Reviewed, UniProtKB/Swiss-Prot P30876 (RPB2_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase II subunit RPB2
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase II subunit B
    RNA polymerase II subunit B2
    RNA polymerase II subunit 2
    DNA-directed RNA polymerase II 140 kDa polypeptide

Gene names

Name:

POLR2B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.
Subcellular location	Nucleus.
Miscellaneous	The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits By similarity.
Sequence similarities	Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome transcription initiation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome
Cellular component	DNA-directed RNA polymerase II, core complex Ref.6 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Ref.1 Traceable author statement. Source: ProtInc DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAGI2	Q86UL8	1	EBI-394712,EBI-311035

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1174	1174	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048085
Regions
	Zinc finger	1119 – 1140	22	C4-type
Sites
	Metal binding	792	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1119	1	Zinc By similarity
	Metal binding	1122	1	Zinc By similarity
	Metal binding	1137	1	Zinc By similarity
	Metal binding	1140	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30876-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 32BEDF7F95E4DE10	FASTA	1,174	133,897
	10 20 30 40 50 60 MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE 70 80 90 100 110 120 DAPPIDLQAE AQHASGEVEE PPRYLLKFEQ IYLSKPTHWE RDGAPSPMMP NEARLRNLTY 130 140 150 160 170 180 SAPLYVDITK TVIKEGEEQL QTQHQKTFIG KIPIMLRSTY CLLNGLTDRD LCELNECPLD 190 200 210 220 230 240 PGGYFIINGS EKVLIAQEKM ATNTVYVFAK KDSKYAYTGE CRSCLENSSR PTSTIWVSML 250 260 270 280 290 300 ARGGQGAKKS AIGQRIVATL PYIKQEVPII IVFRALGFVS DRDILEHIIY DFEDPEMMEM 310 320 330 340 350 360 VKPSLDEAFV IQEQNVALNF IGSRGAKPGV TKEKRIKYAK EVLQKEMLPH VGVSDFCETK 370 380 390 400 410 420 KAYFLGYMVH RLLLAALGRR ELDDRDHYGN KRLDLAGPLL AFLFRGMFKN LLKEVRIYAQ 430 440 450 460 470 480 KFIDRGKDFN LELAIKTRII SDGLKYSLAT GNWGDQKKAH QARAGVSQVL NRLTFASTLS 490 500 510 520 530 540 HLRRLNSPIG RDGKLAKPRQ LHNTLWGMVC PAETPEGHAV GLVKNLALMA YISVGSQPSP 550 560 570 580 590 600 ILEFLEEWSM ENLEEISPAA IADATKIFVN GCWVGIHKDP EQLMNTLRKL RRQMDIIVSE 610 620 630 640 650 660 VSMIRDIRER EIRIYTDAGR ICRPLLIVEK QKLLLKKRHI DQLKEREYNN YSWQDLVASG 670 680 690 700 710 720 VVEYIDTLEE ETVMLAMTPD DLQEKEVAYC STYTHCEIHP SMILGVCASI IPFPDHNQSP 730 740 750 760 770 780 RNTYQSAMGK QAMGVYITNF HVRMDTLAHV LYYPQKPLVT TRSMEYLRFR ELPAGINSIV 790 800 810 820 830 840 AIASYTGYNQ EDSVIMNRSA VDRGFFRSVF YRSYKEQESK KGFDQEEVFE KPTRETCQGM 850 860 870 880 890 900 RHAIYDKLDD DGLIAPGVRV SGDDVIIGKT VTLPENEDEL ESTNRRYTKR DCSTFLRTSE 910 920 930 940 950 960 TGIVDQVMVT LNQEGYKFCK IRVRSVRIPQ IGDKFASRHG QKGTCGIQYR QEDMPFTCEG 970 980 990 1000 1010 1020 ITPDIIINPH AIPSRMTIGH LIECLQGKVS ANKGEIGDAT PFNDAVNVQK ISNLLSDYGY 1030 1040 1050 1060 1070 1080 HLRGNEVLYN GFTGRKITSQ IFIGPTYYQR LKHMVDDKIH SRARGPIQIL NRQPMEGRSR 1090 1100 1110 1120 1130 1140 DGGLRFGEME RDCQIAHGAA QFLRERLFEA SDPYQVHVCN LCGIMAIANT RTHTYECRGC 1150 1160 1170 RNKTQISLVR MPYACKLLFQ ELMSMSIAPR MMSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the second largest subunit of human RNA polymerase II (or B)." Acker J., Wintzerith M., Vigneron M., Kedinger C. J. Mol. Biol. 226:1295-1299(1992) [PubMed: 1518060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	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].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	"Large-scale concatenation cDNA sequencing." Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A. Genome Res. 7:353-358(1997) [PubMed: 9110174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 699-1174. Tissue: Brain.
[6]	"Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes." Kershnar E., Wu S.-Y., Chiang C.-M. J. Biol. Chem. 273:34444-34453(1998) [PubMed: 9852112] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63563 mRNA. Translation: CAA45124.1. AK289823 mRNA. Translation: BAF82512.1. CH471057 Genomic DNA. Translation: EAX05519.1. BC023503 mRNA. Translation: AAH23503.2. AF055028 mRNA. Translation: AAC09367.1.
IPI	IPI00027808.
PIR	S28976.
RefSeq	NP_000929.1.
UniGene	Hs.602757
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P30876. 10 interactions.
STRING	P30876.
PTM databases
PhosphoSite	P30876.
Proteomic databases
PeptideAtlas	P30876.
PRIDE	P30876.
Genome annotation databases
Ensembl	ENST00000314595; ENSP00000312735; ENSG00000047315; Homo sapiens. [Genome view] ENST00000381227; ENSP00000370625; ENSG00000047315; Homo sapiens. [Genome view]
GeneID	5431.
KEGG	hsa:5431.
UCSC	uc003hcl.1. human.
Organism-specific databases
CTD	5431.
GeneCards	GC04P057538.
H-InvDB	HIX0004241.
HGNC	HGNC:9188. POLR2B.
MIM	180661. gene.
PharmGKB	PA33508.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P30876.
HOVERGEN	P30876.
OMA	FGPTYYQ
OrthoDB	EOG9B5RQP
Enzyme and pathway databases
BRENDA	2.7.7.6. 247.
Reactome	REACT_12472. Regulatory RNA pathways. REACT_125. Processing of Capped Intron-Containing Pre-mRNA. REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_1892. Elongation arrest and recovery. REACT_216. DNA Repair. REACT_6143. Pausing and recovery of Tat-mediated HIV-1 elongation. REACT_6167. Influenza Infection. REACT_6185. HIV Infection. REACT_6244. Pausing and recovery of HIV-1 elongation. REACT_6259. HIV-1 elongation arrest and recovery. REACT_6344. Tat-mediated HIV-1 elongation arrest and recovery. REACT_71. Gene Expression. REACT_769. Pausing and recovery of elongation.
Gene expression databases
ArrayExpress	P30876.
Bgee	P30876.
CleanEx	HS_POLR2B.
Genevestigator	P30876.
GermOnline	ENSG00000047315. Homo sapiens.
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]
PANTHER	PTHR20856. RNA_pol_I_sub2. 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 Resources
NextBio	21013.
SOURCE	Search...

Entry information

Entry name

RPB2_HUMAN

Accession

Primary (citable) accession number: P30876
Secondary accession number(s): A8K1A8, Q8IZ61

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	November 24, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.