P08775 (RPB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Name:	Polr2a
Synonyms:	Rpii215, Rpo2-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1970 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Interacts with PAF1. Interacts (via C-terminus) with FTSJD2 and CTDSP1 By similarity. 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 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. Interacts with DDX5 By similarity. Ref.5 Ref.6 Ref.7
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 heptapepdtide 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 heptapepdtide 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.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Repeat
Ligand	DNA-binding Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Methylation Phosphoprotein Ubl conjugation
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 direct assay PubMed 15601870. Source: MGI DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1970	1970	DNA-directed RNA polymerase II subunit RPB1		PRO_0000073941
Regions
	Repeat	1593 – 1599	7	1
	Repeat	1600 – 1606	7	2; approximate
	Repeat	1608 – 1614	7	3
	Repeat	1615 – 1621	7	4
	Repeat	1622 – 1628	7	5
	Repeat	1629 – 1635	7	6
	Repeat	1636 – 1642	7	7
	Repeat	1643 – 1649	7	8
	Repeat	1650 – 1656	7	9
	Repeat	1657 – 1663	7	10
	Repeat	1664 – 1670	7	11
	Repeat	1671 – 1677	7	12
	Repeat	1678 – 1684	7	13
	Repeat	1685 – 1691	7	14
	Repeat	1692 – 1698	7	15
	Repeat	1699 – 1705	7	16
	Repeat	1706 – 1712	7	17
	Repeat	1713 – 1719	7	18
	Repeat	1720 – 1726	7	19
	Repeat	1727 – 1733	7	20
	Repeat	1734 – 1740	7	21
	Repeat	1741 – 1747	7	22
	Repeat	1748 – 1754	7	23
	Repeat	1755 – 1761	7	24
	Repeat	1762 – 1768	7	25
	Repeat	1769 – 1775	7	26
	Repeat	1776 – 1782	7	27
	Repeat	1783 – 1789	7	28
	Repeat	1790 – 1796	7	29
	Repeat	1797 – 1803	7	30
	Repeat	1804 – 1810	7	31
	Repeat	1811 – 1817	7	32
	Repeat	1818 – 1824	7	33
	Repeat	1825 – 1831	7	34
	Repeat	1832 – 1838	7	35
	Repeat	1839 – 1845	7	36
	Repeat	1846 – 1852	7	37
	Repeat	1853 – 1859	7	38
	Repeat	1860 – 1866	7	39
	Repeat	1867 – 1873	7	40
	Repeat	1874 – 1880	7	41
	Repeat	1881 – 1887	7	42
	Repeat	1888 – 1894	7	43
	Repeat	1895 – 1901	7	44
	Repeat	1902 – 1908	7	45
	Repeat	1909 – 1915	7	46
	Repeat	1916 – 1922	7	47
	Repeat	1923 – 1929	7	48
	Repeat	1930 – 1936	7	49
	Repeat	1940 – 1946	7	50
	Repeat	1947 – 1953	7	51; approximate
	Repeat	1954 – 1960	7	52; approximate
	Region	833 – 845	13	Bridging helix
	Region	1593 – 1960	368	52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN]
Sites
	Metal binding	71	1	Zinc 1 By similarity
	Metal binding	74	1	Zinc 1 By similarity
	Metal binding	81	1	Zinc 1 By similarity
	Metal binding	84	1	Zinc 1 By similarity
	Metal binding	111	1	Zinc 2 By similarity
	Metal binding	114	1	Zinc 2 By similarity
	Metal binding	154	1	Zinc 2 By similarity
	Metal binding	184	1	Zinc 2 By similarity
	Metal binding	495	1	Magnesium 1; catalytic By similarity
	Metal binding	495	1	Magnesium 2; shared with RPB2 By similarity
	Metal binding	497	1	Magnesium 1; catalytic By similarity
	Metal binding	497	1	Magnesium 2; shared with RPB2 By similarity
	Metal binding	499	1	Magnesium 1; catalytic By similarity
Amino acid modifications
	Modified residue	1810	1	Omega-N-methylated arginine; by CARM1 By similarity
	Modified residue	1843	1	Phosphoserine By similarity
	Modified residue	1849	1	Phosphoserine By similarity
	Modified residue	1854	1	Phosphothreonine By similarity
	Modified residue	1874	1	Phosphotyrosine By similarity
	Modified residue	1878	1	Phosphoserine
	Modified residue	1882	1	Phosphoserine By similarity
	Modified residue	1896	1	Phosphoserine By similarity
	Modified residue	1899	1	Phosphoserine By similarity
	Modified residue	1909	1	Phosphotyrosine By similarity
	Modified residue	1913	1	Phosphoserine By similarity
	Modified residue	1917	1	Phosphoserine By similarity
	Modified residue	1920	1	Phosphoserine By similarity
	Modified residue	1923	1	Phosphotyrosine
	Modified residue	1927	1	Phosphoserine
	Modified residue	1931	1	Phosphoserine By similarity
	Modified residue	1933	1	Phosphothreonine
	Modified residue	1934	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	1859	1	K → 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
	Mutagenesis	1866	1	K → 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
	Mutagenesis	1873	1	K → 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
	Mutagenesis	1887	1	K → 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
	Mutagenesis	1908	1	K → 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
	Mutagenesis	1922	1	K → 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 conflict	1498	1	P → R in AAA40071. Ref.1
	Sequence conflict	1499 – 1536	38	Missing in AAA40071. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P08775 [UniParc]. Last modified March 1, 1992. Version 3. Checksum: 7D76F38FD92A657E	FASTA	1,970	217,176
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY, INTERACTION WITH WWP2, MUTAGENESIS OF LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND LYS-1922.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12130, M14101 Genomic DNA. Translation: AAA40071.1. AL603707 Genomic DNA. Translation: CAI51953.1.
IPI	IPI00136207.
PIR	A28490.
RefSeq	NP_033115.1. NM_009089.2.
UniGene	Mm.16533.
3D structure databases
DisProt	DP00181.
ProteinModelPortal	P08775.
SMR	P08775. Positions 16-896, 1075-1475.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46369N.
IntAct	P08775. 5 interactions.
MINT	MINT-4133043.
PTM databases
PhosphoSite	P08775.
Proteomic databases
PaxDb	P08775.
PRIDE	P08775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000058470; ENSMUSP00000050771; ENSMUSG00000005198. ENSMUST00000071213; ENSMUSP00000071200; ENSMUSG00000005198.
GeneID	20020.
KEGG	mmu:20020.
UCSC	uc007jrj.1. mouse.
Organism-specific databases
CTD	5430.
MGI	MGI:98086. Polr2a.
Phylogenomic databases
eggNOG	COG0086.
GeneTree	ENSGT00700000104490.
HOGENOM	HOG000222975.
HOVERGEN	HBG004339.
InParanoid	Q5F298.
KO	K03006.
OMA	KVLPWST.
OrthoDB	EOG4JWVCM.
Gene expression databases
Bgee	P08775.
CleanEx	MM_POLR2A.
Genevestigator	P08775.
GermOnline	ENSMUSG00000005198. Mus musculus.
Family and domain databases
Gene3D	2.40.40.20. 2 hits.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR000722. 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]
Pfam	PF04997. 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]
SMART	SM00663. RPOLA_N. 1 hit. [Graphical view]
PROSITE	PS00115. RNA_POL_II_REPEAT. 42 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POLR2A. mouse.
NextBio	297535.
SOURCE	Search...

Entry information

Entry name

RPB1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program