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Q9NW08

- RPC2_HUMAN

UniProt

Q9NW08 - RPC2_HUMAN

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Protein

DNA-directed RNA polymerase III subunit RPC2

Gene

POLR3B

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. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). 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 similarity2 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1080 – 10801ZincBy similarity
Metal bindingi1083 – 10831ZincBy similarity
Metal bindingi1092 – 10921ZincBy similarity
Metal bindingi1095 – 10951ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1080 – 109516C4-typeAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed RNA polymerase activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. ribonucleoside binding Source: InterPro

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 - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Transcription

Keywords - Ligandi

Metal-binding, Zinc

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 RPC2 (EC:2.7.7.6)
Short name:
RNA polymerase III subunit C2
Alternative name(s):
C128
DNA-directed RNA polymerase III 127.6 kDa polypeptide
DNA-directed RNA polymerase III subunit B
Gene namesi
Name:POLR3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:30348. POLR3B.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy, hypomyelinating, 8, with or without oligodontia and/or hypogonadotropic hypogonadism (HLD8) [MIM:614381]: An autosomal recessive neurodegenerative disorder characterized by early childhood onset of cerebellar ataxia and mild intellectual disabilities associated with diffuse hypomyelination apparent on brain MRI. Variable features include oligodontia and/or hypogonadotropic hypogonadism.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti503 – 5031T → K in HLD8. 1 Publication
VAR_067005
Natural varianti523 – 5231V → E in HLD8. 1 Publication
VAR_067006
Natural varianti620 – 65233Missing in HLD8. 1 Publication
VAR_067007Add
BLAST
Natural varianti768 – 7681R → H in HLD8. 1 Publication
VAR_067008
Natural varianti926 – 9261D → E in HLD8. 1 Publication
VAR_067009

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

MIMi614381. phenotype.
Orphaneti88637. Hypomyelination - hypogonadotropic hypogonadism - hypodontia.
PharmGKBiPA134867680.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11331133DNA-directed RNA polymerase III subunit RPC2PRO_0000048092Add
BLAST

Proteomic databases

MaxQBiQ9NW08.
PaxDbiQ9NW08.
PRIDEiQ9NW08.

PTM databases

PhosphoSiteiQ9NW08.

Expressioni

Gene expression databases

BgeeiQ9NW08.
CleanExiHS_POLR3B.
ExpressionAtlasiQ9NW08. baseline and differential.
GenevestigatoriQ9NW08.

Organism-specific databases

HPAiHPA036466.

Interactioni

Subunit structurei

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.By similarity

Protein-protein interaction databases

BioGridi120828. 21 interactions.
IntActiQ9NW08. 1 interaction.
STRINGi9606.ENSP00000228347.

Structurei

3D structure databases

ProteinModelPortaliQ9NW08.
SMRiQ9NW08. Positions 31-498, 880-952, 964-1073.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNA polymerase beta chain family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1080 – 109516C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0085.
GeneTreeiENSGT00760000119346.
HOGENOMiHOG000222962.
HOVERGENiHBG017744.
InParanoidiQ9NW08.
KOiK03021.
OMAiDMIMNPH.
OrthoDBiEOG7288QK.
PhylomeDBiQ9NW08.
TreeFamiTF103047.

Family and domain databases

Gene3Di2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProiIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007646. RNA_pol_Rpb2_4.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
PANTHERiPTHR20856. PTHR20856. 1 hit.
PfamiPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF04566. RNA_pol_Rpb2_4. 1 hit.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEiPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NW08-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF
60 70 80 90 100
INVEIKKIMK ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH
110 120 130 140 150
ECRLRDMTYS APITVDIEYT RGSQRIIRNA LPIGRMPIML RSSNCVLTGK
160 170 180 190 200
TPAEFAKLNE CPLDPGGYFI VKGVEKVILI QEQLSKNRII VEADRKGAVG
210 220 230 240 250
ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIVIIF KAMGVESDQE
260 270 280 290 300
IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG
310 320 330 340 350
PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK
360 370 380 390 400
VDDRDYYGNK RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF
410 420 430 440 450
DVVKHMRQDQ ITNGMVNAIS TGNWSLKRFK MDRQGVTQVL SRLSYISALG
460 470 480 490 500
MMTRISSQFE KTRKVSGPRS LQPSQWGMLC PSDTPEGEAC GLVKNLALMT
510 520 530 540 550
HITTDMEDGP IVKLASNLGV EDVNLLCGEE LSYPNVFLVF LNGNILGVIR
560 570 580 590 600
DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK
610 620 630 640 650
KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI
660 670 680 690 700
NKDTTHLEIE PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN
710 720 730 740 750
QRNRIDTLMY LLAYPQKPMV KTKTIELIEF EKLPAGQNAT VAVMSYSGYD
760 770 780 790 800
IEDALVLNKA SLDRGFGRCL VYKNAKCTLK RYTNQTFDKV MGPMLDAATR
810 820 830 840 850
KPIWRHEILD ADGICSPGEK VENKQVLVNK SMPTVTQIPL EGSNVPQQPQ
860 870 880 890 900
YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTRR PEIGDKFSSR
910 920 930 940 950
HGQKGVCGLI VPQEDMPFCD SGICPDIIMN PHGFPSRMTV GKLIELLAGK
960 970 980 990 1000
AGVLDGRFHY GTAFGGSKVK DVCEDLVRHG YNYLGKDYVT SGITGEPLEA
1010 1020 1030 1040 1050
YIYFGPVYYQ KLKHMVLDKM HARARGPRAV LTRQPTEGRS RDGGLRLGEM
1060 1070 1080 1090 1100
ERDCLIGYGA SMLLLERLMI SSDAFEVDVC GQCGLLGYSG WCHYCKSSCH
1110 1120 1130
VSSLRIPYAC KLLFQELQSM NIIPRLKLSK YNE
Length:1,133
Mass (Da):127,785
Last modified:March 28, 2003 - v2
Checksum:iF0B3AFF892DDED7D
GO
Isoform 2 (identifier: Q9NW08-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Note: No experimental confirmation available.

Show »
Length:1,075
Mass (Da):121,120
Checksum:i48188014A09A87FA
GO

Sequence cautioni

The sequence BAA91527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581E → A in AAM18214. (PubMed:12391170)Curated
Sequence conflicti607 – 6071T → I in BAG53685. (PubMed:14702039)Curated
Sequence conflicti978 – 9781R → C in BAA91527. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti503 – 5031T → K in HLD8. 1 Publication
VAR_067005
Natural varianti523 – 5231V → E in HLD8. 1 Publication
VAR_067006
Natural varianti620 – 65233Missing in HLD8. 1 Publication
VAR_067007Add
BLAST
Natural varianti740 – 7401T → A.
Corresponds to variant rs17038460 [ dbSNP | Ensembl ].
VAR_057255
Natural varianti768 – 7681R → H in HLD8. 1 Publication
VAR_067008
Natural varianti926 – 9261D → E in HLD8. 1 Publication
VAR_067009

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 2. 1 PublicationVSP_045286Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY092084 mRNA. Translation: AAM18214.1.
AK001161 mRNA. Translation: BAA91527.1. Different initiation.
AK001250 mRNA. Translation: BAA91581.1. Different initiation.
AK122713 mRNA. Translation: BAG53685.1.
AK291635 mRNA. Translation: BAF84324.1.
AC009721 Genomic DNA. No translation available.
AC078992 Genomic DNA. No translation available.
AC080012 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97780.1.
BC046238 mRNA. Translation: AAH46238.1.
CCDSiCCDS53824.1. [Q9NW08-2]
CCDS9105.1. [Q9NW08-1]
RefSeqiNP_001154180.1. NM_001160708.1. [Q9NW08-2]
NP_060552.4. NM_018082.5. [Q9NW08-1]
UniGeneiHs.610795.
Hs.62696.

Genome annotation databases

EnsembliENST00000228347; ENSP00000228347; ENSG00000013503. [Q9NW08-1]
ENST00000539066; ENSP00000445721; ENSG00000013503. [Q9NW08-2]
GeneIDi55703.
KEGGihsa:55703.
UCSCiuc001tlp.3. human. [Q9NW08-1]

Polymorphism databases

DMDMi29428029.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY092084 mRNA. Translation: AAM18214.1 .
AK001161 mRNA. Translation: BAA91527.1 . Different initiation.
AK001250 mRNA. Translation: BAA91581.1 . Different initiation.
AK122713 mRNA. Translation: BAG53685.1 .
AK291635 mRNA. Translation: BAF84324.1 .
AC009721 Genomic DNA. No translation available.
AC078992 Genomic DNA. No translation available.
AC080012 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97780.1 .
BC046238 mRNA. Translation: AAH46238.1 .
CCDSi CCDS53824.1. [Q9NW08-2 ]
CCDS9105.1. [Q9NW08-1 ]
RefSeqi NP_001154180.1. NM_001160708.1. [Q9NW08-2 ]
NP_060552.4. NM_018082.5. [Q9NW08-1 ]
UniGenei Hs.610795.
Hs.62696.

3D structure databases

ProteinModelPortali Q9NW08.
SMRi Q9NW08. Positions 31-498, 880-952, 964-1073.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120828. 21 interactions.
IntActi Q9NW08. 1 interaction.
STRINGi 9606.ENSP00000228347.

PTM databases

PhosphoSitei Q9NW08.

Polymorphism databases

DMDMi 29428029.

Proteomic databases

MaxQBi Q9NW08.
PaxDbi Q9NW08.
PRIDEi Q9NW08.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228347 ; ENSP00000228347 ; ENSG00000013503 . [Q9NW08-1 ]
ENST00000539066 ; ENSP00000445721 ; ENSG00000013503 . [Q9NW08-2 ]
GeneIDi 55703.
KEGGi hsa:55703.
UCSCi uc001tlp.3. human. [Q9NW08-1 ]

Organism-specific databases

CTDi 55703.
GeneCardsi GC12P106751.
GeneReviewsi POLR3B.
H-InvDB HIX0037055.
HGNCi HGNC:30348. POLR3B.
HPAi HPA036466.
MIMi 614366. gene.
614381. phenotype.
neXtProti NX_Q9NW08.
Orphaneti 88637. Hypomyelination - hypogonadotropic hypogonadism - hypodontia.
PharmGKBi PA134867680.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0085.
GeneTreei ENSGT00760000119346.
HOGENOMi HOG000222962.
HOVERGENi HBG017744.
InParanoidi Q9NW08.
KOi K03021.
OMAi DMIMNPH.
OrthoDBi EOG7288QK.
PhylomeDBi Q9NW08.
TreeFami TF103047.

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

ChiTaRSi POLR3B. human.
GenomeRNAii 55703.
NextBioi 60549.
PROi Q9NW08.
SOURCEi Search...

Gene expression databases

Bgeei Q9NW08.
CleanExi HS_POLR3B.
ExpressionAtlasi Q9NW08. baseline and differential.
Genevestigatori Q9NW08.

Family and domain databases

Gene3Di 2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProi IPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007646. RNA_pol_Rpb2_4.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view ]
PANTHERi PTHR20856. PTHR20856. 1 hit.
Pfami PF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF04566. RNA_pol_Rpb2_4. 1 hit.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view ]
PROSITEi PS01166. RNA_POL_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1), IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  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] (ISOFORMS 1 AND 2).
    Tissue: Placenta, Teratocarcinoma and Tongue.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 1).
    Tissue: Muscle.
  6. "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.
  7. "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.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Mutations in POLR3A and POLR3B encoding RNA Polymerase III subunits cause an autosomal-recessive hypomyelinating leukoencephalopathy."
    Saitsu H., Osaka H., Sasaki M., Takanashi J., Hamada K., Yamashita A., Shibayama H., Shiina M., Kondo Y., Nishiyama K., Tsurusaki Y., Miyake N., Doi H., Ogata K., Inoue K., Matsumoto N.
    Am. J. Hum. Genet. 89:644-651(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HLD8 620-ASN--LYS-652 DEL; HIS-768 AND GLU-926.
  10. "Recessive mutations in POLR3B, encoding the second largest subunit of Pol III, cause a rare hypomyelinating leukodystrophy."
    Tetreault M., Choquet K., Orcesi S., Tonduti D., Balottin U., Teichmann M., Fribourg S., Schiffmann R., Brais B., Vanderver A., Bernard G.
    Am. J. Hum. Genet. 89:652-655(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HLD8 LYS-503 AND GLU-523.

Entry informationi

Entry nameiRPC2_HUMAN
AccessioniPrimary (citable) accession number: Q9NW08
Secondary accession number(s): A8K6H0
, B3KV73, F5H1E6, Q9NW59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: November 26, 2014
This is version 128 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 12
    Human chromosome 12: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3