ATS1_YEAST
ID ATS1_YEAST Reviewed; 333 AA.
AC P31386; D6VPJ8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein KTI13 {ECO:0000305};
DE AltName: Full=Alpha-tubulin suppressor 1 {ECO:0000303|PubMed:8070652};
DE AltName: Full=Kluyveromyces lactis toxin-insensitive protein 13 {ECO:0000303|PubMed:18466297};
GN Name=ATS1 {ECO:0000303|PubMed:8070652, ECO:0000312|SGD:S000000018};
GN Synonyms=KTI13 {ECO:0000303|PubMed:18466297}; OrderedLocusNames=YAL020C;
GN ORFNames=FUN28, YAL006;
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 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8144453; DOI=10.1128/jb.176.7.1872-1880.1994;
RA Barton A.B., Kaback D.B.;
RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT analysis of the genes in the FUN38-MAK16-SPO7 region.";
RL J. Bacteriol. 176:1872-1880(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 305.
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 [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=1561836; DOI=10.1002/yea.320080208;
RA Clark M.W., Zhong W.-W., Keng T., Storms R.K., Barton A.B., Kaback D.B.,
RA Bussey H.;
RT "Identification of a Saccharomyces cerevisiae homolog of the SNF2
RT transcriptional regulator in the DNA sequence of an 8.6 kb region in the
RT LTE1-CYS1 interval on the left arm of chromosome I.";
RL Yeast 8:133-145(1992).
RN [6]
RP FUNCTION.
RX PubMed=8070652; DOI=10.1093/genetics/137.2.381;
RA Kirkpatrick D., Solomon F.;
RT "Overexpression of yeast homologs of the mammalian checkpoint gene RCC1
RT suppresses the class of alpha-tubulin mutations that arrest with excess
RT microtubules.";
RL Genetics 137:381-392(1994).
RN [7]
RP INTERACTION WITH KTI11.
RX PubMed=18627462; DOI=10.1111/j.1365-2958.2008.06350.x;
RA Baer C., Zabel R., Liu S., Stark M.J., Schaffrath R.;
RT "A versatile partner of eukaryotic protein complexes that is involved in
RT multiple biological processes: Kti11/Dph3.";
RL Mol. Microbiol. 69:1221-1233(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KTI11.
RX PubMed=18466297; DOI=10.1111/j.1365-2958.2008.06273.x;
RA Zabel R., Baer C., Mehlgarten C., Schaffrath R.;
RT "Yeast alpha-tubulin suppressor ATS1/KTI13 relates to the Elongator complex
RT and interacts with Elongator partner protein Kti11.";
RL Mol. Microbiol. 69:175-187(2008).
RN [9]
RP INTERACTION WITH KTI11, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27694803; DOI=10.1038/nchembio.2190;
RA Lin Z., Dong M., Zhang Y., Lee E.A., Lin H.;
RT "Cbr1 is a Dph3 reductase required for the tRNA wobble uridine
RT modification.";
RL Nat. Chem. Biol. 12:995-997(2016).
RN [10] {ECO:0007744|PDB:4X33}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH KTI11, INTERACTION
RP WITH KTI11, AND MUTAGENESIS OF TRP-96; LYS-157; TRP-229; TRP-294 AND
RP HIS-297.
RX PubMed=25604895; DOI=10.1111/febs.13199;
RA Kolaj-Robin O., McEwen A.G., Cavarelli J., Seraphin B.;
RT "Structure of the Elongator cofactor complex Kti11/Kti13 provides insight
RT into the role of Kti13 in Elongator-dependent tRNA modification.";
RL FEBS J. 282:819-833(2015).
RN [11] {ECO:0007744|PDB:4D4O, ECO:0007744|PDB:4D4P, ECO:0007744|PDB:4D4Q}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH KTI11, FUNCTION,
RP INTERACTION WITH KTI11, AND MUTAGENESIS OF TRP-96; TRP-229; TRP-294;
RP GLU-296 AND HIS-297.
RX PubMed=25543256; DOI=10.1016/j.str.2014.11.008;
RA Glatt S., Zabel R., Vonkova I., Kumar A., Netz D.J., Pierik A.J., Rybin V.,
RA Lill R., Gavin A.C., Balbach J., Breunig K.D., Muller C.W.;
RT "Structure of the Kti11/Kti13 heterodimer and its double role in
RT modifications of tRNA and eukaryotic elongation factor 2.";
RL Structure 23:149-160(2015).
CC -!- FUNCTION: Together with KTI11; associates with the elongator complex
CC and is required for tRNA Wobble base modifications mediated by the
CC elongator complex (PubMed:18466297, PubMed:25543256). Association with
CC the elongator complex is mediated via interaction with KTI11
CC (PubMed:18466297, PubMed:25543256). The elongator complex is required
CC for multiple tRNA modifications, including mcm5U (5-
CC methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-
CC thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:25543256).
CC Together with KTI11; also required for diphthamide biosynthesis;
CC diphthamide is a post-translational modification of histidine which
CC occurs in elongation factor 2 (PubMed:25543256). May participate in
CC regulatory interactions between microtubules and the cell cycle
CC (PubMed:8070652). {ECO:0000269|PubMed:18466297,
CC ECO:0000269|PubMed:25543256, ECO:0000269|PubMed:8070652}.
CC -!- SUBUNIT: Interacts with KTI11/DPH3; the interaction is direct.
CC {ECO:0000269|PubMed:18466297, ECO:0000269|PubMed:18627462,
CC ECO:0000269|PubMed:25543256, ECO:0000269|PubMed:25604895,
CC ECO:0000269|PubMed:27694803}.
CC -!- INTERACTION:
CC P31386; Q3E840: KTI11; NbExp=9; IntAct=EBI-2046012, EBI-2055307;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18466297}.
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DR EMBL; L05146; AAC04937.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06968.2; -; Genomic_DNA.
DR PIR; S36714; S36714.
DR RefSeq; NP_009382.2; NM_001178165.2.
DR PDB; 4D4O; X-ray; 2.90 A; A/B/C=1-333.
DR PDB; 4D4P; X-ray; 3.00 A; A/B/C/E/G/H=1-333.
DR PDB; 4D4Q; X-ray; 2.40 A; A/B=1-333.
DR PDB; 4X33; X-ray; 1.45 A; B=1-333.
DR PDBsum; 4D4O; -.
DR PDBsum; 4D4P; -.
DR PDBsum; 4D4Q; -.
DR PDBsum; 4X33; -.
DR AlphaFoldDB; P31386; -.
DR SMR; P31386; -.
DR BioGRID; 31746; 142.
DR DIP; DIP-7890N; -.
DR IntAct; P31386; 2.
DR MINT; P31386; -.
DR STRING; 4932.YAL020C; -.
DR MaxQB; P31386; -.
DR PaxDb; P31386; -.
DR PRIDE; P31386; -.
DR EnsemblFungi; YAL020C_mRNA; YAL020C; YAL020C.
DR GeneID; 851213; -.
DR KEGG; sce:YAL020C; -.
DR SGD; S000000018; ATS1.
DR VEuPathDB; FungiDB:YAL020C; -.
DR eggNOG; KOG1426; Eukaryota.
DR HOGENOM; CLU_005210_0_0_1; -.
DR InParanoid; P31386; -.
DR OMA; WSSIHIL; -.
DR BioCyc; YEAST:G3O-28832-MON; -.
DR PRO; PR:P31386; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31386; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Repeat; tRNA processing.
FT CHAIN 1..333
FT /note="Protein KTI13"
FT /id="PRO_0000206648"
FT REPEAT 1..53
FT /note="RCC1 1"
FT REPEAT 55..104
FT /note="RCC1 2"
FT REPEAT 146..197
FT /note="RCC1 3"
FT REPEAT 286..333
FT /note="RCC1 4"
FT MUTAGEN 96
FT /note="W->A: Slightly reduced interaction with KTI11."
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895"
FT MUTAGEN 157
FT /note="K->D: Does not affect interaction with KTI11."
FT /evidence="ECO:0000269|PubMed:25604895"
FT MUTAGEN 229
FT /note="W->A,C: Abolished interaction with KTI11."
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895"
FT MUTAGEN 294
FT /note="W->A,E: Slightly reduced affinity for KTI11."
FT /evidence="ECO:0000269|PubMed:25604895"
FT MUTAGEN 296
FT /note="E->A: Does not affect interaction with KTI11."
FT /evidence="ECO:0000269|PubMed:25543256"
FT MUTAGEN 297
FT /note="H->A: Does not affect interaction with KTI11."
FT /evidence="ECO:0000269|PubMed:25543256,
FT ECO:0000269|PubMed:25604895"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4D4O"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4D4O"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:4X33"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4X33"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4D4O"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:4D4Q"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4X33"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:4X33"
SQ SEQUENCE 333 AA; 36467 MW; 3C6F4BE180479096 CRC64;
MSCVYAFGSN GQRQLGLGHD EDMDTPQRSV PGDDGAIVRK IACGGNHSVM LTNDGNLVGC
GDNRRGELDS AQALRQVHDW RPVEVPAPVV DVACGWDTTV IVDADGRVWQ RGGGCYEFTQ
QHVPLNSNDE RIAVYGCFQN FVVVQGTRVY GWGSNTKCQL QEPKSRSLKE PVLVYDTGSV
AVDYVAMGKD FMVIVDEGGR IVHASGRLPT GFELKQQQKR HNLVVLCMWT SIHLWNARLN
TVESFGRGTH SQLFPQERLD FPIVGVATGS EHGILTTANQ EGKSHCYNVY CWGWGEHGNC
GPQKGSQPGL QLVGQYSGKP RVFGGCATTW IVL
