ID U3KQB0_HUMAN Unreviewed; 122 AA.
AC U3KQB0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC2 {ECO:0000256|ARBA:ARBA00020808};
DE AltName: Full=DNA-directed RNA polymerase II subunit F {ECO:0000256|ARBA:ARBA00033085};
DE AltName: Full=RPB6 homolog {ECO:0000256|ARBA:ARBA00030456};
GN Name=POLR2F {ECO:0000313|Ensembl:ENSP00000475707.1};
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 {ECO:0000313|Ensembl:ENSP00000475707.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000475707.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [3] {ECO:0000313|Ensembl:ENSP00000475707.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I, II, and III which synthesize
CC ribosomal RNA precursors, mRNA precursors and many functional non-
CC coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC Pol II is the central component of the basal RNA polymerase II
CC transcription machinery. Pols are composed of mobile elements that move
CC relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp
CC element and together with parts of POLR2A/RPB1 and POLR2B/RPB2 forms a
CC pocket to which the POLR2D/RPB4-POLR2G/RPB7 subcomplex binds.
CC {ECO:0000256|ARBA:ARBA00043891}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC least 13, 12 and 17 subunits, respectively. The transcriptionally
CC active Pol III complex consists of a ten-subunit horseshoe-shaped
CC catalytic core composed of POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1,
CC POLR1D/RPAC2, POLR3K/RPC10, POLR2E/RPABC1, POLR2F/RPABC2,
CC POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile stalk composed
CC of two subunits POLR3H/RPC8 and CRCP/RPC9, protruding from the core and
CC functioning primarily in transcription initiation; and additional
CC subunits homologous to general transcription factors of the RNA
CC polymerase II machinery, POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7
CC heterotrimer required for transcription initiation and POLR3D/RPC4-
CC POLR3E/RPC5 heterodimer involved in both transcription initiation and
CC termination. {ECO:0000256|ARBA:ARBA00044010}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC subunit family. {ECO:0000256|ARBA:ARBA00025773}.
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DR EMBL; AL031587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; U3KQB0; -.
DR SMR; U3KQB0; -.
DR MassIVE; U3KQB0; -.
DR MaxQB; U3KQB0; -.
DR PeptideAtlas; U3KQB0; -.
DR Antibodypedia; 227; 154 antibodies from 26 providers.
DR Ensembl; ENST00000470701.1; ENSP00000475707.1; ENSG00000100142.16.
DR UCSC; uc062ech.1; human.
DR HGNC; HGNC:9193; POLR2F.
DR VEuPathDB; HostDB:ENSG00000100142; -.
DR GeneTree; ENSGT00390000010415; -.
DR HOGENOM; CLU_112527_2_0_1; -.
DR ChiTaRS; POLR2F; human.
DR Proteomes; UP000005640; Chromosome 22.
DR Bgee; ENSG00000100142; Expressed in C1 segment of cervical spinal cord and 210 other cell types or tissues.
DR ExpressionAtlas; U3KQB0; baseline and differential.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.90.940.10; -; 1.
DR InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR028363; RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR InterPro; IPR006111; Rpo6/Rpb6.
DR PANTHER; PTHR47227; DNA-DIRECTED RNA POLYMERASE SUBUNIT K; 1.
DR PANTHER; PTHR47227:SF5; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR PIRSF; PIRSF500154; RPB6; 1.
DR PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; RPB6/omega subunit-like; 1.
DR PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:U3KQB0,
KW ECO:0007829|MaxQB:U3KQB0};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13891 MW; 6273F9311667AB8B CRC64;
MSFDGDDFDD VEEDEGLDDL ENAEEEGQEN VEILPSGERP QANQKRITTP YMTKYERARV
LGTRALQIAM CAPVMVELEG ETDPLLIAMK ELKARKIPII IRRYLPDGSY EDWGVDELII
TD
//
