KTI12_YEAST
ID KTI12_YEAST Reviewed; 313 AA.
AC P34253; D6VXH7; Q05155;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein KTI12;
DE AltName: Full=Gamma-toxin target protein 4;
DE AltName: Full=Killer toxin insensitivity protein 12;
GN Name=KTI12; OrderedLocusNames=YKL110C; ORFNames=YKL446, YKL500;
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], AND FUNCTION.
RX PubMed=8065362; DOI=10.1128/mcb.14.9.6306-6316.1994;
RA Butler A.R., White J.H., Folawiyo Y., Edlin A., Gardiner D., Stark M.J.R.;
RT "Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest
RT induced by Kluyveromyces lactis toxin.";
RL Mol. Cell. Biol. 14:6306-6316(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RX PubMed=8109175; DOI=10.1002/yea.320091113;
RA Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H.,
RA Bolotin-Fukuhara M., Sor F.;
RT "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of
RT Saccharomyces cerevisiae suggests the presence of a second aspartate
RT aminotransferase gene in yeast.";
RL Yeast 9:1259-1265(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-313.
RX PubMed=1561835; DOI=10.1002/yea.320080207;
RA Jacquier A., Legrain P., Dujon B.;
RT "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1
RT and the BAF1 loci and reveals one tRNA gene and several new open reading
RT frames including homologs to RAD2 and kinases.";
RL Yeast 8:121-132(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-313.
RX PubMed=2511628; DOI=10.1126/science.2511628;
RA Diffley J.F.X., Stillman B.;
RT "Similarity between the transcriptional silencer binding proteins ABF1 and
RT RAP1.";
RL Science 246:1034-1038(1989).
RN [7]
RP FUNCTION, AND INTERACTION WITH THE ELONGATOR COMPLEX.
RX PubMed=11296232; DOI=10.1093/emboj/20.8.1993;
RA Frohloff F., Fichtner L., Jablonowski D., Breunig K.D., Schaffrath R.;
RT "Saccharomyces cerevisiae Elongator mutations confer resistance to the
RT Kluyveromyces lactis zymocin.";
RL EMBO J. 20:1993-2003(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH THE ELONGATOR COMPLEX.
RX PubMed=11929532; DOI=10.1046/j.1365-2958.2002.02794.x;
RA Fichtner L., Frohloff F., Buerkner K., Larsen M., Breunig K.D.,
RA Schaffrath R.;
RT "Molecular analysis of KTI12/TOT4, a Saccharomyces cerevisiae gene required
RT for Kluyveromyces lactis zymocin action.";
RL Mol. Microbiol. 43:783-791(2002).
RN [9]
RP INTERACTION WITH THE ELONGATOR COMPLEX.
RX PubMed=12139626; DOI=10.1046/j.1365-2958.2002.03055.x;
RA Fichtner L., Frohloff F., Jablonowski D., Stark M.J.R., Schaffrath R.;
RT "Protein interactions within Saccharomyces cerevisiae Elongator, a complex
RT essential for Kluyveromyces lactis zymocicity.";
RL Mol. Microbiol. 45:817-826(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH THE ELONGATOR COMPLEX.
RX PubMed=12424236; DOI=10.1074/jbc.m210060200;
RA Frohloff F., Jablonowski D., Fichtner L., Schaffrath R.;
RT "Subunit communications crucial for the functional integrity of the yeast
RT RNA polymerase II elongator (gamma-toxin target (TOT)) complex.";
RL J. Biol. Chem. 278:956-961(2003).
RN [11]
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 [12]
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 [13]
RP FUNCTION, AND INTERACTION WITH THE ELONGATOR COMPLEX.
RX PubMed=14718557; DOI=10.1091/mbc.e03-10-0750;
RA Jablonowski D., Fichtner L., Stark M.J.R., Schaffrath R.;
RT "The yeast elongator histone acetylase requires Sit4-dependent
RT dephosphorylation for toxin-target capacity.";
RL Mol. Biol. Cell 15:1459-1469(2004).
RN [14]
RP FUNCTION, INTERACTION WITH THE ELONGATOR COMPLEX, AND CHROMATIN BINDING.
RX PubMed=15772087; DOI=10.1074/jbc.m413373200;
RA Petrakis T.G., Soegaard T.M.M., Erdjument-Bromage H., Tempst P.,
RA Svejstrup J.Q.;
RT "Physical and functional interaction between Elongator and the chromatin-
RT associated Kti12 protein.";
RL J. Biol. Chem. 280:19454-19460(2005).
RN [15]
RP FUNCTION.
RX PubMed=15769872; DOI=10.1261/rna.7247705;
RA Huang B., Johansson M.J.O., Bystroem A.S.;
RT "An early step in wobble uridine tRNA modification requires the Elongator
RT complex.";
RL RNA 11:424-436(2005).
RN [16]
RP INTERACTION WITH THE ELONGATOR COMPLEX.
RX PubMed=18986986; DOI=10.1074/jbc.m805312200;
RA Greenwood C., Selth L.A., Dirac-Svejstrup A.B., Svejstrup J.Q.;
RT "An iron-sulfur cluster domain in Elp3 important for the structural
RT integrity of elongator.";
RL J. Biol. Chem. 284:141-149(2009).
RN [17]
RP INTERACTION WITH ELONGATOR COMPLEX COMPONENT ELP1.
RX PubMed=25569479; DOI=10.1371/journal.pgen.1004931;
RA Abdel-Fattah W., Jablonowski D., Di Santo R., Thuering K.L., Scheidt V.,
RA Hammermeister A., Ten Have S., Helm M., Schaffrath R., Stark M.J.;
RT "Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA
RT modification in yeast.";
RL PLoS Genet. 11:e1004931-e1004931(2015).
CC -!- FUNCTION: Elongator complex-associated factor that is not a structural
CC subunit but rather transiently contacts the complex. Regulates
CC elongator complex gamma-toxin target (TOT) activity, resulting in G1
CC block by Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin),
CC probably through regulation of the ELP1/IKI3 subunit phosphorylation
CC state. Required for an early step in synthesis of 5-
CC methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups
CC present on uridines at the wobble position in tRNA.
CC {ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:11929532,
CC ECO:0000269|PubMed:12424236, ECO:0000269|PubMed:14718557,
CC ECO:0000269|PubMed:15769872, ECO:0000269|PubMed:15772087,
CC ECO:0000269|PubMed:8065362}.
CC -!- SUBUNIT: Interacts with the elongator complex.
CC {ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:11929532,
CC ECO:0000269|PubMed:12139626, ECO:0000269|PubMed:12424236,
CC ECO:0000269|PubMed:14718557, ECO:0000269|PubMed:15772087,
CC ECO:0000269|PubMed:18986986, ECO:0000269|PubMed:25569479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
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DR EMBL; X77511; CAA54646.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50447.1; -; Genomic_DNA.
DR EMBL; S93804; AAB22001.1; -; Genomic_DNA.
DR EMBL; Z28110; CAA81950.1; -; Genomic_DNA.
DR EMBL; M29067; AAA66312.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09047.1; -; Genomic_DNA.
DR PIR; S37937; S37937.
DR RefSeq; NP_012812.1; NM_001179676.1.
DR AlphaFoldDB; P34253; -.
DR SMR; P34253; -.
DR BioGRID; 34023; 325.
DR DIP; DIP-1856N; -.
DR IntAct; P34253; 3.
DR MINT; P34253; -.
DR STRING; 4932.YKL110C; -.
DR iPTMnet; P34253; -.
DR MaxQB; P34253; -.
DR PaxDb; P34253; -.
DR PRIDE; P34253; -.
DR EnsemblFungi; YKL110C_mRNA; YKL110C; YKL110C.
DR GeneID; 853750; -.
DR KEGG; sce:YKL110C; -.
DR SGD; S000001593; KTI12.
DR VEuPathDB; FungiDB:YKL110C; -.
DR eggNOG; KOG3062; Eukaryota.
DR GeneTree; ENSGT00390000002443; -.
DR HOGENOM; CLU_027147_2_0_1; -.
DR InParanoid; P34253; -.
DR OMA; LYCEAKA; -.
DR BioCyc; YEAST:G3O-31896-MON; -.
DR PRO; PR:P34253; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34253; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045106; Kti12.
DR InterPro; IPR013641; KTI12/PSTK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12435; PTHR12435; 1.
DR Pfam; PF08433; KTI12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..313
FT /note="Protein KTI12"
FT /id="PRO_0000084335"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 103
FT /note="N -> D (in Ref. 5; AAA66312)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="S -> N (in Ref. 5; AAA66312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35322 MW; 15A9534087A24AE6 CRC64;
MPLVLFTGYP CSGKTTLAKH LVQLLQSKID ATPSLSKYSI TYHSDESLGI KHSDYITSQD
ERKLRSEIIS AVKRDLSKNK IVIVDSLNYI KGFRYQLHCE VKNLSTTFCV IQTLCPPETI
FEWNKTSNPN PWEPELLNQL IQRYEEPNSS NRWDSPLFAI LTPQDNITDY IDDICKVVFQ
TSKSAKNSGH NDPLSKGLQK PNSATVLKPA SQSNFIQVLD IETSKIIKTI MNHIKSLTSI
GGVSNGTRVI VSEGITDIND DGCFFVDLPI GNVVTLAQLQ RLKRQFINFN KLRDIDQDRI
GPLFADYLNK NLN
