Q9NW08 (RPC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase III subunit RPC2
Short name=RNA polymerase III subunit C2
EC=2.7.7.6

Alternative name(s):
C128
DNA-directed RNA polymerase III 127.6 kDa polypeptide
DNA-directed RNA polymerase III subunit B

Gene names

Name:

POLR3B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1133 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. 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. Ref.6 Ref.7
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits By similarity. Ref.1
Subcellular location	Nucleus By similarity.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10
Sequence similarities	Belongs to the RNA polymerase beta chain family.
Sequence caution	The sequence BAA91527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA91581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Leukodystrophy
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of innate immune response Inferred from mutant phenotype Ref.7. Source: UniProtKB positive regulation of interferon-beta production Inferred from mutant phenotype Ref.7. Source: UniProtKB termination of RNA polymerase III transcription Traceable author statement. Source: Reactome transcription elongation from RNA polymerase III promoter Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NW08-1)

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.

Isoform 2 (identifier: Q9NW08-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1133	1133	DNA-directed RNA polymerase III subunit RPC2		PRO_0000048092
Regions
	Zinc finger	1080 – 1095	16	C4-type
Sites
	Metal binding	1080	1	Zinc By similarity
	Metal binding	1083	1	Zinc By similarity
	Metal binding	1092	1	Zinc By similarity
	Metal binding	1095	1	Zinc By similarity
Natural variations
	Alternative sequence	1 – 58	58	Missing in isoform 2.		VSP_045286
	Natural variant	503	1	T → K in HLD8. Ref.10		VAR_067005
	Natural variant	523	1	V → E in HLD8. Ref.10		VAR_067006
	Natural variant	620 – 652	33	Missing in HLD8.		VAR_067007
	Natural variant	740	1	T → A. Corresponds to variant rs17038460 [ dbSNP | Ensembl ].		VAR_057255
	Natural variant	768	1	R → H in HLD8. Ref.9		VAR_067008
	Natural variant	926	1	D → E in HLD8. Ref.9		VAR_067009
Experimental info
	Sequence conflict	258	1	E → A in AAM18214. Ref.1
	Sequence conflict	607	1	T → I in BAG53685. Ref.2
	Sequence conflict	978	1	R → C in BAA91527. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 28, 2003. Version 2. Checksum: F0B3AFF892DDED7D	FASTA	1,133	127,785
	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
	Isoform 2 [UniParc]. Checksum: 48188014A09A87FA	FASTA	1,075	121,120
	10 20 30 40 50 60 MKANEKVTSD ADPMWYLKYL NIYVGLPDVE ESFNVTRPVS PHECRLRDMT YSAPITVDIE 70 80 90 100 110 120 YTRGSQRIIR NALPIGRMPI MLRSSNCVLT GKTPAEFAKL NECPLDPGGY FIVKGVEKVI 130 140 150 160 170 180 LIQEQLSKNR IIVEADRKGA VGASVTSSTH EKKSRTNMAV KQGRFYLRHN TLSEDIPIVI 190 200 210 220 230 240 IFKAMGVESD QEIVQMIGTE EHVMAAFGPS LEECQKAQIF TQMQALKYIG NKVRRQRMWG 250 260 270 280 290 300 GGPKKTKIEE ARELLASTIL THVPVKEFNF RAKCIYTAVM VRRVILAQGD NKVDDRDYYG 310 320 330 340 350 360 NKRLELAGQL LSLLFEDLFK KFNSEMKKIA DQVIPKQRAA QFDVVKHMRQ DQITNGMVNA 370 380 390 400 410 420 ISTGNWSLKR FKMDRQGVTQ VLSRLSYISA LGMMTRISSQ FEKTRKVSGP RSLQPSQWGM 430 440 450 460 470 480 LCPSDTPEGE ACGLVKNLAL MTHITTDMED GPIVKLASNL GVEDVNLLCG EELSYPNVFL 490 500 510 520 530 540 VFLNGNILGV IRDHKKLVNT FRLMRRAGYI NEFVSISTNL TDRCVYISSD GGRLCRPYII 550 560 570 580 590 600 VKKQKPAVTN KHMEELAQGY RNFEDFLHES LVEYLDVNEE NDCNIALYEH TINKDTTHLE 610 620 630 640 650 660 IEPFTLLGVC AGLIPYPHHN QSPRNTYQCA MGKQAMGTIG YNQRNRIDTL MYLLAYPQKP 670 680 690 700 710 720 MVKTKTIELI EFEKLPAGQN ATVAVMSYSG YDIEDALVLN KASLDRGFGR CLVYKNAKCT 730 740 750 760 770 780 LKRYTNQTFD KVMGPMLDAA TRKPIWRHEI LDADGICSPG EKVENKQVLV NKSMPTVTQI 790 800 810 820 830 840 PLEGSNVPQQ PQYKDVPITY KGATDSYIEK VMISSNAEDA FLIKMLLRQT RRPEIGDKFS 850 860 870 880 890 900 SRHGQKGVCG LIVPQEDMPF CDSGICPDII MNPHGFPSRM TVGKLIELLA GKAGVLDGRF 910 920 930 940 950 960 HYGTAFGGSK VKDVCEDLVR HGYNYLGKDY VTSGITGEPL EAYIYFGPVY YQKLKHMVLD 970 980 990 1000 1010 1020 KMHARARGPR AVLTRQPTEG RSRDGGLRLG EMERDCLIGY GASMLLLERL MISSDAFEVD 1030 1040 1050 1060 1070 VCGQCGLLGY SGWCHYCKSS CHVSSLRIPY ACKLLFQELQ SMNIIPRLKL SKYNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00301346. IPI00930490.
RefSeq	NP_001154180.1. NM_001160708.1. NP_060552.4. NM_018082.5.
UniGene	Hs.610795. Hs.62696.
3D structure databases
ProteinModelPortal	Q9NW08.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NW08. 1 interaction.
STRING	9606.ENSP00000228347.
PTM databases
PhosphoSite	Q9NW08.
Polymorphism databases
DMDM	29428029.
Proteomic databases
PaxDb	Q9NW08.
PRIDE	Q9NW08.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000228347; ENSP00000228347; ENSG00000013503. ENST00000539066; ENSP00000445721; ENSG00000013503.
GeneID	55703.
KEGG	hsa:55703.
UCSC	uc001tlp.3. human.
Organism-specific databases
CTD	55703.
GeneCards	GC12P106751.
H-InvDB	HIX0037055.
HGNC	HGNC:30348. POLR3B.
HPA	HPA036466.
MIM	614366. gene. 614381. phenotype.
neXtProt	NX_Q9NW08.
Orphanet	88637. Hypomyelination - hypogonadotropic hypogonadism - hypodontia.
PharmGKB	PA134867680.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0085.
HOGENOM	HOG000222962.
HOVERGEN	HBG017744.
InParanoid	Q9NW08.
KO	K03021.
OMA	DMIMNPH.
OrthoDB	EOG49ZXND.
PhylomeDB	Q9NW08.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9NW08.
Bgee	Q9NW08.
CleanEx	HS_POLR3B.
Genevestigator	Q9NW08.
GermOnline	ENSG00000013503. Homo sapiens.
Family and domain databases
Gene3D	2.40.270.10. 2 hits. 2.40.50.150. 1 hit.
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. IPR014724. RNA_pol_RPB2_OB-fold. [Graphical view]
PANTHER	PTHR20856. PTHR20856. 1 hit.
Pfam	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]
PROSITE	PS01166. RNA_POL_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55703.
NextBio	60549.
SOURCE	Search...

Entry information

Entry name

RPC2_HUMAN

Accession

Primary (citable) accession number: Q9NW08
Secondary accession number(s): A8K6H0 , B3KV73, F5H1E6, Q9NW59

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.