dbPTM

HMGN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGN1_MOUSE
UniProt AC	P18608
Protein Name	Non-histone chromosomal protein HMG-14
Gene Name	Hmgn1
Organism	Mus musculus (Mouse).
Sequence Length	96
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasmic enrichment upon phosphorylation..
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..
Protein Sequence	MPKRKVSADGAAKAEPKRRSARLSAKPAPAKVDAKPKKAAGKDKASDKKVQIKGKRGAKGKQADVADQQTTELPAENGETENQSPASEEEKEAKSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MPKRKVSADGAAKA -CCCCCCCCCCCCCC	24.55	27087446
13	Acetylation	VSADGAAKAEPKRRS CCCCCCCCCCCCHHH	53.39	23806337
13	Malonylation	VSADGAAKAEPKRRS CCCCCCCCCCCCHHH	53.39	26320211
20	Phosphorylation	KAEPKRRSARLSAKP CCCCCHHHHHHCCCC	23.05	26824392
24	ADP-ribosylation	KRRSARLSAKPAPAK CHHHHHHCCCCCCCC	28.79	-
24	Phosphorylation	KRRSARLSAKPAPAK CHHHHHHCCCCCCCC	28.79	26824392
26	Ubiquitination	RSARLSAKPAPAKVD HHHHHCCCCCCCCCC	38.03	-
26	Acetylation	RSARLSAKPAPAKVD HHHHHCCCCCCCCCC	38.03	23806337
31	Ubiquitination	SAKPAPAKVDAKPKK CCCCCCCCCCCCCCH	39.32	-
31	Malonylation	SAKPAPAKVDAKPKK CCCCCCCCCCCCCCH	39.32	26320211
61	Ubiquitination	GKRGAKGKQADVADQ CCCCCCCCCCCCCCC	41.42	-
70	Phosphorylation	ADVADQQTTELPAEN CCCCCCCCCCCCCCC	19.32	25619855
71	Phosphorylation	DVADQQTTELPAENG CCCCCCCCCCCCCCC	31.05	22942356
80	Phosphorylation	LPAENGETENQSPAS CCCCCCCCCCCCCCC	41.45	27087446
84	Phosphorylation	NGETENQSPASEEEK CCCCCCCCCCCHHHH	33.73	27087446
87	Phosphorylation	TENQSPASEEEKEAK CCCCCCCCHHHHHHH	49.26	27087446
91	Ubiquitination	SPASEEEKEAKSD-- CCCCHHHHHHHCC--	67.27	-
94	Ubiquitination	SEEEKEAKSD----- CHHHHHHHCC-----	57.14	-
95	Phosphorylation	EEEKEAKSD------ HHHHHHHCC------	56.45	27087446

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	RPS6KA1	P18653	GPS
7	S	Phosphorylation	Kinase	RPS6KA3	P18654	GPS
7	S	Phosphorylation	Kinase	MSK1	Q8C050	PSP
20	S	Phosphorylation	Kinase	MSK1	Q8C050	PSP
24	S	Phosphorylation	Kinase	RPS6KA5	Q8C050	GPS
24	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
20	S	Phosphorylation	15327773
Phosphorylation on Ser-20 and Ser-24 weakens binding to nucleosomes and increases the rate of H3 phosphorylation.
24	S	Phosphorylation	15327773
Phosphorylation on Ser-20 and Ser-24 weakens binding to nucleosomes and increases the rate of H3 phosphorylation.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HMGN1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of HMGN1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-87, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-80; SER-84; SER-87 ANDSER-95, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Chromosomal protein HMGN1 modulates histone H3 phosphorylation."; Lim J.-H., Catez F., Birger Y., West K.L., Prymakowska-Bosak M.,Postnikov Y.V., Bustin M.; Mol. Cell 15:573-584(2004). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-7; SER-20 AND SER-24.	15327773 [Abstract]
"A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 inits basic amino-terminal domain in vivo and on isolatedmononucleosomes."; Barratt M.J., Hazzalin C.A., Zhelev N., Mahadevan L.C.; EMBO J. 13:4524-4535(1994). Cited for: PHOSPHORYLATION AT SER-7.	7925294 [Abstract]