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Q9UQ80 (PA2G4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proliferation-associated protein 2G4
Alternative name(s):
Cell cycle protein p38-2G4 homolog
Short name=hG4-1
ErbB3-binding protein 1
Gene names
Name:PA2G4
Synonyms:EBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.11 Ref.12

Subunit structure

Interacts with the cytoplasmic domain of non-phosphorylated ERBB3; the interaction requires PKC activity. Interacts with AR. Treatment with HRG leads to dissociation from ERBB3 and increases association with AR. Interacts with NCL/nucleolin. Component of a ribonucleoprotein complex containing at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1 (HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18, RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24. Interacts with HDAC2. Interacts with RB1; the interaction is enhanced upon PA2G4 dephosphorylation. Ref.2 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.23

Subcellular location

Cytoplasm. Nucleusnucleolus. Note: Tranlocates to the nucleus upon treatment with HRG. Ref.2 Ref.9 Ref.11

Tissue specificity

Expressed in several cell lines tested, including primary and transformed cell lines. Ref.11

Post-translational modification

Phosphorylated on serine and threonine residues. Phosphorylation is enhanced by HRG treatment. Basal phosphorylation is PKC-dependent and HRG-induced phosphorylation is predominantly PKC-independent. Ref.7

Sequence similarities

Belongs to the peptidase M24 family.

Caution

Although it belongs to the peptidase M24 family, it does not contain metal cofactors and lacks aminopeptidase activity.

Sequence caution

The sequence AAD00646.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processrRNA processing
Transcription
Transcription regulation
Translation regulation
   Cellular componentCytoplasm
Nucleus
   LigandRNA-binding
   Molecular functionRepressor
Ribonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Traceable author statement PubMed 7556453. Source: ProtInc

cell proliferation

Traceable author statement PubMed 7556453. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15073182. Source: MGI

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19037095. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay PubMed 19037095. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15073182. Source: MGI

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15073182. Source: MGI

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15073182. Source: MGI

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 19037095. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 394393Proliferation-associated protein 2G4
PRO_0000148989

Regions

Region2 – 4847Necessary for nucleolar localization
Region46 – 549RNA-binding
Region301 – 39494Necessary for nucleolar localization
Region361 – 37515Interaction with RNA By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22
Modified residue21Phosphoserine Ref.13 Ref.18 Ref.20
Modified residue3611Phosphoserine Ref.15 Ref.18
Modified residue3661Phosphothreonine Probable
Modified residue3861Phosphothreonine Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20

Experimental info

Mutagenesis20 – 223KYK → AYA: Loss of nucleolar localization. Ref.11
Mutagenesis3631S → A: No effect on in vitro phosphorylation by PKC. Ref.7
Mutagenesis364 – 3652RK → AA: Only partial nucleolar localization.
Mutagenesis3661T → A: Decreases in vitro phosphorylation by PKC. Ref.7
Sequence conflict3811A → P in AAB91536. Ref.1

Secondary structure

.............................................. 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UQ80 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CD45466507AD6047

FASTA39443,787
        10         20         30         40         50         60 
MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE KGDAMIMEET 

        70         80         90        100        110        120 
GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL KEGDLVKIDL GVHVDGFIAN 

       130        140        150        160        170        180 
VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA EAALRLVKPG NQNTQVTEAW NKVAHSFNCT 

       190        200        210        220        230        240 
PIEGMLSHQL KQHVIDGEKT IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA 

       250        260        270        280        290        300 
GQRTTIYKRD PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE 

       310        320        330        340        350        360 
LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ DAELKALLQS 

       370        380        390 
SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and mapping of a human cDNA (PA2G4) that encodes a protein highly homologous to the mouse cell cycle protein p38-2G4."
Lamartine J., Seri M., Cinti R., Heitzmann F., Creaven M., Radomski N., Jost E., Lenoir G.M., Romeo G., Sylla B.S.
Cytogenet. Cell Genet. 78:31-35(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin."
Yoo J.Y., Wang X.W., Rishi A.K., Lessor T., Xia X.M., Gustafson T.A., Hamburger A.W.
Br. J. Cancer 82:683-690(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ERBB3, SUBCELLULAR LOCATION.
Tissue: Brain.
[3]"Genomic structure of the human PA2G4 gene."
Caroli F., Lamartine J., Sylla B.S., Romeo G., Seri M.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Skin.
[5]Bienvenut W.V., Matallanas D., Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-20; 23-30; 34-62; 73-101; 156-172; 200-211; 216-236; 264-281 AND 299-364, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma, Mammary carcinoma and Ovarian carcinoma.
[6]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 34-51; 216-236; 264-271; 299-311; 333-344 AND 377-394, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Regulation of the ErbB3 binding protein Ebp1 by protein kinase C."
Lessor T.J., Hamburger A.W.
Mol. Cell. Endocrinol. 175:185-191(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB3, PHOSPHORYLATION, PHOSPHORYLATION BY PKC, PHOSPHORYLATION AT THR-366, MUTAGENESIS OF SER-363 AND THR-366.
[8]"Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation."
Xia X., Cheng A., Lessor T., Zhang Y., Hamburger A.W.
J. Cell. Physiol. 187:209-217(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH RB1.
[9]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases."
Zhang Y., Woodford N., Xia X., Hamburger A.W.
Nucleic Acids Res. 31:2168-2177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN E2F1-MEDIATED TRANSCRIPTION REPRESSION, INTERACTION WITH HDAC2.
[11]"EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes."
Squatrito M., Mancino M., Donzelli M., Areces L.B., Draetta G.F.
Oncogene 23:4454-4465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RRNA PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX, ASSOCIATION WITH RRNA, ASSOCIATION WITH U3 SNORNA, MUTAGENESIS OF 20-LYS--LYS-22 AND 364-ARG-LYS-365.
[12]"Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling."
Zhang Y., Hamburger A.W.
Br. J. Cancer 92:140-146(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH ERBB3 AND AR.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions."
Kowalinski E., Bange G., Bradatsch B., Hurt E., Wild K., Sinning I.
FEBS Lett. 581:4450-4454(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH 5S RIBOSOMAL RNA, LACK OF METAL COFACTOR, LACK OF AMINOPEPTIDASE ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59435 mRNA. Translation: AAB91536.1.
U87954 mRNA. Translation: AAD00646.1. Different initiation.
AF104670, AF104668, AF104669 Genomic DNA. Translation: AAD05561.1.
BC001951 mRNA. Translation: AAH01951.1.
BC007561 mRNA. Translation: AAH07561.1.
BC069786 mRNA. Translation: AAH69786.1.
RefSeqNP_006182.2. NM_006191.2.
UniGeneHs.524498.
Hs.745109.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q8KX-ray1.60A2-394[»]
3J2Ielectron microscopy11.90A1-394[»]
ProteinModelPortalQ9UQ80.
SMRQ9UQ80. Positions 7-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111075. 75 interactions.
IntActQ9UQ80. 43 interactions.
MINTMINT-5000754.
STRING9606.ENSP00000302886.

Protein family/group databases

MEROPSM24.973.

PTM databases

PhosphoSiteQ9UQ80.

Polymorphism databases

DMDM13632817.

2D gel databases

SWISS-2DPAGEQ9UQ80.

Proteomic databases

PaxDbQ9UQ80.
PRIDEQ9UQ80.

Protocols and materials databases

DNASU5036.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303305; ENSP00000302886; ENSG00000170515.
GeneID5036.
KEGGhsa:5036.
UCSCuc001sjm.3. human.

Organism-specific databases

CTD5036.
GeneCardsGC12P056498.
HGNCHGNC:8550. PA2G4.
HPACAB011711.
CAB012428.
HPA016484.
MIM602145. gene.
neXtProtNX_Q9UQ80.
PharmGKBPA32877.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0024.
HOGENOMHOG000168207.
HOVERGENHBG053117.
InParanoidQ9UQ80.
OMAVWYKPEL.
OrthoDBEOG7SFHXD.
PhylomeDBQ9UQ80.
TreeFamTF300010.

Gene expression databases

ArrayExpressQ9UQ80.
BgeeQ9UQ80.
CleanExHS_PA2G4.
GenevestigatorQ9UQ80.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
InterProIPR004545. Pap_1.
IPR000994. Pept_M24_structural-domain.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. SSF55920. 2 hits.
TIGRFAMsTIGR00495. crvDNA_42K. 1 hit.
PROSITEPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UQ80.
GeneWikiPA2G4.
GenomeRNAi5036.
NextBio19404.
PROQ9UQ80.
SOURCESearch...

Entry information

Entry namePA2G4_HUMAN
AccessionPrimary (citable) accession number: Q9UQ80
Secondary accession number(s): O43846, Q9UM59
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM