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P08775 (RPB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:Rpii215, Rpo2-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1970 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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, CCNL2 and SFRS19. 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. Hyperphosphorylated form on tandem 7 residues repeats specifically interacts with SETD2. Interacts with PAF1. Interacts (via C-terminus) with CMTR1 and CTDSP1. Interacts with MYO1C. Interacts (via C-terminus) with SCAF8. Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82. Interacts with ATF7IP. When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact. Interacts with DDX5. When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Ref.5 Ref.6 Ref.7 Ref.9 Ref.11

Subcellular location

Nucleus.

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 heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed By similarity.

Dephosphorylated by the protein phosphatase CTDSP1 By similarity.

Following UV treatment, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated UV damage sites without leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery (By similarity.) Ubiquitinated by WWP2 leading to proteasomal degradation. Ref.7

Methylated at Arg-1810 by CARM1. Methylation occurs only when the CTD is hypophosphorylated, and phosphorylation at Ser-1805 and Ser-1808 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.

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 temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.

Sequence similarities

Belongs to the RNA polymerase beta' chain family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19701970DNA-directed RNA polymerase II subunit RPB1
PRO_0000073941

Regions

Repeat1593 – 159971
Repeat1600 – 160672; approximate
Repeat1608 – 161473
Repeat1615 – 162174
Repeat1622 – 162875
Repeat1629 – 163576
Repeat1636 – 164277
Repeat1643 – 164978
Repeat1650 – 165679
Repeat1657 – 1663710
Repeat1664 – 1670711
Repeat1671 – 1677712
Repeat1678 – 1684713
Repeat1685 – 1691714
Repeat1692 – 1698715
Repeat1699 – 1705716
Repeat1706 – 1712717
Repeat1713 – 1719718
Repeat1720 – 1726719
Repeat1727 – 1733720
Repeat1734 – 1740721
Repeat1741 – 1747722
Repeat1748 – 1754723
Repeat1755 – 1761724
Repeat1762 – 1768725
Repeat1769 – 1775726
Repeat1776 – 1782727
Repeat1783 – 1789728
Repeat1790 – 1796729
Repeat1797 – 1803730
Repeat1804 – 1810731
Repeat1811 – 1817732
Repeat1818 – 1824733
Repeat1825 – 1831734
Repeat1832 – 1838735
Repeat1839 – 1845736
Repeat1846 – 1852737
Repeat1853 – 1859738
Repeat1860 – 1866739
Repeat1867 – 1873740
Repeat1874 – 1880741
Repeat1881 – 1887742
Repeat1888 – 1894743
Repeat1895 – 1901744
Repeat1902 – 1908745
Repeat1909 – 1915746
Repeat1916 – 1922747
Repeat1923 – 1929748
Repeat1930 – 1936749
Repeat1940 – 1946750
Repeat1947 – 1953751; approximate
Repeat1954 – 1960752; approximate
Region833 – 84513Bridging helix
Region1593 – 196036852 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN]

Sites

Metal binding711Zinc 1 By similarity
Metal binding741Zinc 1 By similarity
Metal binding811Zinc 1 By similarity
Metal binding841Zinc 1 By similarity
Metal binding1111Zinc 2 By similarity
Metal binding1141Zinc 2 By similarity
Metal binding1541Zinc 2 By similarity
Metal binding1841Zinc 2 By similarity
Metal binding4951Magnesium 1; catalytic By similarity
Metal binding4951Magnesium 2; shared with RPB2 By similarity
Metal binding4971Magnesium 1; catalytic By similarity
Metal binding4971Magnesium 2; shared with RPB2 By similarity
Metal binding4991Magnesium 1; catalytic By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue18101Omega-N-methylated arginine; by CARM1 By similarity
Modified residue18431Phosphoserine By similarity
Modified residue18491Phosphoserine By similarity
Modified residue18541Phosphothreonine By similarity
Modified residue18741Phosphotyrosine By similarity
Modified residue18781Phosphoserine
Modified residue18821Phosphoserine By similarity
Modified residue18961Phosphoserine By similarity
Modified residue18991Phosphoserine By similarity
Modified residue19091Phosphotyrosine By similarity
Modified residue19131Phosphoserine By similarity
Modified residue19171Phosphoserine By similarity
Modified residue19201Phosphoserine By similarity
Modified residue19231Phosphotyrosine
Modified residue19271Phosphoserine
Modified residue19311Phosphoserine By similarity
Modified residue19331Phosphothreonine
Modified residue19341Phosphoserine By similarity

Experimental info

Mutagenesis18591K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1866; R-1873; R-1887; R-1908 and R-1922. Ref.7
Mutagenesis18661K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1873; R-1887; R-1908 and R-1922. Ref.7
Mutagenesis18731K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1887; R-1908 and R-1922. Ref.7
Mutagenesis18871K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1908 and R-1922. Ref.7
Mutagenesis19081K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1887 and R-1922. Ref.7
Mutagenesis19221K → R: Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1887 and R-1908. Ref.7
Sequence conflict14981P → R in AAA40071. Ref.1
Sequence conflict1499 – 153638Missing in AAA40071. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P08775 [UniParc].

Last modified March 1, 1992. Version 3.
Checksum: 7D76F38FD92A657E

FASTA1,970217,176
        10         20         30         40         50         60 
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP 

        70         80         90        100        110        120 
RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD 

       130        140        150        160        170        180 
SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG 

       190        200        210        220        230        240 
HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP 

       250        260        270        280        290        300 
RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA 

       310        320        330        340        350        360 
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD 

       370        380        390        400        410        420 
FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII 

       430        440        450        460        470        480 
RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS 

       490        500        510        520        530        540 
TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD 

       550        560        570        580        590        600 
TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI 

       610        620        630        640        650        660 
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM 

       670        680        690        700        710        720 
GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA 

       730        740        750        760        770        780 
HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN 

       790        800        810        820        830        840 
ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA 

       850        860        870        880        890        900 
MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES 

       910        920        930        940        950        960 
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR 

       970        980        990       1000       1010       1020 
EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL 

      1030       1040       1050       1060       1070       1080 
VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI 

      1090       1100       1110       1120       1130       1140 
AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT 

      1150       1160       1170       1180       1190       1200 
VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP 

      1210       1220       1230       1240       1250       1260 
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR 

      1270       1280       1290       1300       1310       1320 
IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI 

      1330       1340       1350       1360       1370       1380 
IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER 

      1390       1400       1410       1420       1430       1440 
ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM 

      1450       1460       1470       1480       1490       1500 
EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG 

      1510       1520       1530       1540       1550       1560 
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG 

      1570       1580       1590       1600       1610       1620 
YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP 

      1630       1640       1650       1660       1670       1680 
SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP 

      1690       1700       1710       1720       1730       1740 
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS 

      1750       1760       1770       1780       1790       1800 
YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT 

      1810       1820       1830       1840       1850       1860 
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS PEYTPASPKY 

      1870       1880       1890       1900       1910       1920 
SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS 

      1930       1940       1950       1960       1970 
PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of the mouse genomic locus encoding the largest subunit of RNA polymerase II."
Ahearn J.M. Jr., Bartolomei M.S., West M.L., Cisek L.J., Corden J.L.
J. Biol. Chem. 262:10695-10705(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II."
Corden J.L., Cadena D.L., Ahearn J.M. Jr., Dahmus M.E.
Proc. Natl. Acad. Sci. U.S.A. 82:7934-7938(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1587-1970.
[4]"Complete sequence of the human RNA polymerase II largest subunit."
Wintzerith M., Acker J., Vicaire S., Vigneron M., Kedinger C.
Nucleic Acids Res. 20:910-910(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, PRESENCE OF AN ADDITIONAL EXON.
[5]"The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins."
Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M., Corden J.L.
Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCAF8.
[6]"A myosin I isoform in the nucleus."
Pestic-Dragovich L., Stojiljkovic L., Philimonenko A.A., Nowak G., Ke Y., Settlage R.E., Shabanowitz J., Hunt D.F., Hozak P., de Lanerolle P.
Science 290:337-341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO1C.
[7]"Wwp2-mediated ubiquitination of the RNA polymerase II large subunit in mouse embryonic pluripotent stem cells."
Li H., Zhang Z., Wang B., Zhang J., Zhao Y., Jin Y.
Mol. Cell. Biol. 27:5296-5305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND LYS-1922, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH WWP2, MUTAGENESIS OF LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND LYS-1922.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation."
Yoh S.M., Lucas J.S., Jones K.A.
Genes Dev. 22:3422-3434(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUPT6H.
[10]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex."
Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.
Science 337:599-602(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A LARGE PER COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12130, M14101 Genomic DNA. Translation: AAA40071.1.
AL603707 Genomic DNA. Translation: CAI51953.1.
PIRA28490.
RefSeqNP_001277997.1. NM_001291068.1.
UniGeneMm.16533.

3D structure databases

DisProtDP00181.
ProteinModelPortalP08775.
SMRP08775. Positions 16-896, 1072-1475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202996. 24 interactions.
DIPDIP-46369N.
IntActP08775. 17 interactions.
MINTMINT-4133043.

PTM databases

PhosphoSiteP08775.

Proteomic databases

MaxQBP08775.
PaxDbP08775.
PRIDEP08775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000058470; ENSMUSP00000050771; ENSMUSG00000005198.
ENSMUST00000071213; ENSMUSP00000071200; ENSMUSG00000005198.
GeneID20020.
KEGGmmu:20020.
UCSCuc007jrj.1. mouse.

Organism-specific databases

CTD5430.
MGIMGI:98086. Polr2a.

Phylogenomic databases

eggNOGCOG0086.
GeneTreeENSGT00730000110946.
HOGENOMHOG000222975.
HOVERGENHBG004339.
InParanoidQ5F298.
KOK03006.
OMAIVFNRQP.
OrthoDBEOG7K0ZB8.
PhylomeDBP08775.
TreeFamTF103036.

Gene expression databases

BgeeP08775.
CleanExMM_POLR2A.
GenevestigatorP08775.

Family and domain databases

InterProIPR000722. RNA_pol_asu.
IPR000684. RNA_pol_II_repeat_euk.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
IPR007075. RNA_pol_Rpb1_6.
IPR007073. RNA_pol_Rpb1_7.
[Graphical view]
PfamPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
PF04992. RNA_pol_Rpb1_6. 1 hit.
PF04990. RNA_pol_Rpb1_7. 1 hit.
PF05001. RNA_pol_Rpb1_R. 25 hits.
[Graphical view]
SMARTSM00663. RPOLA_N. 1 hit.
[Graphical view]
PROSITEPS00115. RNA_POL_II_REPEAT. 42 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOLR2A. mouse.
NextBio297535.
PROP08775.
SOURCESearch...

Entry information

Entry nameRPB1_MOUSE
AccessionPrimary (citable) accession number: P08775
Secondary accession number(s): Q5F298
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 1, 1992
Last modified: July 9, 2014
This is version 149 of the entry and version 3 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