dbPTM

HMGA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGA1_MOUSE
UniProt AC	P17095
Protein Name	High mobility group protein HMG-I/HMG-Y
Gene Name	Hmga1
Organism	Mus musculus (Mouse).
Sequence Length	107
Subcellular Localization	Nucleus. Chromosome.
Protein Description	HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions..
Protein Sequence	MSESGSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKVTTAPGRKPRGRPKKLEKEEEEGISQESSEEEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSESGSKSS ------CCCCCCCCC	40.23	23527152
2	Acetylation	------MSESGSKSS ------CCCCCCCCC	40.23	23806337
4	Phosphorylation	----MSESGSKSSQP ----CCCCCCCCCCC	40.85	25619855
6	Phosphorylation	--MSESGSKSSQPLA --CCCCCCCCCCCCC	38.35	27742792
7	Acetylation	-MSESGSKSSQPLAS -CCCCCCCCCCCCCC	58.62	23806337
7	Ubiquitination	-MSESGSKSSQPLAS -CCCCCCCCCCCCCC	58.62	-
7	Malonylation	-MSESGSKSSQPLAS -CCCCCCCCCCCCCC	58.62	26320211
7	Succinylation	-MSESGSKSSQPLAS -CCCCCCCCCCCCCC	58.62	-
8	ADP-ribosylation	MSESGSKSSQPLASK CCCCCCCCCCCCCCH	35.58	-
8	Phosphorylation	MSESGSKSSQPLASK CCCCCCCCCCCCCCH	35.58	27087446
9	Phosphorylation	SESGSKSSQPLASKQ CCCCCCCCCCCCCHH	39.28	27087446
9	ADP-ribosylation	SESGSKSSQPLASKQ CCCCCCCCCCCCCHH	39.28	-
14	Phosphorylation	KSSQPLASKQEKDGT CCCCCCCCHHCCCCC	42.42	25619855
15	Acetylation	SSQPLASKQEKDGTE CCCCCCCHHCCCCCC	57.79	23806337
26	Asymmetric dimethylarginine	DGTEKRGRGRPRKQP CCCCCCCCCCCCCCC	41.82	-
26	Methylation	DGTEKRGRGRPRKQP CCCCCCCCCCCCCCC	41.82	-
31	Acetylation	RGRGRPRKQPPVSPG CCCCCCCCCCCCCCC	70.60	23806337
36	Phosphorylation	PRKQPPVSPGTALVG CCCCCCCCCCCCCCC	24.32	25521595
38 (in isoform 1)	Phosphorylation	-	19.00	25159016
39	Phosphorylation	QPPVSPGTALVGSQK CCCCCCCCCCCCCCC	21.87	25521595
42 (in isoform 1)	Phosphorylation	-	6.86	26824392
44	Phosphorylation	PGTALVGSQKEPSEV CCCCCCCCCCCCCCC	30.51	17525332
46	Acetylation	TALVGSQKEPSEVPT CCCCCCCCCCCCCCC	73.60	23806337
46	Ubiquitination	TALVGSQKEPSEVPT CCCCCCCCCCCCCCC	73.60	-
49	Phosphorylation	VGSQKEPSEVPTPKR CCCCCCCCCCCCCCC	52.93	11593421
53	Phosphorylation	KEPSEVPTPKRPRGR CCCCCCCCCCCCCCC	46.77	27087446
58	Methylation	VPTPKRPRGRPKGSK CCCCCCCCCCCCCCC	58.76	-
58	Asymmetric dimethylarginine	VPTPKRPRGRPKGSK CCCCCCCCCCCCCCC	58.76	-
60	Methylation	TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC	30.91	-
60	Asymmetric dimethylarginine	TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC	30.91	-
76	Phosphorylation	AAKTRKVTTAPGRKP CCCCCCCCCCCCCCC	21.92	18779572
98	Phosphorylation	EKEEEEGISQESSEE HHHHHCCCCCCCHHH	4.32	-
99	Phosphorylation	KEEEEGISQESSEEE HHHHCCCCCCCHHHC	38.46	27087446
101	Phosphorylation	EEEGISQESSEEEQ- HHCCCCCCCHHHCC-	49.82	24719451
102	Phosphorylation	EEGISQESSEEEQ-- HCCCCCCCHHHCC--	35.10	27087446
103	Phosphorylation	EGISQESSEEEQ--- CCCCCCCHHHCC---	48.55	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
36	S	Phosphorylation	Kinase	CDC2	P11440	Uniprot
36	S	Phosphorylation	Kinase	HIPK2	Q9QZR5	Uniprot
53	T	Phosphorylation	Kinase	CDK1	P11440	GPS
53	T	Phosphorylation	Kinase	CDK1	P11440	GPS
53	T	Phosphorylation	Kinase	HIPK2	Q9QZR5	Uniprot
53	T	Phosphorylation	Kinase	HIPK2	Q9QZR5	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
58	R	Methylation	-
Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.
60	R	Methylation	-
Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.

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 HMGA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_MOUSE	Rb1	physical	19633359
TAF3_MOUSE	Taf3	physical	21417337
CAF1A_MOUSE	Chaf1a	physical	21417337
CBX7_MOUSE	Cbx7	physical	22214847

Drug and Disease Associations

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

Regulatory Network of HMGA1_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Mass spectrometric analysis of the HMGY protein from Lewis lungcarcinoma. Identification of phosphorylation sites."; Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H.,Manfioletti G., Giancotti V.; J. Biol. Chem. 267:22486-22489(1992). Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, ACETYLATION AT SER-2,AND MASS SPECTROMETRY.	1429598 [Abstract]
Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-99; SER-102 ANDSER-103, AND MASS SPECTROMETRY.	19131326 [Abstract]
"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-102 AND SER-103, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, ANDMASS SPECTROMETRY.	18630941 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.	17525332 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103,AND MASS SPECTROMETRY.	17622165 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND THR-53, AND MASSSPECTROMETRY.	14729942 [Abstract]
"Mass spectrometric analysis of the HMGY protein from Lewis lungcarcinoma. Identification of phosphorylation sites."; Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H.,Manfioletti G., Giancotti V.; J. Biol. Chem. 267:22486-22489(1992). Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, ACETYLATION AT SER-2,AND MASS SPECTROMETRY.	1429598 [Abstract]

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