ID TEM1_YEAST STANDARD; PRT; 245 AA. AC P38987; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 21-MAR-2006, entry version 45. DE Protein TEM1. GN Name=TEM1; OrderedLocusNames=YML064C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95021277; PubMed=7935462; RA Shirayama M., Matsui Y., Toh-e A.; RT "The yeast TEM1 gene, which encodes a GTP-binding protein, is involved RT in termination of M phase."; RL Mol. Cell. Biol. 14:7476-7482(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c / AB972; RX MEDLINE=97313268; 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., RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome RT XIII."; RL Nature 387:90-93(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c; RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E., RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E., RA LaBaer J.; RT "Creation of the YFLEX clone resource: cloning of Saccharomyces RT cerevisiae ORFs in the Gateway recombinational cloning system."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., 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. CC May play a role in triggering the degradation of G2 cyclin to CC inactivate M-phase promoting factor at the termination of mitosis. CC Acts upstream of CDC15 kinase and may be required to activate the CC CDC15 protein kinase pathway. CC -!- INTERACTION: CC P14904:APE1; NbExp=1; IntAct=EBI-19113, EBI-2571; CC Q06410:ATG17; NbExp=1; IntAct=EBI-19113, EBI-30856; CC P00812:CAR1; NbExp=1; IntAct=EBI-19113, EBI-2856; CC P38122:ECM31; NbExp=1; IntAct=EBI-19113, EBI-12901; CC P09201:FBP1; NbExp=1; IntAct=EBI-19113, EBI-6744; CC P05373:HEM2; NbExp=1; IntAct=EBI-19113, EBI-8239; CC P39979:HPA3; NbExp=1; IntAct=EBI-19113, EBI-22400; CC P38910:HSP10; NbExp=1; IntAct=EBI-19113, EBI-4553; CC P15992:HSP26; NbExp=1; IntAct=EBI-19113, EBI-8555; CC Q12134:HUA2; NbExp=1; IntAct=EBI-19113, EBI-37262; CC P36010:NDK1; NbExp=1; IntAct=EBI-19113, EBI-11968; CC P53081:NIF3; NbExp=1; IntAct=EBI-19113, EBI-12063; CC Q06178:NMA1; NbExp=1; IntAct=EBI-19113, EBI-11803; CC P17423:THR1; NbExp=1; IntAct=EBI-19113, EBI-9685; CC P32861:UGP1; NbExp=1; IntAct=EBI-19113, EBI-19987; CC P38276:YBR137W; NbExp=1; IntAct=EBI-19113, EBI-21630; CC P38821:YHR113W; NbExp=1; IntAct=EBI-19113, EBI-6008; CC P53633:YIP3; NbExp=1; IntAct=EBI-19113, EBI-25301; CC P39534:YJL199C; NbExp=1; IntAct=EBI-19113, EBI-26211; CC P40892:YJL218W; NbExp=1; IntAct=EBI-19113, EBI-26263; CC -!- MISCELLANEOUS: Present with 573 molecules/cell. 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; D38172; BAA07371.1; -; Genomic_DNA. DR EMBL; Z38114; CAA86257.1; -; Genomic_DNA. DR EMBL; AY557980; AAS56306.1; -; Genomic_DNA. DR PIR; S48334; S48334. DR IntAct; P38987; -. DR GermOnline; 142595; -. DR Ensembl; YML064C; Saccharomyces cerevisiae. DR GenomeReviews; Z71257_GR; YML064C. DR SGD; S000004529; TEM1. DR BioCyc; SCER-S28-01:SCER-S28-01-004432-MONOMER; -. DR LinkHub; P38987; -. DR GO; GO:0005816; C:spindle pole body; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0000087; P:M phase of mitotic cell cycle; IMP. DR GO; GO:0007165; P:signal transduction; NAS. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP_bd. DR PRINTS; PR00449; RASTRNSFRMNG. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW Cell cycle; Cell division; Complete proteome; GTP-binding; Mitosis; KW Nucleotide-binding. FT CHAIN 1 245 Protein TEM1. FT /FTId=PRO_0000122466. FT NP_BIND 27 34 GTP (By similarity). FT NP_BIND 75 79 GTP (By similarity). FT NP_BIND 132 135 GTP (By similarity). 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 //