ID   TEM1_YEAST              Reviewed;         245 AA.
AC   P38987; D6VZA9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Protein TEM1;
GN   Name=TEM1; OrderedLocusNames=YML064C;
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].
RX   PubMed=7935462; DOI=10.1128/mcb.14.11.7476-7482.1994;
RA   Shirayama M., Matsui Y., Toh-e A.;
RT   "The yeast TEM1 gene, which encodes a GTP-binding protein, is involved in
RT   termination of M phase.";
RL   Mol. Cell. Biol. 14:7476-7482(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH AMN1 AND CDC15.
RX   PubMed=12628189; DOI=10.1016/s0092-8674(03)00121-1;
RA   Wang Y., Shirogane T., Liu D., Harper J.W., Elledge S.J.;
RT   "Exit from exit: resetting the cell cycle through Amn1 inhibition of G
RT   protein signaling.";
RL   Cell 112:697-709(2003).
RN   [6]
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).
CC   -!- FUNCTION: GTP-binding protein involved in termination of M phase. May
CC       play a role in triggering the degradation of G2 cyclin to inactivate M-
CC       phase promoting factor at the termination of mitosis. Acts upstream of
CC       CDC15 kinase and may be required to activate the CDC15 protein kinase
CC       pathway. {ECO:0000269|PubMed:12628189}.
CC   -!- SUBUNIT: Interacts with CDC15 and AMN1. AMN1 and CDC15 compete for
CC       association with TEM1. {ECO:0000269|PubMed:12628189}.
CC   -!- INTERACTION:
CC       P38987; P38285: AMN1; NbExp=6; IntAct=EBI-19113, EBI-20853;
CC       P38987; P47113: BFA1; NbExp=3; IntAct=EBI-19113, EBI-3586;
CC       P38987; P26448: BUB2; NbExp=2; IntAct=EBI-19113, EBI-3824;
CC       P38987; P27636: CDC15; NbExp=6; IntAct=EBI-19113, EBI-4200;
CC   -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; D38172; BAA07371.1; -; Genomic_DNA.
DR   EMBL; Z38114; CAA86257.1; -; Genomic_DNA.
DR   EMBL; AY557980; AAS56306.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09833.1; -; Genomic_DNA.
DR   PIR; S48334; S48334.
DR   RefSeq; NP_013647.1; NM_001182423.1.
DR   AlphaFoldDB; P38987; -.
DR   SMR; P38987; -.
DR   BioGRID; 35102; 384.
DR   DIP; DIP-1691N; -.
DR   IntAct; P38987; 121.
DR   MINT; P38987; -.
DR   STRING; 4932.YML064C; -.
DR   iPTMnet; P38987; -.
DR   MaxQB; P38987; -.
DR   PaxDb; 4932-YML064C; -.
DR   PeptideAtlas; P38987; -.
DR   EnsemblFungi; YML064C_mRNA; YML064C; YML064C.
DR   GeneID; 854938; -.
DR   KEGG; sce:YML064C; -.
DR   AGR; SGD:S000004529; -.
DR   SGD; S000004529; TEM1.
DR   VEuPathDB; FungiDB:YML064C; -.
DR   eggNOG; KOG1673; Eukaryota.
DR   HOGENOM; CLU_041217_0_2_1; -.
DR   InParanoid; P38987; -.
DR   OMA; FDLNCTI; -.
DR   OrthoDB; 638at2759; -.
DR   BioCyc; YEAST:G3O-32659-MONOMER; -.
DR   BioGRID-ORCS; 854938; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P38987; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P38987; Protein.
DR   GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:SGD.
DR   GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IMP:SGD.
DR   GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IMP:SGD.
DR   GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:SGD.
DR   GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IBA:GO_Central.
DR   GO; GO:0023056; P:positive regulation of signaling; IDA:SGD.
DR   GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IMP:SGD.
DR   CDD; cd04128; Spg1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR017231; Small_GTPase_Tem1/Spg1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47978; -; 1.
DR   PANTHER; PTHR47978:SF24; PROTEIN TEM1; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; GTP-binding; Mitosis; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..245
FT                   /note="Protein TEM1"
FT                   /id="PRO_0000122466"
FT   REGION          16..244
FT                   /note="Small GTPase-like"
FT   REGION          210..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  27296 MW;  F650C8946A03707C CRC64;
     MATPSTGANN SIPAVRNQVE VQVGLVGDAQ VGKTSLMVKY VQNIYDKEYT QTLGVNFLKR
     KVSIRSTDII FSIMDLGGQR EFINMLPIAT VGSSVIIFLF DLTRPETLSS IKEWYRQAYG
     LNDSAIPILV GTKYDLLIDL DPEYQEQISR TSMKYAQVMN APLIFCSTAK SINIQKIFKI
     ALAKIFNLTL TIPEINEIGD PLLIYKHLGG QQHRHHNKSQ DRKSHNIRKP SSSPSSKAPS
     PGVNT
//