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O15446

- RPA34_HUMAN

UniProt

O15446 - RPA34_HUMAN

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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

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
Complete GO annotation...

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-KW
  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
Complete GO annotation...

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 – 271Phosphoserine1 Publication
Modified residuei80 – 801Phosphotyrosine1 Publication
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei136 – 1361Phosphoserine3 Publications
Modified residuei172 – 1721Phosphoserine2 Publications
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei285 – 2851Phosphoserine3 Publications
Modified residuei287 – 2871Phosphothreonine1 Publication
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei490 – 4901Phosphoserine1 Publication

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

BgeeiO15446.
CleanExiHS_CAST.
HS_CD3EAP.
ExpressionAtlasiO15446. baseline and differential.
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. 19 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.
GeneTreeiENSGT00450000040362.
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

        10         20         30         40         50
MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD
60 70 80 90 100
FAPECFNGRH VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE
110 120 130 140 150
AGGGLTCASA PQGTLRILEG PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC
160 170 180 190 200
AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ VTEAPVTQEA VNGHGALEVD
210 220 230 240 250
MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE PLGVLFPSTT
260 270 280 290 300
KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME
310 320 330 340 350
PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV
360 370 380 390 400
EPEMKPLESP GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE
410 420 430 440 450
TEVVGPELPD DLEPQAAPTS TKKKKKKKER GHTVTEPIQP LEPELPGEGQ
460 470 480 490 500
PEARATPGST KKRKKQSQES RMPETVPQEE MPGPPLNSES GEEAPTGRDK
510
KRKQQQQQPV
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]
CCDS74397.1. [O15446-2]
RefSeqiNP_001284519.1. NM_001297590.1. [O15446-2]
NP_036231.1. NM_012099.1. [O15446-1]
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 ]
CCDS74397.1. [O15446-2 ]
RefSeqi NP_001284519.1. NM_001297590.1. [O15446-2 ]
NP_036231.1. NM_012099.1. [O15446-1 ]
UniGenei Hs.710495.

3D structure databases

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

Protein-protein interaction databases

BioGridi 116060. 19 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.
GeneTreei ENSGT00450000040362.
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

Bgeei O15446.
CleanExi HS_CAST.
HS_CD3EAP.
ExpressionAtlasi O15446. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 112 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