Reviewed, UniProtKB/Swiss-Prot P24928 (RPB1_HUMAN)

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
    RNA-directed RNA polymerase II subunit RPB1
    EC=2.7.7.48

Gene names

Name:

POLR2A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1970 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome. Ref.16
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 By similarity. The phosphorylated C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with SAFB/SAFB1. Interacts with CCNL1 and MYO1C By similarity. Interacts with 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. Interacts with PAF1.
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. 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. Ref.9 Ref.12 Ref.15 Ref.17
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 nucelotide 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. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome regulation of transcription, DNA-dependent Ref.2 Non-traceable author statement. Source: UniProtKB transcription initiation from RNA polymerase II promoter Inferred from Experiment. Source: Reactome
Cellular component	DNA-directed RNA polymerase II, core complex Traceable author statement. Source: ProtInc
Molecular function	DNA binding Ref.2 Non-traceable author statement. Source: UniProtKB DNA-directed RNA polymerase activity Ref.2 Non-traceable author statement. Source: UniProtKB RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin protein ligase binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAGI2	Q86UL8	1	EBI-295301,EBI-311035
SUPT5H	O00267	2	EBI-295301,EBI-710464
XAB2	Q9HCS7	1	EBI-295301,EBI-295232

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_0000073940
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
	Zinc finger	71 – 87	17	C2H2-type By similarity
	Region	833 – 845	13	Bridging helix
	Region	1593 – 1960	368	52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRTEVKGN]
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	145	1	Phosphotyrosine Ref.12
	Modified residue	772	1	Phosphoserine Ref.15
	Modified residue	777	1	Phosphoserine Ref.15
	Modified residue	1849	1	Phosphoserine Ref.17
	Modified residue	1874	1	Phosphotyrosine Ref.17
	Modified residue	1878	1	Phosphoserine By similarity
	Modified residue	1891	1	Phosphothreonine Ref.17
	Modified residue	1896	1	Phosphoserine Ref.9 Ref.17
	Modified residue	1923	1	Phosphotyrosine Ref.17
	Modified residue	1927	1	Phosphoserine Ref.17
	Modified residue	1933	1	Phosphothreonine By similarity
	Modified residue	1934	1	Phosphoserine Ref.9 Ref.17
Natural variations
	Natural variant	292	1	R → C: dbSNP rs2229198.		VAR_051872
Experimental info
	Sequence conflict	1067	1	W → L in CAA52862. Ref.2
	Sequence conflict	1449	1	D → Y in CAA52862. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P24928-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 6876FC25692A657E	FASTA	1,970	217,206
	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 PEYTPTSPKY 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]	"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: 1542581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The human gene encoding the largest subunit of RNA polymerase II." Mita K., Tsuji H., Morimyo M., Takahashi E., Nenoi M., Ichimura S., Yamauchi M., Hongo E., Hayashi A. Gene 159:285-286(1995) [PubMed: 7622068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements." Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L., Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S. Nucleic Acids Res. 26:3542-3549(1998) [PubMed: 9671816] [Abstract] Cited for: INTERACTION WITH SAFB.
[4]	"A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription." Parada C.A., Roeder R.G. EMBO J. 18:3688-3701(1999) [PubMed: 10393184] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; NCL; SUPT5H AND CDK9.
[5]	"Tat-SF1 protein associates with RAP30 and human SPT5 proteins." Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A. Mol. Cell. Biol. 19:5960-5968(1999) [PubMed: 10454543] [Abstract] Cited for: INTERACTION WITH HTATSF1.
[6]	"The structure of an FF domain from human HYPA/FBP11." Allen M., Friedler A., Schon O., Bycroft M. J. Mol. Biol. 323:411-416(2002) [PubMed: 12381297] [Abstract] Cited for: INTERACTION WITH FNBP3.
[7]	"Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing." Carty S.M., Greenleaf A.L. Mol. Cell. Proteomics 1:598-610(2002) [PubMed: 12376575] [Abstract] Cited for: INTERACTION WITH SYNCRIP.
[8]	"Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells." Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X. J. Biol. Chem. 279:11639-11648(2004) [PubMed: 14684736] [Abstract] Cited for: INTERACTION WITH CCNL2.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1896 AND SER-1934, MASS SPECTROMETRY.
[10]	"Expression of the C-terminal domain of novel human SR-A1 protein: interaction with the CTD domain of RNA polymerase II." Katsarou M.E., Papakyriakou A., Katsaros N., Scorilas A. Biochem. Biophys. Res. Commun. 334:61-68(2005) [PubMed: 15992770] [Abstract] Cited for: INTERACTION WITH SFRS19.
[11]	"Identification and characterization of a novel human histone H3 lysine 36 specific methyltransferase." Sun X.-J., Wei J., Wu X.-Y., Hu M., Wang L., Wang H.-H., Zhang Q.-H., Chen S.-J., Huang Q.-H., Chen Z. J. Biol. Chem. 280:35261-35271(2005) [PubMed: 16118227] [Abstract] Cited for: INTERACTION WITH SETD2.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, MASS SPECTROMETRY.
[13]	"Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1." Li M., Phatnani H.P., Guan Z., Sage H., Greenleaf A.L., Zhou P. Proc. Natl. Acad. Sci. U.S.A. 102:17636-17641(2005) [PubMed: 16314571] [Abstract] Cited for: INTERACTION WITH SETD2.
[14]	"The human homologue of the RNA polymerase II-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis." Moniaux N., Nemos C., Schmied B.M., Chauhan S.C., Deb S., Morikane K., Choudhury A., Vanlith M., Sutherlin M., Sikela J.M., Hollingsworth M.A., Batra S.K. Oncogene 25:3247-3257(2006) [PubMed: 16491129] [Abstract] Cited for: INTERACTION WITH PAF1 IN PAF1/RNA POLYMERASE II. Tissue: Fetal pancreas.
[15]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-772 AND SER-777, MASS SPECTROMETRY.
[16]	"Transcription of hepatitis delta virus RNA by RNA polymerase II." Chang J., Nie X., Chang H.E., Han Z., Taylor J. J. Virol. 82:1118-1127(2008) [PubMed: 18032511] [Abstract] Cited for: FUNCTION AS RNA-DIRECTED RNA POLYMERASE.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1849; TYR-1874; THR-1891; SER-1896; TYR-1923; SER-1927 AND SER-1934, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X63564 mRNA. Translation: CAA45125.1.
X74874 , X74873, X74872, X74871, X74870 Genomic DNA. Translation: CAA52862.1.

IPI

IPI00031627.

PIR

I38186.
S21054.

RefSeq

NP_000928.1.

UniGene

Hs.270017

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GHQ	X-ray	2.05	C/D	1795-1803	[»]
2GHT	X-ray	1.80	C/D	1796-1803	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29011N.

IntAct

P24928. 13 interactions.

PTM databases

PhosphoSite

P24928.

Proteomic databases

PRIDE

P24928.

Genome annotation databases

Ensembl

ENSG00000181222. Homo sapiens. [Contig view]

GeneID

5430.

KEGG

hsa:5430.

Organism-specific databases

GeneCards

GC17P007329.

H-InvDB

HIX0039202.

HGNC

HGNC:9187. POLR2A.

HPA

CAB012226.
CAB016388.

MIM

180660. gene+phenotype.

PharmGKB

PA33507.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P24928.

Enzyme and pathway databases

BRENDA

2.7.7.6. 247.

Reactome

REACT_12472. Regulatory RNA pathways.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_6143. Pausing and recovery of Tat-mediated HIV-1 elongation.
REACT_6167. Influenza Infection.
REACT_6185. HIV Infection.
REACT_6244. Pausing and recovery of HIV-1 elongation.
REACT_6259. HIV-1 elongation arrest and recovery.
REACT_6344. Tat-mediated HIV-1 elongation arrest and recovery.
REACT_71. Gene Expression.
REACT_769. Pausing and recovery of elongation.

Gene expression databases

ArrayExpress

P24928.

Bgee

P24928.

CleanEx

HS_POLR2A.

GermOnline

ENSG00000181222. Homo sapiens.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:2.40.40.30. RNA_pol_A. 1 hit.
G3DSA:3.90.1120.10. RNA_pol_Rpb1_1. 1 hit.
G3DSA:3.30.1360.90. RNA_pol_Rpb1_7. 1 hit.

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. 26 hits.
[Graphical view]

SMART

SM00663. RPOLA_N. 1 hit.
[Graphical view]

PROSITE

PS00115. RNA_POL_II_REPEAT. 43 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

21009.

SOURCE

Search...

Entry information

Entry name

RPB1_HUMAN

Accession

Primary (citable) accession number: P24928

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)