位置:首页 > 蛋白库 > T2EB_YEAST
T2EB_YEAST
ID   T2EB_YEAST              Reviewed;         328 AA.
AC   P36145; D6VXC3; P42569;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Transcription initiation factor IIE subunit beta;
DE            Short=TFIIE-beta;
DE   AltName: Full=Factor A 43 kDa subunit;
DE   AltName: Full=Transcription factor A small subunit;
GN   Name=TFA2; OrderedLocusNames=YKR062W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 180-194 AND 254-276,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 208279 / BJ926;
RX   PubMed=7961670; DOI=10.1016/s0021-9258(18)47019-6;
RA   Feaver W.J., Henry N.L., Bushnell D.A., Sayre M.H., Brickner J.H.,
RA   Gileadi O., Kornberg R.D.;
RT   "Yeast TFIIE. Cloning, expression, and homology to vertebrate proteins.";
RL   J. Biol. Chem. 269:27549-27553(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the
CC       RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase
CC       activities of TFIIH. Both TFIIH and TFIIE are required for promoter
CC       clearance by RNA polymerase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: TFIIE is a tetramer of two alpha (TFA1) and two beta (TFA2)
CC       subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1150 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TFIIE beta subunit family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00682}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U12824; AAA62664.1; -; Genomic_DNA.
DR   EMBL; Z28287; CAA82141.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09213.1; -; Genomic_DNA.
DR   PIR; S38138; S38138.
DR   RefSeq; NP_012988.1; NM_001179852.1.
DR   PDB; 5FMF; EM; 6.00 A; S=125-247.
DR   PDB; 5FYW; EM; 4.35 A; X=1-328.
DR   PDB; 5FZ5; EM; 8.80 A; X=1-328.
DR   PDB; 5OQJ; EM; 4.70 A; X=1-328.
DR   PDB; 5OQM; EM; 5.80 A; X=1-328.
DR   PDB; 5SVA; EM; 15.30 A; i=1-328.
DR   PDB; 6GYL; EM; 4.80 A; X=1-328.
DR   PDB; 6GYM; EM; 6.70 A; X=1-328.
DR   PDB; 7O4I; EM; 3.20 A; X=1-328.
DR   PDB; 7O4J; EM; 2.90 A; X=1-328.
DR   PDB; 7O4K; EM; 3.60 A; X=1-328.
DR   PDB; 7O4L; EM; 3.40 A; X=1-328.
DR   PDB; 7O72; EM; 3.40 A; X=1-328.
DR   PDB; 7O73; EM; 3.40 A; X=1-328.
DR   PDB; 7O75; EM; 3.20 A; X=1-328.
DR   PDBsum; 5FMF; -.
DR   PDBsum; 5FYW; -.
DR   PDBsum; 5FZ5; -.
DR   PDBsum; 5OQJ; -.
DR   PDBsum; 5OQM; -.
DR   PDBsum; 5SVA; -.
DR   PDBsum; 6GYL; -.
DR   PDBsum; 6GYM; -.
DR   PDBsum; 7O4I; -.
DR   PDBsum; 7O4J; -.
DR   PDBsum; 7O4K; -.
DR   PDBsum; 7O4L; -.
DR   PDBsum; 7O72; -.
DR   PDBsum; 7O73; -.
DR   PDBsum; 7O75; -.
DR   AlphaFoldDB; P36145; -.
DR   SMR; P36145; -.
DR   BioGRID; 34193; 199.
DR   ComplexPortal; CPX-1658; General transcription factor complex TFIIE.
DR   DIP; DIP-1701N; -.
DR   IntAct; P36145; 6.
DR   MINT; P36145; -.
DR   STRING; 4932.YKR062W; -.
DR   iPTMnet; P36145; -.
DR   MaxQB; P36145; -.
DR   PaxDb; P36145; -.
DR   PRIDE; P36145; -.
DR   EnsemblFungi; YKR062W_mRNA; YKR062W; YKR062W.
DR   GeneID; 853936; -.
DR   KEGG; sce:YKR062W; -.
DR   SGD; S000001770; TFA2.
DR   VEuPathDB; FungiDB:YKR062W; -.
DR   eggNOG; KOG3095; Eukaryota.
DR   GeneTree; ENSGT00390000011749; -.
DR   HOGENOM; CLU_056580_2_0_1; -.
DR   InParanoid; P36145; -.
DR   OMA; MRMVFWN; -.
DR   BioCyc; YEAST:G3O-32030-MON; -.
DR   Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   PRO; PR:P36145; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36145; protein.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0005673; C:transcription factor TFIIE complex; IDA:SGD.
DR   GO; GO:0097550; C:transcription preinitiation complex; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR   CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR   InterPro; IPR040501; TFA2_Winged_2.
DR   InterPro; IPR016656; TFIIE-bsu.
DR   InterPro; IPR003166; TFIIE_bsu_DNA-bd.
DR   PANTHER; PTHR12716; PTHR12716; 1.
DR   Pfam; PF18121; TFA2_Winged_2; 1.
DR   Pfam; PF02186; TFIIE_beta; 1.
DR   PIRSF; PIRSF016398; TFIIE-beta; 1.
DR   PROSITE; PS51351; TFIIE_BETA_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..328
FT                   /note="Transcription initiation factor IIE subunit beta"
FT                   /id="PRO_0000211230"
FT   DNA_BIND        113..187
FT                   /note="TFIIE beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00682"
FT   REGION          32..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        248
FT                   /note="S -> R (in Ref. 1; AAA62664)"
FT                   /evidence="ECO:0000305"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:7O4I"
FT   HELIX           107..115
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           124..136
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           144..150
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           158..165
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   TURN            173..176
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           189..197
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           207..211
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           218..227
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           257..265
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           274..280
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   TURN            316..320
FT                   /evidence="ECO:0007829|PDB:7O4J"
SQ   SEQUENCE   328 AA;  36985 MW;  8751614A7237D3E1 CRC64;
     MSKNRDPLLA NLNAFKSKVK SAPVIAPAKV GQKKTNDTVI TIDGNTRKRT ASERAQENTL
     NSAKNPVLVD IKKEAGSNSS NAISLDDDDD DEDFGSSPSK KVRPGSIAAA ALQANQTDIS
     KSHDSSKLLW ATEYIQKKGK PVLVNELLDY LSMKKDDKVI ELLKKLDRIE FDPKKGTFKY
     LSTYDVHSPS ELLKLLRSQV TFKGISCKDL KDGWPQCDET INQLEEDSKI LVLRTKKDKT
     PRYVWYNSGG NLKCIDEEFV KMWENVQLPQ FAELPRKLQD LGLKPASVDP ATIKRQTKRV
     EVKKKRQRKG KITNTHMTGI LKDYSHRV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024