Full text data of TCEA1
TCEA1
(GTF2S, TFIIS)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1; Transcription elongation factor TFIIS.o)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1; Transcription elongation factor TFIIS.o)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P23193
ID TCEA1_HUMAN Reviewed; 301 AA.
AC P23193; A6NF25; A8K339; Q15563; Q6FG87;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 2.
DT 22-JAN-2014, entry version 149.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RT an 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
RT elongation 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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
RT 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.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA 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.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA 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
RT project: 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 MASS
RP 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
RT and without chromosome 8q12 abnormalities: identification of SII as a
RT new fusion partner gene.";
RL Cancer Res. 59:918-923(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT sequential 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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
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
CC sites in DNA have the property of trapping a certain fraction of
CC elongating RNA polymerases that pass through, resulting in locked
CC ternary complexes. Cleavage of the nascent transcript by S-II
CC allows the resumption of elongation from the new 3'-terminus.
CC -!- SUBUNIT: Interacts with EAF2 (By similarity). Associates with UBR5
CC and forms a transcription regulatory complex made of CDK9, RNAP
CC II, UBR5 and TFIIS/TCEA1 that can stimulate target gene
CC transcription (e.g. gamma fibrinogen/FGG) by recruiting their
CC promoters.
CC -!- INTERACTION:
CC Q8WVC0:LEO1; NbExp=4; IntAct=EBI-2608271, EBI-932432;
CC Q8N7H5:PAF1; NbExp=4; IntAct=EBI-2608271, EBI-2607770;
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
CC cause of salivary gland pleiomorphic adenomas (PA) [181030].
CC Pleiomorphic adenomas are the most common benign epithelial tumors
CC of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.
CC -!- MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of
CC transcription.
CC -!- SIMILARITY: Belongs to the TFS-II family.
CC -!- SIMILARITY: Contains 1 TFIIS central domain.
CC -!- SIMILARITY: Contains 1 TFIIS N-terminal domain.
CC -!- SIMILARITY: Contains 1 TFIIS-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S17361; S17361.
DR PIR; S26831; S26831.
DR PIR; S34159; S34159.
DR RefSeq; NP_006747.1; NM_006756.2.
DR RefSeq; NP_958845.1; NM_201437.1.
DR UniGene; Hs.491745; -.
DR PDB; 1TFI; NMR; -; A=252-301.
DR PDB; 3NDQ; X-ray; 1.93 A; A=131-232.
DR PDBsum; 1TFI; -.
DR PDBsum; 3NDQ; -.
DR ProteinModelPortal; P23193; -.
DR SMR; P23193; 1-84, 132-301.
DR DIP; DIP-48480N; -.
DR IntAct; P23193; 9.
DR MINT; MINT-3009864; -.
DR STRING; 9606.ENSP00000382541; -.
DR PhosphoSite; P23193; -.
DR DMDM; 1174652; -.
DR PaxDb; P23193; -.
DR PRIDE; P23193; -.
DR DNASU; 6917; -.
DR Ensembl; ENST00000396401; ENSP00000395483; ENSG00000187735.
DR Ensembl; ENST00000521604; ENSP00000428426; ENSG00000187735.
DR GeneID; 6917; -.
DR KEGG; hsa:6917; -.
DR UCSC; uc003xru.3; human.
DR CTD; 6917; -.
DR GeneCards; GC08M054929; -.
DR H-InvDB; HIX0057264; -.
DR HGNC; HGNC:11612; TCEA1.
DR HPA; HPA043786; -.
DR MIM; 601425; gene.
DR neXtProt; NX_P23193; -.
DR PharmGKB; PA36371; -.
DR eggNOG; COG1594; -.
DR HOGENOM; HOG000195015; -.
DR HOVERGEN; HBG055022; -.
DR InParanoid; P23193; -.
DR KO; K03145; -.
DR OMA; DSIRIKC; -.
DR OrthoDB; EOG7GQXWQ; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P23193; -.
DR GeneWiki; TCEA1; -.
DR GenomeRNAi; 6917; -.
DR NextBio; 27057; -.
DR PMAP-CutDB; P23193; -.
DR PRO; PR:P23193; -.
DR ArrayExpress; P23193; -.
DR Bgee; P23193; -.
DR CleanEx; HS_TCEA1; -.
DR Genevestigator; P23193; -.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0032784; P:regulation of DNA-dependent transcription, elongation; IEA:InterPro.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR016492; TF_IIS-rel.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR017890; TFS2M.
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;
KW Chromosomal rearrangement; Complete proteome;
KW Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 301 Transcription elongation factor A protein
FT 1.
FT /FTId=PRO_0000121446.
FT DOMAIN 3 80 TFIIS N-terminal.
FT DOMAIN 140 256 TFIIS central.
FT ZN_FING 259 299 TFIIS-type.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 97 97 Phosphoserine.
FT MOD_RES 100 100 Phosphoserine.
FT VAR_SEQ 22 42 Missing (in isoform 2).
FT /FTId=VSP_006409.
FT CONFLICT 127 127 V -> L (in Ref. 2; AAA61138).
FT CONFLICT 141 141 R -> Q (in Ref. 3; CAA51940).
FT CONFLICT 205 205 N -> Y (in Ref. 3; CAA51940).
FT CONFLICT 237 237 R -> W (in Ref. 3; CAA51940).
FT CONFLICT 285 285 M -> V (in Ref. 3; CAA51940).
FT CONFLICT 300 300 F -> I (in Ref. 6; AC100821).
FT HELIX 139 151
FT HELIX 152 156
FT HELIX 157 161
FT HELIX 165 180
FT STRAND 182 184
FT HELIX 185 198
FT HELIX 204 211
FT HELIX 217 222
FT TURN 225 227
FT STRAND 264 266
FT STRAND 271 276
FT STRAND 278 283
FT STRAND 286 294
FT STRAND 297 299
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
//
ID TCEA1_HUMAN Reviewed; 301 AA.
AC P23193; A6NF25; A8K339; Q15563; Q6FG87;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 2.
DT 22-JAN-2014, entry version 149.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RT an 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
RT elongation 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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
RT 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.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA 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.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA 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
RT project: 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 MASS
RP 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
RT and without chromosome 8q12 abnormalities: identification of SII as a
RT new fusion partner gene.";
RL Cancer Res. 59:918-923(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT sequential 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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
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
CC sites in DNA have the property of trapping a certain fraction of
CC elongating RNA polymerases that pass through, resulting in locked
CC ternary complexes. Cleavage of the nascent transcript by S-II
CC allows the resumption of elongation from the new 3'-terminus.
CC -!- SUBUNIT: Interacts with EAF2 (By similarity). Associates with UBR5
CC and forms a transcription regulatory complex made of CDK9, RNAP
CC II, UBR5 and TFIIS/TCEA1 that can stimulate target gene
CC transcription (e.g. gamma fibrinogen/FGG) by recruiting their
CC promoters.
CC -!- INTERACTION:
CC Q8WVC0:LEO1; NbExp=4; IntAct=EBI-2608271, EBI-932432;
CC Q8N7H5:PAF1; NbExp=4; IntAct=EBI-2608271, EBI-2607770;
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
CC cause of salivary gland pleiomorphic adenomas (PA) [181030].
CC Pleiomorphic adenomas are the most common benign epithelial tumors
CC of the salivary gland. Translocation t(3;8)(p21;q12) with PLAG1.
CC -!- MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of
CC transcription.
CC -!- SIMILARITY: Belongs to the TFS-II family.
CC -!- SIMILARITY: Contains 1 TFIIS central domain.
CC -!- SIMILARITY: Contains 1 TFIIS N-terminal domain.
CC -!- SIMILARITY: Contains 1 TFIIS-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S17361; S17361.
DR PIR; S26831; S26831.
DR PIR; S34159; S34159.
DR RefSeq; NP_006747.1; NM_006756.2.
DR RefSeq; NP_958845.1; NM_201437.1.
DR UniGene; Hs.491745; -.
DR PDB; 1TFI; NMR; -; A=252-301.
DR PDB; 3NDQ; X-ray; 1.93 A; A=131-232.
DR PDBsum; 1TFI; -.
DR PDBsum; 3NDQ; -.
DR ProteinModelPortal; P23193; -.
DR SMR; P23193; 1-84, 132-301.
DR DIP; DIP-48480N; -.
DR IntAct; P23193; 9.
DR MINT; MINT-3009864; -.
DR STRING; 9606.ENSP00000382541; -.
DR PhosphoSite; P23193; -.
DR DMDM; 1174652; -.
DR PaxDb; P23193; -.
DR PRIDE; P23193; -.
DR DNASU; 6917; -.
DR Ensembl; ENST00000396401; ENSP00000395483; ENSG00000187735.
DR Ensembl; ENST00000521604; ENSP00000428426; ENSG00000187735.
DR GeneID; 6917; -.
DR KEGG; hsa:6917; -.
DR UCSC; uc003xru.3; human.
DR CTD; 6917; -.
DR GeneCards; GC08M054929; -.
DR H-InvDB; HIX0057264; -.
DR HGNC; HGNC:11612; TCEA1.
DR HPA; HPA043786; -.
DR MIM; 601425; gene.
DR neXtProt; NX_P23193; -.
DR PharmGKB; PA36371; -.
DR eggNOG; COG1594; -.
DR HOGENOM; HOG000195015; -.
DR HOVERGEN; HBG055022; -.
DR InParanoid; P23193; -.
DR KO; K03145; -.
DR OMA; DSIRIKC; -.
DR OrthoDB; EOG7GQXWQ; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P23193; -.
DR GeneWiki; TCEA1; -.
DR GenomeRNAi; 6917; -.
DR NextBio; 27057; -.
DR PMAP-CutDB; P23193; -.
DR PRO; PR:P23193; -.
DR ArrayExpress; P23193; -.
DR Bgee; P23193; -.
DR CleanEx; HS_TCEA1; -.
DR Genevestigator; P23193; -.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0032784; P:regulation of DNA-dependent transcription, elongation; IEA:InterPro.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR016492; TF_IIS-rel.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR017890; TFS2M.
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;
KW Chromosomal rearrangement; Complete proteome;
KW Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 301 Transcription elongation factor A protein
FT 1.
FT /FTId=PRO_0000121446.
FT DOMAIN 3 80 TFIIS N-terminal.
FT DOMAIN 140 256 TFIIS central.
FT ZN_FING 259 299 TFIIS-type.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 97 97 Phosphoserine.
FT MOD_RES 100 100 Phosphoserine.
FT VAR_SEQ 22 42 Missing (in isoform 2).
FT /FTId=VSP_006409.
FT CONFLICT 127 127 V -> L (in Ref. 2; AAA61138).
FT CONFLICT 141 141 R -> Q (in Ref. 3; CAA51940).
FT CONFLICT 205 205 N -> Y (in Ref. 3; CAA51940).
FT CONFLICT 237 237 R -> W (in Ref. 3; CAA51940).
FT CONFLICT 285 285 M -> V (in Ref. 3; CAA51940).
FT CONFLICT 300 300 F -> I (in Ref. 6; AC100821).
FT HELIX 139 151
FT HELIX 152 156
FT HELIX 157 161
FT HELIX 165 180
FT STRAND 182 184
FT HELIX 185 198
FT HELIX 204 211
FT HELIX 217 222
FT TURN 225 227
FT STRAND 264 266
FT STRAND 271 276
FT STRAND 278 283
FT STRAND 286 294
FT STRAND 297 299
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
//
MIM
601425
*RECORD*
*FIELD* NO
601425
*FIELD* TI
*601425 TRANSCRIPTION ELONGATION FACTOR A, 1; TCEA1
;;TCEA;;
TFIIS; TF2S;;
SII
*FIELD* TX
read more
CLONING
Transcription elongation factors help RNA polymerase II (see 180660) to
transcribe past blockages due to specific DNA sequences, DNA-binding
proteins, and transcription-arresting drugs. Transcription elongation
factors in humans fall into 2 classes: the SIII (see 600788)/TF2F (see
189968) class, members of which increase the average rate of RNA chain
elongation (Aso et al., 1995); and the SII class, which releases RNA
polymerase II from transcriptional arrest (Reines, 1994). Park et al.
(1994) cloned and characterized a human gene encoding an SII-type
elongation factor that they called TFIIS. The TFIIS gene produces a
2.5-kb transcript.
GENE FUNCTION
Thomas et al. (1998) addressed whether the intrinsic 3-prime to 5-prime
nuclease activity of human RNA polymerase II (pol II) can proofread
during transcription in vitro. In the presence of SII, a protein that
stimulates the nuclease activity, pol II quantitatively removed
misincorporated nucleotides from the nascent transcript during rapid
chain extension. The basis of discrimination between the correct and
incorrect base was the slow addition of the next nucleotide to the
mismatched terminus. Incorporation of inosine monophosphate inhibited
the next nucleotide addition by a similar magnitude as a mismatched
base. Thomas et al. (1998) demonstrated that addition of SII to a
transcription reaction dramatically altered the RNA base content,
reflecting the stable incorporation of more 'correct' (GMP) and fewer
'incorrect' (IMP) nucleotides.
In vivo transcription by RNA polymerase II takes place in the context of
chromatin. Guermah et al. (2006) found that a purified, reconstituted
RNA polymerase II system that sufficed for activator-dependent
transcription on DNA templates was incapable of transcribing chromatin
templates, even in the presence of factors that effected transcription
in less-purified assay systems. Using a complementation and HeLa cell
nuclear extract fractionation scheme, Guermah et al. (2006) identified
and purified an activity, designated CTEA (chromatin
transcription-enabling activity), that allowed for transcription through
chromatin templates in a manner that was both activator and p300 (EP300;
602700)/acetyl-CoA dependent. CTEA acted primarily at the elongation
step and enabled RNA polymerase II machinery to transcribe efficiently
through several contiguously positioned nucleosomes. Guermah et al.
(2006) identified the major functional component of CTEA as
transcription elongation factor SII. SII was essential for productive
transcription elongation, and its function at this step was dependent on
p300-dependent acetylation. These synergistic transcriptional elongation
activities were potentiated by HMGB2 (163906).
Astrom et al. (1999) showed that activation of PLAG1 (603026) in
salivary gland tumors (181030) is not confined to adenomas with 8q12
abnormalities but is also found in tumors with a normal karyotype. They
showed further that PLAG1 may be activated by cryptic rearrangements in
cases with normal karyotypes, leading to fusions between PLAG1 and
CTNNB1 (116806) or the TCEA1 gene.
GENE STRUCTURE
Park et al. (1994) determined that the TCEA1 gene is 2.8 kb long and
intronless.
MAPPING
DiMarco et al. (1996) designed PCR primers for the TCEA1 gene and mapped
it to human chromosome 3 by analysis of human-rodent hybrid mapping
panel. Further regionalization to chromosome 3p22-p21.3 was accomplished
by fluorescence in situ hybridization using a YAC containing the gene.
DiMarco et al. (1996) cited reports that this region of 3p exhibits loss
of heterozygosity (LOH) in small- and non-small-cell lung carcinomas, as
well as several other malignancies.
*FIELD* RF
1. Aso, T.; Lane, W. S.; Conaway, J. W.; Conaway, R. C.: Elongin
(SIII): a multisubunit regulator of elongation by RNA polymerase II. Science 269:
1439-1443, 1995.
2. Astrom, A.-K.; Voz, M. L.; Kas, K.; Roijer, E.; Wedell, B.; Mandahl,
N.; Van de Ven, W.; Mark, J.; Stenman, G.: Conserved mechanism of
PLAG1 activation in salivary gland tumors with and without chromosome
8q12 abnormalities: identification of SII as a new fusion partner
gene. Cancer Res. 59: 918-923, 1999.
3. DiMarco, S. P.; Glover, T. W.; Miller, D. E.; Reines, D.; Warren,
S. T.: Transcription elongation factor SII (TCEA) maps to human chromosome
3p22-p21.3. Genomics 36: 185-188, 1996.
4. Guermah, M.; Palhan, V. B.; Tackett, A. J.; Chait, B. T.; Roeder,
R. G.: Synergistic functions of SII and p300 in productive activator-dependent
transcription of chromatin templates. Cell 125: 275-286, 2006.
5. Park, H.; Baek, K.; Jeon, C.; Agarwal, K.; Yoo, O.: Characterization
of the gene encoding the human transcriptional elongation factor TFIIS. Gene 139:
263-267, 1994.
6. Reines, D.: Nascent RNA cleavage by transcription elongation complexes.In:
Conaway, R. C.; Conaway, J. W. (eds.): Transcription: Mechanisms
and Regulation. New York: Raven Press 1994. Pp. 263-278.
7. Thomas, M. J.; Platas, A. A.; Hawley, D. K.: Transcriptional fidelity
and proofreading by RNA polymerase II. Cell 93: 627-637, 1998.
*FIELD* CN
Matthew B. Gross - updated: 3/8/2010
Victor A. McKusick - updated: 4/16/1999
Stylianos E. Antonarakis - updated: 6/4/1998
*FIELD* CD
Mark H. Paalman: 9/16/1996
*FIELD* ED
wwang: 03/10/2010
mgross: 3/8/2010
alopez: 5/21/1999
terry: 4/16/1999
carol: 12/15/1998
carol: 6/9/1998
terry: 6/4/1998
mark: 5/14/1997
terry: 9/17/1996
mark: 9/16/1996
*RECORD*
*FIELD* NO
601425
*FIELD* TI
*601425 TRANSCRIPTION ELONGATION FACTOR A, 1; TCEA1
;;TCEA;;
TFIIS; TF2S;;
SII
*FIELD* TX
read more
CLONING
Transcription elongation factors help RNA polymerase II (see 180660) to
transcribe past blockages due to specific DNA sequences, DNA-binding
proteins, and transcription-arresting drugs. Transcription elongation
factors in humans fall into 2 classes: the SIII (see 600788)/TF2F (see
189968) class, members of which increase the average rate of RNA chain
elongation (Aso et al., 1995); and the SII class, which releases RNA
polymerase II from transcriptional arrest (Reines, 1994). Park et al.
(1994) cloned and characterized a human gene encoding an SII-type
elongation factor that they called TFIIS. The TFIIS gene produces a
2.5-kb transcript.
GENE FUNCTION
Thomas et al. (1998) addressed whether the intrinsic 3-prime to 5-prime
nuclease activity of human RNA polymerase II (pol II) can proofread
during transcription in vitro. In the presence of SII, a protein that
stimulates the nuclease activity, pol II quantitatively removed
misincorporated nucleotides from the nascent transcript during rapid
chain extension. The basis of discrimination between the correct and
incorrect base was the slow addition of the next nucleotide to the
mismatched terminus. Incorporation of inosine monophosphate inhibited
the next nucleotide addition by a similar magnitude as a mismatched
base. Thomas et al. (1998) demonstrated that addition of SII to a
transcription reaction dramatically altered the RNA base content,
reflecting the stable incorporation of more 'correct' (GMP) and fewer
'incorrect' (IMP) nucleotides.
In vivo transcription by RNA polymerase II takes place in the context of
chromatin. Guermah et al. (2006) found that a purified, reconstituted
RNA polymerase II system that sufficed for activator-dependent
transcription on DNA templates was incapable of transcribing chromatin
templates, even in the presence of factors that effected transcription
in less-purified assay systems. Using a complementation and HeLa cell
nuclear extract fractionation scheme, Guermah et al. (2006) identified
and purified an activity, designated CTEA (chromatin
transcription-enabling activity), that allowed for transcription through
chromatin templates in a manner that was both activator and p300 (EP300;
602700)/acetyl-CoA dependent. CTEA acted primarily at the elongation
step and enabled RNA polymerase II machinery to transcribe efficiently
through several contiguously positioned nucleosomes. Guermah et al.
(2006) identified the major functional component of CTEA as
transcription elongation factor SII. SII was essential for productive
transcription elongation, and its function at this step was dependent on
p300-dependent acetylation. These synergistic transcriptional elongation
activities were potentiated by HMGB2 (163906).
Astrom et al. (1999) showed that activation of PLAG1 (603026) in
salivary gland tumors (181030) is not confined to adenomas with 8q12
abnormalities but is also found in tumors with a normal karyotype. They
showed further that PLAG1 may be activated by cryptic rearrangements in
cases with normal karyotypes, leading to fusions between PLAG1 and
CTNNB1 (116806) or the TCEA1 gene.
GENE STRUCTURE
Park et al. (1994) determined that the TCEA1 gene is 2.8 kb long and
intronless.
MAPPING
DiMarco et al. (1996) designed PCR primers for the TCEA1 gene and mapped
it to human chromosome 3 by analysis of human-rodent hybrid mapping
panel. Further regionalization to chromosome 3p22-p21.3 was accomplished
by fluorescence in situ hybridization using a YAC containing the gene.
DiMarco et al. (1996) cited reports that this region of 3p exhibits loss
of heterozygosity (LOH) in small- and non-small-cell lung carcinomas, as
well as several other malignancies.
*FIELD* RF
1. Aso, T.; Lane, W. S.; Conaway, J. W.; Conaway, R. C.: Elongin
(SIII): a multisubunit regulator of elongation by RNA polymerase II. Science 269:
1439-1443, 1995.
2. Astrom, A.-K.; Voz, M. L.; Kas, K.; Roijer, E.; Wedell, B.; Mandahl,
N.; Van de Ven, W.; Mark, J.; Stenman, G.: Conserved mechanism of
PLAG1 activation in salivary gland tumors with and without chromosome
8q12 abnormalities: identification of SII as a new fusion partner
gene. Cancer Res. 59: 918-923, 1999.
3. DiMarco, S. P.; Glover, T. W.; Miller, D. E.; Reines, D.; Warren,
S. T.: Transcription elongation factor SII (TCEA) maps to human chromosome
3p22-p21.3. Genomics 36: 185-188, 1996.
4. Guermah, M.; Palhan, V. B.; Tackett, A. J.; Chait, B. T.; Roeder,
R. G.: Synergistic functions of SII and p300 in productive activator-dependent
transcription of chromatin templates. Cell 125: 275-286, 2006.
5. Park, H.; Baek, K.; Jeon, C.; Agarwal, K.; Yoo, O.: Characterization
of the gene encoding the human transcriptional elongation factor TFIIS. Gene 139:
263-267, 1994.
6. Reines, D.: Nascent RNA cleavage by transcription elongation complexes.In:
Conaway, R. C.; Conaway, J. W. (eds.): Transcription: Mechanisms
and Regulation. New York: Raven Press 1994. Pp. 263-278.
7. Thomas, M. J.; Platas, A. A.; Hawley, D. K.: Transcriptional fidelity
and proofreading by RNA polymerase II. Cell 93: 627-637, 1998.
*FIELD* CN
Matthew B. Gross - updated: 3/8/2010
Victor A. McKusick - updated: 4/16/1999
Stylianos E. Antonarakis - updated: 6/4/1998
*FIELD* CD
Mark H. Paalman: 9/16/1996
*FIELD* ED
wwang: 03/10/2010
mgross: 3/8/2010
alopez: 5/21/1999
terry: 4/16/1999
carol: 12/15/1998
carol: 6/9/1998
terry: 6/4/1998
mark: 5/14/1997
terry: 9/17/1996
mark: 9/16/1996