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O15446 (RPA34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CD3EAP
Synonyms:ASE1, CAST, PAF49
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.2 Ref.5

Isoform 2 has been described as a component of preformed T-cell receptor (TCR) complex. Ref.2 Ref.5

Subunit structure

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. Ref.2 Ref.5

Subcellular location

Nucleusnucleolus. Chromosome. 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. Ref.1

Post-translational modification

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. Ref.2 Ref.5

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.

Sequence similarities

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15446-1)

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.
Isoform 2 (identifier: O15446-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510DNA-directed RNA polymerase I subunit RPA34
PRO_0000228120

Regions

Compositional bias174 – 1774Poly-Lys
Compositional bias212 – 2176Poly-Lys
Compositional bias422 – 4287Poly-Lys
Compositional bias504 – 5085Poly-Gln

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.12
Modified residue271Phosphoserine Ref.7
Modified residue801Phosphotyrosine Ref.5
Modified residue1281Phosphoserine Ref.7
Modified residue1361Phosphoserine Ref.7 Ref.9 Ref.11
Modified residue1721Phosphoserine Ref.7 Ref.10
Modified residue2051Phosphoserine Ref.7
Modified residue2851Phosphoserine Ref.7 Ref.10 Ref.11
Modified residue2871Phosphothreonine Ref.7
Modified residue3091Phosphoserine Ref.6
Modified residue4901Phosphoserine Ref.9

Natural variations

Alternative sequence71G → GGE in isoform 2.
VSP_017673
Natural variant2591K → T.
Corresponds to variant rs735482 [ dbSNP | Ensembl ].
VAR_051875
Natural variant2821T → A.
Corresponds to variant rs3212989 [ dbSNP | Ensembl ].
VAR_051876
Natural variant3731K → E.
Corresponds to variant rs762562 [ dbSNP | Ensembl ].
VAR_051877
Natural variant3941D → N.
Corresponds to variant rs2336219 [ dbSNP | Ensembl ].
VAR_051878
Natural variant5031K → Q.
Corresponds to variant rs3212986 [ dbSNP | Ensembl ].
VAR_051879
Natural variant5041Q → K. Ref.3
Corresponds to variant rs3212986 [ dbSNP | Ensembl ].
VAR_051880

Experimental info

Sequence conflict2181N → K in AAH54044. Ref.3
Sequence conflict4221Missing in AAI08890. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D460FB944412D393

FASTA51054,986
        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 

« Hide

Isoform 2 (CAST) [UniParc].

Checksum: 0E5BE70968A5E2C9
Show »

FASTA51255,172

References

« Hide 'large scale' references
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12661.1. [O15446-1]
RefSeqNP_036231.1. NM_012099.1. [O15446-1]
XP_005258482.1. XM_005258425.1. [O15446-2]
UniGeneHs.710495.

3D structure databases

ProteinModelPortalO15446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116060. 16 interactions.
DIPDIP-27616N.
IntActO15446. 6 interactions.
MINTMINT-1144996.
STRING9606.ENSP00000310966.

PTM databases

PhosphoSiteO15446.

Proteomic databases

MaxQBO15446.
PaxDbO15446.
PRIDEO15446.

Protocols and materials databases

DNASU10849.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309424; ENSP00000310966; ENSG00000117877. [O15446-1]
ENST00000589804; ENSP00000465099; ENSG00000117877. [O15446-2]
GeneID10849.
KEGGhsa:10849.
UCSCuc002pbq.1. human. [O15446-1]
uc002pbr.1. human. [O15446-2]

Organism-specific databases

CTD10849.
GeneCardsGC19P045909.
HGNCHGNC:24219. CD3EAP.
HPAHPA041664.
HPA041734.
MIM107325. gene.
neXtProtNX_O15446.
PharmGKBPA142672156.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45026.
HOGENOMHOG000120117.
HOVERGENHBG082101.
InParanoidO15446.
OMAFCAFGGN.
OrthoDBEOG7VTDPJ.
PhylomeDBO15446.
TreeFamTF338162.

Gene expression databases

ArrayExpressO15446.
BgeeO15446.
CleanExHS_CAST.
HS_CD3EAP.
GenevestigatorO15446.

Family and domain databases

InterProIPR013240. DNA-dir_RNA_pol1_su_RPA34.
[Graphical view]
PfamPF08208. RNA_polI_A34. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD3EAP. human.
GeneWikiCD3EAP.
GenomeRNAi10849.
NextBio41189.
PROO15446.
SOURCESearch...

Entry information

Entry nameRPA34_HUMAN
AccessionPrimary (citable) accession number: O15446
Secondary accession number(s): Q32N11, Q7Z5U2, Q9UPF6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM