HMGA2_MOUSE - dbPTM
HMGA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMGA2_MOUSE
UniProt AC P52927
Protein Name High mobility group protein HMGI-C
Gene Name Hmga2
Organism Mus musculus (Mouse).
Sequence Length 108
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. [PubMed: 27446912]
Protein Sequence MSARGEGAGQPSTSAQGQPAAPVPQKRGRGRPRKQQQEPTCEPSPKRPRGRPKGSKNKSPSKAAQKKAETIGEKRPRGRPRKWPQQVVQKKPAQETEETSSQESAEED
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSARGEGAG
------CCCCCCCCC
27.0326824392
2Acetylation------MSARGEGAG
------CCCCCCCCC
27.03-
12PhosphorylationGEGAGQPSTSAQGQP
CCCCCCCCCCCCCCC
27.4028059163
13PhosphorylationEGAGQPSTSAQGQPA
CCCCCCCCCCCCCCC
34.4629514104
14PhosphorylationGAGQPSTSAQGQPAA
CCCCCCCCCCCCCCC
23.9627087446
26AcetylationPAAPVPQKRGRGRPR
CCCCCCCCCCCCCCC
51.23129653
27MethylationAAPVPQKRGRGRPRK
CCCCCCCCCCCCCCC
34.4918966559
40PhosphorylationRKQQQEPTCEPSPKR
CCCCCCCCCCCCCCC
28.8425619855
41GlutathionylationKQQQEPTCEPSPKRP
CCCCCCCCCCCCCCC
12.0924333276
44PhosphorylationQEPTCEPSPKRPRGR
CCCCCCCCCCCCCCC
22.2925521595
59PhosphorylationPKGSKNKSPSKAAQK
CCCCCCCCHHHHHHH
43.7424453211
61PhosphorylationGSKNKSPSKAAQKKA
CCCCCCHHHHHHHHH
41.8524453211
74AcetylationKAETIGEKRPRGRPR
HHHHHHCCCCCCCCC
63.5923806337
96PhosphorylationQKKPAQETEETSSQE
HCCCCCCCCHHCCHH
27.3525619855
99PhosphorylationPAQETEETSSQESAE
CCCCCCHHCCHHHHH
27.6925521595
100PhosphorylationAQETEETSSQESAEE
CCCCCHHCCHHHHHC
33.0525521595
101PhosphorylationQETEETSSQESAEED
CCCCHHCCHHHHHCC
45.4425521595
104PhosphorylationEETSSQESAEED---
CHHCCHHHHHCC---
33.0925521595

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
44SPhosphorylationKinaseCDK1P06493
PSP
59SPhosphorylationKinaseCDK1P06493
PSP
99TPhosphorylationKinaseCSNK2A1P68400
GPS
100SPhosphorylationKinaseCSNK2A1P68400
GPS
101SPhosphorylationKinaseCSNK2A1P68400
GPS
104SPhosphorylationKinaseCSNK2A1P68400
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMGA2_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF3_MOUSETaf3physical
21417337
CAF1A_MOUSEChaf1aphysical
21417337

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMGA2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-104, AND MASSSPECTROMETRY.
"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-104, AND MASSSPECTROMETRY.
"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 SER-104, AND MASSSPECTROMETRY.

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