TDA11_YEAST
ID TDA11_YEAST Reviewed; 504 AA.
AC P38854; D3DLA8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Topoisomerase I damage affected protein 11;
GN Name=TDA11; OrderedLocusNames=YHR159W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 THR-236; SER-244 AND SER-286, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-236 AND SER-244, 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).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21173034; DOI=10.1101/gr.109033.110;
RA Reid R.J., Gonzalez-Barrera S., Sunjevaric I., Alvaro D., Ciccone S.,
RA Wagner M., Rothstein R.;
RT "Selective ploidy ablation, a high-throughput plasmid transfer protocol,
RT identifies new genes affecting topoisomerase I-induced DNA damage.";
RL Genome Res. 21:477-486(2011).
RN [8]
RP IDENTIFICATION BY MASS 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Leads to cell death when overexpressing the
CC camptothecin mimetic TOP1-T(722)A mutant.
CC {ECO:0000269|PubMed:21173034}.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TDA11 family. {ECO:0000305}.
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; U10397; AAB68975.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06852.1; -; Genomic_DNA.
DR PIR; S46752; S46752.
DR RefSeq; NP_012029.1; NM_001179290.1.
DR AlphaFoldDB; P38854; -.
DR SMR; P38854; -.
DR BioGRID; 36593; 77.
DR DIP; DIP-4846N; -.
DR STRING; 4932.YHR159W; -.
DR iPTMnet; P38854; -.
DR MaxQB; P38854; -.
DR PaxDb; P38854; -.
DR PRIDE; P38854; -.
DR EnsemblFungi; YHR159W_mRNA; YHR159W; YHR159W.
DR GeneID; 856564; -.
DR KEGG; sce:YHR159W; -.
DR SGD; S000001202; TDA11.
DR VEuPathDB; FungiDB:YHR159W; -.
DR eggNOG; ENOG502S2SD; Eukaryota.
DR HOGENOM; CLU_046807_0_0_1; -.
DR InParanoid; P38854; -.
DR OMA; WSFVSDV; -.
DR BioCyc; YEAST:G3O-31194-MON; -.
DR PRO; PR:P38854; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38854; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR InterPro; IPR031388; Tda11.
DR Pfam; PF17084; TDA11; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..504
FT /note="Topoisomerase I damage affected protein 11"
FT /id="PRO_0000202928"
FT REGION 32..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..231
FT /evidence="ECO:0000255"
FT COMPBIAS 252..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 504 AA; 56314 MW; AE8B894335D1DB63 CRC64;
MNKFDEFIES NEKDLDVDTS TRNSIISMSP VRKTGRKIRS ASSNGYRLEH HRTSSAGSMH
SQRLMTPTRL NDQDHPLQAK PDARRVVTRH SSVSVPNAMS KRRSLIQPMV VPTTPESQNN
LPSVSHSEGS YGIPLESTTV LSSEQAMASG LRRSRNGSSQ SVNSMIATTI PTNGVDVSAL
LQSLATKELE LLECKQKIED LKKQTQHEEQ NYTRRARELH ELKEQVSKHL DPSLNTPVKN
RAFSPVYQNI PLESRTENAG NSSLPSSVSK PKNMGHQSTN QSRSVSPQDI QERRQRDDSS
DSSKQSLWSK PLALFNQFDK IIQHEIERTL NWDDSLSGTP EVQEGTPTSN SESSAQQYDN
EAPGARQKSP SQGSVSRSLW SFVSDVKAGL LGIEEENDND VITDNRCDPV YKSDRQHEQK
KSTHKITNRG QAEDSGDDSS LNMRKFKTTT KFQKDNAGNN SLTDESGHRT REKKSKRSSN
KLSFIGEPDN DNSSVKNSVE MTDF