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P50580 (PA2G4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proliferation-associated protein 2G4
Alternative name(s):
IRES-specific cellular trans-acting factor 45 kDa
Short name=ITAF45
Mpp1
Proliferation-associated protein 1
Protein p38-2G4
Gene names
Name:Pa2g4
Synonyms:Ebp1, Plfap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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. Ref.4 Ref.7

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 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. Ref.7

Subcellular location

Cytoplasm By similarity. Nucleusnucleolus By similarity.

Tissue specificity

Widely expressed. Ref.5

Developmental stage

Expressed in proliferating cells. Observed between G1 and mid S phase, decrease toward the end of S phase, and disappear at the S/G2 transition.

Induction

By mitogens.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 394393Proliferation-associated protein 2G4
PRO_0000148990

Regions

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

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine Ref.6
Modified residue3611Phosphoserine By similarity
Modified residue3861Phosphothreonine By similarity

Experimental info

Mutagenesis65 – 728KKEKEMKK → SSSSSSSS: No effect on RNA-binding. Ref.7
Sequence conflict2791T → A Ref.4
Sequence conflict3111K → R Ref.4

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P50580 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: ABCD169F064261EB

FASTA39443,699
        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 
VAHTFVIGVA 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 KKKASKTVEN ATSGETLEEN GAGD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle."
Radomski N., Jost E.
Exp. Cell Res. 220:434-445(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NFS.
[2]"cDNA cloning, sequence analysis and expression of a mouse 44-kDa nuclear protein copurified with DNA repair factors for acid-depurinated DNA."
Nakagawa Y., Watanabe S., Akiyama K., Sarker A.H., Tsutsui K., Inoue H., Seki S.
Acta Med. Okayama 51:195-206(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NFS.
[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].
Tissue: Eye.
[4]"A cell cycle-dependent protein serves as a template-specific translation initiation factor."
Pilipenko E.V., Pestova T.V., Kolupaeva V.G., Khitrina E.V., Poperechnaya A.N., Agol V.I., Hellen C.U.
Genes Dev. 14:2028-2045(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, FUNCTION IN VIRAL TRANSLATION.
[5]"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: TISSUE SPECIFICITY.
[6]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[7]"Structural insights into the transcriptional and translational roles of Ebp1."
Monie T.P., Perrin A.J., Birtley J.R., Sweeney T.R., Karakasiliotis I., Chaudhry Y., Roberts L.O., Matthews S., Goodfellow I.G., Curry S.
EMBO J. 26:3936-3944(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 8-360, ABSENCE OF METAL COFACTOR AND OF AMINOPEPTIDASE ACTIVITY, FUNCTION, MUTAGENESIS OF 65-LYS--LYS-72, INTERACTION WITH RNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84789 mRNA. Translation: CAA59260.1. Sequence problems.
U43918 mRNA. Translation: AAB60513.1.
BC046532 mRNA. Translation: AAH46532.1.
CCDSCCDS24282.1.
PIRS54181. I48702.
RefSeqNP_035249.1. NM_011119.3.
UniGeneMm.4742.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V6CX-ray2.50A9-360[»]
ProteinModelPortalP50580.
SMRP50580. Positions 8-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202246. 3 interactions.
IntActP50580. 7 interactions.
MINTMINT-1857756.

Protein family/group databases

MEROPSM24.973.

PTM databases

PhosphoSiteP50580.

Proteomic databases

MaxQBP50580.
PaxDbP50580.
PRIDEP50580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026425; ENSMUSP00000026425; ENSMUSG00000025364.
GeneID18813.
KEGGmmu:18813.
UCSCuc007hnl.1. mouse.

Organism-specific databases

CTD5036.
MGIMGI:894684. Pa2g4.

Phylogenomic databases

eggNOGCOG0024.
HOGENOMHOG000168207.
HOVERGENHBG053117.
InParanoidP50580.
OMAICHFSPI.
OrthoDBEOG7SFHXD.
PhylomeDBP50580.
TreeFamTF300010.

Gene expression databases

ArrayExpressP50580.
BgeeP50580.
CleanExMM_PA2G4.
GenevestigatorP50580.

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

ChiTaRSPA2G4. mouse.
EvolutionaryTraceP50580.
NextBio295158.
PROP50580.
SOURCESearch...

Entry information

Entry namePA2G4_MOUSE
AccessionPrimary (citable) accession number: P50580
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot