DNA-directed RNA polymerase II subunit RPB2

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Q8CFI7 (RPB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 140 kDa polypeptide
DNA-directed RNA polymerase II subunit B
RNA polymerase II subunit 2
RNA polymerase II subunit B2

Gene names

Name:

Polr2b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1174 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	DNA-directed RNA polymerase II, core complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from direct assay PubMed 22287103. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from electronic annotation. Source: Compara ribonucleoside binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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_0000048086

Regions

Zinc finger

1119 – 1140

C4-type

Sites

Metal binding

792

Magnesium; shared with RPB1 By similarity

Metal binding

1119

Zinc By similarity

Metal binding

1122

Zinc By similarity

Metal binding

1137

Zinc By similarity

Metal binding

1140

Zinc By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8CFI7 [UniParc].

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

1,174

133,911

        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

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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.
IPI	IPI00320034.
RefSeq	NP_722493.2. NM_153798.2.
UniGene	Mm.273217.
3D structure databases
ProteinModelPortal	Q8CFI7.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-57023N.
IntAct	Q8CFI7. 3 interactions.
MINT	MINT-4133069.
PTM databases
PhosphoSite	Q8CFI7.
Proteomic databases
PaxDb	Q8CFI7.
PRIDE	Q8CFI7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031167; ENSMUSP00000031167; ENSMUSG00000029250.
GeneID	231329.
KEGG	mmu:231329.
UCSC	uc008xwe.2. mouse.
Organism-specific databases
CTD	5431.
MGI	MGI:2388280. Polr2b.
Phylogenomic databases
eggNOG	COG0085.
GeneTree	ENSGT00690000102234.
HOGENOM	HOG000222962.
HOVERGEN	HBG017744.
InParanoid	Q8CFI7.
KO	K03010.
OMA	IMIVFRA.
OrthoDB	EOG4JQ3WQ.
Gene expression databases
ArrayExpress	Q8CFI7.
Bgee	Q8CFI7.
CleanEx	MM_POLR2B.
Genevestigator	Q8CFI7.
GermOnline	ENSMUSG00000029250. Mus musculus.
Family and domain databases
Gene3D	2.40.270.10. 2 hits. 2.40.50.150. 1 hit. 3.90.1110.10. 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
ChiTaRS	POLR2B. mouse.
NextBio	380519.
SOURCE	Search...

Entry information

Entry name

RPB2_MOUSE

Accession

Primary (citable) accession number: Q8CFI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	May 29, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents