PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16096646-0	2005	Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3.	Lysine	54-60	high mobility group nucleosome binding domain 1	Homo sapiens	20-25
20004154-4	2010	High Mobility Group N1 (HMGN1) protein is an emerging factor that is important for chromatin alterations in response to DNA damage originated from both ultra violet light (UV) and ionizing irradiation (IR).	ultra violet	152-164	high mobility group nucleosome binding domain 1	Homo sapiens	24-29
19524541-2	2009	Here we report that purified recombinant human HMGN1 (HMG14) and HMGN2 (HMG17) potently repress ATP-dependent chromatin remodeling by four different molecular motor proteins.	Adenosine Triphosphate	96-99	high mobility group nucleosome binding domain 1	Homo sapiens	47-52
19524541-2	2009	Here we report that purified recombinant human HMGN1 (HMG14) and HMGN2 (HMG17) potently repress ATP-dependent chromatin remodeling by four different molecular motor proteins.	Adenosine Triphosphate	96-99	high mobility group nucleosome binding domain 1	Homo sapiens	54-59
17154547-0	2006	Chromosomal protein HMGN1 modulates the phosphorylation of serine 1 in histone H2A.	Serine	59-65	high mobility group nucleosome binding domain 1	Homo sapiens	20-25
16729963-4	2006	We found that five serine residues, i.e., Ser6, Ser7, Ser85, Ser88, and Ser98, in HMGN1 can be phosphorylated by the kinase in vitro.	Serine	19-25	high mobility group nucleosome binding domain 1	Homo sapiens	82-87
19079244-6	2009	IR treatments lead to a global increase in the acetylation of Lys 14 of histone H3 (H3K14) in an HMGN1-dependent manner and treatment of cells with histone deacetylase inhibitors bypasses the HMGN1 requirement for efficient ATM activation.	Lysine	62-65	high mobility group nucleosome binding domain 1	Homo sapiens	97-102
19079244-6	2009	IR treatments lead to a global increase in the acetylation of Lys 14 of histone H3 (H3K14) in an HMGN1-dependent manner and treatment of cells with histone deacetylase inhibitors bypasses the HMGN1 requirement for efficient ATM activation.	Lysine	62-65	high mobility group nucleosome binding domain 1	Homo sapiens	192-197
1850110-0	1991	Cyclic adenosine 3",5"-monophosphate-dependent phosphorylation of HMG 14 inhibits its interactions with nucleosomes.	Cyclic AMP	0-36	high mobility group nucleosome binding domain 1	Homo sapiens	66-72
15327773-4	2004	During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin.	Anisomycin	7-17	high mobility group nucleosome binding domain 1	Homo sapiens	52-57
15327773-4	2004	During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin.	Anisomycin	7-17	high mobility group nucleosome binding domain 1	Homo sapiens	131-136
15147216-4	2004	To our knowledge, this is the first demonstration that each of the three serine residues in the acidic C-terminal region of human HMGN1 can be phosphorylated.	Serine	73-79	high mobility group nucleosome binding domain 1	Homo sapiens	130-135
15147216-5	2004	The additional negative charge resulting from the phosphorylation of the C-terminal serine residues is expected to modulate the interaction between HMGN1 and other proteins, which may enhance transcription and facilitate other cellular functions.	Serine	84-90	high mobility group nucleosome binding domain 1	Homo sapiens	148-153
10469656-1	1999	The nucleosomal response refers to the rapid phosphorylation of histone H3 on serine 10 and HMG-14 on serine 6 that occurs concomitantly with immediate-early (IE) gene induction in response to a wide variety of stimuli.	Serine	102-108	high mobility group nucleosome binding domain 1	Homo sapiens	92-98
8805335-4	1996	By using the p38/RK inhibitor SB 203580 [20,21], we show that activation of p38/RK and/or its downstream effectors are essential for anisomycin- and UV-stimulated c-fos/c-jun induction and histone H3/HMG-14 phosphorylation, whereas JNK/SAPK activation and phosphorylation of c-Jun and ATF-2 are insufficient for these responses.	SB 203580	30-39	high mobility group nucleosome binding domain 1	Homo sapiens	200-206
8805335-4	1996	By using the p38/RK inhibitor SB 203580 [20,21], we show that activation of p38/RK and/or its downstream effectors are essential for anisomycin- and UV-stimulated c-fos/c-jun induction and histone H3/HMG-14 phosphorylation, whereas JNK/SAPK activation and phosphorylation of c-Jun and ATF-2 are insufficient for these responses.	Anisomycin	133-143	high mobility group nucleosome binding domain 1	Homo sapiens	200-206
7925294-0	1994	A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes.	Anisomycin	15-25	high mobility group nucleosome binding domain 1	Homo sapiens	59-65
7925294-3	1994	Here, we show that upon IE gene induction, the non-histone high-mobility-group protein HMG-14, but not the related protein HMG-17, becomes serine phosphorylated in its basic, amino-terminal region close to where it binds nucleosomal DNA.	Serine	139-145	high mobility group nucleosome binding domain 1	Homo sapiens	87-93
8496248-5	1993	Consistent with previous reports by Bustin and co-workers [Crippa et al., 1990], HMG 14 and HMG 17 are expressed in proliferating HL-60 promyelocytic leukemia cells and downregulated post-proliferatively following phorbol ester-induced monocytic differentiation.	Phorbol Esters	214-227	high mobility group nucleosome binding domain 1	Homo sapiens	81-87
1321148-5	1992	Nobotanin B caused concentration-dependent inhibition of glucocorticoid-induced de-poly(ADP-ribosyl)ation of HMG 14 and 17 and histone H1 in intact 34I cells.	nobotanin B	0-11	high mobility group nucleosome binding domain 1	Homo sapiens	109-115
1852620-0	1991	Dinucleotide repeat polymorphism at the human non-histone chromosomal protein HMG14 gene.	Dinucleoside Phosphates	0-12	high mobility group nucleosome binding domain 1	Homo sapiens	78-83
1847050-0	1991	HMG 14 and protamine enhance ligation of linear DNA to form linear multimers: phosphorylation of HMG 14 at Ser 20 specifically inhibits intermolecular DNA ligation.	Serine	107-110	high mobility group nucleosome binding domain 1	Homo sapiens	0-6
8107104-1	1994	The position of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores and in chromatosomes lacking linker histones has been mapped by hydroxyl radical footprinting.	Hydroxyl Radical	139-155	high mobility group nucleosome binding domain 1	Homo sapiens	37-43
8514795-5	1993	Induction of human HMG-14 expression by dexamethasone inhibited the myogenic process.	Dexamethasone	40-53	high mobility group nucleosome binding domain 1	Homo sapiens	19-25
8478937-2	1993	The first involves the addition of phosphorylated HMG-14,17 to the histone octamer plus DNA in high concentrations of salt and yields a repeating particle size or spacing of about 165 base-pairs.	Salts	118-122	high mobility group nucleosome binding domain 1	Homo sapiens	50-56
1850110-2	1991	In the thyroid, HMG 14 displays TSH-dependent phosphorylation that is mediated by cAMP-dependent protein kinase (A-kinase).	Thyrotropin	32-35	high mobility group nucleosome binding domain 1	Homo sapiens	16-22
1850110-2	1991	In the thyroid, HMG 14 displays TSH-dependent phosphorylation that is mediated by cAMP-dependent protein kinase (A-kinase).	Cyclic AMP	82-86	high mobility group nucleosome binding domain 1	Homo sapiens	16-22
1850110-3	1991	We have, therefore, studied how phosphorylation of HMG 14 on its major and minor A-kinase sites (Ser-6 and -24) affects its interactions with nucleosomes and various forms of DNA, since this could reflect a means of regulating its function of binding to active chromatin.	Serine	97-100	high mobility group nucleosome binding domain 1	Homo sapiens	51-57
1850110-4	1991	Approximately twice as much Ser-6 phospho- and 4 times as much Ser-6,24 diphospho-HMG 14 were required to produce the same degree of nucleosome band displacement as that caused by native unphosphorylated HMG 14.	Serine	28-31	high mobility group nucleosome binding domain 1	Homo sapiens	204-210
1850110-4	1991	Approximately twice as much Ser-6 phospho- and 4 times as much Ser-6,24 diphospho-HMG 14 were required to produce the same degree of nucleosome band displacement as that caused by native unphosphorylated HMG 14.	Serine	63-66	high mobility group nucleosome binding domain 1	Homo sapiens	82-88
1850110-4	1991	Approximately twice as much Ser-6 phospho- and 4 times as much Ser-6,24 diphospho-HMG 14 were required to produce the same degree of nucleosome band displacement as that caused by native unphosphorylated HMG 14.	Serine	63-66	high mobility group nucleosome binding domain 1	Homo sapiens	204-210
1850110-4	1991	Approximately twice as much Ser-6 phospho- and 4 times as much Ser-6,24 diphospho-HMG 14 were required to produce the same degree of nucleosome band displacement as that caused by native unphosphorylated HMG 14.	diphospho	72-81	high mobility group nucleosome binding domain 1	Homo sapiens	82-88
1850110-6	1991	When the electrophoretic mobility of naked DNA was examined, the Ser-6 phospho-HMG 14 was about half as effective as native HMG 14 in retarding the various forms of double stranded DNA, and Ser-6,24 diphospho-HMG 14 was even less effective.	Serine	65-68	high mobility group nucleosome binding domain 1	Homo sapiens	79-85
1850110-6	1991	When the electrophoretic mobility of naked DNA was examined, the Ser-6 phospho-HMG 14 was about half as effective as native HMG 14 in retarding the various forms of double stranded DNA, and Ser-6,24 diphospho-HMG 14 was even less effective.	Serine	65-68	high mobility group nucleosome binding domain 1	Homo sapiens	124-130
1850110-6	1991	When the electrophoretic mobility of naked DNA was examined, the Ser-6 phospho-HMG 14 was about half as effective as native HMG 14 in retarding the various forms of double stranded DNA, and Ser-6,24 diphospho-HMG 14 was even less effective.	Serine	65-68	high mobility group nucleosome binding domain 1	Homo sapiens	124-130
1850110-6	1991	When the electrophoretic mobility of naked DNA was examined, the Ser-6 phospho-HMG 14 was about half as effective as native HMG 14 in retarding the various forms of double stranded DNA, and Ser-6,24 diphospho-HMG 14 was even less effective.	Serine	190-193	high mobility group nucleosome binding domain 1	Homo sapiens	79-85
1850110-6	1991	When the electrophoretic mobility of naked DNA was examined, the Ser-6 phospho-HMG 14 was about half as effective as native HMG 14 in retarding the various forms of double stranded DNA, and Ser-6,24 diphospho-HMG 14 was even less effective.	Serine	190-193	high mobility group nucleosome binding domain 1	Homo sapiens	124-130
1850110-6	1991	When the electrophoretic mobility of naked DNA was examined, the Ser-6 phospho-HMG 14 was about half as effective as native HMG 14 in retarding the various forms of double stranded DNA, and Ser-6,24 diphospho-HMG 14 was even less effective.	Serine	190-193	high mobility group nucleosome binding domain 1	Homo sapiens	124-130
2563381-3	1989	To identify and isolate a functional human HMG-14 gene, genomic clones, selected with the cDNA, were screened with a set of 6 oligonucleotides.	Oligonucleotides	126-142	high mobility group nucleosome binding domain 1	Homo sapiens	43-49
1847050-0	1991	HMG 14 and protamine enhance ligation of linear DNA to form linear multimers: phosphorylation of HMG 14 at Ser 20 specifically inhibits intermolecular DNA ligation.	Serine	107-110	high mobility group nucleosome binding domain 1	Homo sapiens	97-103
1847050-5	1991	Phosphorylation of HMG 14 at Ser 20 by Ca(++)-phospholipid dependent protein kinase abolished the ability of HMG 14 to stimulate intermolecular ligation, but did not substantially interfere with intramolecular ligation, or the binding of HMG 14 to linear or circular DNA as assessed by gel mobility.	Serine	29-32	high mobility group nucleosome binding domain 1	Homo sapiens	19-25
1847050-5	1991	Phosphorylation of HMG 14 at Ser 20 by Ca(++)-phospholipid dependent protein kinase abolished the ability of HMG 14 to stimulate intermolecular ligation, but did not substantially interfere with intramolecular ligation, or the binding of HMG 14 to linear or circular DNA as assessed by gel mobility.	Serine	29-32	high mobility group nucleosome binding domain 1	Homo sapiens	109-115
1847050-5	1991	Phosphorylation of HMG 14 at Ser 20 by Ca(++)-phospholipid dependent protein kinase abolished the ability of HMG 14 to stimulate intermolecular ligation, but did not substantially interfere with intramolecular ligation, or the binding of HMG 14 to linear or circular DNA as assessed by gel mobility.	Serine	29-32	high mobility group nucleosome binding domain 1	Homo sapiens	109-115
1847050-6	1991	Thus Ser 20, which is located in the amino terminal DNA-binding domain of HMG 14, appears to modulate DNA-DNA interactions.	Serine	5-8	high mobility group nucleosome binding domain 1	Homo sapiens	74-80
1970797-0	1990	Linkage analysis of the human HMG14 gene on chromosome 21 using a GT dinucleotide repeat as polymorphic marker.	Dinucleoside Phosphates	69-81	high mobility group nucleosome binding domain 1	Homo sapiens	30-35
3676353-1	1987	Chromosomal high-mobility-group (HMG) proteins have been examined as substrates for calcium/phospholipid-dependent protein kinase C. Protein kinase C from rat brain phosphorylated efficiently both HMG 14 and HMG 17 derived from calf thymus and the reactions were calcium/phospholipid-dependent.	Calcium	84-91	high mobility group nucleosome binding domain 1	Homo sapiens	197-203
3805203-3	1986	The blue Sepharose column separates HMG I and Y completely from HMG 14 and 17, and should therefore be an useful tool for the identification of these proteins which in several reports have been confused with HMG 14 and 17.	Sepharose	9-18	high mobility group nucleosome binding domain 1	Homo sapiens	64-70
3676353-2	1987	About 1 mol of 32P was incorporated per mol of HMG 14 and HMG 17.	Phosphorus-32	15-18	high mobility group nucleosome binding domain 1	Homo sapiens	47-53
3676353-6	1987	HMG 14 and HMG 17 from transformed human lymphoblasts (Wi-L2) were also phosphorylated in a calcium/phospholipid-dependent manner.	Calcium	92-99	high mobility group nucleosome binding domain 1	Homo sapiens	0-6
3676353-6	1987	HMG 14 and HMG 17 from transformed human lymphoblasts (Wi-L2) were also phosphorylated in a calcium/phospholipid-dependent manner.	Phospholipids	100-112	high mobility group nucleosome binding domain 1	Homo sapiens	0-6
3805203-3	1986	The blue Sepharose column separates HMG I and Y completely from HMG 14 and 17, and should therefore be an useful tool for the identification of these proteins which in several reports have been confused with HMG 14 and 17.	Sepharose	9-18	high mobility group nucleosome binding domain 1	Homo sapiens	208-214
3805203-4	1986	HMG I and Y on the one hand and HMG 14 and 17 on the other exhibited considerable differences in their affinities for Blue Sepharose, probably reflecting fundamental differences in biological function.	Sepharose	123-132	high mobility group nucleosome binding domain 1	Homo sapiens	32-38
4022776-3	1985	Core histone-HMG crosslinking with succinimidyl propionate yields dense HMG 14 in uniformly dense particles and new HMG 17 crosslinked to both dense and light protein, implying that HMG 14 and 17 each deposit nonrandomly; but differently with respect to new core octamers.	N-succinimidyl propionate	35-58	high mobility group nucleosome binding domain 1	Homo sapiens	72-78
2426323-1	1986	A method is presented for sensitive staining of the HMG14 and 17 proteins in polyacrylamide gels pre-stained with Coomassie Blue R250.	polyacrylamide	77-91	high mobility group nucleosome binding domain 1	Homo sapiens	52-57
2426323-1	1986	A method is presented for sensitive staining of the HMG14 and 17 proteins in polyacrylamide gels pre-stained with Coomassie Blue R250.	Coomassie brilliant blue R	114-133	high mobility group nucleosome binding domain 1	Homo sapiens	52-57
3711048-2	1986	Analysis of HMG proteins and histone H1 by acetic acid/urea polyacrylamide gel electrophoresis demonstrated that the (ADP-ribosyl)n-ation of HMG 14 and 17 and histone H1 increased by 12- and 5-fold, respectively, in the metaphase chromosomes as compared with that in the G1 phase cell nuclei.	Acetic Acid	43-54	high mobility group nucleosome binding domain 1	Homo sapiens	141-147
3711048-2	1986	Analysis of HMG proteins and histone H1 by acetic acid/urea polyacrylamide gel electrophoresis demonstrated that the (ADP-ribosyl)n-ation of HMG 14 and 17 and histone H1 increased by 12- and 5-fold, respectively, in the metaphase chromosomes as compared with that in the G1 phase cell nuclei.	Urea	55-59	high mobility group nucleosome binding domain 1	Homo sapiens	141-147
3711048-2	1986	Analysis of HMG proteins and histone H1 by acetic acid/urea polyacrylamide gel electrophoresis demonstrated that the (ADP-ribosyl)n-ation of HMG 14 and 17 and histone H1 increased by 12- and 5-fold, respectively, in the metaphase chromosomes as compared with that in the G1 phase cell nuclei.	polyacrylamide	60-74	high mobility group nucleosome binding domain 1	Homo sapiens	141-147
3711048-2	1986	Analysis of HMG proteins and histone H1 by acetic acid/urea polyacrylamide gel electrophoresis demonstrated that the (ADP-ribosyl)n-ation of HMG 14 and 17 and histone H1 increased by 12- and 5-fold, respectively, in the metaphase chromosomes as compared with that in the G1 phase cell nuclei.	(adp-ribosyl)n-ation	117-137	high mobility group nucleosome binding domain 1	Homo sapiens	141-147
3711048-4	1986	In the G2 phase cell nuclei, the degrees of (ADP-ribosyl)n-ation of HMG 14 and 17 and histone H1 were about 5- and 2-fold greater, respectively, as compared with that in the G1 phase cell nuclei.	(adp-ribosyl)n	44-58	high mobility group nucleosome binding domain 1	Homo sapiens	68-74
3711048-6	1986	The data may imply that the (ADP-ribosyl)n-ation of HMG 14 and 17 and histone H1 is linked to chromatin structural changes in mitosis.	(adp-ribosyl)n-ation	28-48	high mobility group nucleosome binding domain 1	Homo sapiens	52-58
4022776-3	1985	Core histone-HMG crosslinking with succinimidyl propionate yields dense HMG 14 in uniformly dense particles and new HMG 17 crosslinked to both dense and light protein, implying that HMG 14 and 17 each deposit nonrandomly; but differently with respect to new core octamers.	N-succinimidyl propionate	35-58	high mobility group nucleosome binding domain 1	Homo sapiens	182-188
4022776-4	1985	Propionimidate crosslinking yields dense H1-HMG 17 dimers, suggesting that the interactions of new 14/17 with H1 (new HMG 14-old H1, new HMG 17-new H1) are reciprocal to their interactions with the core histones.	propionimidate	0-14	high mobility group nucleosome binding domain 1	Homo sapiens	118-124
2982675-5	1985	Several chromatin proteins are susceptible to cAMP-dependent phosphorylation in vivo, including histones H1 and H3, the high mobility group protein HMG 14 (which is preferentially associated with actively transcribed chromatin), and at least three other basic nonhistone proteins.	Cyclic AMP	46-50	high mobility group nucleosome binding domain 1	Homo sapiens	148-154
4025809-4	1985	The identity and purity of these HMG-14 and -17 protein species were assayed by polyacrylamide gel electrophoresis and amino acid analysis.	polyacrylamide	80-94	high mobility group nucleosome binding domain 1	Homo sapiens	33-47
6238036-7	1984	Preliminary evidence has indicated that lamb thymus HMG 14 is also a substrate for the Ca2+-phospholipid-dependent enzyme.	Phospholipids	92-104	high mobility group nucleosome binding domain 1	Homo sapiens	52-58
6317693-3	1983	It was observed that glucocorticoids quickly decreased endogenous (ADP-ribose)n on the nonhistone high mobility group (HMG) 14 and 17 proteins.	(adp-ribose)n	66-79	high mobility group nucleosome binding domain 1	Homo sapiens	98-126
6317693-8	1983	3-Amino-benzamide, a specific inhibitor of (ADP-ribose)n synthetase, increased mouse mammary tumor virus RNA levels with an accompanying decrease in endogenous ADP-ribosylation of HMG 14 and 17.	3-aminobenzamide	0-17	high mobility group nucleosome binding domain 1	Homo sapiens	180-186
6317693-3	1983	It was observed that glucocorticoids quickly decreased endogenous (ADP-ribose)n on the nonhistone high mobility group (HMG) 14 and 17 proteins.	nonhistone	87-97	high mobility group nucleosome binding domain 1	Homo sapiens	98-126
6317693-6	1983	The rapid loss of (ADP-ribose)n from HMG 14 and 17 occurred in the same time frame as the induction of mouse mammary tumor virus RNA synthesis by glucocorticoids in these cells (Young, H. A., Shih, T. Y., Scolnick, E. M., and Parks, W. P. (1977) J. Virol.	Ribose	23-29	high mobility group nucleosome binding domain 1	Homo sapiens	37-43
6317693-9	1983	These results show that a decrease in endogenous ADP-ribosylation of HMG 14 and 17 is a consequence of glucocorticoid action and suggest that loss of (ADP-ribose)n from these proteins may be an important event in mouse mammary tumor virus gene expression.	Adenosine Diphosphate	49-52	high mobility group nucleosome binding domain 1	Homo sapiens	69-75
6226664-6	1983	Thermal denaturation and circular dichroism show a dramatic reversal of the effects of urea on nucleosomes when HMG 14 or 17 is bound, indicating stabilization of the nucleosome by HMG proteins.	Urea	87-91	high mobility group nucleosome binding domain 1	Homo sapiens	112-118
6220712-10	1983	Furthermore, HMG 14 is resolved into multiple electrophoretic forms as phosphoprotein in the acid-urea system.	Urea	98-102	high mobility group nucleosome binding domain 1	Homo sapiens	13-19
6860668-3	1983	TSH-dependent increases in labeling of histones H1 and H3, and of the high mobility group protein HMG 14, were observed at 2 h; however, there were no apparent changes in TSH-dependent labeling between 2 and 5 h, in nuclease-sensitive or in bulk chromatin.	Thyrotropin	0-3	high mobility group nucleosome binding domain 1	Homo sapiens	98-104
6460611-0	1982	TSH stimulates 32P-labeling of thyroid nuclear HMG 14, a protein associated with actively transcribed chromatin.	Thyrotropin	0-3	high mobility group nucleosome binding domain 1	Homo sapiens	47-53
6281254-9	1982	HMG 14 is phosphorylated both at serine and threonine residues.	Serine	33-39	high mobility group nucleosome binding domain 1	Homo sapiens	0-6
6281254-9	1982	HMG 14 is phosphorylated both at serine and threonine residues.	Threonine	44-53	high mobility group nucleosome binding domain 1	Homo sapiens	0-6
6279643-3	1982	One mol of 32P was incorporated/mol of HMG 14.	Phosphorus-32	11-14	high mobility group nucleosome binding domain 1	Homo sapiens	39-45
6279643-5	1982	Tryptic maps of 32P-labeled phosphopeptides of HMG 14 demonstrated phosphorylation of the same site by both enzymes.	Phosphorus-32	16-19	high mobility group nucleosome binding domain 1	Homo sapiens	47-53
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	h-lys-val	144-153	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Serine	154-157	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Serine	161-164	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Alanine	165-168	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Glutamic Acid	169-172	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Glycine	173-176	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Alanine	177-180	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	Alanine	177-180	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-6	1982	The tryptic fragment containing the major phosphorylation site was identified by amino acid composition and sequence as HMG 14 (residues 4-13): H-Lys-Val-Ser(P)-Ser-Ala-Glu-Gly-Ala-Ala-Lys-OH.	lys-oh	185-191	high mobility group nucleosome binding domain 1	Homo sapiens	120-126
6279643-9	1982	On the basis of amino acid composition, the tryptic peptides carrying the minor phosphorylation sites were identified as H-Leu-Ser(P)-Ala-Lys representing residues 23-26 and 27-30 of HMG 14 and HMG 17, respectively.	Peptides	52-60	high mobility group nucleosome binding domain 1	Homo sapiens	183-189
6279643-9	1982	On the basis of amino acid composition, the tryptic peptides carrying the minor phosphorylation sites were identified as H-Leu-Ser(P)-Ala-Lys representing residues 23-26 and 27-30 of HMG 14 and HMG 17, respectively.	Leucine	121-126	high mobility group nucleosome binding domain 1	Homo sapiens	183-189
6279643-9	1982	On the basis of amino acid composition, the tryptic peptides carrying the minor phosphorylation sites were identified as H-Leu-Ser(P)-Ala-Lys representing residues 23-26 and 27-30 of HMG 14 and HMG 17, respectively.	Serine	127-130	high mobility group nucleosome binding domain 1	Homo sapiens	183-189
6279643-9	1982	On the basis of amino acid composition, the tryptic peptides carrying the minor phosphorylation sites were identified as H-Leu-Ser(P)-Ala-Lys representing residues 23-26 and 27-30 of HMG 14 and HMG 17, respectively.	Alanine	134-137	high mobility group nucleosome binding domain 1	Homo sapiens	183-189
6279643-9	1982	On the basis of amino acid composition, the tryptic peptides carrying the minor phosphorylation sites were identified as H-Leu-Ser(P)-Ala-Lys representing residues 23-26 and 27-30 of HMG 14 and HMG 17, respectively.	Lysine	138-141	high mobility group nucleosome binding domain 1	Homo sapiens	183-189
6460611-0	1982	TSH stimulates 32P-labeling of thyroid nuclear HMG 14, a protein associated with actively transcribed chromatin.	Phosphorus-32	15-18	high mobility group nucleosome binding domain 1	Homo sapiens	47-53
6460611-3	1982	We found that TSH enhanced the labeling of the high mobility group protein HMG 14, a protein that is preferentially associated with actively transcribed chromatin.	Thyrotropin	14-17	high mobility group nucleosome binding domain 1	Homo sapiens	75-81
6460611-4	1982	This observation suggests that changes in HMG 14 phosphorylation may be involved in mediating TSH-induced effects on the structure and function of active chromatin.	Thyrotropin	94-97	high mobility group nucleosome binding domain 1	Homo sapiens	42-48
6458819-4	1981	However, the most significant finding is that there is a 7-fold increase of 32P incorporation into HMG 14 in the G2 phase compared with that in G1, and a 2-fold increase of 32P incorporation into HMG 17 in early S phase relative to the incorporation in the G1 and G2 stages.	Phosphorus-32	76-79	high mobility group nucleosome binding domain 1	Homo sapiens	99-105
6455433-5	1981	Furthermore, automated Edman degradation of intact 3H-labeled HMG-14 and HMG-17 identified the specific sites of acetylation of these proteins.	Tritium	51-53	high mobility group nucleosome binding domain 1	Homo sapiens	62-68
6455433-7	1981	However, one additional site in HMG-14 and two additional sites in HMG-17 were found in the proteins from cells incubated in butyrate.	Butyrates	125-133	high mobility group nucleosome binding domain 1	Homo sapiens	32-38
6455433-8	1981	Finally, studies of the enzymatic deacetylation of HMG-14 and HMG-17 confirmed that both nuclear proteins serve as deacetylase substrates and that butyrate inhibits their deacetylation, just as in the case of other HMG proteins and nucleosomal core histones.	Butyrates	147-155	high mobility group nucleosome binding domain 1	Homo sapiens	51-57
6454141-4	1981	The multiple band pattern of HMG-14 and -17 from butyrate-treated cells results from hyperphosphorylation rather than hyperacetylation.	Butyrates	49-57	high mobility group nucleosome binding domain 1	Homo sapiens	29-35
6217209-8	1983	However, in the course of these experiments we did find that HMG 14 and 17 proteins covalently linked to carbohydrate side chains bind preferentially to the nuclear protein matrix of mammalian cells.	Carbohydrates	105-117	high mobility group nucleosome binding domain 1	Homo sapiens	61-67
6448865-0	1980	Quantitative analysis of non-histone chromosomal proteins HMG 14 and HMG 17 by polyacrylamide gel electrophoresis.	polyacrylamide	79-93	high mobility group nucleosome binding domain 1	Homo sapiens	58-64