TCEA1_HUMAN
ID TCEA1_HUMAN Reviewed; 301 AA.
AC P23193; A6NF25; A8K339; Q15563; Q6FG87;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Transcription elongation factor A protein 1;
DE AltName: Full=Transcription elongation factor S-II protein 1;
DE AltName: Full=Transcription elongation factor TFIIS.o;
GN Name=TCEA1; Synonyms=GTF2S, TFIIS;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RX PubMed=1708494; DOI=10.1093/nar/19.5.1073;
RA Yoo O., Yoon H., Baek K., Jeon C., Miyamoto K., Ueno A., Agarwal K.;
RT "Cloning, expression and characterization of the human transcription
RT elongation factor, TFIIS.";
RL Nucleic Acids Res. 19:1073-1079(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1378807; DOI=10.1016/0378-1119(92)90522-q;
RA Chen H.C., England L., Kane C.M.;
RT "Characterization of a HeLa cDNA clone encoding the human SII protein, an
RT elongation factor for RNA polymerase II.";
RL Gene 116:253-258(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8112616; DOI=10.1016/0378-1119(94)90767-6;
RA Park H.R., Baek K.H., Jeon C.J., Agarwal K., Yoo O.;
RT "Characterization of the gene encoding the human transcriptional elongation
RT factor TFIIS.";
RL Gene 139:263-267(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [9]
RP PROTEIN SEQUENCE OF 1-9 AND 32-44, ACETYLATION AT MET-1, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [10]
RP CHROMOSOMAL TRANSLOCATION WITH PLAG1.
RX PubMed=10029085;
RA Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N.,
RA Van de Ven W., Mark J., Stenman G.;
RT "Conserved mechanism of PLAG1 activation in salivary gland tumors with and
RT without chromosome 8q12 abnormalities: identification of SII as a new
RT fusion partner gene.";
RL Cancer Res. 59:918-923(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP INTERACTION WITH UBR5 AND CDK9.
RX PubMed=21127351; DOI=10.1074/jbc.m110.176628;
RA Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K.,
RA Price D.H., Coulombe B.;
RT "Transcription factor IIS cooperates with the E3 ligase UBR5 to
RT ubiquitinate the CDK9 subunit of the positive transcription elongation
RT factor B.";
RL J. Biol. Chem. 286:5012-5022(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, AND
RP IDENTIFICATION BY 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-81 AND SER-100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [22]
RP STRUCTURE BY NMR OF 256-301.
RX PubMed=7626141; DOI=10.1038/365277a0;
RA Qian X., Jeon C., Yoon H., Agarwal K., Weiss M.A.;
RT "Structure of a new nucleic-acid-binding motif in eukaryotic
RT transcriptional elongation factor TFIIS.";
RL Nature 365:277-279(1993).
CC -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by S-II allows the
CC resumption of elongation from the new 3'-terminus.
CC -!- SUBUNIT: Interacts with EAF2 (By similarity). Associates with UBR5 and
CC forms a transcription regulatory complex made of CDK9, RNAP II, UBR5
CC and TFIIS/TCEA1 that can stimulate target gene transcription (e.g.
CC gamma fibrinogen/FGG) by recruiting their promoters. {ECO:0000250,
CC ECO:0000269|PubMed:21127351}.
CC -!- INTERACTION:
CC P23193; Q92917: GPKOW; NbExp=3; IntAct=EBI-2608271, EBI-746309;
CC P23193; Q8WVC0: LEO1; NbExp=4; IntAct=EBI-2608271, EBI-932432;
CC P23193; Q8N7H5: PAF1; NbExp=4; IntAct=EBI-2608271, EBI-2607770;
CC P23193; P24928: POLR2A; NbExp=5; IntAct=EBI-2608271, EBI-295301;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P23193-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23193-2; Sequence=VSP_006409;
CC -!- DISEASE: Note=A chromosomal aberration involving TCEA1 may be a cause
CC of salivary gland pleiomorphic adenomas (PA) [181030]. Pleiomorphic
CC adenomas are the most common benign epithelial tumors of the salivary
CC gland. Translocation t(3;8)(p21;q12) with PLAG1.
CC {ECO:0000269|PubMed:10029085}.
CC -!- MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of
CC transcription.
CC -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
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DR EMBL; X62585; CAA44470.1; -; mRNA.
DR EMBL; X57198; CAA40484.1; -; mRNA.
DR EMBL; M81601; AAA61138.1; -; mRNA.
DR EMBL; X73534; CAA51940.1; -; Genomic_DNA.
DR EMBL; AK290454; BAF83143.1; -; mRNA.
DR EMBL; CR542221; CAG47017.1; -; mRNA.
DR EMBL; BT019995; AAV38798.1; -; mRNA.
DR EMBL; AC100821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072460; AAH72460.1; -; mRNA.
DR CCDS; CCDS47857.1; -. [P23193-2]
DR CCDS; CCDS47858.1; -. [P23193-1]
DR PIR; S17361; S17361.
DR PIR; S26831; S26831.
DR PIR; S34159; S34159.
DR RefSeq; NP_006747.1; NM_006756.3. [P23193-1]
DR RefSeq; NP_958845.1; NM_201437.2. [P23193-2]
DR PDB; 1TFI; NMR; -; A=252-301.
DR PDB; 3NDQ; X-ray; 1.93 A; A=131-232.
DR PDB; 5IY6; EM; 7.20 A; U=1-301.
DR PDB; 5IY7; EM; 8.60 A; U=1-301.
DR PDB; 5IY8; EM; 7.90 A; U=1-301.
DR PDB; 5IYA; EM; 5.40 A; U=1-301.
DR PDB; 5IYB; EM; 3.90 A; U=1-301.
DR PDB; 5IYC; EM; 3.90 A; U=1-301.
DR PDB; 6O9L; EM; 7.20 A; U=1-301.
DR PDB; 6ZUY; NMR; -; A=1-79.
DR PDB; 6ZV4; NMR; -; A=1-77.
DR PDB; 7CNF; NMR; -; A=1-96.
DR PDBsum; 1TFI; -.
DR PDBsum; 3NDQ; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6ZUY; -.
DR PDBsum; 6ZV4; -.
DR PDBsum; 7CNF; -.
DR AlphaFoldDB; P23193; -.
DR SMR; P23193; -.
DR BioGRID; 112779; 105.
DR DIP; DIP-48480N; -.
DR IntAct; P23193; 44.
DR MINT; P23193; -.
DR STRING; 9606.ENSP00000428426; -.
DR GlyGen; P23193; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P23193; -.
DR MetOSite; P23193; -.
DR PhosphoSitePlus; P23193; -.
DR SwissPalm; P23193; -.
DR BioMuta; TCEA1; -.
DR DMDM; 1174652; -.
DR EPD; P23193; -.
DR jPOST; P23193; -.
DR MassIVE; P23193; -.
DR MaxQB; P23193; -.
DR PaxDb; P23193; -.
DR PeptideAtlas; P23193; -.
DR PRIDE; P23193; -.
DR ProteomicsDB; 54061; -. [P23193-1]
DR ProteomicsDB; 54062; -. [P23193-2]
DR Antibodypedia; 6001; 215 antibodies from 27 providers.
DR DNASU; 6917; -.
DR Ensembl; ENST00000396401.7; ENSP00000395483.2; ENSG00000187735.15. [P23193-2]
DR Ensembl; ENST00000521604.7; ENSP00000428426.2; ENSG00000187735.15. [P23193-1]
DR GeneID; 6917; -.
DR KEGG; hsa:6917; -.
DR MANE-Select; ENST00000521604.7; ENSP00000428426.2; NM_006756.4; NP_006747.1.
DR UCSC; uc003xru.5; human. [P23193-1]
DR CTD; 6917; -.
DR DisGeNET; 6917; -.
DR GeneCards; TCEA1; -.
DR HGNC; HGNC:11612; TCEA1.
DR HPA; ENSG00000187735; Low tissue specificity.
DR MIM; 601425; gene.
DR neXtProt; NX_P23193; -.
DR OpenTargets; ENSG00000187735; -.
DR PharmGKB; PA36371; -.
DR VEuPathDB; HostDB:ENSG00000187735; -.
DR eggNOG; KOG1105; Eukaryota.
DR GeneTree; ENSGT00940000155121; -.
DR HOGENOM; CLU_037637_2_0_1; -.
DR InParanoid; P23193; -.
DR OMA; TTFCECT; -.
DR OrthoDB; 1579101at2759; -.
DR PhylomeDB; P23193; -.
DR TreeFam; TF314970; -.
DR PathwayCommons; P23193; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
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-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-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-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; P23193; -.
DR SIGNOR; P23193; -.
DR BioGRID-ORCS; 6917; 27 hits in 1074 CRISPR screens.
DR ChiTaRS; TCEA1; human.
DR EvolutionaryTrace; P23193; -.
DR GeneWiki; TCEA1; -.
DR GenomeRNAi; 6917; -.
DR Pharos; P23193; Tbio.
DR PRO; PR:P23193; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P23193; protein.
DR Bgee; ENSG00000187735; Expressed in trabecular bone tissue and 214 other tissues.
DR ExpressionAtlas; P23193; baseline and differential.
DR Genevisible; P23193; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035100; TF_IIS-typ.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR006289; TFSII.
DR InterPro; IPR001222; Znf_TFIIS.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR PIRSF; PIRSF006704; TF_IIS; 1.
DR SMART; SM00510; TFS2M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR TIGRFAMs; TIGR01385; TFSII; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..301
FT /note="Transcription elongation factor A protein 1"
FT /id="PRO_0000121446"
FT DOMAIN 3..80
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 140..256
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 259..299
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 80..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 100
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 ECO:0007744|PubMed:24275569"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15560"
FT VAR_SEQ 22..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1708494"
FT /id="VSP_006409"
FT CONFLICT 127
FT /note="V -> L (in Ref. 2; AAA61138)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="R -> Q (in Ref. 3; CAA51940)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="N -> Y (in Ref. 3; CAA51940)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="R -> W (in Ref. 3; CAA51940)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="M -> V (in Ref. 3; CAA51940)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="F -> I (in Ref. 6; AC100821)"
FT /evidence="ECO:0000305"
FT HELIX 2..17
FT /evidence="ECO:0007829|PDB:6ZUY"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6ZV4"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:6ZUY"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:6ZUY"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:6ZUY"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:6ZUY"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:7CNF"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3NDQ"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:3NDQ"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:3NDQ"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:3NDQ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3NDQ"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3NDQ"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:3NDQ"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:3NDQ"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3NDQ"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1TFI"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1TFI"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:1TFI"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:1TFI"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1TFI"
SQ SEQUENCE 301 AA; 33970 MW; 8A685107A56D2DA1 CRC64;
MEDEVVRFAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV NAIRKQSTDE
EVTSLAKSLI KSWKKLLDGP STEKDLDEKK KEPAITSQNS PEAREESTSS GNVSNRKDET
NARDTYVSSF PRAPSTSDSV RLKCREMLAA ALRTGDDYIA IGADEEELGS QIEEAIYQEI
RNTDMKYKNR VRSRISNLKD AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL
TKEAIREHQM AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF
C
