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P11414 (RPB1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase II subunit RPB1
Short name=RNA polymerase II subunit B1
EC=2.7.7.6
Alternative name(s):
DNA-directed RNA polymerase II subunit A
DNA-directed RNA polymerase III largest subunit
Gene names
Name:POLR2A
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length467 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second 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. RPB1 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. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing 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. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2, MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with FTSJD2, CTDSP1 and SCAF8. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82 By similarity. Interacts with ATF7IP By similarity. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapepdtide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphataes, and a "CTD code" that specifies the position of Pol II within the transcription cycle has been proposed.

Dephosphorylated by the protein phosphatase CTDSP1 By similarity.

Ubiquitinated by WWP2 leading to proteasomal degradation By similarity.

Methylated at Arg-307 by CARM1. Methylation occurs only when the CTD is hypophosphorylated, and phosphorylation at Ser-302 and Ser-305 prevent methylation (in vitro). It is assumed that methylation occurs prior to phosphorylation and transcription initiation. CTD methylation may facilitate the expression of select RNAs By similarity.

Sequence similarities

Belongs to the RNA polymerase beta' chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 467›467DNA-directed RNA polymerase II subunit RPB1
PRO_0000073938

Regions

Repeat90 – 9671
Repeat112 – 11872
Repeat119 – 12573
Repeat126 – 13274
Repeat133 – 13975
Repeat140 – 14676
Repeat147 – 15377
Repeat154 – 16078
Repeat161 – 16779
Repeat168 – 174710
Repeat175 – 181711
Repeat182 – 188712
Repeat189 – 195713
Repeat196 – 202714
Repeat203 – 209715
Repeat210 – 216716
Repeat217 – 223717
Repeat224 – 230718
Repeat231 – 237719
Repeat238 – 244720
Repeat245 – 251721
Repeat252 – 258722
Repeat259 – 265723
Repeat266 – 272724
Repeat273 – 279725
Repeat280 – 286726
Repeat287 – 293727
Repeat294 – 300728
Repeat301 – 307729
Repeat308 – 314730
Repeat315 – 321731
Repeat322 – 328732
Repeat329 – 335733
Repeat336 – 342734
Repeat343 – 349735
Repeat350 – 356736
Repeat357 – 363737
Repeat364 – 370738
Repeat371 – 377739
Repeat378 – 384740
Repeat385 – 391741
Repeat392 – 398742
Repeat399 – 405743
Repeat406 – 412744
Repeat413 – 419745
Repeat420 – 426746
Repeat427 – 433747
Repeat437 – 443748
Repeat444 – 450749
Repeat451 – 457750; approximate
Region90 – 45736850 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SNTRKEVG]

Amino acid modifications

Modified residue3071Omega-N-methylated arginine; by CARM1 By similarity
Modified residue3121Phosphoserine By similarity
Modified residue3361Phosphotyrosine By similarity
Modified residue3371Phosphothreonine By similarity
Modified residue3391Phosphothreonine By similarity
Modified residue3401Phosphoserine By similarity
Modified residue3421Phosphoserine By similarity
Modified residue3441Phosphoserine By similarity
Modified residue3461Phosphoserine By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3501Phosphotyrosine By similarity
Modified residue3511Phosphothreonine By similarity
Modified residue3541Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity
Modified residue3711Phosphotyrosine By similarity
Modified residue3721Phosphoserine By similarity
Modified residue3741Phosphothreonine By similarity
Modified residue3751Phosphoserine By similarity
Modified residue3781Phosphotyrosine By similarity
Modified residue3791Phosphoserine By similarity
Modified residue3811Phosphothreonine By similarity
Modified residue3851Phosphotyrosine By similarity
Modified residue3861Phosphoserine By similarity
Modified residue3881Phosphothreonine By similarity
Modified residue3891Phosphoserine By similarity
Modified residue3911Phosphothreonine By similarity
Modified residue3921Phosphotyrosine By similarity
Modified residue3951Phosphothreonine By similarity
Modified residue3961Phosphoserine By similarity
Modified residue3991Phosphotyrosine By similarity
Modified residue4001Phosphothreonine By similarity
Modified residue4031Phosphoserine By similarity
Modified residue4061Phosphotyrosine By similarity
Modified residue4101Phosphoserine By similarity
Modified residue4141Phosphoserine By similarity
Modified residue4161Phosphothreonine By similarity
Modified residue4171Phosphoserine By similarity
Modified residue4201Phosphotyrosine By similarity
Modified residue4211Phosphoserine By similarity
Modified residue4231Phosphothreonine By similarity
Modified residue4241Phosphoserine By similarity
Modified residue4261Phosphothreonine By similarity
Modified residue4271Phosphotyrosine By similarity
Modified residue4281Phosphoserine By similarity
Modified residue4301Phosphothreonine By similarity
Modified residue4591Phosphoserine By similarity
Modified residue4631Phosphoserine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P11414 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 0AADFD923B5D2BCE

FASTA46748,167
        10         20         30         40         50         60 
AGTGCFDLLL DAEKCKYGME IPTNIPGLGA AGRSGMTPGA AGFSPSAASD ASGFSPGYSP 

        70         80         90        100        110        120 
AWSPTPGSPG SPGPSSPYIP SPGGAMSPSY SPTSPAYEPR SPGGYTPQSP SYSPTSPSYS 

       130        140        150        160        170        180 
PTSPSYSPTS PNYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP 

       190        200        210        220        230        240 
SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP 

       250        260        270        280        290        300 
TSPNYSPTSP NYTPTSPSYS PTSPSYSPTS PNYTPTSPNY SPTSPSYSPT SPSYSPTSPS 

       310        320        330        340        350        360 
YSPSSPRYTP QSPTYTPSSP SYSPSSPSYS PTSPKYTPTS PSYSPSSPEY TPTSPKYSPT 

       370        380        390        400        410        420 
SPKYSPTSPK YSPTSPTYSP TTPKYSPTSP TYSPTSPVYT PTSPKYSPTS PTYSPTSPKY 

       430        440        450        460 
SPTSPTYSPT SPKGSTYSPT SPGYSPTSPT YSLTSPAISP DDSDEEN

« Hide

References

[1]"The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved structure with an essential function."
Allison L.A., Wong J.K.-C., Fitzpatrick V.D., Moyle M., Ingles C.J.
Mol. Cell. Biol. 8:321-329(1988) [PubMed: 3122024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M19538 Genomic DNA. Translation: AAA37008.1.
PIRA27677.

3D structure databases

ProteinModelPortalP11414.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000684. RNA_pol_II_repeat_euk.
[Graphical view]
PfamPF05001. RNA_pol_Rpb1_R. 43 hits.
[Graphical view]
PROSITEPS00115. RNA_POL_II_REPEAT. 43 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRPB1_CRIGR
AccessionPrimary (citable) accession number: P11414
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: January 25, 2012
This is version 73 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents