RPB9_HUMAN
ID RPB9_HUMAN Reviewed; 125 AA.
AC P36954; B2R5J2; Q6NW05;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB9;
DE Short=RNA polymerase II subunit B9;
DE AltName: Full=DNA-directed RNA polymerase II subunit I;
DE AltName: Full=RNA polymerase II 14.5 kDa subunit;
DE Short=RPB14.5;
GN Name=POLR2I;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8265347; DOI=10.1093/nar/21.23.5345;
RA Acker J., Wintzerith M., Vigneron M., Kedinger C.;
RT "Structure of the gene encoding the 14.5 kDa subunit of human RNA
RT polymerase II.";
RL Nucleic Acids Res. 21:5345-5350(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines that
RT conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB9 is part of the
CC upper jaw surrounding the central large cleft and thought to grab the
CC incoming DNA template (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC P36954; P55212: CASP6; NbExp=3; IntAct=EBI-395202, EBI-718729;
CC P36954; P30519: HMOX2; NbExp=3; IntAct=EBI-395202, EBI-712096;
CC P36954; P13473-2: LAMP2; NbExp=3; IntAct=EBI-395202, EBI-21591415;
CC P36954; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-395202, EBI-5280197;
CC P36954; P62826: RAN; NbExp=3; IntAct=EBI-395202, EBI-286642;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9852112}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; Z23102; CAA80649.1; -; Genomic_DNA.
DR EMBL; AK312206; BAG35139.1; -; mRNA.
DR EMBL; AD001527; AAB51181.1; -; Genomic_DNA.
DR EMBL; BC017112; AAH17112.1; -; mRNA.
DR EMBL; BC067794; AAH67794.1; -; mRNA.
DR CCDS; CCDS12487.1; -.
DR PIR; S41621; S41621.
DR RefSeq; NP_006224.1; NM_006233.4.
DR PDB; 5IY6; EM; 7.20 A; I=1-125.
DR PDB; 5IY7; EM; 8.60 A; I=1-125.
DR PDB; 5IY8; EM; 7.90 A; I=1-125.
DR PDB; 5IY9; EM; 6.30 A; I=1-125.
DR PDB; 5IYA; EM; 5.40 A; I=1-125.
DR PDB; 5IYB; EM; 3.90 A; I=1-125.
DR PDB; 5IYC; EM; 3.90 A; I=1-125.
DR PDB; 5IYD; EM; 3.90 A; I=1-125.
DR PDB; 6DRD; EM; 3.90 A; I=1-125.
DR PDB; 6O9L; EM; 7.20 A; I=1-125.
DR PDB; 6XRE; EM; 4.60 A; I=1-125.
DR PDB; 7LBM; EM; 4.80 A; I=1-125.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 6DRD; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6XRE; -.
DR PDBsum; 7LBM; -.
DR AlphaFoldDB; P36954; -.
DR SMR; P36954; -.
DR BioGRID; 111434; 114.
DR CORUM; P36954; -.
DR DIP; DIP-32917N; -.
DR IntAct; P36954; 47.
DR MINT; P36954; -.
DR STRING; 9606.ENSP00000221859; -.
DR iPTMnet; P36954; -.
DR PhosphoSitePlus; P36954; -.
DR BioMuta; POLR2I; -.
DR DMDM; 548702; -.
DR EPD; P36954; -.
DR jPOST; P36954; -.
DR MassIVE; P36954; -.
DR MaxQB; P36954; -.
DR PaxDb; P36954; -.
DR PeptideAtlas; P36954; -.
DR PRIDE; P36954; -.
DR ProteomicsDB; 55242; -.
DR Antibodypedia; 29696; 192 antibodies from 28 providers.
DR DNASU; 5438; -.
DR Ensembl; ENST00000221859.9; ENSP00000221859.3; ENSG00000105258.9.
DR GeneID; 5438; -.
DR KEGG; hsa:5438; -.
DR MANE-Select; ENST00000221859.9; ENSP00000221859.3; NM_006233.5; NP_006224.1.
DR UCSC; uc002ode.4; human.
DR CTD; 5438; -.
DR GeneCards; POLR2I; -.
DR HGNC; HGNC:9196; POLR2I.
DR HPA; ENSG00000105258; Low tissue specificity.
DR MIM; 180662; gene.
DR neXtProt; NX_P36954; -.
DR OpenTargets; ENSG00000105258; -.
DR PharmGKB; PA33516; -.
DR VEuPathDB; HostDB:ENSG00000105258; -.
DR eggNOG; KOG2691; Eukaryota.
DR GeneTree; ENSGT00550000075063; -.
DR HOGENOM; CLU_093932_0_1_1; -.
DR InParanoid; P36954; -.
DR OMA; CRDCNNM; -.
DR OrthoDB; 1421187at2759; -.
DR PhylomeDB; P36954; -.
DR TreeFam; TF103032; -.
DR PathwayCommons; P36954; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR SignaLink; P36954; -.
DR SIGNOR; P36954; -.
DR BioGRID-ORCS; 5438; 796 hits in 1097 CRISPR screens.
DR ChiTaRS; POLR2I; human.
DR GeneWiki; POLR2I; -.
DR GenomeRNAi; 5438; -.
DR Pharos; P36954; Tbio.
DR PRO; PR:P36954; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P36954; protein.
DR Bgee; ENSG00000105258; Expressed in left testis and 203 other tissues.
DR ExpressionAtlas; P36954; baseline and differential.
DR Genevisible; P36954; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0001193; P:maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
DR CDD; cd10508; Zn-ribbon_RPB9; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034012; Zn_ribbon_RPB9_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-directed RNA polymerase; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Zinc; Zinc-finger.
FT CHAIN 1..125
FT /note="DNA-directed RNA polymerase II subunit RPB9"
FT /id="PRO_0000121467"
FT ZN_FING 17..42
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 82..124
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27999"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 125 AA; 14523 MW; 6520687BB57EE018 CRC64;
MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH
EVDELTQIIA DVSQDPTLPR TEDHPCQKCG HKEAVFFQSH SARAEDAMRL YYVCTAPHCG
HRWTE
