(data stored in ACNUC11299 zone)

HOGENOM: HS17_PE388

ID   HS17_PE388                           STANDARD;      PRT;   1970 AA.
AC   HS17_PE388; P24928; A6NN93; B9EH88;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB1; Short=RNA
DE   polymerase II subunit B1; EC=2.7.7.6;AltName: Full=DNA-directed RNA
DE   polymerase II subunit A;AltName: Full=DNA-directed RNA polymerase III
DE   largest subunit;AltName: Full=RNA-directed RNA polymerase II subunit
DE   RPB1; EC=2.7.7 48; (HS17.PE388).
GN   Name=POLR2A; Synonyms=POLR2;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS17.PE388.
CC       Homo sapiens chromosome 17 GRCh37  sequence 1..81195210 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:RPB1_HUMAN
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Largest and catalytic component of RNA polymerase II
CC       which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Forms the polymerase active center together with the second
CC       largest subunit. Pol II is the central component of the basal RNA
CC       polymerase II transcription machinery. It is composed of mobile
CC       elements that move relative to each other. RPB1 is part of the
CC       core element with the central large cleft, the clamp element that
CC       moves to open and close the cleft and the jaws that are thought to
CC       grab the incoming DNA template. At the start of transcription, a
CC       single stranded DNA template strand of the promoter is positioned
CC       within the central active site cleft of Pol II. A bridging helix
CC       emanates from RPB1 and crosses the cleft near the catalytic site
CC       and is thought to promote translocation of Pol II by acting as a
CC       ratchet that moves the RNA-DNA hybrid through the active site by
CC       switching from straight to bent conformations at each step of
CC       nucleotide addition. During transcription elongation, Pol II moves
CC       on the template as the transcript elongates. Elongation is
CC       influenced by the phosphorylation status of the C-terminal domain
CC       (CTD) of Pol II largest subunit (RPB1), which serves as a platform
CC       for assembly of factors that regulate transcription initiation,
CC       elongation, termination and mRNA processing. Acts as a RNA-
CC       dependent RNA polymerase when associated with small delta antigen
CC       of Hepatitis delta virus, acting both as a replicate and
CC       transcriptase for the viral RNA circular genome.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC       consisting of 12 subunits. The phosphorylated C-terminal domain
CC       interacts with FNBP3 and SYNCRIP. Interacts with SAFB/SAFB1.
CC       Interacts with CCNL1 and MYO1C (By similarity). Interacts with
CC       CCNL2 and SFRS19. Component of a complex which is at least
CC       composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9
CC       and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. Interacts
CC       with PAF1. Interacts (via C-terminus) with FTSJD2, CTDSP1 and
CC       SCAF8. Interacts via the phosphorylated C-terminal domain with
CC       WDR82 and with SETD1A and SETD1B only in the presence of WDR82.
CC       Interacts with ATF7IP. When phosphorylated at 'Ser-5', interacts
CC       with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2'
CC       does not interact.
CC   -!- INTERACTION:
CC       O00267:SUPT5H; NbExp=2; IntAct=EBI-295301, EBI-710464;
CC       Q9HCS7:XAB2; NbExp=2; IntAct=EBI-295301, EBI-295232;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD)
CC       can be highly phosphorylated. The phosphorylation activates Pol
CC       II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5'
CC       of the heptapeptide repeat. The phosphorylation state is believed
CC       to result from the balanced action of site-specific CTD kinases
CC       and phosphataes, and a "CTD code" that specifies the position of
CC       Pol II within the transcription cycle has been proposed.
CC   -!- PTM: Dephosphorylated by the protein phosphatase CTDSP1.
CC   -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation (By
CC       similarity).
CC   -!- PTM: Methylated at Arg-1810 by CARM1. Methylation occurs only when
CC       the CTD is hypophosphorylated, and phosphorylation at Ser-1805 and
CC       Ser-1808 prevent methylation (in vitro). It is assumed that
CC       methylation occurs prior to phosphorylation and transcription
CC       initiation. CTD methylation may facilitate the expression of
CC       select RNAs.
CC   -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the
CC       RNA polymerase II transcribing complex probably involves a two-
CC       step mechanism. The initial binding seems to occur at the entry
CC       (E) site and involves a magnesium ion temporarily coordinated by
CC       three conserved aspartate residues of the two largest RNA Pol II
CC       subunits. The ribonucleoside triphosphate is transferred by a
CC       rotation to the nucelotide addition (A) site for pairing with the
CC       template DNA. The catalytic A site involves three conserved
CC       aspartate residues of the RNA Pol II largest subunit which
CC       permanently coordinate a second magnesium ion.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC   -!- GENE_FAMILY: HOG000222975 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000181222;ENST00000322644;ENSP00000314949.
DR   EMBL; AC113189; - ;
DR   EMBL; AK293777; - ;
DR   EMBL; AK304882; - ;
DR   EMBL; BC067295; - ;
DR   EMBL; BC137231; - ;
DR   EMBL; CH471108; - ;
DR   EMBL; X63564; - ;
DR   EMBL; X74870; - ;
DR   EMBL; X74871; - ;
DR   EMBL; X74872; - ;
DR   EMBL; X74873; - ;
DR   EMBL; X74874; - ;
DR   UniProtKB/Swiss-Prot; P24928; A6NN93; B9EH88; -.
DR   EMBL; X63564; CAA45125.1; -; mRNA.
DR   EMBL; X74874; CAA52862.1; -; Genomic_DNA.
DR   EMBL; X74873; CAA52862.1; JOINED; Genomic_DNA.
DR   EMBL; X74872; CAA52862.1; JOINED; Genomic_DNA.
DR   EMBL; X74871; CAA52862.1; JOINED; Genomic_DNA.
DR   EMBL; X74870; CAA52862.1; JOINED; Genomic_DNA.
DR   EMBL; AC113189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90181.1; -; Genomic_DNA.
DR   EMBL; BC137231; AAI37232.1; -; mRNA.
DR   IPI; IPI00031627; -.
DR   PIR; I38186; I38186.
DR   PIR; S21054; S21054.
DR   RefSeq; NP_000928.1; NM_000937.4.
DR   UniGene; Hs.270017; -.
DR   PDB; 2GHQ; X-ray; 2.05 A; C/D=1795-1803.
DR   PDB; 2GHT; X-ray; 1.80 A; C/D=1796-1803.
DR   PDBsum; 2GHQ; -.
DR   PDBsum; 2GHT; -.
DR   ProteinModelPortal; P24928; -.
DR   SMR; P24928; 16-903, 1054-1477.
DR   DIP; DIP-29011N; -.
DR   IntAct; P24928; 21.
DR   MINT; MINT-156582; -.
DR   STRING; P24928; -.
DR   PhosphoSite; P24928; -.
DR   PRIDE; P24928; -.
DR   Ensembl; ENST00000322644; ENSP00000314949; ENSG00000181222.
DR   GeneID; 5430; -.
DR   KEGG; hsa:5430; -.
DR   UCSC; uc002ghf.2; human.
DR   CTD; 5430; -.
DR   GeneCards; GC17P007329; -.
DR   H-InvDB; HIX0039202; -.
DR   HGNC; HGNC:9187; POLR2A.
DR   HPA; CAB012226; -.
DR   HPA; CAB016388; -.
DR   HPA; CAB022311; -.
DR   HPA; HPA021563; -.
DR   MIM; 180660; gene+phenotype.
DR   neXtProt; NX_P24928; -.
DR   PharmGKB; PA33507; -.
DR   eggNOG; prNOG15419; -.
DR   InParanoid; P24928; -.
DR   OMA; SPTSPHY; -.
DR   OrthoDB; EOG4JWVCM; -.
DR   PhylomeDB; P24928; -.
DR   Reactome; REACT_12472; Regulatory RNA pathways.
DR   Reactome; REACT_1675; mRNA Processing.
DR   Reactome; REACT_1788; Transcription.
DR   Reactome; REACT_1892; Elongation arrest and recovery.
DR   Reactome; REACT_216; DNA Repair.
DR   Reactome; REACT_6185; HIV Infection.
DR   Reactome; REACT_71; Gene Expression.
DR   Reactome; REACT_769; Pausing and recovery of elongation.
DR   NextBio; 21009; -.
DR   ArrayExpress; P24928; -.
DR   Bgee; P24928; -.
DR   CleanEx; HS_POLR2A; -.
DR   Genevestigator; P24928; -.
DR   GermOnline; ENSG00000181222; Homo sapiens.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; NAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:EC.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR   GO; GO:0006370; P:mRNA capping; TAS:Reactome.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; TAS:Reactome.
DR   GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:GOC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; EXP:Reactome.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; EXP:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0016032; P:viral reproduction; TAS:Reactome.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 46.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 42.
DR   HOGENOMDNA; HS17.PE388; -.
KW   ENSG000001812221755old_1320000031; ENSP000003149497901old_1320000031;
KW   B4DET1_HUMAN; B4E3V7_HUMAN; Q6NX41_HUMAN; AC113189; AK293777; AK304882;
KW   BC137231; CH471108; X63564; X74870; X74871; X74872; X74873; X74874;
KW   3D-structure; Acetylation; Complete proteome; DNA-binding;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding; Methylation;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Transcription; Transferase;
KW   Ubl conjugation; Zinc.
SQ   SEQUENCE   1970 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
     RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
     SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
     HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
     RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
     HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
     FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
     RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
     TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
     TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
     NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
     GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
     HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN
     ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA
     MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
     VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR
     EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL
     VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI
     AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT
     VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
     DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR
     IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI
     IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER
     ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM
     EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
     MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG
     YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP
     SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
     TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
     YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
     SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPASPKYT PTSPSYSPSS PEYTPTSPKY
     SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS
     PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN
//

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