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Reviewed, UniProtKB/Swiss-Prot P24928 (RPB1_HUMAN)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    RNA-directed RNA polymerase II subunit RPB1
    EC=2.7.7.48
Gene names
Name: POLR2A
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1970 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19701970DNA-directed RNA polymerase II subunit RPB1
PRO_0000073940

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
Zinc finger71 – 8717C2H2-type By similarity
Region833 – 84513Bridging helix
Region1593 – 196036852 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRTEVKGN]

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 residue1451Phosphotyrosine Ref.12
Modified residue7721Phosphoserine Ref.15
Modified residue7771Phosphoserine Ref.15
Modified residue18491Phosphoserine Ref.17
Modified residue18741Phosphotyrosine Ref.17
Modified residue18781Phosphoserine By similarity
Modified residue18911Phosphothreonine Ref.17
Modified residue18961Phosphoserine Ref.9 Ref.17
Modified residue19231Phosphotyrosine Ref.17
Modified residue19271Phosphoserine Ref.17
Modified residue19331Phosphothreonine By similarity
Modified residue19341Phosphoserine Ref.9 Ref.17

Natural variations

Natural variant2921R → C: dbSNP rs2229198.
VAR_051872

Experimental info

Sequence conflict10671W → L in CAA52862. Ref.2
Sequence conflict14491D → Y in CAA52862. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24928-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 6876FC25692A657E

FASTA1,970217,206
        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 

« Hide

References

« Hide '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

X63564 mRNA. Translation: CAA45125.1.
X74874 expand/collapse EMBL AC list , X74873, X74872, X74871, X74870 Genomic DNA. Translation: CAA52862.1.
IPIIPI00031627.
PIRI38186.
S21054.
RefSeqNP_000928.1.
UniGeneHs.270017

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GHQX-ray2.05C/D1795-1803[»]
2GHTX-ray1.80C/D1796-1803[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29011N.
IntActP24928. 13 interactions.

PTM databases

PhosphoSiteP24928.

Proteomic databases

PRIDEP24928.

Genome annotation databases

EnsemblENSG00000181222. Homo sapiens. [Contig view]
GeneID5430.
KEGGhsa:5430.

Organism-specific databases

GeneCardsGC17P007329.
H-InvDBHIX0039202.
HGNCHGNC:9187. POLR2A.
HPACAB012226.
CAB016388.
MIM180660. gene+phenotype.
PharmGKBPA33507.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP24928.

Enzyme and pathway databases

BRENDA2.7.7.6. 247.
ReactomeREACT_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

ArrayExpressP24928.
BgeeP24928.
CleanExHS_POLR2A.
GermOnlineENSG00000181222. Homo sapiens.

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]
Gene3DG3DSA: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.
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. 26 hits.
[Graphical view]
SMARTSM00663. RPOLA_N. 1 hit.
[Graphical view]
PROSITEPS00115. RNA_POL_II_REPEAT. 43 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21009.
SOURCESearch...

Entry information

Entry nameRPB1_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents