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   04-NOV-2026, entry version 239.
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).
RN   [23]
RP   STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH ZN(2+), AND 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).
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, Pol II, UBR5 and
CC       TCEA1/TFIIS (PubMed:21127351). Part of TBP-based Pol II pre-initiation
CC       complex (PIC), in which Pol II core assembles with general
CC       transcription factors and other specific initiation factors including
CC       GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3,
CC       GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit
CC       PIC complex mediates DNA unwinding and targets Pol II core to the
CC       transcription start site where the first phosphodiester bond forms
CC       (PubMed:27193682). {ECO:0000250, ECO:0000269|PubMed:21127351,
CC       ECO:0000269|PubMed:27193682}.
CC   -!- INTERACTION:
CC       P23193; Q5VW32: BROX; NbExp=2; IntAct=EBI-2608271, EBI-6286053;
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_006756.4. [P23193-1]
DR   RefSeq; NP_958845.1; NM_201437.3. [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   PDB; 7UNC; EM; 3.00 A; O=1-301.
DR   PDB; 7UND; EM; 3.00 A; O=1-301.
DR   PDB; 8A40; EM; 3.00 A; U=1-301.
DR   PDB; 8UIS; EM; 3.23 A; S=1-301.
DR   PDB; 9EGX; EM; 2.90 A; S=1-301.
DR   PDB; 9EGY; EM; 2.90 A; S=1-301.
DR   PDB; 9EGZ; EM; 2.90 A; S=1-301.
DR   PDB; 9EH0; EM; 3.60 A; S=1-301.
DR   PDB; 9EH2; EM; 3.10 A; S=1-301.
DR   PDB; 9J0N; EM; 3.40 A; M=1-301.
DR   PDB; 9MLC; EM; 2.40 A; S=1-301.
DR   PDB; 9S0U; EM; 6.72 A; S=1-301.
DR   PDB; 9S3G; EM; 6.40 A; S=1-301.
DR   AlphaFoldDB; P23193; -.
DR   EMDB; EMD-15129; -.
DR   EMDB; EMD-26620; -.
DR   EMDB; EMD-26621; -.
DR   EMDB; EMD-42303; -.
DR   EMDB; EMD-48039; -.
DR   EMDB; EMD-48040; -.
DR   EMDB; EMD-48041; -.
DR   EMDB; EMD-48042; -.
DR   EMDB; EMD-48043; -.
DR   EMDB; EMD-48044; -.
DR   EMDB; EMD-48353; -.
DR   EMDB; EMD-54425; -.
DR   EMDB; EMD-54537; -.
DR   EMDB; EMD-61058; -.
DR   EMDB; EMD-8132; -.
DR   EMDB; EMD-8133; -.
DR   EMDB; EMD-8135; -.
DR   EMDB; EMD-8136; -.
DR   EMDB; EMD-8137; -.
DR   MDposit; P23193; -.
DR   SMR; P23193; -.
DR   BioGRID; 112779; 143.
DR   DIP; DIP-48480N; -.
DR   FunCoup; P23193; 4497.
DR   IntAct; P23193; 57.
DR   STRING; 9606.ENSP00000428426; -.
DR   BindingDB; P23193; -.
DR   ChEMBL; CHEMBL6066940; -.
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   jPOST; P23193; -.
DR   MassIVE; P23193; -.
DR   PaxDb; 9606-ENSP00000428426; -.
DR   PeptideAtlas; P23193; -.
DR   ProteomicsDB; 54061; -. [P23193-1]
DR   ProteomicsDB; 54062; -. [P23193-2]
DR   Pumba; P23193; -.
DR   Antibodypedia; 6001; 301 antibodies from 31 providers.
DR   DNASU; 6917; -.
DR   Ensembl; ENST00000396401.7; ENSP00000395483.2; ENSG00000187735.17. [P23193-2]
DR   Ensembl; ENST00000521604.7; ENSP00000428426.2; ENSG00000187735.17. [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   AGR; HGNC:11612; -.
DR   ClinPGx; PA36371; -.
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   OpenTargets; ENSG00000187735; -.
DR   VEuPathDB; HostDB:ENSG00000187735; -.
DR   eggNOG; KOG1105; Eukaryota.
DR   GeneTree; ENSGT00940000155121; -.
DR   HOGENOM; CLU_037637_2_0_1; -.
DR   InParanoid; P23193; -.
DR   OMA; AAYQEFK; -.
DR   OrthoDB; 44867at2759; -.
DR   PAN-GO; P23193; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P23193; -.
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   Reactome; R-HSA-9938024; Somatic hypermutation of immunoglobulin genes.
DR   SignaLink; P23193; -.
DR   SIGNOR; P23193; -.
DR   Agora; ENSG00000187735; -.
DR   BioGRID-ORCS; 6917; 29 hits in 1152 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   CD-CODE; DEE660B4; Stress granule.
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 216 other cell types or tissues.
DR   ExpressionAtlas; P23193; baseline and differential.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003711; F:transcription elongation factor activity; IDA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:GO_Central.
DR   CDD; cd00183; TFIIS_I; 1.
DR   CDD; cd13749; Zn-ribbon_TFIIS; 1.
DR   FunFam; 2.20.25.10:FF:000001; Probable Transcription elongation factor S-II; 1.
DR   FunFam; 1.10.472.30:FF:000001; Transcription elongation factor A (SII), 1; 1.
DR   FunFam; 1.20.930.10:FF:000002; Transcription elongation factor A (SII), 1; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 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   NCBIfam; TIGR01385; TFSII; 1.
DR   PANTHER; PTHR11477:SF1; TRANSCRIPTION ELONGATION FACTOR A PROTEIN 1; 1.
DR   PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   Pfam; PF01096; Zn_ribbon_TFIIS; 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; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 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; Proteomics identification; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   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..93
FT                   /note="Basic and acidic 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                   ECO:0000269|PubMed:27193682, ECO:0000312|PDB:5IY6"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT                   ECO:0000269|PubMed:27193682, ECO:0000312|PDB:5IY6"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT                   ECO:0000269|PubMed:27193682, ECO:0000312|PDB:5IY6"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT                   ECO:0000269|PubMed:27193682, ECO:0000312|PDB:5IY6"
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           154..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..212
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   HELIX           231..247
FT                   /evidence="ECO:0007829|PDB:9MLC"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:9EGX"
FT   STRAND          256..261
FT                   /evidence="ECO:0007829|PDB:9EGX"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:9EGX"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:9MLC"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:8A40"
FT   STRAND          287..293
FT                   /evidence="ECO:0007829|PDB:9MLC"
FT   STRAND          297..300
FT                   /evidence="ECO:0007829|PDB:9MLC"
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
//