Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-directed RNA polymerase III subunit RPC3

Gene

POLR3C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. 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.2 Publications

GO - Molecular functioni

  • DNA binding Source: InterPro
  • DNA-directed RNA polymerase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Transcription

Enzyme and pathway databases

ReactomeiR-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase III subunit RPC3
Short name:
RNA polymerase III subunit C3
Alternative name(s):
DNA-directed RNA polymerase III subunit C
RNA polymerase III 62 kDa subunit
Short name:
RPC62
Gene namesi
Name:POLR3C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30076. POLR3C.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • DNA-directed RNA polymerase III complex Source: MGI
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134870963.

Polymorphism and mutation databases

BioMutaiPOLR3C.
DMDMi60393871.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534DNA-directed RNA polymerase III subunit RPC3PRO_0000073963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BUI4.
MaxQBiQ9BUI4.
PaxDbiQ9BUI4.
PRIDEiQ9BUI4.

PTM databases

iPTMnetiQ9BUI4.
PhosphoSiteiQ9BUI4.

Expressioni

Gene expression databases

BgeeiQ9BUI4.
CleanExiHS_POLR3C.
ExpressionAtlasiQ9BUI4. baseline and differential.
GenevisibleiQ9BUI4. HS.

Organism-specific databases

HPAiHPA027494.
HPA027508.
HPA027516.

Interactioni

Subunit structurei

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits (By similarity). RPC3/POLR3C, RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex. Interacts with GTF3C4 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PNMA5Q96PV43EBI-5452779,EBI-10171633
ROCK1Q134643EBI-5452779,EBI-876651
ROPN1Q9HAT03EBI-5452779,EBI-1378139
TNRA1L3063EBI-5452779,EBI-10182881
TRIM27P143733EBI-5452779,EBI-719493

Protein-protein interaction databases

BioGridi115868. 43 interactions.
DIPiDIP-59078N.
IntActiQ9BUI4. 7 interactions.
STRINGi9606.ENSP00000334564.

Structurei

Secondary structure

1
534
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 3129Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 438Combined sources
Helixi47 – 5913Combined sources
Beta strandi62 – 687Combined sources
Turni69 – 713Combined sources
Beta strandi72 – 776Combined sources
Helixi79 – 835Combined sources
Helixi84 – 874Combined sources
Helixi88 – 11326Combined sources
Helixi118 – 13114Combined sources
Beta strandi133 – 1364Combined sources
Helixi141 – 15313Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi234 – 2374Combined sources
Helixi239 – 25820Combined sources
Helixi261 – 27212Combined sources
Turni273 – 2775Combined sources
Helixi290 – 2956Combined sources
Helixi305 – 31612Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi333 – 3375Combined sources
Helixi338 – 35821Combined sources
Helixi360 – 37112Combined sources
Helixi377 – 3848Combined sources
Helixi388 – 40013Combined sources
Helixi428 – 45629Combined sources
Helixi458 – 47215Combined sources
Helixi485 – 4884Combined sources
Helixi493 – 52937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUBX-ray2.80A1-534[»]
2XV4X-ray2.95S1-534[»]
5AFQX-ray7.00A/B1-534[»]
ProteinModelPortaliQ9BUI4.
SMRiQ9BUI4. Positions 1-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BUI4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2587. Eukaryota.
ENOG410XPVH. LUCA.
GeneTreeiENSGT00390000002799.
HOGENOMiHOG000046475.
HOVERGENiHBG059543.
InParanoidiQ9BUI4.
KOiK03023.
OMAiNQLPTAR.
PhylomeDBiQ9BUI4.
TreeFamiTF103048.

Family and domain databases

InterProiIPR013197. RNA_pol_III_RPC82-rel_HTH.
IPR008806. RNA_pol_III_Rpc82_C.
[Graphical view]
PfamiPF08221. HTH_9. 1 hit.
PF05645. RNA_pol_Rpc82. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BUI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV
60 70 80 90 100
KKALCVLVQH NLVSYQVHKR GVVEYEAQCS RVLRMLRYPR YIYTTKTLYS
110 120 130 140 150
DTGELIVEEL LLNGKLTMSA VVKKVADRLT ETMEDGKTMD YAEVSNTFVR
160 170 180 190 200
LADTHFVQRC PSVPTTENSD PGPPPPAPTL VINEKDMYLV PKLSLIGKGK
210 220 230 240 250
RRRSSDEDAA GEPKAKRPKY TTDNKEPIPD DGIYWQANLD RFHQHFRDQA
260 270 280 290 300
IVSAVANRMD QTSSEIVRTM LRMSEITTSS SAPFTQPLSS NEIFRSLPVG
310 320 330 340 350
YNISKQVLDQ YLTLLADDPL EFVGKSGDSG GGMYVINLHK ALASLATATL
360 370 380 390 400
ESVVQERFGS RCARIFRLVL QKKHIEQKQV EDFAMIPAKE AKDMLYKMLS
410 420 430 440 450
ENFMSLQEIP KTPDHAPSRT FYLYTVNILS AARMLLHRCY KSIANLIERR
460 470 480 490 500
QFETKENKRL LEKSQRVEAI IASMQATGAE EAQLQEIEEM ITAPERQQLE
510 520 530
TLKRNVNKLD ASEIQVDETI FLLESYIECT MKRQ
Length:534
Mass (Da):60,612
Last modified:June 1, 2001 - v1
Checksum:i0E4CFEE295EE1A55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 862ML → IV in AAB63675 (PubMed:9171375).Curated
Sequence conflicti119 – 1202SA → CT in AAB63675 (PubMed:9171375).Curated
Sequence conflicti216 – 23722KRPKY…IYWQA → RDQNILQITRXPFQMMGFIG RP in AAB63675 (PubMed:9171375).CuratedAdd
BLAST
Sequence conflicti289 – 2891S → F in AAB63675 (PubMed:9171375).Curated
Sequence conflicti343 – 3431A → R in AAB63675 (PubMed:9171375).Curated
Sequence conflicti366 – 3661F → C in AAB63675 (PubMed:9171375).Curated
Sequence conflicti387 – 3893PAK → LQ in AAB63675 (PubMed:9171375).Curated
Sequence conflicti401 – 4011E → G in AAB63675 (PubMed:9171375).Curated
Sequence conflicti436 – 4372LH → FD in AAB63675 (PubMed:9171375).Curated
Sequence conflicti517 – 5171D → E in CAB41919 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti243 – 2431H → R.1 Publication
Corresponds to variant rs1044697 [ dbSNP | Ensembl ].
VAR_019083

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93867 mRNA. Translation: AAB63675.1.
AY091463 mRNA. Translation: AAM12033.1.
AJ238221
, AJ238222, AJ238223, AJ238224, AJ238225, AJ238226, AJ238227, AJ238228, AJ238229, AJ238230, AJ238231, AJ238232, AJ238233, AJ238234 Genomic DNA. Translation: CAB41919.1.
BC002586 mRNA. Translation: AAH02586.1.
CCDSiCCDS72864.1.
RefSeqiNP_001290385.1. NM_001303456.1.
NP_006459.3. NM_006468.7.
UniGeneiHs.515768.
Hs.591457.

Genome annotation databases

EnsembliENST00000334163; ENSP00000334564; ENSG00000186141.
GeneIDi10623.
KEGGihsa:10623.
UCSCiuc001eoh.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93867 mRNA. Translation: AAB63675.1.
AY091463 mRNA. Translation: AAM12033.1.
AJ238221
, AJ238222, AJ238223, AJ238224, AJ238225, AJ238226, AJ238227, AJ238228, AJ238229, AJ238230, AJ238231, AJ238232, AJ238233, AJ238234 Genomic DNA. Translation: CAB41919.1.
BC002586 mRNA. Translation: AAH02586.1.
CCDSiCCDS72864.1.
RefSeqiNP_001290385.1. NM_001303456.1.
NP_006459.3. NM_006468.7.
UniGeneiHs.515768.
Hs.591457.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUBX-ray2.80A1-534[»]
2XV4X-ray2.95S1-534[»]
5AFQX-ray7.00A/B1-534[»]
ProteinModelPortaliQ9BUI4.
SMRiQ9BUI4. Positions 1-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115868. 43 interactions.
DIPiDIP-59078N.
IntActiQ9BUI4. 7 interactions.
STRINGi9606.ENSP00000334564.

PTM databases

iPTMnetiQ9BUI4.
PhosphoSiteiQ9BUI4.

Polymorphism and mutation databases

BioMutaiPOLR3C.
DMDMi60393871.

Proteomic databases

EPDiQ9BUI4.
MaxQBiQ9BUI4.
PaxDbiQ9BUI4.
PRIDEiQ9BUI4.

Protocols and materials databases

DNASUi10623.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334163; ENSP00000334564; ENSG00000186141.
GeneIDi10623.
KEGGihsa:10623.
UCSCiuc001eoh.3. human.

Organism-specific databases

CTDi10623.
GeneCardsiPOLR3C.
HGNCiHGNC:30076. POLR3C.
HPAiHPA027494.
HPA027508.
HPA027516.
neXtProtiNX_Q9BUI4.
PharmGKBiPA134870963.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2587. Eukaryota.
ENOG410XPVH. LUCA.
GeneTreeiENSGT00390000002799.
HOGENOMiHOG000046475.
HOVERGENiHBG059543.
InParanoidiQ9BUI4.
KOiK03023.
OMAiNQLPTAR.
PhylomeDBiQ9BUI4.
TreeFamiTF103048.

Enzyme and pathway databases

ReactomeiR-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Miscellaneous databases

ChiTaRSiPOLR3C. human.
EvolutionaryTraceiQ9BUI4.
GeneWikiiPOLR3C.
GenomeRNAii10623.
NextBioi40364.
PROiQ9BUI4.

Gene expression databases

BgeeiQ9BUI4.
CleanExiHS_POLR3C.
ExpressionAtlasiQ9BUI4. baseline and differential.
GenevisibleiQ9BUI4. HS.

Family and domain databases

InterProiIPR013197. RNA_pol_III_RPC82-rel_HTH.
IPR008806. RNA_pol_III_Rpc82_C.
[Graphical view]
PfamiPF08221. HTH_9. 1 hit.
PF05645. RNA_pol_Rpc82. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation."
    Wang Z., Roeder R.G.
    Genes Dev. 11:1315-1326(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR3G AND POLR3F, VARIANT ARG-243.
    Tissue: Cervix carcinoma.
  2. "Identification of an immunodominant epitope on RNA polymerase III recognized by systemic sclerosis sera: application to enzyme-linked immunosorbent assay."
    Kuwana M., Kimura K., Kawakami Y.
    Arthritis Rheum. 46:2742-2747(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION AS ANTIGEN IN SYSTEMIC SCLEROSIS.
  3. "Genomic structure of human RNA polymerase III subunit (RPC62)."
    Totaro A.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: Ovary.
  5. "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity."
    Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.
    Mol. Cell. Biol. 19:7697-7704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GTF3C4.
  6. "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: IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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.
  9. "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.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPC3_HUMAN
AccessioniPrimary (citable) accession number: Q9BUI4
Secondary accession number(s): O15317, Q9Y3R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: June 1, 2001
Last modified: April 13, 2016
This is version 124 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

Antibodies against POLR3C have been found in the sera of patients with systemic sclerosis (SSc).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.