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UniProtKB/Swiss-Prot entry Q9NW08


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPC2_HUMAN
Primary accession number Q9NW08
Secondary accession number Q9NW59
Integrated into Swiss-Prot on March 28, 2003
Sequence was last modified on March 28, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name DNA-directed RNA polymerase III subunit RPC2
Synonyms RNA polymerase III subunit C2
EC 2.7.7.6
DNA-directed RNA polymerase III subunit B
DNA-directed RNA polymerase III 127.6 kDa polypeptide
C128
Gene name
Name: POLR3B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL III COMPLEX, AND MASS SPECTROMETRY.
DOI=10.1128/MCB.22.22.8044-8055.2002; PubMed=12391170 [NCBI, ExPASy, EBI, Israel, Japan]
Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
"Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits.";
Mol. Cell. Biol. 22:8044-8055(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 751-1133.
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-206, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Comments
  • FUNCTION: 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).
  • CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • SUBUNIT: Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits (By similarity).
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • SIMILARITY: Belongs to the RNA polymerase beta chain family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY092084; AAM18214.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC046238; AAH46238.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001161; BAA91527.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001250; BAA91581.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Hs.610795
3D structure databases
HSSP P08518; 1I50. [HSSP ENTRY / PDB]
ModBase Q9NW08.
PTM databases
PhosphoSite Q9NW08; -.
Enzyme and pathway databases
Reactome REACT_1788; Transcription.
Organism-specific databases
H-InvDB HIX0037055; -.
HGNC HGNC:30348; POLR3B.
GenAtlas POLR3B.
PharmGKB PA134867680; -.
GeneCards Q9NW08.
Gene expression databases
ArrayExpress Q9NW08; -.
CleanEx HS_POLR3B; -.
GermOnline ENSG00000013503; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003899; Molecular function: DNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro 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.
Graphical view of domain structure.
PANTHER PTHR20856; RNA_pol_I_sub2; 1.
Pfam PF04563; RNA_pol_Rpb2_1; 1.
PF04561; RNA_pol_Rpb2_2; 1.
PF04565; RNA_pol_Rpb2_3; 1.
PF04566; RNA_pol_Rpb2_4; 1.
PF04567; RNA_pol_Rpb2_5; 1.
PF00562; RNA_pol_Rpb2_6; 1.
PF04560; RNA_pol_Rpb2_7; 1.
Pfam graphical view of domain structure.
PROSITE PS01166; RNA_POL_BETA; 1.
ProtoNet Q9NW08.
Genome annotation databases
Ensembl ENSG00000013503; Homo sapiens. [Contig view]
NMPDR fig|9606.3.peg.8167; -.
Phylogenomic databases
HOGENOM Q9NW08; -.
HOVERGEN Q9NW08; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Transcription; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1133  1133     DNA-directed RNA polymerase III subunit RPC2. PRO_0000048092
ZN_FING   1080   1095  16     C4-type (By similarity). 
METAL   1080   1080        Zinc (By similarity). 
METAL   1083   1083        Zinc (By similarity). 
METAL   1092   1092        Zinc (By similarity). 
METAL   1095   1095        Zinc (By similarity). 
MOD_RES   202    202        Phosphoserine. 
MOD_RES   206    206        Phosphoserine. 
CONFLICT   258    258        E -> A (in Ref. 1; AAM18214). 
CONFLICT   978    978        R -> C (in Ref. 3; BAA91527). 
Sequence information
Length: 1133 AA [This is the length of the unprocessed precursor] Molecular weight: 127785 Da [This is the MW of the unprocessed precursor] CRC64: F0B3AFF892DDED7D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK 

        70         80         90        100        110        120 
ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH ECRLRDMTYS APITVDIEYT 

       130        140        150        160        170        180 
RGSQRIIRNA LPIGRMPIML RSSNCVLTGK TPAEFAKLNE CPLDPGGYFI VKGVEKVILI 

       190        200        210        220        230        240 
QEQLSKNRII VEADRKGAVG ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIVIIF 

       250        260        270        280        290        300 
KAMGVESDQE IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG 

       310        320        330        340        350        360 
PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK VDDRDYYGNK 

       370        380        390        400        410        420 
RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF DVVKHMRQDQ ITNGMVNAIS 

       430        440        450        460        470        480 
TGNWSLKRFK MDRQGVTQVL SRLSYISALG MMTRISSQFE KTRKVSGPRS LQPSQWGMLC 

       490        500        510        520        530        540 
PSDTPEGEAC GLVKNLALMT HITTDMEDGP IVKLASNLGV EDVNLLCGEE LSYPNVFLVF 

       550        560        570        580        590        600 
LNGNILGVIR DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK 

       610        620        630        640        650        660 
KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI NKDTTHLEIE 

       670        680        690        700        710        720 
PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN QRNRIDTLMY LLAYPQKPMV 

       730        740        750        760        770        780 
KTKTIELIEF EKLPAGQNAT VAVMSYSGYD IEDALVLNKA SLDRGFGRCL VYKNAKCTLK 

       790        800        810        820        830        840 
RYTNQTFDKV MGPMLDAATR KPIWRHEILD ADGICSPGEK VENKQVLVNK SMPTVTQIPL 

       850        860        870        880        890        900 
EGSNVPQQPQ YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTRR PEIGDKFSSR 

       910        920        930        940        950        960 
HGQKGVCGLI VPQEDMPFCD SGICPDIIMN PHGFPSRMTV GKLIELLAGK AGVLDGRFHY 

       970        980        990       1000       1010       1020 
GTAFGGSKVK DVCEDLVRHG YNYLGKDYVT SGITGEPLEA YIYFGPVYYQ KLKHMVLDKM 

      1030       1040       1050       1060       1070       1080 
HARARGPRAV LTRQPTEGRS RDGGLRLGEM ERDCLIGYGA SMLLLERLMI SSDAFEVDVC 

      1090       1100       1110       1120       1130 
GQCGLLGYSG WCHYCKSSCH VSSLRIPYAC KLLFQELQSM NIIPRLKLSK YNE 

Q9NW08 in FASTA format

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