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UniProtKB/Swiss-Prot entry P30876


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

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Entry information
Entry name RPB2_HUMAN
Primary accession number P30876
Secondary accession number Q8IZ61
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 76)
Name and origin of the protein
Protein name DNA-directed RNA polymerase II subunit RPB2
Synonyms EC 2.7.7.6
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 name
Name: POLR2B
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].
DOI=10.1016/0022-2836(92)91071-V; PubMed=1518060 [NCBI, ExPASy, EBI, Israel, Japan]
Acker J., Wintzerith M., Vigneron M., Kedinger C.;
"Primary structure of the second largest subunit of human RNA polymerase II (or B).";
J. Mol. Biol. 226:1295-1299(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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 699-1174.
TISSUE=Brain;
PubMed=9110174 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
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: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits (By similarity).
  • INTERACTION:
    Q86UL8:MAGI2; NbExp=1; IntAct=EBI-394712, EBI-311035;
  • 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).
  • 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
X63563; CAA45124.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023503; AAH23503.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF055028; AAC09367.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S28976; S28976.
RefSeq NP_000929.1; -.
UniGene Hs.602757
3D structure databases
HSSP P08518; 1I50. [HSSP ENTRY / PDB]
ModBase P30876.
Protein-protein interaction databases
IntAct P30876; -.
PTM databases
PhosphoSite P30876; -.
Enzyme and pathway databases
Reactome 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.
Organism-specific databases
H-InvDB HIX0004241; -.
HGNC HGNC:9188; POLR2B.
GenAtlas POLR2B.
MIM 180661; gene. [NCBI / EBI]
PharmGKB PA33508; -.
GeneCards P30876.
Gene expression databases
ArrayExpress P30876; -.
CleanEx HS_POLR2B; -.
GermOnline ENSG00000047315; Homo sapiens.
Ontologies
GO
GO:0005665; Cellular component: DNA-directed RNA polymerase II, core complex (traceable author statement from ProtInc).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
GO:0006368; Biological process: RNA elongation from RNA polymerase II promoter (inferred from experiment from Reactome).
GO:0006367; Biological process: transcription initiation from RNA polymerase II promoter (inferred from experiment from Reactome).
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.
BLOCKS P30876.
Proteomic databases
PeptideAtlas P30876; -.
Genome annotation databases
Ensembl ENSG00000047315; Homo sapiens. [Contig view]
GeneID 5431; -.
KEGG hsa:5431; -.
Phylogenomic databases
HOGENOM P30876; -.
HOVERGEN P30876; -.
Other
SOURCE POLR2B; Homo sapiens.
ProtoNet P30876.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
DNA-directed RNA polymerase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1174  1174     DNA-directed RNA polymerase II subunit RPB2. PRO_0000048085
ZN_FING   1119   1140  22     C4-type (By similarity). 
METAL   792    792        Magnesium (shared with heteromeric partner) (By similarity). 
METAL   1119   1119        Zinc (By similarity). 
METAL   1122   1122        Zinc (By similarity). 
METAL   1137   1137        Zinc (By similarity). 
METAL   1140   1140        Zinc (By similarity). 
Sequence information
Length: 1174 AA [This is the length of the unprocessed precursor] Molecular weight: 133897 Da [This is the MW of the unprocessed precursor] CRC64: 32BEDF7F95E4DE10 [This is a checksum on the sequence]
        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 

P30876 in FASTA format

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