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RPB9_MOUSE
ID   RPB9_MOUSE              Reviewed;         125 AA.
AC   P60898;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 143.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC       of 12 subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P32529}.
CC   -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; BC062812; AAH62812.1; -; mRNA.
DR   CCDS; CCDS21084.1; -.
DR   RefSeq; NP_081535.1; NM_027259.1.
DR   AlphaFoldDB; P60898; -.
DR   SMR; P60898; -.
DR   BioGRID; 213757; 9.
DR   IntAct; P60898; 11.
DR   MINT; P60898; -.
DR   STRING; 10090.ENSMUSP00000019882; -.
DR   PhosphoSitePlus; P60898; -.
DR   EPD; P60898; -.
DR   MaxQB; P60898; -.
DR   PaxDb; P60898; -.
DR   PeptideAtlas; P60898; -.
DR   PRIDE; P60898; -.
DR   ProteomicsDB; 260922; -.
DR   Antibodypedia; 29696; 192 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000019882; ENSMUSP00000019882; ENSMUSG00000019738.
DR   GeneID; 69920; -.
DR   KEGG; mmu:69920; -.
DR   UCSC; uc009gdt.1; mouse.
DR   CTD; 5438; -.
DR   MGI; MGI:1917170; Polr2i.
DR   VEuPathDB; HostDB:ENSMUSG00000019738; -.
DR   eggNOG; KOG2691; Eukaryota.
DR   GeneTree; ENSGT00550000075063; -.
DR   InParanoid; P60898; -.
DR   OMA; CRDCNNM; -.
DR   OrthoDB; 1421187at2759; -.
DR   PhylomeDB; P60898; -.
DR   TreeFam; TF103032; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 69920; 28 hits in 113 CRISPR screens.
DR   ChiTaRS; Polr2i; mouse.
DR   PRO; PR:P60898; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P60898; protein.
DR   Bgee; ENSMUSG00000019738; Expressed in internal carotid artery and 254 other tissues.
DR   ExpressionAtlas; P60898; baseline and differential.
DR   Genevisible; P60898; MM.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; ISS: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   Acetylation; DNA-directed RNA polymerase; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Zinc; Zinc-finger.
FT   CHAIN           1..125
FT                   /note="DNA-directed RNA polymerase II subunit RPB9"
FT                   /id="PRO_0000121468"
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:0000250|UniProtKB:P36954"
SQ   SEQUENCE   125 AA;  14523 MW;  6520687BB57EE018 CRC64;
     MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH
     EVDELTQIIA DVSQDPTLPR TEDHPCQKCG HKEAVFFQSH SARAEDAMRL YYVCTAPHCG
     HRWTE
 
 
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