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TOF2_YEAST
ID   TOF2_YEAST              Reviewed;         771 AA.
AC   Q02208; D6VX76;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Topoisomerase 1-associated factor 2;
GN   Name=TOF2; OrderedLocusNames=YKR010C; ORFNames=YK109;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1441752; DOI=10.1002/yea.320080908;
RA   Duesterhoeft A., Philippsen P.;
RT   "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT   CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT   reading frames.";
RL   Yeast 8:749-759(1992).
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   IDENTIFICATION, AND INTERACTION WITH HPR1.
RX   PubMed=10028183;
RX   DOI=10.1002/(sici)1097-0061(19990115)15:1<35::aid-yea340>3.0.co;2-r;
RA   Park H., Sternglanz R.;
RT   "Identification and characterization of the genes for two topoisomerase I-
RT   interacting proteins from Saccharomyces cerevisiae.";
RL   Yeast 15:35-41(1999).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397 AND THR-405, AND
RP   IDENTIFICATION BY 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   -!- SUBUNIT: Interacts with HPR1. {ECO:0000269|PubMed:10028183}.
CC   -!- INTERACTION:
CC       Q02208; Q00684: CDC14; NbExp=8; IntAct=EBI-27048, EBI-4192;
CC       Q02208; P25651: CSM1; NbExp=4; IntAct=EBI-27048, EBI-22001;
CC       Q02208; P47035: NET1; NbExp=6; IntAct=EBI-27048, EBI-25953;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: To yeast YJL076w. {ECO:0000305}.
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DR   EMBL; X65124; CAA46242.1; -; Genomic_DNA.
DR   EMBL; Z28235; CAA82080.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09166.1; -; Genomic_DNA.
DR   PIR; S25814; S25814.
DR   RefSeq; NP_012935.3; NM_001179800.3.
DR   PDB; 5HOI; X-ray; 3.30 A; D/E/F=497-517.
DR   PDB; 5V3N; X-ray; 1.30 A; B=384-398.
DR   PDBsum; 5HOI; -.
DR   PDBsum; 5V3N; -.
DR   AlphaFoldDB; Q02208; -.
DR   SMR; Q02208; -.
DR   BioGRID; 34143; 155.
DR   DIP; DIP-3803N; -.
DR   IntAct; Q02208; 18.
DR   MINT; Q02208; -.
DR   STRING; 4932.YKR010C; -.
DR   iPTMnet; Q02208; -.
DR   MaxQB; Q02208; -.
DR   PaxDb; Q02208; -.
DR   PRIDE; Q02208; -.
DR   EnsemblFungi; YKR010C_mRNA; YKR010C; YKR010C.
DR   GeneID; 853880; -.
DR   KEGG; sce:YKR010C; -.
DR   SGD; S000001718; TOF2.
DR   VEuPathDB; FungiDB:YKR010C; -.
DR   eggNOG; ENOG502QW4V; Eukaryota.
DR   GeneTree; ENSGT00940000176631; -.
DR   HOGENOM; CLU_362533_0_0_1; -.
DR   InParanoid; Q02208; -.
DR   OMA; DIGENCR; -.
DR   BioCyc; YEAST:G3O-31987-MON; -.
DR   PRO; PR:Q02208; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; Q02208; protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0019211; F:phosphatase activator activity; IDA:SGD.
DR   GO; GO:0000182; F:rDNA binding; IBA:GO_Central.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IBA:GO_Central.
DR   GO; GO:0007000; P:nucleolus organization; IMP:SGD.
DR   GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IMP:SGD.
DR   GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR   GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR   InterPro; IPR018844; Dnt1-like_N.
DR   InterPro; IPR043185; Dnt1/Tof2/Net1.
DR   PANTHER; PTHR28196; PTHR28196; 2.
DR   Pfam; PF10407; Cytokin_check_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..771
FT                   /note="Topoisomerase 1-associated factor 2"
FT                   /id="PRO_0000072621"
FT   REGION          48..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         405
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   HELIX           503..512
FT                   /evidence="ECO:0007829|PDB:5HOI"
SQ   SEQUENCE   771 AA;  86366 MW;  DDA5E96B833575A3 CRC64;
     MIKMWRLQIV LVPPSAQDII TFLEARLNTP QSVSPMVQYN EDIITHNNSI NNCSDPSPTS
     PSSQNSIQSN RSSDFINYLP NCKKFLHFTD GDNTLLQLSN EILTKFDRLY PNFKESIEIV
     SLQDRHGCDL DSEFIIKDVF ENDGVVLVIL KDELDWSRNQ HISLLQLARQ RRRQDNKPST
     KSIVTEKRKK ISKEDLSSIS NKDTMHLIAK SSLKNNFINK SRVSTPLMNE ILPLASKYDA
     LNKEKCPMPL TSTVVASNVH KDVKDHARAK EGVVTQGSDN NKENIPSSTQ QQKNDGAKRA
     ESKDLDLLRN SSEDADYEPA DENSPQISFD SIDTDFQLST TSHTNSDMHI QYSNPSSGAH
     SPRKSSLEIK VQNKKGDDLP LNDKDIGENC RRIEAFSDEE DFNETDNDRA DSFINNSKKA
     SMGFRDINSD LDSVSFNSDI ENAVQSTQST KNVVSPPFFP EKELNNRLHQ SQGKEALFRL
     VEKEFPDKSL GAASSTSHAK DVKIQETIRK LNRFKPTGET KVQKRNSITE PYYGKFGIMK
     KDKPKSITSK GVSLETKHFD DPNTIISGEK FAKFGKIKVK RKTDDVGSKV IEFKRKRNMG
     NRSLKDIFAN AGKPPNAAST IKVVKLMRDP VDNSKDKVEA TSNSTAQEQE QVSPKLPVMN
     STPGKRKNGQ AIPSSLERTP QLKKVKVTRS HSSPSSSSSM SLESSLDSSS SDDSDDDSDS
     RNVQVKKINF KTSHGPAGNS NGKPMLDVDD NEINTKKYQT PKYVESDEDD Q
 
 
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