UniProt Accession

 PA2G4_HUMAN; Q9UQ80; O43846; Q9UM59 

Genbank Protein ID

 U59435; U87954; AF104670; AF104668; AF104669; BC001951; BC007561; BC069786 

Genbank Nucleotide ID

 AAB91536.1; AAD00646.1; AAD05561.1; AAD05561.1; AAD05561.1; AAH01951.1; AAH07561.1; AAH69786.1 

Protein Name

 Proliferation-associated protein 2G4 

Protein Synonyms/Alias

 Cell cycle protein p38-2G4 homolog; hG4-1; ErbB3-binding protein 1 

Gene Name

 PA2G4 

Gene Synonyms/Alias

 EBP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
20	AEDLVVTKYKMGGDI	ubiquitination	[1, 2, 3, 4]
22	DLVVTKYKMGGDIAN	ubiquitination	[2, 3]
62	MIMEETGKIFKKEKE	ubiquitination	[5]
66	ETGKIFKKEKEMKKG	ubiquitination	[3]
93	VCHFSPLKSDQDYIL	sumoylation	[6]
93	VCHFSPLKSDQDYIL	ubiquitination	[3]
101	SDQDYILKEGDLVKI	ubiquitination	[3, 7]
144	GRKADVIKAAHLCAE	ubiquitination	[3]
158	EAALRLVKPGNQNTQ	ubiquitination	[1, 3, 4, 7]
172	QVTEAWNKVAHSFNC	ubiquitination	[3]
191	GMLSHQLKQHVIDGE	ubiquitination	[3]
199	QHVIDGEKTIIQNPT	ubiquitination	[3, 7]
210	QNPTDQQKKDHEKAE	ubiquitination	[3, 7]
211	NPTDQQKKDHEKAEF	ubiquitination	[3]
248	GQRTTIYKRDPSKQY	ubiquitination	[3]
253	IYKRDPSKQYGLKMK	ubiquitination	[3]
258	PSKQYGLKMKTSRAF	ubiquitination	[3]
287	LRAFEDEKKARMGVV	acetylation	[8]
287	LRAFEDEKKARMGVV	ubiquitination	[7]
298	MGVVECAKHELLQPF	acetylation	[8]
298	MGVVECAKHELLQPF	sumoylation	[6]
298	MGVVECAKHELLQPF	ubiquitination	[3, 8, 9]
311	PFNVLYEKEGEFVAQ	ubiquitination	[3, 9]
344	PFEPDLYKSEMEVQD	ubiquitination	[3, 7, 9]
355	EVQDAELKALLQSSA	ubiquitination	[3, 7, 9]
373	TQKKKKKKASKTAEN	ubiquitination	[2, 3, 9]
376	KKKKKASKTAENATS	ubiquitination	[2, 3, 7, 8, 9, 10, 11]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity.
 Oh SM, Liu Z, Okada M, Jang SW, Liu X, Chan CB, Luo H, Ye K.
 Oncogene. 2010 Feb 18;29(7):1017-30. [PMID: 19946338]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional 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. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). 

Sequence Annotation

 REGION 2 48 Necessary for nucleolar localization.
 REGION 46 54 RNA-binding.
 REGION 301 394 Necessary for nucleolar localization.
 REGION 361 375 Interaction with RNA (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 361 361 Phosphoserine.
 MOD_RES 366 366 Phosphothreonine (Probable).
 MOD_RES 386 386 Phosphothreonine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; rRNA processing; Transcription; Transcription regulation; Translation regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 394 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IDA:MGI.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
 GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR004545; Pap_1.
 IPR000994; Pept_M24_structural-domain.
 IPR018349; Pept_M24A_MAP2_BS.
 IPR011991; WHTH_DNA-bd_dom. 

Pfam

 PF00557; Peptidase_M24 

SMART

  

PROSITE

 PS01202; MAP_2 

PRINTS