dbPTM

HMGA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGA2_HUMAN
UniProt AC	P52926
Protein Name	High mobility group protein HMGI-C
Gene Name	HMGA2
Organism	Homo sapiens (Human).
Sequence Length	109
Subcellular Localization	Nucleus.
Protein Description	Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation (By similarity)..
Protein Sequence	MSARGEGAGQPSTSAQGQPAAPAPQKRGRGRPRKQQQEPTGEPSPKRPRGRPKGSKNKSPSKAAQKKAEATGEKRPRGRPRKWPQQVVQKKPAQEETEETSSQESAEED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSARGEGAG ------CCCCCCCCC	27.03	28450419
2	Acetylation	------MSARGEGAG ------CCCCCCCCC	27.03	19413330
4	Methylation	----MSARGEGAGQP ----CCCCCCCCCCC	36.07	115478789
12	Phosphorylation	GEGAGQPSTSAQGQP CCCCCCCCCCCCCCC	27.40	29116813
13	Phosphorylation	EGAGQPSTSAQGQPA CCCCCCCCCCCCCCC	34.46	29116813
14	Phosphorylation	GAGQPSTSAQGQPAA CCCCCCCCCCCCCCC	23.96	30631047
26	Ubiquitination	PAAPAPQKRGRGRPR CCCCCCCCCCCCCCC	56.62	21906983
26	Ubiquitination	PAAPAPQKRGRGRPR CCCCCCCCCCCCCCC	56.62	21906983
26	Ubiquitination	PAAPAPQKRGRGRPR CCCCCCCCCCCCCCC	56.62	21906983
26	Ubiquitination	PAAPAPQKRGRGRPR CCCCCCCCCCCCCCC	56.62	2190698
26	Acetylation	PAAPAPQKRGRGRPR CCCCCCCCCCCCCCC	56.62	129651
26	Methylation	PAAPAPQKRGRGRPR CCCCCCCCCCCCCCC	56.62	129651
40	Phosphorylation	RKQQQEPTGEPSPKR CCCCCCCCCCCCCCC	54.12	30266825
44	Phosphorylation	QEPTGEPSPKRPRGR CCCCCCCCCCCCCCC	38.46	19664994
59	Phosphorylation	PKGSKNKSPSKAAQK CCCCCCCCHHHHHHH	43.74	27422710
61	Phosphorylation	GSKNKSPSKAAQKKA CCCCCCHHHHHHHHH	41.85	23836654
66	Sumoylation	SPSKAAQKKAEATGE CHHHHHHHHHHHHCC	49.58	-
97	Phosphorylation	KKPAQEETEETSSQE CCCCCHHHHHHCHHH	38.07	23927012
100	Phosphorylation	AQEETEETSSQESAE CCHHHHHHCHHHHHH	27.69	29255136
101	Phosphorylation	QEETEETSSQESAEE CHHHHHHCHHHHHHC	33.05	29255136
102	Phosphorylation	EETEETSSQESAEED HHHHHHCHHHHHHCC	45.44	29255136
105	Phosphorylation	EETSSQESAEED--- HHHCHHHHHHCC---	33.09	29255136

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
44	S	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
59	S	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HMGA2_HUMAN !!

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 HMGA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF65_HUMAN	RELA	physical	12693954
NFKB1_HUMAN	NFKB1	physical	12693954
PIAS3_HUMAN	PIAS3	physical	11390395
ANM6_HUMAN	PRMT6	physical	16293633
NPM_HUMAN	NPM1	physical	16293633
SMAD1_HUMAN	SMAD1	physical	18425117
SMAD5_HUMAN	SMAD5	physical	18425117
SMAD9_HUMAN	SMAD9	physical	18425117
PTBP1_HUMAN	PTBP1	physical	18850631
APEX1_HUMAN	APEX1	physical	18850631
HNRPQ_HUMAN	SYNCRIP	physical	18850631
XRCC6_HUMAN	XRCC6	physical	18850631
PSIP1_HUMAN	PSIP1	physical	18850631
PA2G4_HUMAN	PA2G4	physical	18850631
PCBP2_HUMAN	PCBP2	physical	18850631
E4F1_HUMAN	E4F1	physical	14645522

Drug and Disease Associations

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

Regulatory Network of HMGA2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-14; THR-40 AND SER-44,AND MASS SPECTROMETRY.	19413330 [Abstract]