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P05423

- RPC4_HUMAN

UniProt

P05423 - RPC4_HUMAN

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Protein

DNA-directed RNA polymerase III subunit RPC4

Gene

POLR3D

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. 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).By similarity

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA binding Source: InterPro
  3. DNA-directed RNA polymerase activity Source: UniProtKB-KW

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. innate immune response Source: Reactome
  4. positive regulation of innate immune response Source: UniProtKB
  5. positive regulation of interferon-beta production Source: UniProtKB
  6. positive regulation of type I interferon production Source: Reactome
  7. termination of RNA polymerase III transcription Source: Reactome
  8. transcription elongation from RNA polymerase III promoter Source: Reactome
  9. transcription from RNA polymerase III promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Transcription

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_63. RNA Polymerase III Transcription Termination.
REACT_756. RNA Polymerase III Chain Elongation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:POLR3D
Synonyms:BN51, BN51T
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:1080. POLR3D.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. DNA-directed RNA polymerase III complex Source: MGI
  3. nuclear chromatin Source: Ensembl
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 398397DNA-directed RNA polymerase III subunit RPC4PRO_0000073967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP05423.
PaxDbiP05423.
PeptideAtlasiP05423.
PRIDEiP05423.

PTM databases

PhosphoSiteiP05423.

Expressioni

Gene expression databases

BgeeiP05423.
CleanExiHS_POLR3D.
ExpressionAtlasiP05423. baseline and differential.
GenevestigatoriP05423.

Interactioni

Subunit structurei

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits (By similarity). Interacts with POLR3E/RPC5.By similarity1 Publication

Protein-protein interaction databases

BioGridi107129. 33 interactions.
DIPiDIP-56155N.
IntActiP05423. 5 interactions.
MINTiMINT-3004820.
STRINGi9606.ENSP00000303088.

Structurei

3D structure databases

ProteinModelPortaliP05423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG239914.
GeneTreeiENSGT00390000013948.
HOGENOMiHOG000008080.
HOVERGENiHBG039777.
InParanoidiP05423.
KOiK03026.
OMAiWDKTVDM.
OrthoDBiEOG7J180B.
PhylomeDBiP05423.

Family and domain databases

InterProiIPR007811. RPC4.
[Graphical view]
PANTHERiPTHR13408. PTHR13408. 1 hit.
PfamiPF05132. RNA_pol_Rpc4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05423-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEGNAAGEP STPGGPRPLL TGARGLIGRR PAPPLTPGRL PSIRSRDLTL
60 70 80 90 100
GGVKKKTFTP NIISRKIKEE PKEEVTVKKE KRERDRDRQR EGHGRGRGRP
110 120 130 140 150
EVIQSHSIFE QGPAEMMKKK GNWDKTVDVS DMGPSHIINI KKEKRETDEE
160 170 180 190 200
TKQILRMLEK DDFLDDPGLR NDTRNMPVQL PLAHSGWLFK EENDEPDVKP
210 220 230 240 250
WLAGPKEEDM EVDIPAVKVK EEPRDEEEEA KMKAPPKAAR KTPGLPKDVS
260 270 280 290 300
VAELLRELSL TKEEELLFLQ LPDTLPGQPP TQDIKPIKTE VQGEDGQVVL
310 320 330 340 350
IKQEKDREAK LAENACTLAD LTEGQVGKLL IRKSGRVQLL LGKVTLDVTM
360 370 380 390
GTACSFLQEL VSVGLGDSRT GEMTVLGHVK HKLVCSPDFE SLLDHKHR
Length:398
Mass (Da):44,396
Last modified:March 28, 2003 - v2
Checksum:iCD8AFF3257B78410
GO

Sequence cautioni

The sequence BC000516 differs from that shown. Reason: Frameshift at position 175. Curated
The sequence BC003039 differs from that shown. Reason: Frameshift at position 175. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 1810EPSTPGGPRP → RPARQGPDL in AAA51838. (PubMed:3683386)Curated
Sequence conflicti9 – 124EPST → RPAR in AAA72377. 1 PublicationCurated
Sequence conflicti26 – 4015LIGRR…TPGRL → SSGGGGLPSPPAV(PubMed:3683386)CuratedAdd
BLAST
Sequence conflicti98 – 981G → R in AAA51838. (PubMed:3683386)Curated
Sequence conflicti233 – 2331K → R in AAM18216. (PubMed:12391170)Curated
Sequence conflicti286 – 2861P → L in AAM18216. (PubMed:12391170)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34858.1.
PIRiA43700.
RefSeqiNP_001713.2. NM_001722.2.
UniGeneiHs.148342.

Genome annotation databases

EnsembliENST00000306433; ENSP00000303088; ENSG00000168495.
ENST00000397802; ENSP00000380904; ENSG00000168495.
GeneIDi661.
KEGGihsa:661.
UCSCiuc003xbl.3. human.

Polymorphism databases

DMDMi29429159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS34858.1.
PIRi A43700.
RefSeqi NP_001713.2. NM_001722.2.
UniGenei Hs.148342.

3D structure databases

ProteinModelPortali P05423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107129. 33 interactions.
DIPi DIP-56155N.
IntActi P05423. 5 interactions.
MINTi MINT-3004820.
STRINGi 9606.ENSP00000303088.

PTM databases

PhosphoSitei P05423.

Polymorphism databases

DMDMi 29429159.

Proteomic databases

MaxQBi P05423.
PaxDbi P05423.
PeptideAtlasi P05423.
PRIDEi P05423.

Protocols and materials databases

DNASUi 661.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306433 ; ENSP00000303088 ; ENSG00000168495 .
ENST00000397802 ; ENSP00000380904 ; ENSG00000168495 .
GeneIDi 661.
KEGGi hsa:661.
UCSCi uc003xbl.3. human.

Organism-specific databases

CTDi 661.
GeneCardsi GC08P022102.
HGNCi HGNC:1080. POLR3D.
MIMi 187280. gene.
neXtProti NX_P05423.
PharmGKBi PA25390.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239914.
GeneTreei ENSGT00390000013948.
HOGENOMi HOG000008080.
HOVERGENi HBG039777.
InParanoidi P05423.
KOi K03026.
OMAi WDKTVDM.
OrthoDBi EOG7J180B.
PhylomeDBi P05423.

Enzyme and pathway databases

Reactomei REACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_63. RNA Polymerase III Transcription Termination.
REACT_756. RNA Polymerase III Chain Elongation.

Miscellaneous databases

GeneWikii POLR3D.
GenomeRNAii 661.
NextBioi 2690.
PROi P05423.
SOURCEi Search...

Gene expression databases

Bgeei P05423.
CleanExi HS_POLR3D.
ExpressionAtlasi P05423. baseline and differential.
Genevestigatori P05423.

Family and domain databases

InterProi IPR007811. RPC4.
[Graphical view ]
PANTHERi PTHR13408. PTHR13408. 1 hit.
Pfami PF05132. RNA_pol_Rpc4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPC4_HUMAN
AccessioniPrimary (citable) accession number: P05423
Secondary accession number(s): Q6FI28
, Q9BPV7, Q9BPZ1, Q9BXB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 28, 2003
Last modified: November 26, 2014
This is version 140 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3