RPB1C_HUMAN
ID RPB1C_HUMAN Reviewed; 115 AA.
AC Q9H1A7; A6NKA1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB11-b2;
DE Short=RNA polymerase II subunit B11-b2;
DE Short=RPB11b2;
DE AltName: Full=DNA-directed RNA polymerase II subunit J3;
GN Name=POLR2J3;
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=Cervix carcinoma;
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 [2]
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).
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}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits.
CC -!- INTERACTION:
CC Q9H1A7; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12818681, EBI-1166928;
CC Q9H1A7; O15160: POLR1C; NbExp=3; IntAct=EBI-12818681, EBI-1055079;
CC Q9H1A7; Q9UPW6: SATB2; NbExp=3; IntAct=EBI-12818681, EBI-8298169;
CC Q9H1A7; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-12818681, EBI-3650647;
CC Q9H1A7; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-12818681, EBI-9090990;
CC Q9H1A7; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12818681, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC polymerase subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ277741; CAC18331.1; -; mRNA.
DR EMBL; AC004084; AAP22342.1; -; Genomic_DNA.
DR CCDS; CCDS47673.1; -.
DR AlphaFoldDB; Q9H1A7; -.
DR SMR; Q9H1A7; -.
DR IntAct; Q9H1A7; 6.
DR STRING; 9606.ENSP00000483328; -.
DR iPTMnet; Q9H1A7; -.
DR PhosphoSitePlus; Q9H1A7; -.
DR BioMuta; POLR2J3; -.
DR jPOST; Q9H1A7; -.
DR MassIVE; Q9H1A7; -.
DR MaxQB; Q9H1A7; -.
DR PaxDb; Q9H1A7; -.
DR PeptideAtlas; Q9H1A7; -.
DR PRIDE; Q9H1A7; -.
DR ProteomicsDB; 80386; -.
DR Ensembl; ENST00000379340.9; ENSP00000368645.5; ENSG00000168255.20.
DR UCSC; uc011kkw.2; human.
DR GeneCards; POLR2J3; -.
DR HGNC; HGNC:33853; POLR2J3.
DR neXtProt; NX_Q9H1A7; -.
DR PharmGKB; PA164724678; -.
DR VEuPathDB; HostDB:ENSG00000168255; -.
DR eggNOG; KOG4392; Eukaryota.
DR HOGENOM; CLU_090381_2_2_1; -.
DR InParanoid; Q9H1A7; -.
DR PathwayCommons; Q9H1A7; -.
DR SignaLink; Q9H1A7; -.
DR SIGNOR; Q9H1A7; -.
DR ChiTaRS; POLR2J3; human.
DR Pharos; Q9H1A7; Tdark.
DR PRO; PR:Q9H1A7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9H1A7; protein.
DR Bgee; ENSG00000168255; Expressed in lower esophagus mucosa and 98 other tissues.
DR ExpressionAtlas; Q9H1A7; baseline and differential.
DR Genevisible; Q9H1A7; HS.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001055; F:RNA polymerase II activity; IEA:InterPro.
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 DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription.
FT CHAIN 1..115
FT /note="DNA-directed RNA polymerase II subunit RPB11-b2"
FT /id="PRO_0000316947"
SQ SEQUENCE 115 AA; 13092 MW; F03331C8024E00D8 CRC64;
MNAPPAFESF LLFEGEKITI NKDTKVPNAC LFTMNKEDHT LGNIIKSQLL KDPQVLFAGY
KVPHPLEHKI IIRVQTTPDY SPQEAFTNAI TDLISELSLL EERFRTCLLP LRLLP
