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P19387 (RPB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
DNA-directed RNA polymerase II subunit RPB3

Short name=RNA polymerase II subunit 3
Short name=RNA polymerase II subunit B3
Alternative name(s):
DNA-directed RNA polymerase II 33 kDa polypeptide
Short name=RPB33
DNA-directed RNA polymerase II subunit C
RPB31
Gene names
Name:POLR2C
ORF Names:A-152E5.7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft By similarity. Ref.7

Subunit structure

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB11/POLR2J and RPB3/POLR2C subunits interact with each other. Ref.7

Subcellular location

Nucleus Ref.7.

Sequence similarities

Belongs to the archaeal RpoD/eukaryotic RPB3 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase II, core complex

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 275274DNA-directed RNA polymerase II subunit RPB3
PRO_0000132743

Regions

Compositional bias88 – 9710Cys-rich

Amino acid modifications

Modified residue1241Phosphoserine Ref.8

Experimental info

Sequence conflict1941H → T Ref.1
Sequence conflict1941H → T Ref.3

Sequences

Sequence LengthMass (Da)Tools
P19387 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: EF663BE096046A4B

FASTA27531,441
        10         20         30         40         50         60 
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH 

        70         80         90        100        110        120 
DEFIAHRLGL IPLISDDIVD KLQYSRDCTC EEFCPECSVE FTLDVRCNED QTRHVTSRDL 

       130        140        150        160        170        180 
ISNSPRVIPV TSRNRDNDPN DYVEQDDILI VKLRKGQELR LRAYAKKGFG KEHAKWNPTA 

       190        200        210        220        230        240 
GVAFEYDPDN ALRHTVYPKP EEWPKSEYSE LDEDESQAPY DPNGKPERFY YNVESCGSLR 

       250        260        270 
PETIVLSALS GLKKKLSDLQ TQLSHEIQSD VLTIN 

« Hide

References

« Hide 'large scale' references
[1]"The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB 33 is highly conserved among eukaryotes."
Pati U.K., Weissman S.M.
J. Biol. Chem. 265:8400-8403(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and characterization of the human RNA polymerase I subunit hRPA40."
Dammann R., Pfeifer G.P.
Biochim. Biophys. Acta 1396:153-157(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Bruno T., di Padova M., de Angelis R., Iacobini C., Lovari S., Passananti C., Fanciulli M.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[4]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Brain, Kidney and Muscle.
[6]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-35; 68-86; 134-152; 176-193 AND 256-275, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
Kershnar E., Wu S.-Y., Chiang C.-M.
J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
[8]"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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05448 mRNA. Translation: AAA36586.1.
AF008443 mRNA. Translation: AAC14355.1.
AJ224143 mRNA. Translation: CAA11842.1.
AJ224144 mRNA. Translation: CAA11843.1.
AC004382 Genomic DNA. Translation: AAC24309.1.
BC000409 mRNA. Translation: AAH00409.1.
BC003159 mRNA. Translation: AAH03159.1.
BC028157 mRNA. Translation: AAH28157.1.
CCDSCCDS10782.1.
PIRA36264.
RefSeqNP_116558.1. NM_032940.2.
UniGeneHs.79402.

3D structure databases

ProteinModelPortalP19387.
SMRP19387. Positions 7-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111428. 91 interactions.
DIPDIP-32911N.
IntActP19387. 18 interactions.
MINTMINT-270053.
STRING9606.ENSP00000219252.

PTM databases

PhosphoSiteP19387.

Polymorphism databases

DMDM3915850.

Proteomic databases

MaxQBP19387.
PaxDbP19387.
PeptideAtlasP19387.
PRIDEP19387.

Protocols and materials databases

DNASU5432.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219252; ENSP00000219252; ENSG00000102978.
GeneID5432.
KEGGhsa:5432.
UCSCuc002elt.1. human.

Organism-specific databases

CTD5432.
GeneCardsGC16P057496.
HGNCHGNC:9189. POLR2C.
HPAHPA040919.
HPA041826.
MIM180663. gene.
neXtProtNX_P19387.
PharmGKBPA33509.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0202.
HOVERGENHBG000897.
InParanoidP19387.
KOK03011.
OMAPINTEEF.
OrthoDBEOG70S761.
PhylomeDBP19387.
TreeFamTF103038.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP19387.
BgeeP19387.
CleanExHS_POLR2C.
GenevestigatorP19387.

Family and domain databases

Gene3D2.170.120.12. 1 hit.
InterProIPR001514. DNA-dir_RNA_pol_30-40kDasu_CS.
IPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR009025. RBP11-like_dimer.
[Graphical view]
PfamPF01000. RNA_pol_A_bac. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view]
SMARTSM00662. RPOLD. 1 hit.
[Graphical view]
SUPFAMSSF55257. SSF55257. 2 hits.
SSF56553. SSF56553. 1 hit.
PROSITEPS00446. RNA_POL_D_30KD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPOLR2C.
GenomeRNAi5432.
NextBio21017.
PROP19387.
SOURCESearch...

Entry information

Entry nameRPB3_HUMAN
AccessionPrimary (citable) accession number: P19387
Secondary accession number(s): O15161
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 153 of the entry and version 2 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM