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   27-MAR-2024, entry version 175.
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};
GN   OrderedLocusNames=YAL020C; 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; 144.
DR   DIP; DIP-7890N; -.
DR   IntAct; P31386; 2.
DR   MINT; P31386; -.
DR   STRING; 4932.YAL020C; -.
DR   MaxQB; P31386; -.
DR   PaxDb; 4932-YAL020C; -.
DR   PeptideAtlas; P31386; -.
DR   EnsemblFungi; YAL020C_mRNA; YAL020C; YAL020C.
DR   GeneID; 851213; -.
DR   KEGG; sce:YAL020C; -.
DR   AGR; SGD:S000000018; -.
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   OrthoDB; 5475808at2759; -.
DR   BioCyc; YEAST:G3O-28832-MONOMER; -.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 851213; 3 hits in 10 CRISPR screens.
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; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   PANTHER; PTHR45622:SF70; BTB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 1.
DR   Pfam; PF13540; RCC1_2; 2.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 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
//