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Protein

DNA-directed RNA polymerase III subunit RPC7

Gene

POLR3G

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 peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G 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-directed RNA polymerase activity Source: ProtInc

GO - Biological processi

  • cell proliferation Source: MGI
  • defense response to virus Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • positive regulation of innate immune response Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • regulation of transcription from RNA polymerase III promoter Source: ProtInc
  • transcription initiation from RNA polymerase III promoter Source: GO_Central
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 RPC7
Short name:
RNA polymerase III subunit C7
Alternative name(s):
DNA-directed RNA polymerase III subunit G
RNA polymerase III 32 kDa subunit
Short name:
RPC32
Gene namesi
Name:POLR3G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:30075. POLR3G.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134986024.

Polymorphism and mutation databases

BioMutaiPOLR3G.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223DNA-directed RNA polymerase III subunit RPC7PRO_0000073978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei133 – 1331PhosphothreonineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO15318.
MaxQBiO15318.
PaxDbiO15318.
PRIDEiO15318.

PTM databases

iPTMnetiO15318.
PhosphoSiteiO15318.

Expressioni

Gene expression databases

BgeeiO15318.
CleanExiHS_POLR3G.
ExpressionAtlasiO15318. baseline and differential.
GenevisibleiO15318. HS.

Organism-specific databases

HPAiCAB010109.
HPA052658.

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi115867. 14 interactions.
DIPiDIP-59079N.
STRINGi9606.ENSP00000382058.

Structurei

3D structure databases

ProteinModelPortaliO15318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 19650Glu-richAdd
BLAST
Compositional biasi175 – 1817Poly-Asp

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IKHU. Eukaryota.
ENOG4112311. LUCA.
GeneTreeiENSGT00390000002422.
HOGENOMiHOG000293249.
HOVERGENiHBG054922.
InParanoidiO15318.
KOiK03024.
PhylomeDBiO15318.
TreeFamiTF103052.

Family and domain databases

InterProiIPR024661. RNA_pol_III_Rpc31.
[Graphical view]
PANTHERiPTHR15367. PTHR15367. 1 hit.
PfamiPF11705. RNA_pol_3_Rpc31. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGNKGRGRA AYTFNIEAVG FSKGEKLPDV VLKPPPLFPD TDYKPVPLKT
60 70 80 90 100
GEGEEYMLAL KQELRETMKR MPYFIETPEE RQDIERYSKR YMKVYKEEWI
110 120 130 140 150
PDWRRLPREM MPRNKCKKAG PKPKKAKDAG KGTPLTNTED VLKKMEELEK
160 170 180 190 200
RGDGEKSDEE NEEKEGSKEK SKEGDDDDDD DAAEQEEYDE EEQEEENDYI
210 220
NSYFEDGDDF GADSDDNMDE ATY
Length:223
Mass (Da):25,914
Last modified:December 16, 2008 - v2
Checksum:i95E506D527962DD9
GO

Sequence cautioni

The sequence AAB63676.1 differs from that shown. Reason: Frameshift at position 214. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961K → Q in AAB63676 (PubMed:9171375).Curated
Sequence conflicti146 – 1461E → V in AAB63676 (PubMed:9171375).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93868 mRNA. Translation: AAB63676.1. Frameshift.
AK295434 mRNA. Translation: BAG58376.1.
AC027323 Genomic DNA. No translation available.
AC093510 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95980.1.
CCDSiCCDS43337.1.
RefSeqiNP_006458.2. NM_006467.2.
XP_005248461.1. XM_005248404.2.
XP_006714582.1. XM_006714519.2.
XP_006714583.1. XM_006714520.2.
XP_011541402.1. XM_011543100.1.
XP_011541403.1. XM_011543101.1.
XP_011541404.1. XM_011543102.1.
UniGeneiHs.282387.

Genome annotation databases

EnsembliENST00000399107; ENSP00000382058; ENSG00000113356.
ENST00000504930; ENSP00000421637; ENSG00000113356.
GeneIDi10622.
KEGGihsa:10622.
UCSCiuc003kjq.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93868 mRNA. Translation: AAB63676.1. Frameshift.
AK295434 mRNA. Translation: BAG58376.1.
AC027323 Genomic DNA. No translation available.
AC093510 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95980.1.
CCDSiCCDS43337.1.
RefSeqiNP_006458.2. NM_006467.2.
XP_005248461.1. XM_005248404.2.
XP_006714582.1. XM_006714519.2.
XP_006714583.1. XM_006714520.2.
XP_011541402.1. XM_011543100.1.
XP_011541403.1. XM_011543101.1.
XP_011541404.1. XM_011543102.1.
UniGeneiHs.282387.

3D structure databases

ProteinModelPortaliO15318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115867. 14 interactions.
DIPiDIP-59079N.
STRINGi9606.ENSP00000382058.

PTM databases

iPTMnetiO15318.
PhosphoSiteiO15318.

Polymorphism and mutation databases

BioMutaiPOLR3G.

Proteomic databases

EPDiO15318.
MaxQBiO15318.
PaxDbiO15318.
PRIDEiO15318.

Protocols and materials databases

DNASUi10622.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000399107; ENSP00000382058; ENSG00000113356.
ENST00000504930; ENSP00000421637; ENSG00000113356.
GeneIDi10622.
KEGGihsa:10622.
UCSCiuc003kjq.3. human.

Organism-specific databases

CTDi10622.
GeneCardsiPOLR3G.
HGNCiHGNC:30075. POLR3G.
HPAiCAB010109.
HPA052658.
neXtProtiNX_O15318.
PharmGKBiPA134986024.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKHU. Eukaryota.
ENOG4112311. LUCA.
GeneTreeiENSGT00390000002422.
HOGENOMiHOG000293249.
HOVERGENiHBG054922.
InParanoidiO15318.
KOiK03024.
PhylomeDBiO15318.
TreeFamiTF103052.

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

GenomeRNAii10622.
PROiO15318.

Gene expression databases

BgeeiO15318.
CleanExiHS_POLR3G.
ExpressionAtlasiO15318. baseline and differential.
GenevisibleiO15318. HS.

Family and domain databases

InterProiIPR024661. RNA_pol_III_Rpc31.
[Graphical view]
PANTHERiPTHR15367. PTHR15367. 1 hit.
PfamiPF11705. RNA_pol_3_Rpc31. 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 POLR3C AND POLR3F.
    Tissue: Cervix carcinoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Corpus callosum.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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. "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-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPC7_HUMAN
AccessioniPrimary (citable) accession number: O15318
Secondary accession number(s): A8MTH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: December 16, 2008
Last modified: June 8, 2016
This is version 112 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. 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.