitin like modifier 1	Homo sapiens	134-140
17101795-3	2007	Here, we found that myocardin"s activity was strongly enhanced by SUMO-1 via modification of a lysine residue primarily located at position 445 and that the conversion of this residue to arginine (K445R) impaired myocardin transactivation.	Lysine	95-101	small ubiquitin like modifier 1	Homo sapiens	66-72
17060459-5	2007	TDG is also posttranslationally modified by covalent conjugation of SUMO-1 (sumoylation) to lysine 341.	Lysine	92-98	small ubiquitin like modifier 1	Homo sapiens	68-74
17101795-3	2007	Here, we found that myocardin"s activity was strongly enhanced by SUMO-1 via modification of a lysine residue primarily located at position 445 and that the conversion of this residue to arginine (K445R) impaired myocardin transactivation.	Arginine	187-195	small ubiquitin like modifier 1	Homo sapiens	66-72
17077080-2	2006	Conjugation of small ubiquitin-like modifier type 1 (SUMO-1) to lysines in the negative regulatory domain strongly suppresses its transcriptional activity.	Lysine	64-71	small ubiquitin like modifier 1	Homo sapiens	15-51
17077080-2	2006	Conjugation of small ubiquitin-like modifier type 1 (SUMO-1) to lysines in the negative regulatory domain strongly suppresses its transcriptional activity.	Lysine	64-71	small ubiquitin like modifier 1	Homo sapiens	53-59
17077080-5	2006	These lysines are in the negative regulatory domain of c-Myb and also serve as acceptor sites for SUMO-1.	Lysine	6-13	small ubiquitin like modifier 1	Homo sapiens	98-104
16912044-3	2006	RXRalpha was modified by SUMO-1 in vivo as well as in vitro, and the Lys-108 residue within the IKPP sequence of RXRalpha AF-1 domain was identified as the major SUMO-1 acceptor site.	Lysine	69-72	small ubiquitin like modifier 1	Homo sapiens	162-168
17012228-9	2006	Site-directed mutagenesis studies showed that Lys-386 of p53, the SUMO-1 modification site, is also the modification site for SUMO-2/3.	Lysine	46-49	small ubiquitin like modifier 1	Homo sapiens	66-72
16828461-8	2006	These findings imply that SUMO-1 modification on lysine 75 may participate in regulating SOD1 stability and its aggregation process.	Lysine	49-55	small ubiquitin like modifier 1	Homo sapiens	26-32
16824543-0	2006	Residue-level NMR view of the urea-driven equilibrium folding transition of SUMO-1 (1-97): native preferences do not increase monotonously.	Urea	30-34	small ubiquitin like modifier 1	Homo sapiens	76-82
16791211-4	2006	Using SUMmOn, we demonstrate for the first time that human SUMO-1 multimerizes in vitro primarily via three N-terminal lysines, Lys7, Lys16 and Lys17.	Lysine	119-126	small ubiquitin like modifier 1	Homo sapiens	59-65
16428803-1	2006	Human (h) DNA topoisomerase I has been identified as a major SUMO1 target in camptothecin-treated cells.	Camptothecin	77-89	small ubiquitin like modifier 1	Homo sapiens	61-66
16501610-3	2006	In the NB4 cell line, which was derived from an APL patient and expresses PML:RARalpha, we observed a retinoic acid-dependent change in the modification of specific proteins by SUMO-1.	Tretinoin	102-115	small ubiquitin like modifier 1	Homo sapiens	177-183
16428803-2	2006	In response to TOP1-mediated DNA damage induced by camptothecin, multiple SUMO1 molecules are conjugated to the N-terminal domain of a single TOP1 molecule.	Camptothecin	51-63	small ubiquitin like modifier 1	Homo sapiens	74-79
16428803-5	2006	Systematic analysis has identified a single major SUMO1 conjugation site located between amino acid residues 110 and 125 that contains a single lysine residue at 117 (Lys-117).	Lysine	144-150	small ubiquitin like modifier 1	Homo sapiens	50-55
16428803-5	2006	Systematic analysis has identified a single major SUMO1 conjugation site located between amino acid residues 110 and 125 that contains a single lysine residue at 117 (Lys-117).	Lysine	167-170	small ubiquitin like modifier 1	Homo sapiens	50-55
16428803-6	2006	Using a short peptide spanning this region, we showed that a poly-SUMO1 chain was assembled in this peptide at Lys-117.	Lysine	111-114	small ubiquitin like modifier 1	Homo sapiens	66-71
16194093-7	2005	Six sites of in vitro SUMOylation in RanBP2 along with four branch-point lysines in SUMO-1 and three in SUMO-2 were identified.	Lysine	73-80	small ubiquitin like modifier 1	Homo sapiens	84-90
16501224-6	2006	In consistent fashion, TUG-UBL1 is not expected to participate in a covalent protein modification reaction as it lacks the characteristic C-terminal diglycine ("GG") motif required for conjugation to an acceptor lysine, and also lacks the three most common acceptor lysine residues involved in polyubiquitination.	Glycylglycine	149-158	small ubiquitin like modifier 1	Homo sapiens	27-31
16501224-6	2006	In consistent fashion, TUG-UBL1 is not expected to participate in a covalent protein modification reaction as it lacks the characteristic C-terminal diglycine ("GG") motif required for conjugation to an acceptor lysine, and also lacks the three most common acceptor lysine residues involved in polyubiquitination.	Lysine	212-218	small ubiquitin like modifier 1	Homo sapiens	27-31
16501224-6	2006	In consistent fashion, TUG-UBL1 is not expected to participate in a covalent protein modification reaction as it lacks the characteristic C-terminal diglycine ("GG") motif required for conjugation to an acceptor lysine, and also lacks the three most common acceptor lysine residues involved in polyubiquitination.	Lysine	266-272	small ubiquitin like modifier 1	Homo sapiens	27-31
16287980-2	2005	Here, we show that CREB-binding protein (CBP), a versatile transcriptional coactivator for numerous transcription factors in response to diverse signaling events, can be modified by SUMO-1 at lysine residues 999, 1034, and 1057 both in vitro and in vivo.	Lysine	192-198	small ubiquitin like modifier 1	Homo sapiens	182-188
16198310-3	2005	Here, we report that SUMO-4 differs from SUMO-1, -2, and -3 in that the maturation process of SUMO-4 to active form containing C-terminal di-glycine residues is inhibited by a unique proline residue located at position 90 (Pro-90).	Glycylglycine	138-148	small ubiquitin like modifier 1	Homo sapiens	41-59
16198310-3	2005	Here, we report that SUMO-4 differs from SUMO-1, -2, and -3 in that the maturation process of SUMO-4 to active form containing C-terminal di-glycine residues is inhibited by a unique proline residue located at position 90 (Pro-90).	Proline	183-190	small ubiquitin like modifier 1	Homo sapiens	41-59
16120648-3	2005	Our results further show that human ADAR1 is modified by SUMO-1 on lysine residue 418.	Lysine	67-73	small ubiquitin like modifier 1	Homo sapiens	57-63
16120648-4	2005	An arginine substitution of K418 abolishes SUMO-1 conjugation and although it does not interfere with ADAR1 proper localization, it stimulates the ability of the enzyme to edit RNA both in vivo and in vitro.	Arginine	3-11	small ubiquitin like modifier 1	Homo sapiens	43-49
16120648-4	2005	An arginine substitution of K418 abolishes SUMO-1 conjugation and although it does not interfere with ADAR1 proper localization, it stimulates the ability of the enzyme to edit RNA both in vivo and in vitro.	1,3,3,3-tetrafluoropropene	28-32	small ubiquitin like modifier 1	Homo sapiens	43-49
16142216-7	2005	However, SUMO-1 failed to interact with ASK 1(3M) and to suppress ASK 1(3M) activation, indicating that the three lysines are important for regulation by SUMO-1.	Lysine	114-121	small ubiquitin like modifier 1	Homo sapiens	154-160
15748426-8	2005	As(2)O(3) binds ubiquitin like SUMO-1 through the lysine 160 of PML, resulting in the degradation of PML-RAR alpha.	Lysine	50-56	small ubiquitin like modifier 1	Homo sapiens	31-37
16098147-6	2005	Mutational analysis showed that lysine residues at 499, 576, and 624 are the major acceptor sites for SUMO-1.	Lysine	32-38	small ubiquitin like modifier 1	Homo sapiens	102-108
16055710-3	2005	We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229.	Lysine	20-26	small ubiquitin like modifier 1	Homo sapiens	98-104
16055710-3	2005	We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229.	Lysine	161-167	small ubiquitin like modifier 1	Homo sapiens	98-104
16055710-3	2005	We report here that lysine 265 of c-Fos is conjugated by the peptidic posttranslational modifiers SUMO-1, SUMO-2, and SUMO-3 and that c-Jun can be sumoylated on lysine 257 as well as on the previously described lysine 229.	Lysine	161-167	small ubiquitin like modifier 1	Homo sapiens	98-104
15823533-6	2005	SUMO1 conjugation to the C-terminal K330 of TDG modulates the DNA binding function of the N terminus to induce dissociation of the glycosylase from the AP site while it leaves the catalytic properties of base release in the active site pocket of the enzyme unaffected.	(3R,4R)-4-Acetoxy-3-[(R)-1-(tert-butyldimethylsilyloxy) ethyl]azetidin-2-one	36-40	small ubiquitin like modifier 1	Homo sapiens	0-5
15958389-3	2005	Here we demonstrate that human HIPK2 is small ubiquitin-related modifier-1 (SUMO-1)-modified in vitro and in vivo at lysine residue 25, a SUMO consensus modification motif conserved in human and mouse HIPK family proteins.	Lysine	117-123	small ubiquitin like modifier 1	Homo sapiens	40-74
15958389-3	2005	Here we demonstrate that human HIPK2 is small ubiquitin-related modifier-1 (SUMO-1)-modified in vitro and in vivo at lysine residue 25, a SUMO consensus modification motif conserved in human and mouse HIPK family proteins.	Lysine	117-123	small ubiquitin like modifier 1	Homo sapiens	76-82
15766567-0	2005	Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability.	Lysine	85-91	small ubiquitin like modifier 1	Homo sapiens	75-81
15881673-10	2005	Mutation of two lysine residues greatly reduced the amount of the sumoylated form of OZF though their surrounding sequences differ from the consensus sequence reported for most proteins modified by SUMO-1 conjugation.	Lysine	16-22	small ubiquitin like modifier 1	Homo sapiens	198-204
15881673-12	2005	Addition of zinc finger 7 restored SUMO-1 modification and UBC9 interaction and provides evidence that a region downstream of the target lysines is required for interaction with UBC9, in order to achieve SUMO-1 modification.	Lysine	137-144	small ubiquitin like modifier 1	Homo sapiens	204-210
15881673-12	2005	Addition of zinc finger 7 restored SUMO-1 modification and UBC9 interaction and provides evidence that a region downstream of the target lysines is required for interaction with UBC9, in order to achieve SUMO-1 modification.	ubc9	178-182	small ubiquitin like modifier 1	Homo sapiens	204-210
15569683-5	2005	In contrast, another mutant of TDGb (TDGb(KR)) in which the lysine residue targeted for SUMO-1 conjugation is replaced with arginine retained the ability to bind SUMO-1 non-covalently.	Lysine	60-66	small ubiquitin like modifier 1	Homo sapiens	88-94
15569683-5	2005	In contrast, another mutant of TDGb (TDGb(KR)) in which the lysine residue targeted for SUMO-1 conjugation is replaced with arginine retained the ability to bind SUMO-1 non-covalently.	Arginine	124-132	small ubiquitin like modifier 1	Homo sapiens	162-168
15660128-2	2005	Structures of human heterodimeric Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes were determined at 2.2 and 2.75 A resolution, respectively.	Adenosine Triphosphate	75-78	small ubiquitin like modifier 1	Homo sapiens	65-71
15660128-3	2005	Despite the presence of Mg.ATP, the Sae1/Sae2-SUMO-1-Mg.ATP structure reveals a substrate complex insomuch as the SUMO C-terminus remains unmodified within the adenylation site and 35 A from the catalytic cysteine, suggesting that additional changes within the adenylation site may be required to facilitate chemistry prior to adenylation and thioester transfer.	Adenosine Triphosphate	56-59	small ubiquitin like modifier 1	Homo sapiens	46-52
15660128-3	2005	Despite the presence of Mg.ATP, the Sae1/Sae2-SUMO-1-Mg.ATP structure reveals a substrate complex insomuch as the SUMO C-terminus remains unmodified within the adenylation site and 35 A from the catalytic cysteine, suggesting that additional changes within the adenylation site may be required to facilitate chemistry prior to adenylation and thioester transfer.	Cysteine	205-213	small ubiquitin like modifier 1	Homo sapiens	46-52
15192092-3	2004	SF-1 was modified predominantly at Lys(194) and much less at Lys(119) when free SUMO-1 was supplied.	Lysine	61-64	small ubiquitin like modifier 1	Homo sapiens	80-86
15465032-8	2004	Altogether, we demonstrate that HIF-1alpha is upregulated through SUMO-1 modification at Lys(391)/Lys(477) residues, which may stabilize HIF-1alpha and enhance its transcriptional activity.	Lysine	89-92	small ubiquitin like modifier 1	Homo sapiens	66-72
15465032-8	2004	Altogether, we demonstrate that HIF-1alpha is upregulated through SUMO-1 modification at Lys(391)/Lys(477) residues, which may stabilize HIF-1alpha and enhance its transcriptional activity.	Lysine	98-101	small ubiquitin like modifier 1	Homo sapiens	66-72
15611636-3	2005	SUMO-1 attachment targets DeltaNp63alpha for proteasome mediated degradation while it does not influence p63alpha intracellular localization, as wild-type protein and a mutant carring the K637 mutated into arginine (K637R), have the same nuclear localization.	Arginine	206-214	small ubiquitin like modifier 1	Homo sapiens	0-6
15613319-7	2005	Of the two lysine residues in p6, lysine 27 uniquely served as a site of covalent SUMO-1 attachment.	Lysine	11-17	small ubiquitin like modifier 1	Homo sapiens	82-88
15613319-7	2005	Of the two lysine residues in p6, lysine 27 uniquely served as a site of covalent SUMO-1 attachment.	Lysine	34-40	small ubiquitin like modifier 1	Homo sapiens	82-88
15606148-10	2004	Treatment with 4-hydroxynonenal caused a near-complete redistribution of sumo-1 and sumo-3 to different protein targets, which included chaperones, antioxidant, and DNA damage signaling proteins.	4-hydroxy-2-nonenal	15-31	small ubiquitin like modifier 1	Homo sapiens	73-79
15355965-3	2004	Based on amide chemical shift and 15N relaxation measurements, we show that the C terminus of SUMO-1 and the loop containing the consensus sumoylation site in RanGAP1 are both conformationally flexible.	Amides	9-14	small ubiquitin like modifier 1	Homo sapiens	94-100
15355965-3	2004	Based on amide chemical shift and 15N relaxation measurements, we show that the C terminus of SUMO-1 and the loop containing the consensus sumoylation site in RanGAP1 are both conformationally flexible.	15n	34-37	small ubiquitin like modifier 1	Homo sapiens	94-100
15117942-6	2004	Furthermore, we found that treatment with both ionomycin and phorbol 12-myristate 13-acetate ensured efficient nuclear anchorage with the recruitment of NFAT1 into the SUMO-1 bodies, whereas treatment with ionomycin alone induced nuclear translocation of NFAT1 but not recruitment into the SUMO-1 bodies.	Ionomycin	47-56	small ubiquitin like modifier 1	Homo sapiens	168-174
15246872-3	2004	Here, we have shown that Fhit protein interacts with hUbc9, a recombinant human SUMO-1 conjugating enzyme, in an adenosine(5")triphospho(5")nucleoside (Ap3N)-dependent manner.	adenosine(5")triphospho(5")nucleoside	113-150	small ubiquitin like modifier 1	Homo sapiens	80-86
15246872-3	2004	Here, we have shown that Fhit protein interacts with hUbc9, a recombinant human SUMO-1 conjugating enzyme, in an adenosine(5")triphospho(5")nucleoside (Ap3N)-dependent manner.	ap3n	152-156	small ubiquitin like modifier 1	Homo sapiens	80-86
15296745-2	2004	X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins.	thiohemiacetal	80-94	small ubiquitin like modifier 1	Homo sapiens	168-174
15117942-6	2004	Furthermore, we found that treatment with both ionomycin and phorbol 12-myristate 13-acetate ensured efficient nuclear anchorage with the recruitment of NFAT1 into the SUMO-1 bodies, whereas treatment with ionomycin alone induced nuclear translocation of NFAT1 but not recruitment into the SUMO-1 bodies.	Ionomycin	47-56	small ubiquitin like modifier 1	Homo sapiens	290-296
15117942-6	2004	Furthermore, we found that treatment with both ionomycin and phorbol 12-myristate 13-acetate ensured efficient nuclear anchorage with the recruitment of NFAT1 into the SUMO-1 bodies, whereas treatment with ionomycin alone induced nuclear translocation of NFAT1 but not recruitment into the SUMO-1 bodies.	Tetradecanoylphorbol Acetate	61-92	small ubiquitin like modifier 1	Homo sapiens	168-174
15117942-6	2004	Furthermore, we found that treatment with both ionomycin and phorbol 12-myristate 13-acetate ensured efficient nuclear anchorage with the recruitment of NFAT1 into the SUMO-1 bodies, whereas treatment with ionomycin alone induced nuclear translocation of NFAT1 but not recruitment into the SUMO-1 bodies.	Tetradecanoylphorbol Acetate	61-92	small ubiquitin like modifier 1	Homo sapiens	290-296
15117942-6	2004	Furthermore, we found that treatment with both ionomycin and phorbol 12-myristate 13-acetate ensured efficient nuclear anchorage with the recruitment of NFAT1 into the SUMO-1 bodies, whereas treatment with ionomycin alone induced nuclear translocation of NFAT1 but not recruitment into the SUMO-1 bodies.	Ionomycin	206-215	small ubiquitin like modifier 1	Homo sapiens	290-296
15117942-7	2004	Our results suggest that the recruitment of NFAT1 into SUMO-1 bodies may be required for the progressive transcriptional activity of NFAT1 upon co-stimulation with ionomycin and phorbol 12-myristate 13-acetate, whereas anergic transcription stimulated by ionomycin alone may occur without recruitment into the SUMO-1 bodies.	Ionomycin	164-173	small ubiquitin like modifier 1	Homo sapiens	55-61
15117942-7	2004	Our results suggest that the recruitment of NFAT1 into SUMO-1 bodies may be required for the progressive transcriptional activity of NFAT1 upon co-stimulation with ionomycin and phorbol 12-myristate 13-acetate, whereas anergic transcription stimulated by ionomycin alone may occur without recruitment into the SUMO-1 bodies.	Ionomycin	164-173	small ubiquitin like modifier 1	Homo sapiens	310-316
15117942-7	2004	Our results suggest that the recruitment of NFAT1 into SUMO-1 bodies may be required for the progressive transcriptional activity of NFAT1 upon co-stimulation with ionomycin and phorbol 12-myristate 13-acetate, whereas anergic transcription stimulated by ionomycin alone may occur without recruitment into the SUMO-1 bodies.	Tetradecanoylphorbol Acetate	178-209	small ubiquitin like modifier 1	Homo sapiens	55-61
15117942-7	2004	Our results suggest that the recruitment of NFAT1 into SUMO-1 bodies may be required for the progressive transcriptional activity of NFAT1 upon co-stimulation with ionomycin and phorbol 12-myristate 13-acetate, whereas anergic transcription stimulated by ionomycin alone may occur without recruitment into the SUMO-1 bodies.	Ionomycin	255-264	small ubiquitin like modifier 1	Homo sapiens	55-61
15497507-4	2004	We found that, similar to its human counterpart, Xenopus Hsf2 is sumoylated at lysine 82 and that, as it does in human Hsf2, the modification event of the small ubiquitin-related modifier 1 functions to increase the deoxyribonucleic acid-binding activity of this transcription factor in Xenopus.	Lysine	79-85	small ubiquitin like modifier 1	Homo sapiens	155-189
15173587-3	2004	Here, we demonstrate that the erythroid transcription factor GATA-1 is sumoylated in vitro and in vivo and map the single lysine residue involved in SUMO-1 attachment.	Lysine	122-128	small ubiquitin like modifier 1	Homo sapiens	149-155
14671118-7	2004	EBNA3C m1 and m2 point mutations, DDD(507-509) mutated to AAA and DVIEVID(509-513) mutated to AVIAVIA, respectively, diminished SUMO-1 and SUMO-3 interaction in directed yeast two-hybrid and glutathione S-transferase pulldown assays.	Glutathione	191-202	small ubiquitin like modifier 1	Homo sapiens	128-134
14563852-7	2004	Consistent with the prediction that the protease is a member of the cysteine family of proteases, we mutated a key cysteine residue and observed that expression of this catalytic mutant had a dominant negative phenotype, resulting in the accumulation of high molecular weight SUMO-1 conjugates.	Cysteine	68-76	small ubiquitin like modifier 1	Homo sapiens	276-282
14563852-7	2004	Consistent with the prediction that the protease is a member of the cysteine family of proteases, we mutated a key cysteine residue and observed that expression of this catalytic mutant had a dominant negative phenotype, resulting in the accumulation of high molecular weight SUMO-1 conjugates.	Cysteine	115-123	small ubiquitin like modifier 1	Homo sapiens	276-282
12855578-5	2003	Furthermore, activation of STAT1 by IFN-gamma or pervanadate induced SUMO-1 conjugation.	pervanadate	49-60	small ubiquitin like modifier 1	Homo sapiens	69-75
14500761-7	2003	Deciphering the unique sumoylation pattern of hMR, which possesses five consensus SUMO-1 binding sites, by combinatorial lysine substitutions, revealed a major impact of sumoylation on hMR properties.	Lysine	121-127	small ubiquitin like modifier 1	Homo sapiens	82-88
12866878-4	2003	In the current work, a heteromeric complex containing UBC9 (an E2 conjugating enzyme) and SUMO-1 (a ubiquitin-like modifier) was investigated by incubating the complex in D2O and measuring the amount of deuterium incorporation with MS. SUMO-1 had significant changes in deuterium levels when bound to UBC9.	Deuterium Oxide	171-174	small ubiquitin like modifier 1	Homo sapiens	63-123
12788062-4	2003	Here, we report that SRF is modified by SUMO-1 chiefly at lysine(147) within the DNA-binding domain.	Lysine	58-64	small ubiquitin like modifier 1	Homo sapiens	40-46
14516784-8	2003	One SUMO-1 acceptor site at lysine residue 560 could be identified within this region.	Lysine	28-34	small ubiquitin like modifier 1	Homo sapiens	4-10
12885887-11	2003	Using a transfection-based approach and a family of deletion and point mutations of PML, we found that efficient ICP0-induced PML degradation requires sequences within the C-terminal part of PML and lysine residue 160, one of the principal targets for SUMO-1 modification of the protein.	Lysine	199-205	small ubiquitin like modifier 1	Homo sapiens	252-258
12866878-4	2003	In the current work, a heteromeric complex containing UBC9 (an E2 conjugating enzyme) and SUMO-1 (a ubiquitin-like modifier) was investigated by incubating the complex in D2O and measuring the amount of deuterium incorporation with MS. SUMO-1 had significant changes in deuterium levels when bound to UBC9.	Deuterium	270-279	small ubiquitin like modifier 1	Homo sapiens	90-96
12866878-4	2003	In the current work, a heteromeric complex containing UBC9 (an E2 conjugating enzyme) and SUMO-1 (a ubiquitin-like modifier) was investigated by incubating the complex in D2O and measuring the amount of deuterium incorporation with MS. SUMO-1 had significant changes in deuterium levels when bound to UBC9.	Deuterium Oxide	171-174	small ubiquitin like modifier 1	Homo sapiens	90-96
12866878-4	2003	In the current work, a heteromeric complex containing UBC9 (an E2 conjugating enzyme) and SUMO-1 (a ubiquitin-like modifier) was investigated by incubating the complex in D2O and measuring the amount of deuterium incorporation with MS. SUMO-1 had significant changes in deuterium levels when bound to UBC9.	Deuterium	203-212	small ubiquitin like modifier 1	Homo sapiens	63-123
12866878-4	2003	In the current work, a heteromeric complex containing UBC9 (an E2 conjugating enzyme) and SUMO-1 (a ubiquitin-like modifier) was investigated by incubating the complex in D2O and measuring the amount of deuterium incorporation with MS. SUMO-1 had significant changes in deuterium levels when bound to UBC9.	Deuterium	203-212	small ubiquitin like modifier 1	Homo sapiens	90-96
12866878-4	2003	In the current work, a heteromeric complex containing UBC9 (an E2 conjugating enzyme) and SUMO-1 (a ubiquitin-like modifier) was investigated by incubating the complex in D2O and measuring the amount of deuterium incorporation with MS. SUMO-1 had significant changes in deuterium levels when bound to UBC9.	Deuterium	270-279	small ubiquitin like modifier 1	Homo sapiens	63-123
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Adenosine Triphosphate	6-9	small ubiquitin like modifier 1	Homo sapiens	46-52
12679040-4	2003	In vitro, CtBP sumoylation minimally requires the SUMO E1 and E2 (Ubc9) and SUMO-1.	ctbp	10-14	small ubiquitin like modifier 1	Homo sapiens	76-82
12641448-1	2003	The small ubiquitin-like modifier SUMO-1 is covalently attached to lysine residues on target proteins by a specific conjugation pathway involving the E1 enzyme SAE1/SAE2 and the E2 enzyme Ubc9.	Lysine	67-73	small ubiquitin like modifier 1	Homo sapiens	34-40
12529333-11	2003	This observation suggests that among the many protein partners involved in steroid hormone-mediated gene regulation several are probably targets of SUMO-1 modification.	Steroids	75-90	small ubiquitin like modifier 1	Homo sapiens	148-154
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Adenosine Triphosphate	6-9	small ubiquitin like modifier 1	Homo sapiens	157-163
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Adenosine Triphosphate	6-9	small ubiquitin like modifier 1	Homo sapiens	157-163
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Cysteine	93-101	small ubiquitin like modifier 1	Homo sapiens	46-52
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Lysine	286-292	small ubiquitin like modifier 1	Homo sapiens	46-52
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Lysine	286-292	small ubiquitin like modifier 1	Homo sapiens	157-163
12641448-2	2003	In an ATP-dependent manner, the C-terminus of SUMO-1 forms consecutive thiolester bonds with cysteine residues in the SAE2 subunit and Ubc9, before the Ubc9.SUMO-1 thiolester complex catalyzes the formation of an isopeptide bond between SUMO-1 and the epsilon-amino group of the target lysine residue on the protein substrate.	Lysine	286-292	small ubiquitin like modifier 1	Homo sapiens	157-163
12641448-5	2003	These residues are found close to the active site Cys in the tertiary structure of Ubc9, and although they are shown to inhibit the transesterification reaction from SAE1/SAE2, they are important for substrate recognition in the context of the thiolester complex with SUMO-1.	Cysteine	50-53	small ubiquitin like modifier 1	Homo sapiens	268-274
12161447-9	2002	Importantly, the RDM is similar to the recognition sequence for attachment of the ubiquitin-like protein, small ubiquitin-like modifier-1 (SUMO-1), and the conserved lysine residue of each C/EBP RDM served as an attachment site for SUMO-1.	Lysine	166-172	small ubiquitin like modifier 1	Homo sapiens	106-137
12439742-0	2002	SUMO-1 conjugation to intact DNA topoisomerase I amplifies cleavable complex formation induced by camptothecin.	Camptothecin	98-110	small ubiquitin like modifier 1	Homo sapiens	0-6
12552083-9	2003	Mutation of K304 also results in loss of CREB nuclear localization, implying a role for SUMO-1 modification at this site in the subcellular localization of CREB.	k304	12-16	small ubiquitin like modifier 1	Homo sapiens	88-94
12354770-5	2002	Here, we report that ARNT is modified by SUMO-1 chiefly at Lys(245) within the PAS domain of this protein, both in vivo and in vitro.	Lysine	59-62	small ubiquitin like modifier 1	Homo sapiens	41-47
12161447-9	2002	Importantly, the RDM is similar to the recognition sequence for attachment of the ubiquitin-like protein, small ubiquitin-like modifier-1 (SUMO-1), and the conserved lysine residue of each C/EBP RDM served as an attachment site for SUMO-1.	Lysine	166-172	small ubiquitin like modifier 1	Homo sapiens	232-238
11861864-11	2002	Lysine 450 is within a sumoylation consensus site (I,V,L)KXE; changing lysine 450 to arginine by point mutation abolishes SUMO-1 modification of IE72.	Lysine	0-6	small ubiquitin like modifier 1	Homo sapiens	122-128
12419227-4	2002	Removal of SUMO-1 from Sp3 by mutation of the SUMO acceptor lysines or expression of the SUMO-1 protease SuPr-1 converted Sp3 to a strong activator with a diffuse nuclear localization.	Lysine	60-67	small ubiquitin like modifier 1	Homo sapiens	11-17
12200128-7	2002	Mutation of lysine 1086 of SALL1 to arginine abrogates SALL1 sumoylation, suggesting the presence of a polymeric SUMO-1 chain in the wild type state.	Lysine	12-18	small ubiquitin like modifier 1	Homo sapiens	113-119
12060666-3	2002	In this work, we demonstrate that lysine residues 239, 731, and 788 of GRIP1 serve as principal attachment sites for SUMO-1.	Lysine	34-40	small ubiquitin like modifier 1	Homo sapiens	117-123
11779867-5	2002	Interestingly, the single mutation K523R completely abolished modification of c-Myb with SUMO-1, suggesting that sumolation of Lys(523) is required for modification of other lysines in c-Myb.	Lysine	127-130	small ubiquitin like modifier 1	Homo sapiens	89-95
11779867-6	2002	In accordance with this observation, we found that the SUMO-1-conjugating enzyme Ubc9 interacted only with a region surrounding Lys(523) (also called the PEST/EVES motif).	Lysine	128-131	small ubiquitin like modifier 1	Homo sapiens	55-61
11602710-5	2001	Lysine 450 was mapped as the major SUMO-1 conjugation site, but a point mutation of this lysine residue in IE1 did not interfere with its targeting to and disruption of the PODs.	Lysine	0-6	small ubiquitin like modifier 1	Homo sapiens	35-41
11413191-3	2001	PML is conjugated by the ubiquitin-related peptide SUMO-1, a process enhanced by As2O3 and proposed to target PML to the nuclear matrix.	Arsenic Trioxide	81-86	small ubiquitin like modifier 1	Homo sapiens	51-57
11514557-3	2001	We report that HSF1 undergoes stress-induced modification at lysine 298 by the small ubiquitin-related protein called SUMO-1.	Lysine	61-67	small ubiquitin like modifier 1	Homo sapiens	118-124
11514557-5	2001	HSF1 colocalizes with SUMO-1 in nuclear stress granules, which is prevented by mutation of lysine 298.	Lysine	91-97	small ubiquitin like modifier 1	Homo sapiens	22-28
11489887-4	2001	The SMT3IP2 expressed by Escherichia coli could cleave SUMO-1, Smt3a, or Smt3b from a SUMO-1/RanGAP1, Smt3a/RanGAP1, or Smt3b/RanGAP1 conjugate, respectively, and had the activity of a carboxyl-terminal hydrolase to produce a glycine residue in the carboxyl terminus of these ubiquitin-like proteins.	Glycine	226-233	small ubiquitin like modifier 1	Homo sapiens	55-61
11489887-4	2001	The SMT3IP2 expressed by Escherichia coli could cleave SUMO-1, Smt3a, or Smt3b from a SUMO-1/RanGAP1, Smt3a/RanGAP1, or Smt3b/RanGAP1 conjugate, respectively, and had the activity of a carboxyl-terminal hydrolase to produce a glycine residue in the carboxyl terminus of these ubiquitin-like proteins.	Glycine	226-233	small ubiquitin like modifier 1	Homo sapiens	86-92
11158586-5	2001	After 6-10 h of MG132 treatment, PML, Sp100, and SUMO-1 were no longer detectable in the PODs and accumulated mainly in the nucleolus.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	16-21	small ubiquitin like modifier 1	Homo sapiens	49-55
11259410-6	2001	The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates.	Cesium	38-40	small ubiquitin like modifier 1	Homo sapiens	4-10
11259410-6	2001	The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates.	Cesium	38-40	small ubiquitin like modifier 1	Homo sapiens	31-37
11259410-6	2001	The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates.	Cesium	38-40	small ubiquitin like modifier 1	Homo sapiens	31-37
11259410-6	2001	The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates.	Lysine	100-106	small ubiquitin like modifier 1	Homo sapiens	4-10
11259410-6	2001	The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates.	Lysine	100-106	small ubiquitin like modifier 1	Homo sapiens	31-37
11259410-6	2001	The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates.	Lysine	100-106	small ubiquitin like modifier 1	Homo sapiens	31-37
11259410-7	2001	This motif conforms to the sequence "PsiKXE," where Psi is a large hydrophobic residue, K is the lysine to which SUMO-1 is conjugated, X is any amino acid, and E is glutamic acid.	Lysine	97-103	small ubiquitin like modifier 1	Homo sapiens	113-119
11259410-10	2001	These findings have important implications for how SUMO-1 substrates are recognized and for how SUMO-1 is ultimately transferred to specific lysine residues on these substrates.	Lysine	141-147	small ubiquitin like modifier 1	Homo sapiens	51-57
11259410-10	2001	These findings have important implications for how SUMO-1 substrates are recognized and for how SUMO-1 is ultimately transferred to specific lysine residues on these substrates.	Lysine	141-147	small ubiquitin like modifier 1	Homo sapiens	96-102
11278381-4	2001	Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a "wing" within the DNA-binding domain of this protein.	Lysine	21-27	small ubiquitin like modifier 1	Homo sapiens	52-58
11264375-6	2001	Two lysine residues at positions 175 and 180 were mapped as major alternative SUMO-1 conjugation sites in both cotransfected cells and an in vitro sumoylation assay and could be conjugated by SUMO-1 simultaneously.	Lysine	4-10	small ubiquitin like modifier 1	Homo sapiens	78-84
11264375-6	2001	Two lysine residues at positions 175 and 180 were mapped as major alternative SUMO-1 conjugation sites in both cotransfected cells and an in vitro sumoylation assay and could be conjugated by SUMO-1 simultaneously.	Lysine	4-10	small ubiquitin like modifier 1	Homo sapiens	192-198
10788439-4	2000	In contrast to ubiquitin, SUMO-1 preferentially targets a single lysine residue in c-Jun (Lys-229), and the abrogation of SUMO-1 modification does not compromise its ubiquitination.	Lysine	65-71	small ubiquitin like modifier 1	Homo sapiens	26-32
10961991-5	2000	The major SUMO-1-modified residue in p73alpha is the C-terminal lysine (Lys(627)).	Lysine	64-70	small ubiquitin like modifier 1	Homo sapiens	10-16
10961991-5	2000	The major SUMO-1-modified residue in p73alpha is the C-terminal lysine (Lys(627)).	Lysine	72-75	small ubiquitin like modifier 1	Homo sapiens	10-16
10961991-6	2000	The sequence surrounding this lysine conforms to a consensus SUMO-1 modification site b(X)XXhKXE, where b is a basic amino acid.	Lysine	30-36	small ubiquitin like modifier 1	Homo sapiens	61-67
10961991-6	2000	The sequence surrounding this lysine conforms to a consensus SUMO-1 modification site b(X)XXhKXE, where b is a basic amino acid.	Amino Acids, Basic	111-127	small ubiquitin like modifier 1	Homo sapiens	61-67
10862613-1	2000	Topoisomerase I-mediated DNA damage induced by camptothecin has been shown to induce rapid small ubiquitin-related modifier (SUMO)-1 conjugation to topoisomerase I.	Camptothecin	47-59	small ubiquitin like modifier 1	Homo sapiens	97-132
10892746-2	2000	We demonstrate that Mdm2 is conjugated with SUMO-1 (sumoylated) at Lys-446, which is located within the RING finger domain and plays a critical role in Mdm2 self-ubiquitination.	Lysine	67-70	small ubiquitin like modifier 1	Homo sapiens	44-50
11112409-2	2000	However, the mechanism by which sentrin exerts its effect upon Fas-mediated apoptosis is not well known.	ammonium ferrous sulfate	63-66	small ubiquitin like modifier 1	Homo sapiens	32-39
10788439-6	2000	Accordingly, loss of the two major Jun NH(2)-terminal kinase phosphorylation sites in c-Jun, Ser-63 and Ser-73, greatly enhances conjugation by SUMO-1.	Serine	104-107	small ubiquitin like modifier 1	Homo sapiens	144-150
10788439-9	2000	The SUMO-1 attachment site in p53 (Lys-386) resides within a region known to regulate the DNA binding activity of the protein.	Lysine	35-38	small ubiquitin like modifier 1	Homo sapiens	4-10
10788439-4	2000	In contrast to ubiquitin, SUMO-1 preferentially targets a single lysine residue in c-Jun (Lys-229), and the abrogation of SUMO-1 modification does not compromise its ubiquitination.	Lysine	90-93	small ubiquitin like modifier 1	Homo sapiens	26-32
10788439-6	2000	Accordingly, loss of the two major Jun NH(2)-terminal kinase phosphorylation sites in c-Jun, Ser-63 and Ser-73, greatly enhances conjugation by SUMO-1.	Serine	93-96	small ubiquitin like modifier 1	Homo sapiens	144-150
10759568-2	2000	In the current study, we show that treatment of mammalian cells or yeast cells expressing human DNA TOP1 with camptothecin (CPT) induces covalent modification of the TOP1 by SUMO-1/Smt3p, a ubiquitin-like protein.	Camptothecin	110-122	small ubiquitin like modifier 1	Homo sapiens	174-180
10759568-2	2000	In the current study, we show that treatment of mammalian cells or yeast cells expressing human DNA TOP1 with camptothecin (CPT) induces covalent modification of the TOP1 by SUMO-1/Smt3p, a ubiquitin-like protein.	Camptothecin	110-122	small ubiquitin like modifier 1	Homo sapiens	181-186
10759568-2	2000	In the current study, we show that treatment of mammalian cells or yeast cells expressing human DNA TOP1 with camptothecin (CPT) induces covalent modification of the TOP1 by SUMO-1/Smt3p, a ubiquitin-like protein.	Camptothecin	124-127	small ubiquitin like modifier 1	Homo sapiens	174-180
10759568-2	2000	In the current study, we show that treatment of mammalian cells or yeast cells expressing human DNA TOP1 with camptothecin (CPT) induces covalent modification of the TOP1 by SUMO-1/Smt3p, a ubiquitin-like protein.	Camptothecin	124-127	small ubiquitin like modifier 1	Homo sapiens	181-186
10728754-3	2000	METHODS: The expression of sentrin-1 mRNA was examined by in situ hybridization on snap-frozen sections of normal and RA synovial tissues as well as on paraffin-embedded RA synovial specimens, including the interface of cartilage-bone and invading synovium.	Paraffin	152-160	small ubiquitin like modifier 1	Homo sapiens	27-34
10655495-8	2000	The mUbc9 sentrin-conjugating enzyme represents a novel regulator of GLUT1 and GLUT4 protein levels with potential importance as a determinant of basal and insulin-stimulated glucose uptake in normal and pathophysiological states.	Glucose	175-182	small ubiquitin like modifier 1	Homo sapiens	10-17
10212234-7	1999	The lysine residue of the Sp100 protein, to which SUMO-1 is covalently linked, was mapped within and may therefore modulate the previously described HP1 protein-binding site.	Lysine	4-10	small ubiquitin like modifier 1	Homo sapiens	50-56
11193908-0	2000	Ubiquitin, SUMO-1, and UCRP in camptothecin sensitivity and resistance.	Camptothecin	31-43	small ubiquitin like modifier 1	Homo sapiens	11-17
10531301-6	1999	The activity of SUMO-1 hydrolase was almost completely inhibited by N-ethylmaleimide, but not by phenylmethanesulfonyl fluoride, EDTA, and ubiquitin-aldehyde known as a potent inhibitor of deubiquitinylating enzymes.	Ethylmaleimide	68-84	small ubiquitin like modifier 1	Homo sapiens	16-22
10562558-3	1999	A lysine residue at amino acid position 386 of p53 is required for this previously undescribed modification, strongly suggesting that this lysine residue serves as the major attachment site for SUMO-1.	Lysine	2-8	small ubiquitin like modifier 1	Homo sapiens	194-200
10562558-3	1999	A lysine residue at amino acid position 386 of p53 is required for this previously undescribed modification, strongly suggesting that this lysine residue serves as the major attachment site for SUMO-1.	Lysine	139-145	small ubiquitin like modifier 1	Homo sapiens	194-200
10373566-0	1999	PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia.	Arsenic Trioxide	64-80	small ubiquitin like modifier 1	Homo sapiens	0-5
10373566-0	1999	PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia.	Arsenic Trioxide	64-80	small ubiquitin like modifier 1	Homo sapiens	6-12
10075924-3	1999	We have shown recently that Vmw110 can induce the proteasome-dependent loss of several cellular proteins, including a number of probable SUMO-1-conjugated isoforms of PML, and this results in the disruption of ND10.	vmw110	28-34	small ubiquitin like modifier 1	Homo sapiens	137-143
10187858-5	1999	In vitro, recombinant SAE1/SAE2 (SUMO-1-activating enzyme) was capable of catalyzing the ATP-dependent formation of a thioester linkage between SUMO-1 and SAE2.	Adenosine Triphosphate	89-92	small ubiquitin like modifier 1	Homo sapiens	33-39
10187858-5	1999	In vitro, recombinant SAE1/SAE2 (SUMO-1-activating enzyme) was capable of catalyzing the ATP-dependent formation of a thioester linkage between SUMO-1 and SAE2.	Adenosine Triphosphate	89-92	small ubiquitin like modifier 1	Homo sapiens	144-150
10187858-7	1999	In the presence of SAE1/SAE2, Ubch9, and ATP, SUMO-1 was efficiently conjugated to the protein substrate IkappaBalpha.	Adenosine Triphosphate	41-44	small ubiquitin like modifier 1	Homo sapiens	46-52
10217437-5	1999	Human UBA2 could form a beta-mercaptoethanol-sensitive conjugate with members of the sentrin family, but not with ubiquitin of NEDD8, in the presence of AOS1.	Mercaptoethanol	24-44	small ubiquitin like modifier 1	Homo sapiens	85-92
9834237-9	1998	The mechanism of antimony action is likely to be similar to that of As2O3, notably both substances induce the attachment of the ubiquitin-like SUMO-1 molecule to the PML moiety of PML-RAR.	Arsenic Trioxide	68-73	small ubiquitin like modifier 1	Homo sapiens	143-149
9654451-8	1998	Furthermore, ubiquitin Lys48, required to generate ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the same position, which provides an explanation of why SUMO-1 has not been observed to form polymers.	Polymers	201-209	small ubiquitin like modifier 1	Homo sapiens	89-95
9654451-8	1998	Furthermore, ubiquitin Lys48, required to generate ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the same position, which provides an explanation of why SUMO-1 has not been observed to form polymers.	Polymers	201-209	small ubiquitin like modifier 1	Homo sapiens	164-170
9654451-6	1998	In addition, the position of the two C-terminal Gly residues required for isopeptide bond formation is conserved between ubiquitin and SUMO-1.	Glycine	48-51	small ubiquitin like modifier 1	Homo sapiens	135-141
9442102-1	1998	The mammalian guanosine triphosphate (GTP)ase-activating protein RanGAP1 is the first example of a protein covalently linked to the ubiquitin-related protein SUMO-1.	Guanosine Triphosphate	14-36	small ubiquitin like modifier 1	Homo sapiens	158-164
9654451-8	1998	Furthermore, ubiquitin Lys48, required to generate ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the same position, which provides an explanation of why SUMO-1 has not been observed to form polymers.	Polymers	61-69	small ubiquitin like modifier 1	Homo sapiens	89-95
9654451-8	1998	Furthermore, ubiquitin Lys48, required to generate ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the same position, which provides an explanation of why SUMO-1 has not been observed to form polymers.	Polymers	61-69	small ubiquitin like modifier 1	Homo sapiens	164-170
9452416-5	1998	Covalent modification of PML requires the conserved Gly residue near the C termini of sentrin proteins.	Glycine	52-55	small ubiquitin like modifier 1	Homo sapiens	86-93
9442102-1	1998	The mammalian guanosine triphosphate (GTP)ase-activating protein RanGAP1 is the first example of a protein covalently linked to the ubiquitin-related protein SUMO-1.	Guanosine Triphosphate	38-41	small ubiquitin like modifier 1	Homo sapiens	158-164
9442102-3	1998	SUMO-1 is linked to RanGAP1 via glycine 97, indicating that the last 4 amino acids of this 101- amino acid protein are proteolytically removed before its attachment to RanGAP1.	Glycine	32-39	small ubiquitin like modifier 1	Homo sapiens	0-6
9442102-5	1998	In contrast to most ubiquitinated proteins, only a single lysine residue (K526) in RanGAP1 can serve as the acceptor site for modification by SUMO-1.	Lysine	58-64	small ubiquitin like modifier 1	Homo sapiens	142-148
9442102-5	1998	In contrast to most ubiquitinated proteins, only a single lysine residue (K526) in RanGAP1 can serve as the acceptor site for modification by SUMO-1.	Hexahydrophthalic anhydride	74-78	small ubiquitin like modifier 1	Homo sapiens	142-148
9361375-1	1997	Nitric Oxide (NO) inhibits platelet aggregation via activation of an intraplatelet soluble guanylate cyclase which induces an increase in cyclic GMP (1).	Nitric Oxide	0-12	small ubiquitin like modifier 1	Homo sapiens	145-152
9427741-7	1998	As2O3 administration strikingly increases the pool of SUMO-1-PML conjugates that, subsequently, accumulate in enlarged nuclear bodies.	Arsenic Trioxide	0-5	small ubiquitin like modifier 1	Homo sapiens	54-60
9353268-8	1997	The interaction between sentrin and Ubc9 required the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.	Glycine	90-93	small ubiquitin like modifier 1	Homo sapiens	24-31
9353268-8	1997	The interaction between sentrin and Ubc9 required the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.	Glycine	90-93	small ubiquitin like modifier 1	Homo sapiens	110-117
9353268-8	1997	The interaction between sentrin and Ubc9 required the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.	Glycine	94-97	small ubiquitin like modifier 1	Homo sapiens	24-31
9353268-8	1997	The interaction between sentrin and Ubc9 required the ubiquitin domain and the C-terminal Gly-Gly residues of sentrin.	Glycine	94-97	small ubiquitin like modifier 1	Homo sapiens	110-117
9353268-11	1997	A beta-mercaptoethanol-sensitive Ubc9-sentrin conjugate could also be identified in the in vitro binding assay.	Mercaptoethanol	2-22	small ubiquitin like modifier 1	Homo sapiens	38-45
9353268-12	1997	Substitution of the conserved cysteine residue of Ubc9 by serine abolished the formation of the Ubc9-sentrin conjugate.	Cysteine	30-38	small ubiquitin like modifier 1	Homo sapiens	101-108
9353268-12	1997	Substitution of the conserved cysteine residue of Ubc9 by serine abolished the formation of the Ubc9-sentrin conjugate.	Serine	58-64	small ubiquitin like modifier 1	Homo sapiens	101-108
9312010-5	1997	Smt3p undergoes ATP-dependent activation by a novel heterodimeric enzyme consisting of Uba2p, a previously identified 71 kDa protein similar to the C-terminus of ubiquitin-activating enzymes (E1s), and Aos1p (activation of Smt3p), a 40 kDa protein similar to the N-terminus of E1s.	Adenosine Triphosphate	16-19	small ubiquitin like modifier 1	Homo sapiens	0-5
9312010-5	1997	Smt3p undergoes ATP-dependent activation by a novel heterodimeric enzyme consisting of Uba2p, a previously identified 71 kDa protein similar to the C-terminus of ubiquitin-activating enzymes (E1s), and Aos1p (activation of Smt3p), a 40 kDa protein similar to the N-terminus of E1s.	Adenosine Triphosphate	16-19	small ubiquitin like modifier 1	Homo sapiens	223-228
9162015-3	1997	Because sentrin possesses the conserved Gly-Gly residues near the C terminus, it is likely that these additional bands represent conjugation of sentrin to other proteins in a manner that is similar to the ubiquitination pathway.	Glycine	40-43	small ubiquitin like modifier 1	Homo sapiens	8-15
9162015-3	1997	Because sentrin possesses the conserved Gly-Gly residues near the C terminus, it is likely that these additional bands represent conjugation of sentrin to other proteins in a manner that is similar to the ubiquitination pathway.	Glycine	44-47	small ubiquitin like modifier 1	Homo sapiens	8-15
9162015-7	1997	When the conserved Gly-Gly residues of sentrin were changed to Gly-Ala, only sentrin monomer and p90 but not the high molecular mass bands were observed.	Glycine	19-22	small ubiquitin like modifier 1	Homo sapiens	39-46
9162015-4	1997	Transient expression of hemagglutinin epitope-tagged sentrin mutants in COS cells demonstrated that the sentrin C terminus is cleaved, which allows it to be conjugated to other proteins via the conserved C-terminal Gly residue.	Glycine	215-218	small ubiquitin like modifier 1	Homo sapiens	104-111
9162015-7	1997	When the conserved Gly-Gly residues of sentrin were changed to Gly-Ala, only sentrin monomer and p90 but not the high molecular mass bands were observed.	Glycine	19-22	small ubiquitin like modifier 1	Homo sapiens	77-84
9162015-4	1997	Transient expression of hemagglutinin epitope-tagged sentrin mutants in COS cells demonstrated that the sentrin C terminus is cleaved, which allows it to be conjugated to other proteins via the conserved C-terminal Gly residue.	Glycine	215-218	small ubiquitin like modifier 1	Homo sapiens	53-60
9162015-7	1997	When the conserved Gly-Gly residues of sentrin were changed to Gly-Ala, only sentrin monomer and p90 but not the high molecular mass bands were observed.	Glycine	23-26	small ubiquitin like modifier 1	Homo sapiens	39-46
9019411-2	1997	This interaction requires the ATP-dependent posttranslational conjugation of RanGAP1 with SUMO-1 (for small ubiquitin-related modifier), a novel protein of 101 amino acids that contains low but significant homology to ubiquitin.	Adenosine Triphosphate	30-33	small ubiquitin like modifier 1	Homo sapiens	90-96
9162015-7	1997	When the conserved Gly-Gly residues of sentrin were changed to Gly-Ala, only sentrin monomer and p90 but not the high molecular mass bands were observed.	N-glycylalanine	63-70	small ubiquitin like modifier 1	Homo sapiens	77-84
8943400-5	1996	GMP1 consisted of four short consensus repeats (SCRs), regions corresponding to the human serine/threonine/proline-rich C (STP(C)) domain and a human region of unknown significance, a hydrophobic region presumed to be a transmembrane domain, and a cytoplasmic region.	Serine	90-96	small ubiquitin like modifier 1	Homo sapiens	0-4
8943400-5	1996	GMP1 consisted of four short consensus repeats (SCRs), regions corresponding to the human serine/threonine/proline-rich C (STP(C)) domain and a human region of unknown significance, a hydrophobic region presumed to be a transmembrane domain, and a cytoplasmic region.	Threonine	97-106	small ubiquitin like modifier 1	Homo sapiens	0-4
8943400-5	1996	GMP1 consisted of four short consensus repeats (SCRs), regions corresponding to the human serine/threonine/proline-rich C (STP(C)) domain and a human region of unknown significance, a hydrophobic region presumed to be a transmembrane domain, and a cytoplasmic region.	Proline	107-114	small ubiquitin like modifier 1	Homo sapiens	0-4
8806687-9	1996	However, following all trans retinoic acid treatment of NB4 cells a significant relocalisation of PIC1 and PML is observed.	2-octenal	23-28	small ubiquitin like modifier 1	Homo sapiens	98-102
8806687-9	1996	However, following all trans retinoic acid treatment of NB4 cells a significant relocalisation of PIC1 and PML is observed.	Tretinoin	29-42	small ubiquitin like modifier 1	Homo sapiens	98-102
1649410-6	1991	Bt2cGMP (0.1 and 1 mmol/l) enhanced O2- formation induced by 0.1 mumol/1 C5a by 23% and 49%, respectively, and Bt2cGMP antagonized inhibition of O2- formation caused by Bt2cAMP.	Superoxides	36-38	small ubiquitin like modifier 1	Homo sapiens	0-18
21556614-8	1995	Single-strand conformation polymorphism and direct cycle DNA sequencing analyses demonstrated a PIC1 variant (with an AGC to AGA substitution at codon 31 culminating in a serine to arginine replacement) in Mahlavu, PLC/PRF/5, SiHa, A549 and Raji cell lines.	Serine	171-177	small ubiquitin like modifier 1	Homo sapiens	96-100
21556614-8	1995	Single-strand conformation polymorphism and direct cycle DNA sequencing analyses demonstrated a PIC1 variant (with an AGC to AGA substitution at codon 31 culminating in a serine to arginine replacement) in Mahlavu, PLC/PRF/5, SiHa, A549 and Raji cell lines.	Arginine	181-189	small ubiquitin like modifier 1	Homo sapiens	96-100
1649410-6	1991	Bt2cGMP (0.1 and 1 mmol/l) enhanced O2- formation induced by 0.1 mumol/1 C5a by 23% and 49%, respectively, and Bt2cGMP antagonized inhibition of O2- formation caused by Bt2cAMP.	Bucladesine	169-176	small ubiquitin like modifier 1	Homo sapiens	0-18
16415059-0	2006	Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.	Urea	62-66	small ubiquitin like modifier 1	Homo sapiens	86-92
16415059-1	2006	We have investigated by multidimensional NMR the structural and dynamic characteristics of the urea-denatured state of activated SUMO-1, a 97-residue protein belonging to the growing family of ubiquitin-like proteins involved in post-translational modifications.	Urea	95-99	small ubiquitin like modifier 1	Homo sapiens	129-135
16415059-9	2006	The implications of these observations for the early folding events starting from the urea-denatured state of activated SUMO-1 have been discussed.	Urea	86-90	small ubiquitin like modifier 1	Homo sapiens	120-126
34535770-9	2021	Simultaneously, sEV-miR-151a-3p targets YTHDF3 to decrease the transcriptional inhibitory activity of SP3 by reducing SUMO1 translation in a N6-methyladenosine-dependent manner.	N-methyladenosine	141-159	small ubiquitin like modifier 1	Homo sapiens	118-123
34663464-0	2021	SUMO1 modification of IGF-1R combining with SNAI2 inhibited osteogenic differentiation of PDLSCs stimulated by high glucose.	Glucose	116-123	small ubiquitin like modifier 1	Homo sapiens	0-5
34663464-13	2021	CONCLUSION: Our data demonstrated that SUMO1 modification of IGF-1R inhibited osteogenic differentiation of PDLSCs by binding to SNAI2 in high glucose environment, a key factor leading to alveolar bone loss in diabetic patients.	Glucose	143-150	small ubiquitin like modifier 1	Homo sapiens	39-44
33508304-7	2021	GA prevented IGF-1R from binding to SUMO1, thereby suppressing its nuclear accumulation.	ginkgolic acid	0-2	small ubiquitin like modifier 1	Homo sapiens	36-41
35426585-5	2022	Genetic variants in MTR, PCYT1A, ASS1, SLC 25A13, GSTM1, GSTT1, SUMO1 BHMT1, and BHMT2 are being reported to be linked with CL/P risk.	Phosphorus	127-128	small ubiquitin like modifier 1	Homo sapiens	64-69
35001170-3	2022	PML proteins are rapidly modified both with SUMO2/3 and SUMO1 after exposure to arsenite (As3+) and SUMOylated PML are further ubiquitinated and degraded by proteasomes.	arsenite	80-88	small ubiquitin like modifier 1	Homo sapiens	56-61
35001170-3	2022	PML proteins are rapidly modified both with SUMO2/3 and SUMO1 after exposure to arsenite (As3+) and SUMOylated PML are further ubiquitinated and degraded by proteasomes.	as3+	90-94	small ubiquitin like modifier 1	Homo sapiens	56-61
2830255-1	1987	We have shown that the phosphorylation of smooth muscle regulatory myosin light chain (L20) with myosin light chain kinase (MLCK) produces faster moving bands (GMP1: heterodimer myosin with 1 unphosphorylated L20 and 1 mono-phosphorylated L20, GMP2: homodimer myosin with 2 mono-phosphorylated L20S) on native pyrophosphate polyacrylamide gel electrophoresis (PP1 PAGE) (J. Biochem.	diphosphoric acid	310-323	small ubiquitin like modifier 1	Homo sapiens	160-164
2830255-1	1987	We have shown that the phosphorylation of smooth muscle regulatory myosin light chain (L20) with myosin light chain kinase (MLCK) produces faster moving bands (GMP1: heterodimer myosin with 1 unphosphorylated L20 and 1 mono-phosphorylated L20, GMP2: homodimer myosin with 2 mono-phosphorylated L20S) on native pyrophosphate polyacrylamide gel electrophoresis (PP1 PAGE) (J. Biochem.	polyacrylamide	324-338	small ubiquitin like modifier 1	Homo sapiens	160-164
34452288-8	2021	RLS-0071, also known as peptide inhibitor of complement C1 (PIC1), is a 15-amino-acid anti-inflammatory peptide that inhibits classical complement pathway activation and modulates neutrophil activation.	15-amino-acid	72-85	small ubiquitin like modifier 1	Homo sapiens	60-64
34367411-2	2021	We demonstrate that ETV1 can be posttranslationally modified by covalent attachment of small ubiquitin-like modifier 1 (SUMO1) onto four different lysine residues.	Lysine	147-153	small ubiquitin like modifier 1	Homo sapiens	87-118
34367411-2	2021	We demonstrate that ETV1 can be posttranslationally modified by covalent attachment of small ubiquitin-like modifier 1 (SUMO1) onto four different lysine residues.	Lysine	147-153	small ubiquitin like modifier 1	Homo sapiens	120-125
35054494-4	2022	In connection therewith, we emphasize the evaluation of exosomal hypoxamiR expression (miR-27b-3p, miR-92b-3p, miR-181a-5p, and miR-186-5p) using quantitative RT-PCR, as well as SUMO 1-4 and UBC9 (by Western blotting), in pregnant women with early-onset PE.	hypoxamir	65-74	small ubiquitin like modifier 1	Homo sapiens	178-186
35054494-11	2022	In conclusion, the diagnostic potential of exosomal hypoxamiRs mediated by sumoylation may form the basis for the development of combined specific targets for the treatment of early-onset PE, as hnRNPA2/B1 is a target of miR-27b-3p, and its sumoylation creates miR-27b-3p-hnRNPA2/B1-SUMO 1-4 cross-talk.	hypoxamirs	52-62	small ubiquitin like modifier 1	Homo sapiens	283-291
3796586-4	1986	First, the species-dependent factor, designated TFID, bound to the rDNA template, forming a preinitiation complex (PIC-1) which was resistant to a moderate concentration (0.015 to 0.02%) of Sarkosyl.	sarkosyl	190-198	small ubiquitin like modifier 1	Homo sapiens	115-120
33736815-4	2021	Upon trypsin digestion, the SUMO1- and SUMO2/3-modified peptides contained SUMO remnants with 7 and 9 acidic amino acids respectively, which carried more negative charges at high pH and could interact with strong anion exchange (SAX) materials more strongly than non-SUMOylated peptides, thus enabling the specific enrichment of endogenous SUMOylated peptides.	Amino Acids, Acidic	102-120	small ubiquitin like modifier 1	Homo sapiens	28-33
33508304-10	2021	Furthermore, the co-transfection of SUMO1, UBC9 and IGF-1R vectors or the overexpression of SNAI2 reversed the inhibitory effects of GA on cell proliferation, migration and EMT.	ginkgolic acid	133-135	small ubiquitin like modifier 1	Homo sapiens	36-41