dbPTM

HMGN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGN1_HUMAN
UniProt AC	P05114
Protein Name	Non-histone chromosomal protein HMG-14
Gene Name	HMGN1
Organism	Homo sapiens (Human).
Sequence Length	100
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasmic enrichment upon phosphorylation. The RNA edited version localizes to the nucleus.
Protein Description	Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity)..
Protein Sequence	MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MPKRKVSSAE -----CCCCCCCCCC	64.65	10753971
5	Methylation	---MPKRKVSSAEGA ---CCCCCCCCCCCC	53.23	59707
5	Acetylation	---MPKRKVSSAEGA ---CCCCCCCCCCCC	53.23	59707
5	Ubiquitination	---MPKRKVSSAEGA ---CCCCCCCCCCCC	53.23	-
7	Phosphorylation	-MPKRKVSSAEGAAK -CCCCCCCCCCCCCC	27.19	23927012
7	ADP-ribosylation	-MPKRKVSSAEGAAK -CCCCCCCCCCCCCC	27.19	28190768
8	Phosphorylation	MPKRKVSSAEGAAKE CCCCCCCCCCCCCCC	33.07	19664994
14	Acetylation	SSAEGAAKEEPKRRS CCCCCCCCCCCCHHH	63.17	19608861
14	Ubiquitination	SSAEGAAKEEPKRRS CCCCCCCCCCCCHHH	63.17	10753971
18	Acetylation	GAAKEEPKRRSARLS CCCCCCCCHHHHHHC	64.82	10753971
21	Phosphorylation	KEEPKRRSARLSAKP CCCCCHHHHHHCCCC	23.05	25159151
25	Phosphorylation	KRRSARLSAKPPAKV CHHHHHHCCCCCCCC	28.79	30266825
25	ADP-ribosylation	KRRSARLSAKPPAKV CHHHHHHCCCCCCCC	28.79	28190768
27	Acetylation	RSARLSAKPPAKVEA HHHHHCCCCCCCCCC	48.43	23749302
27	Ubiquitination	RSARLSAKPPAKVEA HHHHHCCCCCCCCCC	48.43	-
31	Ubiquitination	LSAKPPAKVEAKPKK HCCCCCCCCCCCCCC	46.51	10753971
31	Acetylation	LSAKPPAKVEAKPKK HCCCCCCCCCCCCCC	46.51	23236377
35	Acetylation	PPAKVEAKPKKAAAK CCCCCCCCCCCHHHC	43.81	26051181
38	Acetylation	KVEAKPKKAAAKDKS CCCCCCCCHHHCCCC	52.35	10753971
42	Acetylation	KPKKAAAKDKSSDKK CCCCHHHCCCCCCCC	62.05	10753971
48	Acetylation	AKDKSSDKKVQTKGK HCCCCCCCCHHCCCH	57.71	10753971
53	Acetylation	SDKKVQTKGKRGAKG CCCCHHCCCHHCCCC	45.39	10753971
55	Acetylation	KKVQTKGKRGAKGKQ CCHHCCCHHCCCCHH	49.57	10753971
59	Acetylation	TKGKRGAKGKQAEVA CCCHHCCCCHHHHHC	70.26	20167786
61	Acetylation	GKRGAKGKQAEVANQ CHHCCCCHHHHHCCH	45.70	20167786
61	Ubiquitination	GKRGAKGKQAEVANQ CHHCCCCHHHHHCCH	45.70	10753971
70	Phosphorylation	AEVANQETKEDLPAE HHHCCHHHHHCCCCC	29.94	21082442
71	Ubiquitination	EVANQETKEDLPAEN HHCCHHHHHCCCCCC	48.77	21906983
71	Acetylation	EVANQETKEDLPAEN HHCCHHHHHCCCCCC	48.77	26051181
81	Phosphorylation	LPAENGETKTEESPA CCCCCCCCCCCCCCC	44.67	26503892
82	Ubiquitination	PAENGETKTEESPAS CCCCCCCCCCCCCCC	50.03	10753971
82	Acetylation	PAENGETKTEESPAS CCCCCCCCCCCCCCC	50.03	19608861
83	Phosphorylation	AENGETKTEESPASD CCCCCCCCCCCCCCH	53.02	25159151
86	Phosphorylation	GETKTEESPASDEAG CCCCCCCCCCCHHHH	21.38	29255136
89	Phosphorylation	KTEESPASDEAGEKE CCCCCCCCHHHHHHH	39.09	29255136
95	Ubiquitination	ASDEAGEKEAKSD-- CCHHHHHHHHHCC--	63.15	21906983
95	Acetylation	ASDEAGEKEAKSD-- CCHHHHHHHHHCC--	63.15	25953088
98	Ubiquitination	EAGEKEAKSD----- HHHHHHHHCC-----	57.14	-
99	Phosphorylation	AGEKEAKSD------ HHHHHHHCC------	56.45	23401153

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
7	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
8	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
21	S	Phosphorylation	Kinase	RPS6KA5	O75582	Uniprot
21	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
21	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
21	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
21	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
25	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
25	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
25	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
25	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
25	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
25	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
86	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
89	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
99	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
21	S	Phosphorylation	10739259
Phosphorylation on Ser-21 and Ser-25 weakens binding to nucleosomes and increases the rate of H3 phosphorylation (By similarity).
25	S	Phosphorylation	10739259
Phosphorylation on Ser-21 and Ser-25 weakens binding to nucleosomes and increases the rate of H3 phosphorylation (By similarity).

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HMGN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433Z_HUMAN	YWHAZ	physical	12215538
HMGN1_HUMAN	HMGN1	physical	7563062
NFE2_HUMAN	NFE2	physical	20211142
VIP1_HUMAN	PPIP5K1	physical	22939629
S38A3_HUMAN	SLC38A3	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HMGN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-82, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-89 AND SER-99,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-86 AND SER-89,AND MASS SPECTROMETRY.	15302935 [Abstract]
"Phosphorylation and subcellular redistribution of high mobility groupproteins 14 and 17, analyzed by mass spectrometry."; Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., Ahn N.G.; Protein Sci. 9:170-179(2000). Cited for: PROTEIN SEQUENCE OF 19-31, PHOSPHORYLATION AT SER-21 AND SER-25,SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.	10739259 [Abstract]

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