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Protein

Proliferation-associated protein 2G4

Gene

Pa2g4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Together with PTBP1 is required for the translation initiation on the foot-and-mouth disease virus (FMDV) IRES (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation.1 PublicationBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

RNA-binding

Protein family/group databases

MEROPSiM24.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Proliferation-associated protein 2G4
Gene namesi
Name:Pa2g4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1302994. Pa2g4.

Subcellular locationi

Isoform 1 :
  • Cytoplasm 1 Publication
  • Nucleusnucleolus 1 Publication

  • Note: Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.By similarity
Isoform 2 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • membrane Source: Ensembl
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 394393Proliferation-associated protein 2G4PRO_0000431530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei361 – 3611Phosphoserine; by PKC/PRKCDBy similarity
Modified residuei386 – 3861PhosphothreonineBy similarity

Post-translational modificationi

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. Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization.By similarity
Isoform 2 is polyubiquitinated, leading to proteasomal degradation and phosphorylation by PKC/PRKCD enhances polyubiquitination.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6AYD3.
PRIDEiQ6AYD3.

PTM databases

iPTMnetiQ6AYD3.

Expressioni

Gene expression databases

ExpressionAtlasiQ6AYD3. baseline and differential.
GenevisibleiQ6AYD3. RN.

Interactioni

Subunit structurei

Isoform 2 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 nucleolin/NCL. 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 (By similarity). Isoform 1 and isoform 2 interact with RNF20 (By similarity). Isoform 2 interacts with HUWE1 (By similarity). Interacts with AKT1.By similarity1 Publication

Protein-protein interaction databases

IntActiQ6AYD3. 1 interaction.
STRINGi10116.ENSRNOP00000006578.

Structurei

3D structure databases

ProteinModelPortaliQ6AYD3.
SMRiQ6AYD3. Positions 8-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4847Necessary for nucleolar localizationBy similarityAdd
BLAST
Regioni46 – 549RNA-bindingBy similarity
Regioni301 – 39494Necessary for nucleolar localizationBy similarityAdd
BLAST
Regioni361 – 37515Interaction with RNABy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M24 family.Curated

Phylogenomic databases

eggNOGiKOG2776. Eukaryota.
COG0024. LUCA.
GeneTreeiENSGT00530000063220.
HOGENOMiHOG000168207.
HOVERGENiHBG053117.
OMAiKNWAVTE.
OrthoDBiEOG7SFHXD.
PhylomeDBiQ6AYD3.
TreeFamiTF300010.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
InterProiIPR004545. PA2G4.
IPR000994. Pept_M24_structural-domain.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00495. crvDNA_42K. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q6AYD3-1) [UniParc]FASTAAdd to basket

Also known as: p481 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE
60 70 80 90 100
KGDAMIMEET GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL
110 120 130 140 150
KEGDLVKIDL GVHVDGFIAN VAHTFVIGVA QGSQVTGRKA DVIKAAHLCA
160 170 180 190 200
EAALRLVKPG NQNTQVTEAW NKVAHSFNCT PIEGMLSHQL KQHVIDGEKT
210 220 230 240 250
IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA GQRTTIYKRD
260 270 280 290 300
PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE
310 320 330 340 350
LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ
360 370 380 390
DAELKALLQS SASRKTQKKK KKKASKTAEN ATSGETLEEN GAGD
Length:394
Mass (Da):43,657
Last modified:September 13, 2004 - v1
Checksum:iB3799DCF064371BB
GO
Isoform 2Curated (identifier: Q6AYD3-2) [UniParc]FASTAAdd to basket

Also known as: p421 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.

Show »
Length:340
Mass (Da):37,929
Checksum:i1DA65807D48C815F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5454Missing in isoform 2. 1 PublicationVSP_057324Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06047173 Genomic DNA. No translation available.
CH474104 Genomic DNA. Translation: EDL84836.1.
BC079095 mRNA. Translation: AAH79095.1.
RefSeqiNP_001004206.1. NM_001004206.1. [Q6AYD3-1]
UniGeneiRn.9485.

Genome annotation databases

EnsembliENSRNOT00000006578; ENSRNOP00000006578; ENSRNOG00000004904. [Q6AYD3-1]
GeneIDi288778.
KEGGirno:288778.
UCSCiRGD:1302994. rat. [Q6AYD3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06047173 Genomic DNA. No translation available.
CH474104 Genomic DNA. Translation: EDL84836.1.
BC079095 mRNA. Translation: AAH79095.1.
RefSeqiNP_001004206.1. NM_001004206.1. [Q6AYD3-1]
UniGeneiRn.9485.

3D structure databases

ProteinModelPortaliQ6AYD3.
SMRiQ6AYD3. Positions 8-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6AYD3. 1 interaction.
STRINGi10116.ENSRNOP00000006578.

Protein family/group databases

MEROPSiM24.978.

PTM databases

iPTMnetiQ6AYD3.

Proteomic databases

PaxDbiQ6AYD3.
PRIDEiQ6AYD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000006578; ENSRNOP00000006578; ENSRNOG00000004904. [Q6AYD3-1]
GeneIDi288778.
KEGGirno:288778.
UCSCiRGD:1302994. rat. [Q6AYD3-1]

Organism-specific databases

CTDi5036.
RGDi1302994. Pa2g4.

Phylogenomic databases

eggNOGiKOG2776. Eukaryota.
COG0024. LUCA.
GeneTreeiENSGT00530000063220.
HOGENOMiHOG000168207.
HOVERGENiHBG053117.
OMAiKNWAVTE.
OrthoDBiEOG7SFHXD.
PhylomeDBiQ6AYD3.
TreeFamiTF300010.

Miscellaneous databases

PROiQ6AYD3.

Gene expression databases

ExpressionAtlasiQ6AYD3. baseline and differential.
GenevisibleiQ6AYD3. RN.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.90.230.10. 2 hits.
InterProiIPR004545. PA2G4.
IPR000994. Pept_M24_structural-domain.
IPR018349. Pept_M24A_MAP2_BS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55920. SSF55920. 2 hits.
TIGRFAMsiTIGR00495. crvDNA_42K. 1 hit.
PROSITEiPS01202. MAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "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] (ISOFORM 1).
    Tissue: Lung.
  4. "Ebp1 isoforms distinctively regulate cell survival and differentiation."
    Liu Z., Ahn J.Y., Liu X., Ye K.
    Proc. Natl. Acad. Sci. U.S.A. 103:10917-10922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AKT1.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPA2G4_RAT
AccessioniPrimary (citable) accession number: Q6AYD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 7, 2015
Last sequence update: September 13, 2004
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.