Reviewed,
UniProtKB/Swiss-Prot P11414 (RPB1_CRIGR)
Last modified
October 13, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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Names and origin
| Protein names | Recommended 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 |
| ||
| Organism | Cricetulus griseus (Chinese hamster) | ||
| Taxonomic identifier | 10029 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus |
Protein attributes
| Sequence length | 467 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred 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. 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 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. |
| Sequence similarities | Belongs to the RNA polymerase beta' chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription |
| Cellular component | DNA-directed RNA polymerase Nucleus |
| Domain | Repeat |
| Ligand | DNA-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| PTM | Phosphoprotein |
| 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: UniProtKB-KW DNA-directed RNA polymerase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 467 | ›467 | DNA-directed RNA polymerase II subunit RPB1 | PRO_0000073938 | |||||
Regions | |||||||||
| Repeat | 90 – 96 | 7 | 1 | ||||||
| Repeat | 112 – 118 | 7 | 2 | ||||||
| Repeat | 119 – 125 | 7 | 3 | ||||||
| Repeat | 126 – 132 | 7 | 4 | ||||||
| Repeat | 133 – 139 | 7 | 5 | ||||||
| Repeat | 140 – 146 | 7 | 6 | ||||||
| Repeat | 147 – 153 | 7 | 7 | ||||||
| Repeat | 154 – 160 | 7 | 8 | ||||||
| Repeat | 161 – 167 | 7 | 9 | ||||||
| Repeat | 168 – 174 | 7 | 10 | ||||||
| Repeat | 175 – 181 | 7 | 11 | ||||||
| Repeat | 182 – 188 | 7 | 12 | ||||||
| Repeat | 189 – 195 | 7 | 13 | ||||||
| Repeat | 196 – 202 | 7 | 14 | ||||||
| Repeat | 203 – 209 | 7 | 15 | ||||||
| Repeat | 210 – 216 | 7 | 16 | ||||||
| Repeat | 217 – 223 | 7 | 17 | ||||||
| Repeat | 224 – 230 | 7 | 18 | ||||||
| Repeat | 231 – 237 | 7 | 19 | ||||||
| Repeat | 238 – 244 | 7 | 20 | ||||||
| Repeat | 245 – 251 | 7 | 21 | ||||||
| Repeat | 252 – 258 | 7 | 22 | ||||||
| Repeat | 259 – 265 | 7 | 23 | ||||||
| Repeat | 266 – 272 | 7 | 24 | ||||||
| Repeat | 273 – 279 | 7 | 25 | ||||||
| Repeat | 280 – 286 | 7 | 26 | ||||||
| Repeat | 287 – 293 | 7 | 27 | ||||||
| Repeat | 294 – 300 | 7 | 28 | ||||||
| Repeat | 301 – 307 | 7 | 29 | ||||||
| Repeat | 308 – 314 | 7 | 30 | ||||||
| Repeat | 315 – 321 | 7 | 31 | ||||||
| Repeat | 322 – 328 | 7 | 32 | ||||||
| Repeat | 329 – 335 | 7 | 33 | ||||||
| Repeat | 336 – 342 | 7 | 34 | ||||||
| Repeat | 343 – 349 | 7 | 35 | ||||||
| Repeat | 350 – 356 | 7 | 36 | ||||||
| Repeat | 357 – 363 | 7 | 37 | ||||||
| Repeat | 364 – 370 | 7 | 38 | ||||||
| Repeat | 371 – 377 | 7 | 39 | ||||||
| Repeat | 378 – 384 | 7 | 40 | ||||||
| Repeat | 385 – 391 | 7 | 41 | ||||||
| Repeat | 392 – 398 | 7 | 42 | ||||||
| Repeat | 399 – 405 | 7 | 43 | ||||||
| Repeat | 406 – 412 | 7 | 44 | ||||||
| Repeat | 413 – 419 | 7 | 45 | ||||||
| Repeat | 420 – 426 | 7 | 46 | ||||||
| Repeat | 427 – 433 | 7 | 47 | ||||||
| Repeat | 437 – 443 | 7 | 48 | ||||||
| Repeat | 444 – 450 | 7 | 49 | ||||||
| Repeat | 451 – 457 | 7 | 50; approximate | ||||||
| Region | 90 – 457 | 368 | 50 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SNTRKEVG] | ||||||
Amino acid modifications | |||||||||
| Modified residue | 346 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 371 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 375 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 388 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 420 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 424 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 430 | 1 | Phosphothreonine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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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]. |
Cross-references
Sequence databases | |
|---|---|
| M19538 Genomic DNA. Translation: AAA37008.1. | |
| PIR | A27677. |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P11414. |
Enzyme and pathway databases | |
| BRENDA | 2.7.7.6. 18. |
Family and domain databases | |
| InterPro | IPR000684. RNA_pol_II_repeat_euk. [Graphical view] |
| Pfam | PF05001. RNA_pol_Rpb1_R. 26 hits. [Graphical view] |
| PROSITE | PS00115. RNA_POL_II_REPEAT. 43 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RPB1_CRIGR | ||||||||
| Accession | Primary (citable) accession number: P11414 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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