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Q8CFI7 (RPB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase II subunit RPB2

EC=2.7.7.6
Alternative name(s):
DNA-directed RNA polymerase II 140 kDa polypeptide
DNA-directed RNA polymerase II subunit B
RNA polymerase II subunit 2
RNA polymerase II subunit B2
Gene names
Name:Polr2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1174 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Interacts with WDR82 By similarity. Interacts with MEN1 By similarity.

Subcellular location

Nucleus By similarity.

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.

Sequence caution

The sequence AAH38472.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11741174DNA-directed RNA polymerase II subunit RPB2
PRO_0000048086

Regions

Zinc finger1119 – 114022C4-type

Sites

Metal binding7921Magnesium; shared with RPB1 By similarity
Metal binding11191Zinc By similarity
Metal binding11221Zinc By similarity
Metal binding11371Zinc By similarity
Metal binding11401Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CFI7 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: F941FA6EC03E2160

FASTA1,174133,911
        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 
RHAIYEKLDD 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 

« Hide

References

[1]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC038472 mRNA. Translation: AAH38472.1. Different initiation.
CCDSCCDS51528.1.
RefSeqNP_722493.2. NM_153798.2.
UniGeneMm.273217.

3D structure databases

ProteinModelPortalQ8CFI7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231111. 8 interactions.
DIPDIP-57023N.
IntActQ8CFI7. 8 interactions.
MINTMINT-4133069.

PTM databases

PhosphoSiteQ8CFI7.

Proteomic databases

MaxQBQ8CFI7.
PaxDbQ8CFI7.
PRIDEQ8CFI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031167; ENSMUSP00000031167; ENSMUSG00000029250.
GeneID231329.
KEGGmmu:231329.
UCSCuc008xwe.2. mouse.

Organism-specific databases

CTD5431.
MGIMGI:2388280. Polr2b.

Phylogenomic databases

eggNOGCOG0085.
GeneTreeENSGT00750000117589.
HOGENOMHOG000222962.
HOVERGENHBG017744.
InParanoidQ8CFI7.
KOK03010.
OMADSQMLEM.
OrthoDBEOG7JT6VC.
PhylomeDBQ8CFI7.
TreeFamTF103037.

Gene expression databases

BgeeQ8CFI7.
CleanExMM_POLR2B.
GenevestigatorQ8CFI7.

Family and domain databases

Gene3D2.40.270.10. 2 hits.
2.40.50.150. 1 hit.
3.90.1110.10. 1 hit.
InterProIPR015712. 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]
PANTHERPTHR20856. PTHR20856. 1 hit.
PfamPF04563. 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]
PROSITEPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOLR2B. mouse.
NextBio380519.
PROQ8CFI7.
SOURCESearch...

Entry information

Entry nameRPB2_MOUSE
AccessionPrimary (citable) accession number: Q8CFI7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot