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P24928

- RPB1_HUMAN

UniProt

P24928 - RPB1_HUMAN

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Protein

DNA-directed RNA polymerase II subunit RPB1

Gene

POLR2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 an 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.4 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Zinc 1By similarity
Metal bindingi74 – 741Zinc 1By similarity
Metal bindingi81 – 811Zinc 1By similarity
Metal bindingi84 – 841Zinc 1By similarity
Metal bindingi111 – 1111Zinc 2By similarity
Metal bindingi114 – 1141Zinc 2By similarity
Metal bindingi154 – 1541Zinc 2By similarity
Metal bindingi184 – 1841Zinc 2By similarity
Metal bindingi495 – 4951Magnesium 1; catalyticBy similarity
Metal bindingi495 – 4951Magnesium 2; shared with RPB2By similarity
Metal bindingi497 – 4971Magnesium 1; catalyticBy similarity
Metal bindingi497 – 4971Magnesium 2; shared with RPB2By similarity
Metal bindingi499 – 4991Magnesium 1; catalyticBy similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. DNA-directed RNA polymerase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. poly(A) RNA binding Source: UniProtKB
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: Reactome
  2. DNA repair Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: Reactome
  5. nucleotide-excision repair Source: Reactome
  6. positive regulation of viral transcription Source: Reactome
  7. regulation of transcription, DNA-templated Source: UniProtKB
  8. RNA splicing Source: Reactome
  9. transcription-coupled nucleotide-excision repair Source: Reactome
  10. transcription elongation from RNA polymerase II promoter Source: Reactome
  11. transcription from RNA polymerase II promoter Source: UniProtKB
  12. transcription initiation from RNA polymerase II promoter Source: Reactome
  13. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, RNA-directed RNA polymerase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1470. mRNA Capping.
REACT_1628. Transcription-coupled NER (TC-NER).
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase II subunit RPB1 (EC:2.7.7.6)
Short name:
RNA polymerase II subunit B1
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 namesi
Name:POLR2A
Synonyms:POLR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9187. POLR2A.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. DNA-directed RNA polymerase II, core complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1810 – 18101R → A: Misexpression of a variety of small nuclear RNAs and small nucleolar RNAs. 1 Publication

Organism-specific databases

MIMi180660. gene+phenotype.
PharmGKBiPA33507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19701970DNA-directed RNA polymerase II subunit RPB1PRO_0000073940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei1810 – 18101Omega-N-methylated arginine; by CARM11 Publication
Modified residuei1843 – 18431Phosphoserine1 Publication
Modified residuei1849 – 18491Phosphoserine1 Publication
Modified residuei1854 – 18541Phosphothreonine1 Publication
Modified residuei1874 – 18741Phosphotyrosine1 Publication
Modified residuei1878 – 18781Phosphoserine1 Publication
Modified residuei1882 – 18821Phosphoserine1 Publication
Modified residuei1896 – 18961Phosphoserine1 Publication
Modified residuei1899 – 18991Phosphoserine1 Publication
Modified residuei1909 – 19091Phosphotyrosine2 Publications
Modified residuei1913 – 19131Phosphoserine2 Publications
Modified residuei1917 – 19171Phosphoserine2 Publications
Modified residuei1920 – 19201Phosphoserine2 Publications
Modified residuei1923 – 19231Phosphotyrosine2 Publications
Modified residuei1927 – 19271Phosphoserine2 Publications
Modified residuei1931 – 19311Phosphoserine2 Publications
Modified residuei1933 – 19331PhosphothreonineBy similarity
Modified residuei1934 – 19341Phosphoserine2 Publications

Post-translational modificationi

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 phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1.
Ubiquitinated by WWP2 leading to proteasomal degradation (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 similarity1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP24928.
PaxDbiP24928.
PRIDEiP24928.

PTM databases

PhosphoSiteiP24928.

Expressioni

Gene expression databases

BgeeiP24928.
CleanExiHS_POLR2A.
GenevestigatoriP24928.

Organism-specific databases

HPAiCAB012226.
CAB016388.
CAB022311.
HPA021563.
HPA053012.

Interactioni

Subunit structurei

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 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. Interacts (via C-terminus) with CMTR1, CTDSP1 and 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. Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding. 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). Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA and may couple transcription to pre-mRNA splicing.By similarity22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC73Q6P1J95EBI-295301,EBI-930143
DDX5P178443EBI-295301,EBI-351962
PAF1Q8N7H55EBI-295301,EBI-2607770
RPRD1BQ9NQG55EBI-295301,EBI-747925
SNF8Q96H202EBI-295301,EBI-747719
SUPT5HO002672EBI-295301,EBI-710464
XAB2Q9HCS72EBI-295301,EBI-295232

Protein-protein interaction databases

BioGridi111426. 224 interactions.
DIPiDIP-29011N.
IntActiP24928. 40 interactions.
MINTiMINT-156582.
STRINGi9606.ENSP00000314949.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GHQX-ray2.05C/D1795-1803[»]
2GHTX-ray1.80C/D1796-1803[»]
2LTONMR-B1804-1816[»]
3D9KX-ray2.20Y/Z1790-1803[»]
3D9LX-ray2.20Y/Z1790-1803[»]
3D9MX-ray1.75Y/Z1790-1803[»]
3D9NX-ray1.60Y/Z1790-1803[»]
3D9OX-ray2.00Z1790-1803[»]
3D9PX-ray2.10Y/Z1790-1803[»]
4JXTX-ray1.90B1787-1805[»]
ProteinModelPortaliP24928.
SMRiP24928. Positions 16-896, 1072-1475.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24928.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1593 – 159971
Repeati1600 – 160672; approximate
Repeati1608 – 161473
Repeati1615 – 162174
Repeati1622 – 162875
Repeati1629 – 163576
Repeati1636 – 164277
Repeati1643 – 164978
Repeati1650 – 165679
Repeati1657 – 1663710
Repeati1664 – 1670711
Repeati1671 – 1677712
Repeati1678 – 1684713
Repeati1685 – 1691714
Repeati1692 – 1698715
Repeati1699 – 1705716
Repeati1706 – 1712717
Repeati1713 – 1719718
Repeati1720 – 1726719
Repeati1727 – 1733720
Repeati1734 – 1740721
Repeati1741 – 1747722
Repeati1748 – 1754723
Repeati1755 – 1761724
Repeati1762 – 1768725
Repeati1769 – 1775726
Repeati1776 – 1782727
Repeati1783 – 1789728
Repeati1790 – 1796729
Repeati1797 – 1803730
Repeati1804 – 1810731
Repeati1811 – 1817732
Repeati1818 – 1824733
Repeati1825 – 1831734
Repeati1832 – 1838735
Repeati1839 – 1845736
Repeati1846 – 1852737
Repeati1853 – 1859738
Repeati1860 – 1866739
Repeati1867 – 1873740
Repeati1874 – 1880741
Repeati1881 – 1887742
Repeati1888 – 1894743
Repeati1895 – 1901744
Repeati1902 – 1908745
Repeati1909 – 1915746
Repeati1916 – 1922747
Repeati1923 – 1929748
Repeati1930 – 1936749
Repeati1940 – 1946750
Repeati1947 – 1953751; approximate
Repeati1954 – 1960752; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni833 – 84513Bridging helixAdd
BLAST
Regioni1593 – 1960368C-terminal domain (CTD); 52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRTEVKGN]Add
BLAST

Domaini

The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.1 Publication

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0086.
GeneTreeiENSGT00730000110946.
HOGENOMiHOG000222975.
HOVERGENiHBG004339.
InParanoidiP24928.
KOiK03006.
OMAiIVFNRQP.
OrthoDBiEOG7K0ZB8.
PhylomeDBiP24928.
TreeFamiTF103036.

Family and domain databases

InterProiIPR000722. 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]
PfamiPF04997. 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. 46 hits.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
PROSITEiPS00115. RNA_POL_II_REPEAT. 42 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P24928-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG
60 70 80 90 100
RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL
110 120 130 140 150
VKTMKVLRCV CFFCSKLLVD SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG
160 170 180 190 200
KNICEGGEEM DNKFGVEQPE GDEDLTKEKG HGGCGRYQPR IRRSGLELYA
210 220 230 240 250
EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP RYARPEWMIV
260 270 280 290 300
TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
310 320 330 340 350
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV
360 370 380 390 400
RGNLMGKRVD FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID
410 420 430 440 450
RLQELVRRGN SQYPGAKYII RDNGDRIDLR FHPKPSDLHL QTGYKVERHM
460 470 480 490 500
CDGDIVIFNR QPTLHKMSMM GHRVRILPWS TFRLNLSVTT PYNADFDGDE
510 520 530 540 550
MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD TLTAVRKFTK
560 570 580 590 600
RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
610 620 630 640 650
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG
660 670 680 690 700
SLVHISYLEM GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ
710 720 730 740 750
DIQNTIKKAK QDVIEVIEKA HNNELEPTPG NTLRQTFENQ VNRILNDARD
760 770 780 790 800
KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN ISQVIAVVGQ QNVEGKRIPF
810 820 830 840 850
GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT
860 870 880 890 900
AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
910 920 930 940 950
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN
960 970 980 990 1000
ELEREFERMR EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL
1010 1020 1030 1040 1050
PSDLHPIKVV EGVKELSKKL VIVNGDDPLS RQAQENATLL FNIHLRSTLC
1060 1070 1080 1090 1100
SRRMAEEFRL SGEAFDWLLG EIESKFNQAI AHPGEMVGAL AAQSLGEPAT
1110 1120 1130 1140 1150
QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT VFLLGQSARD
1160 1170 1180 1190 1200
AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
1210 1220 1230 1240 1250
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD
1260 1270 1280 1290 1300
NAEKLVLRIR IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG
1310 1320 1330 1340 1350
IEQISKVYMH LPQTDNKKKI IITEDGEFKA LQEWILETDG VSLMRVLSEK
1360 1370 1380 1390 1400
DVDPVRTTSN DIVEIFTVLG IEAVRKALER ELYHVISFDG SYVNYRHLAL
1410 1420 1430 1440 1450
LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM EAAAHGESDP
1460 1470 1480 1490 1500
MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
1510 1520 1530 1540 1550
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA
1560 1570 1580 1590 1600
ASDASGFSPG YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY
1610 1620 1630 1640 1650
EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY
1660 1670 1680 1690 1700
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
1710 1720 1730 1740 1750
PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPNYSP
1760 1770 1780 1790 1800
TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
1810 1820 1830 1840 1850
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPASPKYT PTSPSYSPSS
1860 1870 1880 1890 1900
PEYTPTSPKY SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP
1910 1920 1930 1940 1950
VYTPTSPKYS PTSPTYSPTS PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT
1960 1970
SPTYSLTSPA ISPDDSDEEN
Length:1,970
Mass (Da):217,176
Last modified:December 15, 2009 - v2
Checksum:i28D6FD25693A6472
GO
Isoform 2 (identifier: P24928-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     558-566: GEVMNLLMF → VCGPNGNLA
     567-1970: Missing.

Note: No experimental confirmation available.

Show »
Length:566
Mass (Da):63,641
Checksum:i0F3049DAF63F3B20
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1067 – 10671W → L in CAA52862. (PubMed:7622068)Curated
Sequence conflicti1449 – 14491D → Y in CAA52862. (PubMed:7622068)Curated
Sequence conflicti1835 – 18351A → T in CAA45125. (PubMed:1542581)Curated
Sequence conflicti1835 – 18351A → T in CAA52862. (PubMed:7622068)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921R → C.
Corresponds to variant rs2229198 [ dbSNP | Ensembl ].
VAR_051872

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei558 – 5669GEVMNLLMF → VCGPNGNLA in isoform 2. 1 PublicationVSP_056184
Alternative sequencei567 – 19701404Missing in isoform 2. 1 PublicationVSP_056185Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63564 mRNA. Translation: CAA45125.1.
X74874
, X74873, X74872, X74871, X74870 Genomic DNA. Translation: CAA52862.1.
AC113189 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90181.1.
BC067295 mRNA. Translation: AAH67295.1.
BC137231 mRNA. Translation: AAI37232.1.
PIRiI38186.
S21054.
RefSeqiNP_000928.1. NM_000937.4.
UniGeneiHs.270017.

Genome annotation databases

EnsembliENST00000572844; ENSP00000461879; ENSG00000181222. [P24928-2]
ENST00000621442; ENSP00000483957; ENSG00000181222.
GeneIDi5430.
KEGGihsa:5430.
UCSCiuc002ghf.4. human. [P24928-1]

Polymorphism databases

DMDMi281185484.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63564 mRNA. Translation: CAA45125.1 .
X74874
, X74873 , X74872 , X74871 , X74870 Genomic DNA. Translation: CAA52862.1 .
AC113189 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90181.1 .
BC067295 mRNA. Translation: AAH67295.1 .
BC137231 mRNA. Translation: AAI37232.1 .
PIRi I38186.
S21054.
RefSeqi NP_000928.1. NM_000937.4.
UniGenei Hs.270017.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
2LTO NMR - B 1804-1816 [» ]
3D9K X-ray 2.20 Y/Z 1790-1803 [» ]
3D9L X-ray 2.20 Y/Z 1790-1803 [» ]
3D9M X-ray 1.75 Y/Z 1790-1803 [» ]
3D9N X-ray 1.60 Y/Z 1790-1803 [» ]
3D9O X-ray 2.00 Z 1790-1803 [» ]
3D9P X-ray 2.10 Y/Z 1790-1803 [» ]
4JXT X-ray 1.90 B 1787-1805 [» ]
ProteinModelPortali P24928.
SMRi P24928. Positions 16-896, 1072-1475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111426. 224 interactions.
DIPi DIP-29011N.
IntActi P24928. 40 interactions.
MINTi MINT-156582.
STRINGi 9606.ENSP00000314949.

Chemistry

BindingDBi P24928.
ChEMBLi CHEMBL1641353.

PTM databases

PhosphoSitei P24928.

Polymorphism databases

DMDMi 281185484.

Proteomic databases

MaxQBi P24928.
PaxDbi P24928.
PRIDEi P24928.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000572844 ; ENSP00000461879 ; ENSG00000181222 . [P24928-2 ]
ENST00000621442 ; ENSP00000483957 ; ENSG00000181222 .
GeneIDi 5430.
KEGGi hsa:5430.
UCSCi uc002ghf.4. human. [P24928-1 ]

Organism-specific databases

CTDi 5430.
GeneCardsi GC17P007387.
H-InvDB HIX0173727.
HGNCi HGNC:9187. POLR2A.
HPAi CAB012226.
CAB016388.
CAB022311.
HPA021563.
HPA053012.
MIMi 180660. gene+phenotype.
neXtProti NX_P24928.
PharmGKBi PA33507.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0086.
GeneTreei ENSGT00730000110946.
HOGENOMi HOG000222975.
HOVERGENi HBG004339.
InParanoidi P24928.
KOi K03006.
OMAi IVFNRQP.
OrthoDBi EOG7K0ZB8.
PhylomeDBi P24928.
TreeFami TF103036.

Enzyme and pathway databases

Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1470. mRNA Capping.
REACT_1628. Transcription-coupled NER (TC-NER).
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSi POLR2A. human.
EvolutionaryTracei P24928.
GeneWikii POLR2A.
GenomeRNAii 5430.
NextBioi 21009.
PROi P24928.
SOURCEi Search...

Gene expression databases

Bgeei P24928.
CleanExi HS_POLR2A.
Genevestigatori P24928.

Family and domain databases

InterProi 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 ]
Pfami 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. 46 hits.
[Graphical view ]
SMARTi SM00663. RPOLA_N. 1 hit.
[Graphical view ]
PROSITEi PS00115. RNA_POL_II_REPEAT. 42 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Testis.
  6. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
    Kershnar E., Wu S.-Y., Chiang C.-M.
    J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
  7. Cited for: INTERACTION WITH SAFB.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; NCL; SUPT5H AND CDK9.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTATSF1.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FNBP3.
  11. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNCRIP.
  12. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
    Rossow K.L., Janknecht R.
    Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX5.
  13. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNL2.
  15. Cited for: INTERACTION WITH MEN1.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFRS19.
  17. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETD2.
  18. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETD2.
  19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1909 AND TYR-1923, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAF1 IN PAF1/RNA POLYMERASE II.
    Tissue: Fetal pancreas.
  21. "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export."
    Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.
    Genes Dev. 21:160-174(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT6H, PHOSPHORYLATION.
  22. "The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity."
    Haline-Vaz T., Silva T.C.L., Zanchin N.I.T.
    Biochem. Biophys. Res. Commun. 372:719-724(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CMTR1.
  23. "Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II."
    Becker R., Loll B., Meinhart A.
    J. Biol. Chem. 283:22659-22669(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAF8.
  24. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS RNA-DIRECTED RNA POLYMERASE.
  25. "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
    Lee J.H., Skalnik D.G.
    Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETD1A; SETD1B AND WDR82.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1849; TYR-1874; SER-1896; TYR-1909; SER-1913; SER-1920; TYR-1923; SER-1927 AND SER-1934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
    Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
    J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF7IP.
  29. "TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II."
    Akhtar M.S., Heidemann M., Tietjen J.R., Zhang D.W., Chapman R.D., Eick D., Ansari A.Z.
    Mol. Cell 34:387-393(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK7.
  30. "TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II."
    Glover-Cutter K., Larochelle S., Erickson B., Zhang C., Shokat K., Fisher R.P., Bentley D.L.
    Mol. Cell. Biol. 29:5455-5464(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK7 AND CDK9.
  31. "Binding to DNA of the RNA-polymerase II C-terminal domain allows discrimination between Cdk7 and Cdk9 phosphorylation."
    Lolli G.
    Nucleic Acids Res. 37:1260-1268(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK7.
  32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1843; THR-1854; SER-1878; SER-1882; SER-1899; SER-1913; SER-1917; SER-1920; SER-1927; SER-1931 AND SER-1934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  33. "RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."
    Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.
    Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RECQL5, FUNCTION.
  34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "The RNA polymerase II C-terminal domain promotes splicing activation through recruitment of a U2AF65-Prp19 complex."
    David C.J., Boyne A.R., Millhouse S.R., Manley J.L.
    Genes Dev. 25:972-983(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH U2AF2.
  37. "Transcription factor IIS cooperates with the E3 ligase UBR5 to ubiquitinate the CDK9 subunit of the positive transcription elongation factor B."
    Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K., Price D.H., Coulombe B.
    J. Biol. Chem. 286:5012-5022(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK9.
  38. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1917 AND SER-1931, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "The C-terminal domain of RNA polymerase II is modified by site-specific methylation."
    Sims R.J. III, Rojas L.A., Beck D., Bonasio R., Schuller R., Drury W.J. III, Eick D., Reinberg D.
    Science 332:99-103(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-1810 BY CARM1, MUTAGENESIS OF ARG-1810.
  40. "Ser7 phosphorylation of the CTD recruits the RPAP2 Ser5 phosphatase to snRNA genes."
    Egloff S., Zaborowska J., Laitem C., Kiss T., Murphy S.
    Mol. Cell 45:111-122(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DOMAIN.
  41. "Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair."
    Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M., Nardo T., Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M., Kinoshita A., Ono S., Takenaka K., Masuyama R., Kudo T., Slor H., Utani A.
    , Tateishi S., Yamashita S., Stefanini M., Lehmann A.R., Yoshiura K.I., Ogi T.
    Nat. Genet. 44:586-592(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  42. "Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1."
    Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., Dixon J.E., Noel J.P.
    Mol. Cell 24:759-770(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1796-1803 IN COMPLEX WITH CTDSP1, DEPHOSPHORYLATION.
  43. "Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5."
    Kassube S.A., Jinek M., Fang J., Tsutakawa S., Nogales E.
    Nat. Struct. Mol. Biol. 20:892-899(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH RECQL5, INTERACTION WITH RECQL5 AND TCEA1, SUBUNIT, FUNCTION.

Entry informationi

Entry nameiRPB1_HUMAN
AccessioniPrimary (citable) accession number: P24928
Secondary accession number(s): A6NN93, B9EH88, Q6NX41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 2009
Last modified: November 26, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3