RPA43_HUMAN
ID RPA43_HUMAN Reviewed; 338 AA.
AC Q3B726; A0PJ45; B7Z724;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA43;
DE AltName: Full=DNA-directed RNA polymerase I subunit F {ECO:0000312|HGNC:HGNC:18027};
DE AltName: Full=Twist neighbor protein {ECO:0000305|PubMed:12438708};
GN Name=POLR1F {ECO:0000312|HGNC:HGNC:18027};
GN Synonyms=TWISTNB {ECO:0000303|PubMed:12438708};
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 [LARGE SCALE MRNA].
RC TISSUE=Synovium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [5]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12438708; DOI=10.1159/000066618;
RA Kosan C., Kunz J.;
RT "Identification and characterisation of the gene TWIST NEIGHBOR (TWISTNB)
RT located in the microdeletion syndrome 7p21 region.";
RL Cytogenet. Genome Res. 97:167-170(2002).
RN [6]
RP INTERACTION WITH RRN3.
RX PubMed=12393749; DOI=10.1093/embo-reports/kvf212;
RA Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.;
RT "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits
RT regulate preinitiation complex assembly at the ribosomal gene promoter.";
RL EMBO Rep. 3:1082-1087(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-304; SER-316;
RP THR-322 AND SER-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 I which synthesizes ribosomal RNA
CC precursors. Through its association with RRN3/TIF-IA may be involved in
CC recruitment of Pol I to rDNA promoters.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits (By similarity). Interacts with RRN3/TIF-IA.
CC {ECO:0000250, ECO:0000269|PubMed:12393749}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in all fetal and adult
CC tissues tested, with highest expression in fetal lung, liver, and
CC kidney, and low expression in all adult tissues.
CC {ECO:0000269|PubMed:12438708}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA43 RNA polymerase subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14574.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK301329; BAH13460.1; -; mRNA.
DR EMBL; CH236948; EAL24277.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93714.1; -; Genomic_DNA.
DR EMBL; BC014574; AAH14574.1; ALT_FRAME; mRNA.
DR EMBL; BC130298; AAI30299.1; -; mRNA.
DR EMBL; BC130300; AAI30301.1; -; mRNA.
DR EMBL; BK000492; DAA05732.1; -; Genomic_DNA.
DR CCDS; CCDS34606.1; -.
DR RefSeq; NP_001002926.1; NM_001002926.1.
DR PDB; 7OB9; EM; 2.70 A; G=1-338.
DR PDB; 7OBA; EM; 3.10 A; G=1-338.
DR PDB; 7OBB; EM; 3.30 A; G=1-338.
DR PDB; 7VBA; EM; 2.89 A; G=1-338.
DR PDB; 7VBB; EM; 2.81 A; G=1-338.
DR PDB; 7VBC; EM; 3.01 A; G=1-338.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; Q3B726; -.
DR SMR; Q3B726; -.
DR BioGRID; 128759; 46.
DR IntAct; Q3B726; 15.
DR STRING; 9606.ENSP00000222567; -.
DR GlyGen; Q3B726; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q3B726; -.
DR PhosphoSitePlus; Q3B726; -.
DR BioMuta; TWISTNB; -.
DR DMDM; 121942339; -.
DR EPD; Q3B726; -.
DR jPOST; Q3B726; -.
DR MassIVE; Q3B726; -.
DR MaxQB; Q3B726; -.
DR PaxDb; Q3B726; -.
DR PeptideAtlas; Q3B726; -.
DR PRIDE; Q3B726; -.
DR ProteomicsDB; 61646; -.
DR Antibodypedia; 11907; 96 antibodies from 21 providers.
DR DNASU; 221830; -.
DR Ensembl; ENST00000222567.6; ENSP00000222567.5; ENSG00000105849.6.
DR GeneID; 221830; -.
DR KEGG; hsa:221830; -.
DR MANE-Select; ENST00000222567.6; ENSP00000222567.5; NM_001002926.2; NP_001002926.1.
DR UCSC; uc003sup.2; human.
DR CTD; 221830; -.
DR DisGeNET; 221830; -.
DR GeneCards; POLR1F; -.
DR HGNC; HGNC:18027; POLR1F.
DR HPA; ENSG00000105849; Low tissue specificity.
DR MIM; 608312; gene.
DR neXtProt; NX_Q3B726; -.
DR OpenTargets; ENSG00000105849; -.
DR VEuPathDB; HostDB:ENSG00000105849; -.
DR eggNOG; KOG4134; Eukaryota.
DR GeneTree; ENSGT00390000005553; -.
DR HOGENOM; CLU_048289_0_0_1; -.
DR InParanoid; Q3B726; -.
DR OMA; CLVVGPH; -.
DR OrthoDB; 1196232at2759; -.
DR PhylomeDB; Q3B726; -.
DR TreeFam; TF325602; -.
DR PathwayCommons; Q3B726; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q3B726; -.
DR SIGNOR; Q3B726; -.
DR BioGRID-ORCS; 221830; 784 hits in 1083 CRISPR screens.
DR ChiTaRS; TWISTNB; human.
DR GenomeRNAi; 221830; -.
DR Pharos; Q3B726; Tdark.
DR PRO; PR:Q3B726; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q3B726; protein.
DR Bgee; ENSG00000105849; Expressed in decidua and 176 other tissues.
DR Genevisible; Q3B726; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR CDD; cd04328; RNAP_I_Rpa43_N; 1.
DR Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR041901; RNAP_I_Rpa43_N.
DR InterPro; IPR045113; Rpb7-like.
DR PANTHER; PTHR12709; PTHR12709; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT CHAIN 1..338
FT /note="DNA-directed RNA polymerase I subunit RPA43"
FT /id="PRO_0000288632"
FT REGION 209..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7OBA"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7OBA"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 88..105
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:7OBA"
SQ SEQUENCE 338 AA; 37432 MW; 6DA3829E74E5D25C CRC64;
MAAGCSEAPR PAAASDGSLV GQAGVLPCLE LPTYAAACAL VNSRYSCLVA GPHQRHIALS
PRYLNRKRTG IREQLDAELL RYSESLLGVP IAYDNIKVVG ELGDIYDDQG HIHLNIEADF
VIFCPEPGQK LMGIVNKVSS SHIGCLVHGC FNASIPKPEQ LSAEQWQTME INMGDELEFE
VFRLDSDAAG VFCIRGKLNI TSLQFKRSEV SEEVTENGTE EAAKKPKKKK KKKDPETYEV
DSGTTKLADD ADDTPMEESA LQNTNNANGI WEEEPKKKKK KKKHQEVQDQ DPVFQGSDSS
GYQSDHKKKK KKRKHSEEAE FTPPLKCSPK RKGKSNFL
