RPB11_HUMAN
ID RPB11_HUMAN Reviewed; 117 AA.
AC P52435; A5D6V8; O43375;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB11-a;
DE Short=RNA polymerase II subunit B11-a;
DE Short=RPB11a;
DE AltName: Full=DNA-directed RNA polymerase II subunit J-1;
DE AltName: Full=RNA polymerase II 13.3 kDa subunit;
GN Name=POLR2J; Synonyms=POLR2J1;
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 [MRNA].
RC TISSUE=Colon;
RX PubMed=8797801; DOI=10.1016/0014-5793(96)00277-3;
RA Fanciulli M., Bruno T., Cerboni C., Bonetto F., Iacobini C., Frati L.,
RA Piccoli M., Floridi A., Santoni A., Punturieri A.;
RT "Cloning of a novel human RNA polymerase II subunit downregulated by
RT doxorubicin: new potential mechanisms of drug related toxicity.";
RL FEBS Lett. 384:48-52(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9201987; DOI=10.1074/jbc.272.27.16815;
RA Acker J., de Graaff M., Cheynel I., Khazak V., Kedinger C., Vigneron M.;
RT "Interactions between the human RNA polymerase II subunits.";
RL J. Biol. Chem. 272:16815-16821(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Kidney;
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 [6]
RP PROTEIN SEQUENCE OF 1-18; 27-37; 48-62 AND 75-104, ACETYLATION AT MET-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
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 [8]
RP INTERACTION WITH AATF.
RX PubMed=10783144; DOI=10.1096/fasebj.14.7.904;
RA Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S., Iacobini C.,
RA Floridi A., Passananti C.;
RT "Identification of a novel partner of RNA polymerase II subunit 11, Che-1,
RT which interacts with and affects the growth suppression function of Rb.";
RL FASEB J. 14:904-912(2000).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=11747469; DOI=10.1186/1471-2199-2-14;
RA Grandemange S., Schaller S., Yamano S., Du Manoir S., Shpakovski G.V.,
RA Mattei M.-G., Kedinger C., Vigneron M.;
RT "A human RNA polymerase II subunit is encoded by a recently generated
RT multigene family.";
RL BMC Mol. Biol. 2:14-14(2001).
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. RPB11 is part of the
CC core element with the central large cleft (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. Interacts with AATF. {ECO:0000269|PubMed:10783144,
CC ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC P52435; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-394753, EBI-11974185;
CC P52435; P15173: MYOG; NbExp=3; IntAct=EBI-394753, EBI-3906629;
CC P52435; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-394753, EBI-741158;
CC P52435; O43482: OIP5; NbExp=3; IntAct=EBI-394753, EBI-536879;
CC P52435; O15160: POLR1C; NbExp=11; IntAct=EBI-394753, EBI-1055079;
CC P52435; O00560: SDCBP; NbExp=3; IntAct=EBI-394753, EBI-727004;
CC P52435; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-394753, EBI-12004298;
CC P52435; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-394753, EBI-3650647;
CC P52435; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-394753, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. High expression was found
CC in heart and skeletal muscle. {ECO:0000269|PubMed:11747469}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC polymerase subunit family. {ECO:0000305}.
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DR EMBL; X82385; CAA57785.1; -; mRNA.
DR EMBL; L37127; AAD05361.1; -; mRNA.
DR EMBL; X98433; CAA67075.1; -; mRNA.
DR EMBL; AK290515; BAF83204.1; -; mRNA.
DR EMBL; AC093668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024165; AAH24165.1; -; mRNA.
DR EMBL; BC065711; AAH65711.1; -; mRNA.
DR EMBL; BC139902; AAI39903.1; -; mRNA.
DR EMBL; BC141830; AAI41831.1; -; mRNA.
DR CCDS; CCDS5724.1; -.
DR PIR; S71325; S71325.
DR RefSeq; NP_006225.1; NM_006234.4.
DR PDB; 5IY6; EM; 7.20 A; K=1-117.
DR PDB; 5IY7; EM; 8.60 A; K=1-117.
DR PDB; 5IY8; EM; 7.90 A; K=1-117.
DR PDB; 5IY9; EM; 6.30 A; K=1-117.
DR PDB; 5IYA; EM; 5.40 A; K=1-117.
DR PDB; 5IYB; EM; 3.90 A; K=1-117.
DR PDB; 5IYC; EM; 3.90 A; K=1-117.
DR PDB; 5IYD; EM; 3.90 A; K=1-117.
DR PDB; 6DRD; EM; 3.90 A; K=1-117.
DR PDB; 6O9L; EM; 7.20 A; K=1-117.
DR PDB; 6XRE; EM; 4.60 A; K=1-117.
DR PDB; 7LBM; EM; 4.80 A; K=1-117.
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; P52435; -.
DR SMR; P52435; -.
DR BioGRID; 111435; 136.
DR CORUM; P52435; -.
DR DIP; DIP-32913N; -.
DR IntAct; P52435; 49.
DR MINT; P52435; -.
DR STRING; 9606.ENSP00000292614; -.
DR iPTMnet; P52435; -.
DR PhosphoSitePlus; P52435; -.
DR BioMuta; POLR2J; -.
DR EPD; P52435; -.
DR jPOST; P52435; -.
DR MassIVE; P52435; -.
DR MaxQB; P52435; -.
DR PaxDb; P52435; -.
DR PeptideAtlas; P52435; -.
DR PRIDE; P52435; -.
DR ProteomicsDB; 56486; -.
DR Antibodypedia; 31080; 300 antibodies from 27 providers.
DR DNASU; 5439; -.
DR Ensembl; ENST00000292614.10; ENSP00000292614.5; ENSG00000005075.16.
DR GeneID; 5439; -.
DR KEGG; hsa:5439; -.
DR MANE-Select; ENST00000292614.10; ENSP00000292614.5; NM_006234.6; NP_006225.1.
DR UCSC; uc003uzp.2; human.
DR CTD; 5439; -.
DR DisGeNET; 5439; -.
DR GeneCards; POLR2J; -.
DR HGNC; HGNC:9197; POLR2J.
DR HPA; ENSG00000005075; Low tissue specificity.
DR MIM; 604150; gene.
DR neXtProt; NX_P52435; -.
DR OpenTargets; ENSG00000005075; -.
DR PharmGKB; PA33517; -.
DR VEuPathDB; HostDB:ENSG00000005075; -.
DR eggNOG; KOG4392; Eukaryota.
DR GeneTree; ENSGT00550000074975; -.
DR HOGENOM; CLU_090381_2_2_1; -.
DR InParanoid; P52435; -.
DR OMA; NQPERYE; -.
DR OrthoDB; 1398114at2759; -.
DR PhylomeDB; P52435; -.
DR TreeFam; TF103044; -.
DR PathwayCommons; P52435; -.
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; P52435; -.
DR SIGNOR; P52435; -.
DR BioGRID-ORCS; 5439; 421 hits in 659 CRISPR screens.
DR ChiTaRS; POLR2J; human.
DR GeneWiki; POLR2J; -.
DR GenomeRNAi; 5439; -.
DR Pharos; P52435; Tbio.
DR PRO; PR:P52435; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P52435; protein.
DR Bgee; ENSG00000005075; Expressed in gastrocnemius and 103 other tissues.
DR ExpressionAtlas; P52435; baseline and differential.
DR Genevisible; P52435; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001055; F:RNA polymerase II activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR CDD; cd06926; RNAP_II_RPB11; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR InterPro; IPR037685; RBP11.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR009025; RBP11-like_dimer.
DR InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR Pfam; PF13656; RNA_pol_L_2; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription.
FT CHAIN 1..117
FT /note="DNA-directed RNA polymerase II subunit RPB11-a"
FT /id="PRO_0000149309"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6"
SQ SEQUENCE 117 AA; 13293 MW; 6F78AB256EF8F647 CRC64;
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG
YKVPHPLEHK IIIRVQTTPD YSPQEAFTNA ITDLISELSL LEERFRVAIK DKQEGIE
