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   02-SEP-2026, entry version 217.
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).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH PTPN6.
RX   PubMed=37595871; DOI=10.1016/j.jbc.2023.105164;
RA   Kumar A., Schwab M., Laborit Labrada B., Silveira M.A.D., Goudreault M.,
RA   Fournier E., Bellmann K., Beauchemin N., Gingras A.C., Bilodeau S.,
RA   Laplante M., Marette A.;
RT   "SHP-1 phosphatase acts as a coactivator of PCK1 transcription to control
RT   gluconeogenesis.";
RL   J. Biol. Chem. 299:105164-105164(2023).
RN   [11]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION OF POL II, AND
RP   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   [12]
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. {ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596,
CC       ECO:0000269|PubMed:37595871, 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 (PubMed:27193682, PubMed:30190596,
CC       PubMed:9852112). Interacts with AATF (PubMed:10783144). Interacts with
CC       PTPN6; this interaction promotes the recruitment of RNA pol II to the
CC       PCK1 promoter (PubMed:37595871). {ECO:0000269|PubMed:10783144,
CC       ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596,
CC       ECO:0000269|PubMed:37595871, ECO:0000269|PubMed:9852112}.
CC   -!- INTERACTION:
CC       P52435; Q494R4-2: DRC12; 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=12; 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_006234.6.
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   PDB; 8XRJ; EM; 3.60 A; K=1-117.
DR   PDB; 8XRM; EM; 3.13 A; K=1-117.
DR   PDB; 8XSO; EM; 2.70 A; K=1-117.
DR   PDB; 8XVS; EM; 4.10 A; K=1-117.
DR   PDB; 9EHZ; EM; 2.60 A; K=1-117.
DR   PDB; 9EI1; EM; 3.20 A; K=1-117.
DR   PDB; 9EI3; EM; 3.20 A; K=1-117.
DR   PDB; 9EI4; EM; 3.70 A; K=1-117.
DR   PDB; 9VD9; EM; 4.60 A; 9=1-117.
DR   AlphaFoldDB; P52435; -.
DR   EMDB; EMD-22294; -.
DR   EMDB; EMD-23255; -.
DR   EMDB; EMD-38604; -.
DR   EMDB; EMD-38607; -.
DR   EMDB; EMD-38624; -.
DR   EMDB; EMD-38717; -.
DR   EMDB; EMD-48071; -.
DR   EMDB; EMD-48073; -.
DR   EMDB; EMD-48075; -.
DR   EMDB; EMD-48076; -.
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; P52435; -.
DR   BioGRID; 111435; 158.
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; P52435; -.
DR   DIP; DIP-32913N; -.
DR   FunCoup; P52435; 1937.
DR   IntAct; P52435; 118.
DR   MINT; P52435; -.
DR   NDEx; IQUERY-CP-POLR2J; 5 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000292614; -.
DR   iPTMnet; P52435; -.
DR   PhosphoSitePlus; P52435; -.
DR   BioMuta; POLR2J; -.
DR   jPOST; P52435; -.
DR   MassIVE; P52435; -.
DR   PaxDb; 9606-ENSP00000292614; -.
DR   PeptideAtlas; P52435; -.
DR   ProteomicsDB; 56486; -.
DR   Pumba; P52435; -.
DR   Antibodypedia; 31080; 298 antibodies from 28 providers.
DR   DNASU; 5439; -.
DR   Ensembl; ENST00000292614.10; ENSP00000292614.5; ENSG00000005075.17.
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   AGR; HGNC:9197; -.
DR   ClinPGx; PA33517; -.
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   OpenTargets; ENSG00000005075; -.
DR   VEuPathDB; HostDB:ENSG00000005075; -.
DR   eggNOG; KOG4392; Eukaryota.
DR   GeneTree; ENSGT00550000074975; -.
DR   HOGENOM; CLU_090381_2_2_1; -.
DR   InParanoid; P52435; -.
DR   OMA; QATPENC; -.
DR   OrthoDB; 10248581at2759; -.
DR   PAN-GO; P52435; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P52435; -.
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   Reactome; R-HSA-9770562; mRNA Polyadenylation.
DR   Reactome; R-HSA-9918481; Dengue Virus-Host Interactions.
DR   SignaLink; P52435; -.
DR   SIGNOR; P52435; -.
DR   Agora; ENSG00000005075; -.
DR   BioGRID-ORCS; 5439; 439 hits in 734 CRISPR screens.
DR   ChiTaRS; POLR2J; human.
DR   EvolutionaryTrace; P52435; -.
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 105 other cell types or tissues.
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 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:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal.
DR   CDD; cd06926; RNAP_II_RPB11; 1.
DR   FunFam; 3.30.1360.10:FF:000003; DNA-directed RNA polymerase II subunit RPB11; 1.
DR   Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 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   InterPro; IPR022905; Rpo11-like.
DR   PANTHER; PTHR13946; DNA-DIRECTED RNA POLYMERASE I,II,III; 1.
DR   PANTHER; PTHR13946:SF16; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11; 1.
DR   Pfam; PF13656; RNA_pol_L_2; 1.
DR   SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1.
DR   PROSITE; PS01154; RNA_POL_L_13KD; 1.
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   PDBsum; 8XRJ; -.
DR   PDBsum; 8XRM; -.
DR   PDBsum; 8XSO; -.
DR   PDBsum; 8XVS; -.
DR   PDBsum; 9EHZ; -.
DR   PDBsum; 9EI1; -.
DR   PDBsum; 9EI3; -.
DR   PDBsum; 9EI4; -.
DR   PDBsum; 9VD9; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   DNA-directed RNA polymerase; Nucleus; Proteomics identification;
KW   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"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   TURN            6..10
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   HELIX           40..51
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:8XRM"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:9EHZ"
FT   HELIX           83..112
FT                   /evidence="ECO:0007829|PDB:9EHZ"
SQ   SEQUENCE   117 AA;  13293 MW;  6F78AB256EF8F647 CRC64;
     MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG
     YKVPHPLEHK IIIRVQTTPD YSPQEAFTNA ITDLISELSL LEERFRVAIK DKQEGIE
//