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   27-MAR-2024, entry version 213.
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).
RN   [8]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH ZN(2+),
RP   FUNCTION OF POL II, AND SUBUNIT.
RX   PubMed=27193682; DOI=10.1038/nature17970;
RA   He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.;
RT   "Near-atomic resolution visualization of human transcription promoter
RT   opening.";
RL   Nature 533:359-365(2016).
RN   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION OF POL II, AND
RP   SUBUNIT.
RX   PubMed=30190596; DOI=10.1038/s41594-018-0118-5;
RA   Jishage M., Yu X., Shi Y., Ganesan S.J., Chen W.Y., Sali A., Chait B.T.,
RA   Asturias F.J., Roeder R.G.;
RT   "Architecture of Pol II(G) and molecular mechanism of transcription
RT   regulation by Gdown1.";
RL   Nat. Struct. Mol. Biol. 25:859-867(2018).
CC   -!- FUNCTION: Core component of RNA polymerase II (Pol II), a DNA-dependent
CC       RNA polymerase which synthesizes mRNA precursors and many functional
CC       non-coding RNAs using the four ribonucleoside triphosphates as
CC       substrates. Pol II is the central component of the basal RNA polymerase
CC       II transcription machinery. It is composed of mobile elements that move
CC       relative to each other. POLR2I/RPB9 is part of the upper jaw
CC       surrounding the central large cleft and thought to grab the incoming
CC       DNA template. {ECO:0000250|UniProtKB:P27999,
CC       ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596,
CC       ECO:0000269|PubMed:9852112}.
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) core complex
CC       consisting of 12 subunits: a ten-subunit catalytic core composed of
CC       POLR2A/RPB1, POLR2B/RPB2, POLR2C/RPB3, POLR2I/RPB9, POLR2J/RPB11,
CC       POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and
CC       POLR2L/RPABC5 and a mobile stalk composed of two subunits POLR2D/RPB4
CC       and POLR2G/RPB7, protruding from the core and functioning primarily in
CC       transcription initiation. Part of Pol II(G) complex, in which Pol II
CC       core associates with an additional subunit POLR2M; unlike conventional
CC       Pol II, Pol II(G) functions as a transcriptional repressor. Part of
CC       TBP-based Pol II pre-initiation complex (PIC), in which Pol II core
CC       assembles with general transcription factors and other specific
CC       initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1,
CC       ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and
CC       TBP; this large multi-subunit PIC complex mediates DNA unwinding and
CC       targets Pol II core to the transcription start site where the first
CC       phosphodiester bond forms. {ECO:0000269|PubMed:27193682,
CC       ECO:0000269|PubMed:30190596, 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   EMDB; EMD-22294; -.
DR   EMDB; EMD-23255; -.
DR   EMDB; EMD-7997; -.
DR   EMDB; EMD-8132; -.
DR   EMDB; EMD-8133; -.
DR   EMDB; EMD-8134; -.
DR   EMDB; EMD-8135; -.
DR   EMDB; EMD-8136; -.
DR   EMDB; EMD-8137; -.
DR   EMDB; EMD-8138; -.
DR   SMR; P36954; -.
DR   BioGRID; 111434; 133.
DR   ComplexPortal; CPX-2387; DNA-directed RNA polymerase II complex, Pol II(G) variant.
DR   ComplexPortal; CPX-7481; DNA-directed RNA polymerase II complex.
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; 9606-ENSP00000221859; -.
DR   PeptideAtlas; P36954; -.
DR   ProteomicsDB; 55242; -.
DR   Pumba; P36954; -.
DR   Antibodypedia; 29696; 206 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   AGR; HGNC:9196; -.
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; DTSMVLF; -.
DR   OrthoDB; 19808at2759; -.
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; 831 hits in 1172 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 205 other cell types or tissues.
DR   ExpressionAtlas; P36954; baseline and differential.
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 transcription elongation by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation at 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   Gene3D; 2.20.25.10; -; 2.
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; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR11239:SF1; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9; 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   SUPFAM; SSF57783; Zinc beta-ribbon; 2.
DR   PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
DR   Genevisible; P36954; HS.
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:0000269|PubMed:27193682,
FT                   ECO:0007744|PDB:5IY6"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27193682,
FT                   ECO:0007744|PDB:5IY6"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27193682,
FT                   ECO:0007744|PDB:5IY6"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27193682,
FT                   ECO:0007744|PDB:5IY6"
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                   ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IY6"
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                   ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IY6"
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                   ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IY6"
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                   ECO:0000269|PubMed:27193682, ECO:0007744|PDB:5IY6"
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
//