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UniProtKB/Swiss-Prot entry O15446

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPA34_HUMAN
Primary accession number O15446
Secondary accession numbers Q32N11 Q7Z5U2 Q9UPF6
Integrated into Swiss-Prot on March 21, 2006
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 64)
Name and origin of the protein
Protein name DNA-directed RNA polymerase I subunit RPA34
Synonyms RNA polymerase I-associated factor PAF49
Anti-sense to ERCC-1 protein
ASE-1
CD3-epsilon-associated protein
CD3E-associated protein
CAST
A34.5
Gene name
Name: CD3EAP
Synonyms: ASE1, CAST, PAF49
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
TISSUE=Serum;
DOI=10.1007/s004120050271; PubMed=9426281 [NCBI, ExPASy, EBI, Israel, Japan]
Whitehead C.M., Winkfein R.J., Fritzler M.J., Rattner J.B.;
"ASE-1: a novel protein of the fibrillar centres of the nucleolus and nucleolus organizer region of mitotic chromosomes.";
Chromosoma 106:493-502(1997).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN T CELL RECEPTOR SIGNALING, PHOSPHORYLATION, AND INTERACTION WITH CD3E.
DOI=10.1074/jbc.274.26.18173; PubMed=10373416 [NCBI, ExPASy, EBI, Israel, Japan]
Yamazaki T., Hamano Y., Tashiro H., Itoh K., Nakano H., Miyatake S., Saito T.;
"CAST, a novel CD3epsilon-binding protein transducing activation signal for interleukin-2 production in T cells.";
J. Biol. Chem. 274:18173-18180(1999).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-504.
TISSUE=Skin, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
 IDENTIFICATION IN THE RNA POL I COMPLEX, MASS SPECTROMETRY, FUNCTION, INTERACTION WITH TAF1A AND UBTF, AND PHOSPHORYLATION AT TYR-80.
DOI=10.1128/MCB.00230-06; PubMed=16809778 [NCBI, ExPASy, EBI, Israel, Japan]
Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M.;
"RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor.";
Mol. Cell. Biol. 26:5436-5448(2006).
[5]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[7]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-128; SER-136; SER-172; SER-205; SER-285 AND THR-287, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
  • FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation.
  • FUNCTION: Isoform 2 has been described as a component of preformed T-cell receptor (TCR) complex.
  • SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. Interacts with TAF1A thereby associates with the SL1 complex. Interacts with UBTF. Interacts with POLR1E/PRAF1 through its N-terminal region (By similarity). Isoform 2 interacts with CD3E.
  • SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Found at the fibrillar centers of the nucleolus in interphase and during cell division it is localized to the nucleolus organizer regions of the chromosomes.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO15446-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsCAST
    Isoform IDO15446-2
    Note: No experimental confirmation available. Has sharply different functional characteristics.
    Features which should be applied to build the isoform sequence: VSP_017673.
  • PTM: Isoform 2 undergoes tyrosine phosphorylation upon T-cell receptor (TCR) stimulation. This phosphorylation has not been confirmed by other group.
  • PTM: Isoform 1 is phosphorylated on tyrosine residues in initiation-competent Pol I-beta complexes but not in Pol I-alpha complexes.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • MISCELLANEOUS: It is in an antisense orientation to and overlaps the gene of the DNA repair enzyme ERCC1. This gene overlap is conserved in mouse suggesting an important biologic function.
  • SIMILARITY: Belongs to the eukaryotic RPA34 RNA polymerase subunit family.
  • CAUTION: It is not known whether the so-called human ASE1 and human CAST proteins represent two sides of a single gene product with sharply different functional characteristics. Experiments done with the mouse homolog protein are in favor of an implication of this gene in rRNA transcription instead of T-cell receptor signaling.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U86751; AAB68608.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF017633; AAD41158.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038992; AAH38992.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054044; AAH54044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108889; AAI08890.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00012788; -.
IPI00645816; -.
RefSeq NP_036231.1; -.
UniGene Hs.710495
3D structure databases
ModBase O15446.
Protein-protein interaction databases
IntAct O15446; 3.
PTM databases
PhosphoSite O15446; -.
Organism-specific databases
GeneCards GC19P050602; -.
H-InvDB HIX0039946; -.
HGNC HGNC:24219; CD3EAP.
GenAtlas CD3EAP.
MIM 107325; gene. [NCBI / EBI]
PharmGKB PA142672156; -.
Gene expression databases
ArrayExpress O15446; -.
Bgee O15446; -.
CleanEx HS_CAST; -.
HS_CD3EAP; -.
GermOnline ENSG00000117877; Homo sapiens.
Ontologies
GO
GO:0000120; Cellular component: RNA polymerase I transcription factor complex (traceable author statement from ProtInc).
GO:0003899; Molecular function: DNA-directed RNA polymerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (traceable author statement from ProtInc).
GO:0009303; Biological process: rRNA transcription (traceable author statement from ProtInc).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR013240; RNA_pol1_su_RPA34.
Graphical view of domain structure.
Pfam PF08208; RNA_polI_A34; 1.
Pfam graphical view of domain structure.
Proteomic databases
PRIDE O15446; -.
Genome annotation databases
Ensembl ENSG00000117877; Homo sapiens. [Contig view]
GeneID 10849; -.
KEGG hsa:10849; -.
Phylogenomic databases
HOGENOM O15446; -.
HOVERGEN O15446; -.
OMA O15446; IQAPADF.
Other
NextBio 41189; -.
SOURCE CD3EAP; Homo sapiens.
ProtoNet O15446.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; DNA-directed RNA polymerase; Nucleus; Phosphoprotein; Polymorphism; Transcription.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   510  510     DNA-directed RNA polymerase I subunit RPA34. PRO_0000228120
COMPBIAS   174   177  4     Poly-Lys. 
COMPBIAS   212   217  6     Poly-Lys. 
COMPBIAS   422   428  7     Poly-Lys. 
COMPBIAS   504   508  5     Poly-Gln. 
MOD_RES   27    27        Phosphoserine. 
MOD_RES   80    80        Phosphotyrosine. 
MOD_RES   128   128        Phosphoserine. 
MOD_RES   136   136        Phosphoserine. 
MOD_RES   172   172        Phosphoserine. 
MOD_RES   205   205        Phosphoserine. 
MOD_RES   285   285        Phosphoserine. 
MOD_RES   287   287        Phosphothreonine. 
MOD_RES   309   309        Phosphoserine. 
VAR_SEQ   7     7        G -> GGE (in isoform 2). VSP_017673
VARIANT   259   259  1     K -> T (in dbSNP:rs735482 [NCBI]). VAR_051875 
VARIANT   282   282  1     T -> A (in dbSNP:rs3212989 [NCBI]). VAR_051876 
VARIANT   373   373  1     K -> E (in dbSNP:rs762562 [NCBI]). VAR_051877 
VARIANT   394   394  1     D -> N (in dbSNP:rs2336219 [NCBI]). VAR_051878 
VARIANT   503   503  1     K -> Q (in dbSNP:rs3212986 [NCBI]). VAR_051879 
VARIANT   504   504  1     Q -> K (in dbSNP:rs3212986 [NCBI]). VAR_051880 
CONFLICT   218   218        N -> K (in Ref. 3; AAH54044). 
CONFLICT   422   422        Missing (in Ref. 3; AAI08890). 
Sequence information
Length: 510 AA [This is the length of the unprocessed precursor] Molecular weight: 54986 Da [This is the MW of the unprocessed precursor] CRC64: D460FB944412D393 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH 

        70         80         90        100        110        120 
VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE AGGGLTCASA PQGTLRILEG 

       130        140        150        160        170        180 
PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ 

       190        200        210        220        230        240 
VTEAPVTQEA VNGHGALEVD MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE 

       250        260        270        280        290        300 
PLGVLFPSTT KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME 

       310        320        330        340        350        360 
PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV EPEMKPLESP 

       370        380        390        400        410        420 
GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE TEVVGPELPD DLEPQAAPTS 

       430        440        450        460        470        480 
TKKKKKKKER GHTVTEPIQP LEPELPGEGQ PEARATPGST KKRKKQSQES RMPETVPQEE 

       490        500        510 
MPGPPLNSES GEEAPTGRDK KRKQQQQQPV
O15446 in FASTA format

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