PA2G4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PA2G4_MOUSE
• UniProt AC: P50580
• Protein Name: Proliferation-associated protein 2G4
• Gene Name: Pa2g4
• Organism: Mus musculus (Mouse).
• Sequence Length: 394
• Subcellular Localization: Isoform 1: Cytoplasm . Nucleus, nucleolus . Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.; Isoform 2: Cytoplasm .
• Protein Description: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly (By similarity). Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). Together with PTBP1 is required for the translation initiation on the foot-and-mouth disease virus (FMDV) IRES. Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity)..
• Protein Sequence: MSGEDEQQEQTIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVIGVAQGTQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAKDAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTVENATSGETLEENGAGD

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
2	Phosphorylation	------MSGEDEQQE ------CCCCHHHHH	51.38	26824392
2	Acetylation	------MSGEDEQQE ------CCCCHHHHH	51.38	-
11	Phosphorylation	EDEQQEQTIAEDLVV CHHHHHHHHHHHHHH	22.77	27566939
19	Phosphorylation	IAEDLVVTKYKMGGD HHHHHHHEEECCCHH	22.60	25619855
21	Phosphorylation	EDLVVTKYKMGGDIA HHHHHEEECCCHHHH	9.24	22345495
22	Ubiquitination	DLVVTKYKMGGDIAN HHHHEEECCCHHHHH	32.40	22790023
49	S-nitrosylation	GVSVLSLCEKGDAMI CCEEHHHHHHCCEEE	4.57	24926564
49	Glutathionylation	GVSVLSLCEKGDAMI CCEEHHHHHHCCEEE	4.57	24333276
101	Succinylation	SDQDYILKEGDLVKI CCCCEEECCCCEEEE	50.52	23954790
101	Acetylation	SDQDYILKEGDLVKI CCCCEEECCCCEEEE	50.52	22826441
149	Glutathionylation	VIKAAHLCAEAALRL HHHHHHHHHHHHHHH	2.00	24333276
158	Ubiquitination	EAALRLVKPGNQNTQ HHHHHHCCCCCCCCH	52.37	22790023
164	Phosphorylation	VKPGNQNTQVTEAWN CCCCCCCCHHHHHHH	18.04	20531401
167	Phosphorylation	GNQNTQVTEAWNKVA CCCCCHHHHHHHHHH	15.35	20531401
179	Glutathionylation	KVAHSFNCTPIEGML HHHHHCCCCCCCCHH	4.51	24333276
180	Phosphorylation	VAHSFNCTPIEGMLS HHHHCCCCCCCCHHH	28.53	25890499
210	Malonylation	QNPTDQQKKDHEKAE ECCCHHHHHHHHHHE	55.31	32601280
244	Phosphorylation	AKDAGQRTTIYKRDP CCCCCCCCEEEECCH	15.06	28576409
267	Phosphorylation	KTSRAFFSEVERRFD HHCHHHHHHHHHHHH	33.99	18779572
296	Glutathionylation	ARMGVVECAKHELLQ HHCCHHHHHHHHHHH	4.06	24333276
335	Phosphorylation	NGPMRITSGPFEPDL CCCEEECCCCCCCCH	41.94	29514104
360	Phosphorylation	ELKALLQSSASRKTQ HHHHHHHHHHHHHHH	28.04	23984901
361	Phosphorylation	LKALLQSSASRKTQK HHHHHHHHHHHHHHH	19.80	26824392
363	Phosphorylation	ALLQSSASRKTQKKK HHHHHHHHHHHHHHH	35.94	26824392
366	Phosphorylation	QSSASRKTQKKKKKK HHHHHHHHHHHHHHH	44.50	25266776
373	Ubiquitination	TQKKKKKKASKTVEN HHHHHHHHHCHHHHC	67.77	-
375	Phosphorylation	KKKKKKASKTVENAT HHHHHHHCHHHHCCC	37.43	23984901
376	Ubiquitination	KKKKKASKTVENATS HHHHHHCHHHHCCCC	62.54	-
377	Phosphorylation	KKKKASKTVENATSG HHHHHCHHHHCCCCC	30.47	26745281
382	Phosphorylation	SKTVENATSGETLEE CHHHHCCCCCCCHHH	49.17	26745281
383	Phosphorylation	KTVENATSGETLEEN HHHHCCCCCCCHHHC	32.02	26745281
386	Phosphorylation	ENATSGETLEENGAG HCCCCCCCHHHCCCC	42.89	26745281

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
361	S	Phosphorylation	Kinase	PRKCD	P28867	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
361	S	Phosphorylation	Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PA2G4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P85A_MOUSE	Pik3r1	physical	24651434
HSP74_HUMAN	HSPA4	physical	24651434
CHIP_HUMAN	STUB1	physical	24651434

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY.
PubMed: 16452087

Phosphorylation

"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-2, AND MASSSPECTROMETRY.
PubMed: 19131326

"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY.
PubMed: 16452087