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P05423 (RPC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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 III subunit RPC4

Short name=RNA polymerase III subunit C4
Alternative name(s):
DNA-directed RNA polymerase III subunit D
Protein BN51
RNA polymerase III 47 kDa subunit
RPC53 homolog
Gene names
Name:POLR3D
Synonyms:BN51, BN51T
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 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. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway By similarity. Ref.7 Ref.8

Subunit structure

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits By similarity. Interacts with POLR3E/RPC5. Ref.2

Subcellular location

Nucleus.

Sequence similarities

Belongs to the eukaryotic RPC4/POLR3D RNA polymerase subunit family.

Sequence caution

The sequence BC000516 differs from that shown. Reason: Frameshift at position 175.

The sequence BC003039 differs from that shown. Reason: Frameshift at position 175.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
Transcription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

positive regulation of innate immune response

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of interferon-beta production

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

termination of RNA polymerase III transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase III promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase III promoter

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase III complex

Inferred from direct assay PubMed 24107381. Source: MGI

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 398397DNA-directed RNA polymerase III subunit RPC4
PRO_0000073967

Amino acid modifications

Modified residue21N-acetylserine Ref.10

Experimental info

Sequence conflict9 – 1810EPSTPGGPRP → RPARQGPDL in AAA51838. Ref.1
Sequence conflict9 – 124EPST → RPAR in AAA72377. Ref.6
Sequence conflict26 – 4015LIGRR…TPGRL → SSGGGGLPSPPAV Ref.1
Sequence conflict981G → R in AAA51838. Ref.1
Sequence conflict2331K → R in AAM18216. Ref.2
Sequence conflict2861P → L in AAM18216. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P05423 [UniParc].

Last modified March 28, 2003. Version 2.
Checksum: CD8AFF3257B78410

FASTA39844,396
        10         20         30         40         50         60 
MSEGNAAGEP STPGGPRPLL TGARGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP 

        70         80         90        100        110        120 
NIISRKIKEE PKEEVTVKKE KRERDRDRQR EGHGRGRGRP EVIQSHSIFE QGPAEMMKKK 

       130        140        150        160        170        180 
GNWDKTVDVS DMGPSHIINI KKEKRETDEE TKQILRMLEK DDFLDDPGLR NDTRNMPVQL 

       190        200        210        220        230        240 
PLAHSGWLFK EENDEPDVKP WLAGPKEEDM EVDIPAVKVK EEPRDEEEEA KMKAPPKAAR 

       250        260        270        280        290        300 
KTPGLPKDVS VAELLRELSL TKEEELLFLQ LPDTLPGQPP TQDIKPIKTE VQGEDGQVVL 

       310        320        330        340        350        360 
IKQEKDREAK LAENACTLAD LTEGQVGKLL IRKSGRVQLL LGKVTLDVTM GTACSFLQEL 

       370        380        390 
VSVGLGDSRT GEMTVLGHVK HKLVCSPDFE SLLDHKHR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of the human gene that complements a temperature-sensitive cell cycle mutation in BHK cells."
Ittmann M., Greco A., Basilico C.
Mol. Cell. Biol. 7:3386-3393(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits."
Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.
Mol. Cell. Biol. 22:8044-8055(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH POLR3E.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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: Lung and Lymph.
[5]"Reconstitution of transcription from the human U6 small nuclear RNA promoter with eight recombinant polypeptides and a partially purified RNA polymerase III complex."
Chong S.S., Hu P., Hernandez N.
J. Biol. Chem. 276:20727-20734(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-50.
[6]"Promoter structure and cell cycle control of the BN51 cell cycle gene, which encodes a subunit of RNA polymerase III."
Ittmann M.
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[7]"RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway."
Chiu Y.-H., Macmillan J.B., Chen Z.J.
Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate."
Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., Hornung V.
Nat. Immunol. 10:1065-1072(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17754 mRNA. Translation: AAA51838.1.
AY092086 mRNA. Translation: AAM18216.1.
CR536509 mRNA. Translation: CAG38747.1.
CR541803 mRNA. Translation: CAG46602.1.
BC000516 mRNA. No translation available.
BC003039 mRNA. No translation available.
BC002603 mRNA. Translation: AAH02603.1.
BC004484 mRNA. Translation: AAH04484.1.
AF346574 mRNA. Translation: AAK15371.1.
L15301 Genomic DNA. Translation: AAA72377.1.
CCDSCCDS34858.1.
PIRA43700.
RefSeqNP_001713.2. NM_001722.2.
UniGeneHs.148342.

3D structure databases

ProteinModelPortalP05423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107129. 29 interactions.
DIPDIP-56155N.
IntActP05423. 5 interactions.
MINTMINT-3004820.
STRING9606.ENSP00000303088.

Chemistry

BindingDBP05423.

PTM databases

PhosphoSiteP05423.

Polymorphism databases

DMDM29429159.

Proteomic databases

MaxQBP05423.
PaxDbP05423.
PeptideAtlasP05423.
PRIDEP05423.

Protocols and materials databases

DNASU661.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306433; ENSP00000303088; ENSG00000168495.
ENST00000397802; ENSP00000380904; ENSG00000168495.
GeneID661.
KEGGhsa:661.
UCSCuc003xbl.3. human.

Organism-specific databases

CTD661.
GeneCardsGC08P022102.
HGNCHGNC:1080. POLR3D.
MIM187280. gene.
neXtProtNX_P05423.
PharmGKBPA25390.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239914.
HOGENOMHOG000008080.
HOVERGENHBG039777.
InParanoidP05423.
KOK03026.
OMAWDKTVDM.
OrthoDBEOG7J180B.
PhylomeDBP05423.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP05423.
BgeeP05423.
CleanExHS_POLR3D.
GenevestigatorP05423.

Family and domain databases

InterProIPR007811. RPC4.
[Graphical view]
PANTHERPTHR13408. PTHR13408. 1 hit.
PfamPF05132. RNA_pol_Rpc4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPOLR3D.
GenomeRNAi661.
NextBio2690.
PROP05423.
SOURCESearch...

Entry information

Entry nameRPC4_HUMAN
AccessionPrimary (citable) accession number: P05423
Secondary accession number(s): Q6FI28 expand/collapse secondary AC list , Q9BPV7, Q9BPZ1, Q9BXB3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 28, 2003
Last modified: July 9, 2014
This is version 136 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 8

Human chromosome 8: entries, gene names and cross-references to MIM