PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 37-47 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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