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O15446

- RPA34_HUMAN

UniProt

O15446 - RPA34_HUMAN

Protein

DNA-directed RNA polymerase I subunit RPA34

Gene

CD3EAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    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.
    Isoform 2 has been described as a component of preformed T-cell receptor (TCR) complex.

    GO - Molecular functioni

    1. DNA-directed RNA polymerase activity Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. rRNA transcription Source: ProtInc
    2. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc

    Keywords - Biological processi

    Transcription

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-directed RNA polymerase I subunit RPA34
    Alternative name(s):
    A34.5
    Antisense to ERCC-1 protein
    Short name:
    ASE-1
    CD3-epsilon-associated protein
    Short name:
    CAST
    Short name:
    CD3E-associated protein
    RNA polymerase I-associated factor PAF49
    Gene namesi
    Name:CD3EAP
    Synonyms:ASE1, CAST, PAF49
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24219. CD3EAP.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Chromosome 1 Publication
    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.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. DNA-directed RNA polymerase I complex Source: Ensembl
    4. mitochondrion Source: HPA
    5. nucleolus Source: HPA
    6. nucleus Source: HPA
    7. RNA polymerase I transcription factor complex Source: ProtInc

    Keywords - Cellular componenti

    Chromosome, DNA-directed RNA polymerase, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672156.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 510510DNA-directed RNA polymerase I subunit RPA34PRO_0000228120Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei27 – 271Phosphoserine2 Publications
    Modified residuei80 – 801Phosphotyrosine2 Publications
    Modified residuei128 – 1281Phosphoserine2 Publications
    Modified residuei136 – 1361Phosphoserine4 Publications
    Modified residuei172 – 1721Phosphoserine3 Publications
    Modified residuei205 – 2051Phosphoserine2 Publications
    Modified residuei285 – 2851Phosphoserine4 Publications
    Modified residuei287 – 2871Phosphothreonine2 Publications
    Modified residuei309 – 3091Phosphoserine2 Publications
    Modified residuei490 – 4901Phosphoserine2 Publications

    Post-translational modificationi

    Isoform 2 undergoes tyrosine phosphorylation upon T-cell receptor (TCR) stimulation. This phosphorylation has not been confirmed by other groups.
    Isoform 1 is phosphorylated on tyrosine residues in initiation-competent Pol I-beta complexes but not in Pol I-alpha complexes.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO15446.
    PaxDbiO15446.
    PRIDEiO15446.

    PTM databases

    PhosphoSiteiO15446.

    Expressioni

    Gene expression databases

    ArrayExpressiO15446.
    BgeeiO15446.
    CleanExiHS_CAST.
    HS_CD3EAP.
    GenevestigatoriO15446.

    Organism-specific databases

    HPAiHPA041664.
    HPA041734.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi116060. 17 interactions.
    DIPiDIP-27616N.
    IntActiO15446. 6 interactions.
    MINTiMINT-1144996.
    STRINGi9606.ENSP00000310966.

    Structurei

    3D structure databases

    ProteinModelPortaliO15446.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi174 – 1774Poly-Lys
    Compositional biasi212 – 2176Poly-Lys
    Compositional biasi422 – 4287Poly-Lys
    Compositional biasi504 – 5085Poly-Gln

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG45026.
    HOGENOMiHOG000120117.
    HOVERGENiHBG082101.
    InParanoidiO15446.
    OMAiFCAFGGN.
    OrthoDBiEOG7VTDPJ.
    PhylomeDBiO15446.
    TreeFamiTF338162.

    Family and domain databases

    InterProiIPR013240. DNA-dir_RNA_pol1_su_RPA34.
    [Graphical view]
    PfamiPF08208. RNA_polI_A34. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15446-1) [UniParc]FASTAAdd to Basket

    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

    MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD    50
    FAPECFNGRH VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE 100
    AGGGLTCASA PQGTLRILEG PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC 150
    AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ VTEAPVTQEA VNGHGALEVD 200
    MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE PLGVLFPSTT 250
    KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME 300
    PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV 350
    EPEMKPLESP GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE 400
    TEVVGPELPD DLEPQAAPTS TKKKKKKKER GHTVTEPIQP LEPELPGEGQ 450
    PEARATPGST KKRKKQSQES RMPETVPQEE MPGPPLNSES GEEAPTGRDK 500
    KRKQQQQQPV 510
    Length:510
    Mass (Da):54,986
    Last modified:January 1, 1998 - v1
    Checksum:iD460FB944412D393
    GO
    Isoform 2 (identifier: O15446-2) [UniParc]FASTAAdd to Basket

    Also known as: CAST

    The sequence of this isoform differs from the canonical sequence as follows:
         7-7: G → GGE

    Note: No experimental confirmation available. Has sharply different functional characteristics.

    Show »
    Length:512
    Mass (Da):55,172
    Checksum:i0E5BE70968A5E2C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti218 – 2181N → K in AAH54044. (PubMed:15489334)Curated
    Sequence conflicti422 – 4221Missing in AAI08890. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti259 – 2591K → T.
    Corresponds to variant rs735482 [ dbSNP | Ensembl ].
    VAR_051875
    Natural varianti282 – 2821T → A.
    Corresponds to variant rs3212989 [ dbSNP | Ensembl ].
    VAR_051876
    Natural varianti373 – 3731K → E.
    Corresponds to variant rs762562 [ dbSNP | Ensembl ].
    VAR_051877
    Natural varianti394 – 3941D → N.
    Corresponds to variant rs2336219 [ dbSNP | Ensembl ].
    VAR_051878
    Natural varianti503 – 5031K → Q.
    Corresponds to variant rs3212986 [ dbSNP | Ensembl ].
    VAR_051879
    Natural varianti504 – 5041Q → K.1 Publication
    Corresponds to variant rs3212986 [ dbSNP | Ensembl ].
    VAR_051880

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 71G → GGE in isoform 2. 1 PublicationVSP_017673

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86751 mRNA. Translation: AAB68608.1.
    AF017633 mRNA. Translation: AAD41158.1.
    BC038992 mRNA. Translation: AAH38992.1.
    BC054044 mRNA. Translation: AAH54044.1.
    BC108889 mRNA. Translation: AAI08890.1.
    CCDSiCCDS12661.1. [O15446-1]
    RefSeqiNP_036231.1. NM_012099.1. [O15446-1]
    XP_005258482.1. XM_005258425.1. [O15446-2]
    UniGeneiHs.710495.

    Genome annotation databases

    EnsembliENST00000309424; ENSP00000310966; ENSG00000117877. [O15446-1]
    ENST00000589804; ENSP00000465099; ENSG00000117877. [O15446-2]
    GeneIDi10849.
    KEGGihsa:10849.
    UCSCiuc002pbq.1. human. [O15446-1]
    uc002pbr.1. human. [O15446-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86751 mRNA. Translation: AAB68608.1 .
    AF017633 mRNA. Translation: AAD41158.1 .
    BC038992 mRNA. Translation: AAH38992.1 .
    BC054044 mRNA. Translation: AAH54044.1 .
    BC108889 mRNA. Translation: AAI08890.1 .
    CCDSi CCDS12661.1. [O15446-1 ]
    RefSeqi NP_036231.1. NM_012099.1. [O15446-1 ]
    XP_005258482.1. XM_005258425.1. [O15446-2 ]
    UniGenei Hs.710495.

    3D structure databases

    ProteinModelPortali O15446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116060. 17 interactions.
    DIPi DIP-27616N.
    IntActi O15446. 6 interactions.
    MINTi MINT-1144996.
    STRINGi 9606.ENSP00000310966.

    PTM databases

    PhosphoSitei O15446.

    Proteomic databases

    MaxQBi O15446.
    PaxDbi O15446.
    PRIDEi O15446.

    Protocols and materials databases

    DNASUi 10849.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309424 ; ENSP00000310966 ; ENSG00000117877 . [O15446-1 ]
    ENST00000589804 ; ENSP00000465099 ; ENSG00000117877 . [O15446-2 ]
    GeneIDi 10849.
    KEGGi hsa:10849.
    UCSCi uc002pbq.1. human. [O15446-1 ]
    uc002pbr.1. human. [O15446-2 ]

    Organism-specific databases

    CTDi 10849.
    GeneCardsi GC19P045909.
    HGNCi HGNC:24219. CD3EAP.
    HPAi HPA041664.
    HPA041734.
    MIMi 107325. gene.
    neXtProti NX_O15446.
    PharmGKBi PA142672156.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45026.
    HOGENOMi HOG000120117.
    HOVERGENi HBG082101.
    InParanoidi O15446.
    OMAi FCAFGGN.
    OrthoDBi EOG7VTDPJ.
    PhylomeDBi O15446.
    TreeFami TF338162.

    Miscellaneous databases

    ChiTaRSi CD3EAP. human.
    GeneWikii CD3EAP.
    GenomeRNAii 10849.
    NextBioi 41189.
    PROi O15446.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15446.
    Bgeei O15446.
    CleanExi HS_CAST.
    HS_CD3EAP.
    Genevestigatori O15446.

    Family and domain databases

    InterProi IPR013240. DNA-dir_RNA_pol1_su_RPA34.
    [Graphical view ]
    Pfami PF08208. RNA_polI_A34. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ASE-1: a novel protein of the fibrillar centres of the nucleolus and nucleolus organizer region of mitotic chromosomes."
      Whitehead C.M., Winkfein R.J., Fritzler M.J., Rattner J.B.
      Chromosoma 106:493-502(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Serum.
    2. "CAST, a novel CD3epsilon-binding protein transducing activation signal for interleukin-2 production in T cells."
      Yamazaki T., Hamano Y., Tashiro H., Itoh K., Nakano H., Miyatake S., Saito T.
      J. Biol. Chem. 274:18173-18180(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN T-CELL RECEPTOR SIGNALING, PHOSPHORYLATION, INTERACTION WITH CD3E.
    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), VARIANT LYS-504.
      Tissue: Skin and Testis.
    4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor."
      Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M.
      Mol. Cell. Biol. 26:5436-5448(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH TAF1A AND UBTF, PHOSPHORYLATION AT TYR-80.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-128; SER-136; SER-172; SER-205; SER-285 AND THR-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 SER-136 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPA34_HUMAN
    AccessioniPrimary (citable) accession number: O15446
    Secondary accession number(s): Q32N11, Q7Z5U2, Q9UPF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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 biological function.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3