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AMN1_YEAST
ID   AMN1_YEAST              Reviewed;         549 AA.
AC   P38285; D6VQF3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Antagonist of mitotic exit network protein 1;
DE   AltName: Full=Chromosome stability protein 13;
DE   AltName: Full=Increased copper-sensitivity protein 4;
GN   Name=AMN1; Synonyms=CST13, ICS4; OrderedLocusNames=YBR158W;
GN   ORFNames=YBR1208;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=10628851; DOI=10.1007/pl00013817;
RA   Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA   Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G., Kramer W.,
RA   Klein S., Koetter P., Kricke J., Launhardt H., Mannhaupt G., Maierl A.,
RA   Meyer P., Mewes W., Munder T., Niedenthal R.K., Ramezani Rad M.,
RA   Roehmer A., Roemer A., Rose M., Schaefer B., Siegler M.-L., Vetter J.,
RA   Wilhelm N., Wolf K., Zimmermann F.K., Zollner A., Hinnen A.;
RT   "Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by
RT   a systematic approach.";
RL   Mol. Gen. Genet. 262:683-702(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=10454593; DOI=10.1093/nar/27.15.3001;
RA   Ouspenski I.I., Elledge S.J., Brinkley B.R.;
RT   "New yeast genes important for chromosome integrity and segregation
RT   identified by dosage effects on genome stability.";
RL   Nucleic Acids Res. 27:3001-3008(1999).
RN   [6]
RP   INDUCTION.
RX   PubMed=11309124; DOI=10.1046/j.1365-2958.2001.02388.x;
RA   Doolin M.-T., Johnson A.L., Johnston L.H., Butler G.;
RT   "Overlapping and distinct roles of the duplicated yeast transcription
RT   factors Ace2p and Swi5p.";
RL   Mol. Microbiol. 40:422-432(2001).
RN   [7]
RP   FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TEM1.
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [9]
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   [10]
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   [11]
RP   FUNCTION.
RX   PubMed=12897782; DOI=10.1038/ng1222;
RA   Yvert G., Brem R.B., Whittle J., Akey J.M., Foss E., Smith E.N.,
RA   Mackelprang R., Kruglyak L.;
RT   "Trans-acting regulatory variation in Saccharomyces cerevisiae and the role
RT   of transcription factors.";
RL   Nat. Genet. 35:57-64(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=16079183; DOI=10.1091/mbc.e04-12-1109;
RA   Wang Y., Ng T.-Y.;
RT   "Phosphatase 2A negatively regulates mitotic exit in Saccharomyces
RT   cerevisiae.";
RL   Mol. Biol. Cell 17:80-89(2006).
CC   -!- FUNCTION: Negative regulator of the mitotic exit network (MEN),
CC       required for multiple cell cycle checkpoints. Acts in the daughter cell
CC       to inhibit the mitotic exit pathway once MEN has executed its function.
CC       Through its binding ability to TEM1, interferes with the TEM1-CDC5
CC       association, required for CDC5 kinase activation and MEN activation.
CC       Required for daughter cell separation and chromosome stability.
CC       Involved in copper sensitivity. {ECO:0000269|PubMed:10454593,
CC       ECO:0000269|PubMed:10628851, ECO:0000269|PubMed:12628189,
CC       ECO:0000269|PubMed:12897782, ECO:0000269|PubMed:16079183}.
CC   -!- SUBUNIT: Interacts with TEM1. {ECO:0000269|PubMed:12628189}.
CC   -!- INTERACTION:
CC       P38285; P38987: TEM1; NbExp=6; IntAct=EBI-20853, EBI-19113;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12628189}. Nucleus
CC       {ECO:0000269|PubMed:12628189, ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Expressed in daughter cells after execution of mitotic exit.
CC       Expression is controlled by the ACE2 and SWI5 transcription factors.
CC       {ECO:0000269|PubMed:11309124, ECO:0000269|PubMed:12628189}.
CC   -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the AMN1 family. {ECO:0000305}.
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DR   EMBL; Z36027; CAA85117.1; -; Genomic_DNA.
DR   EMBL; AY723760; AAU09677.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07273.1; -; Genomic_DNA.
DR   PIR; S46029; S46029.
DR   RefSeq; NP_009716.1; NM_001178506.1.
DR   AlphaFoldDB; P38285; -.
DR   SMR; P38285; -.
DR   BioGRID; 32857; 74.
DR   DIP; DIP-4930N; -.
DR   IntAct; P38285; 8.
DR   STRING; 4932.YBR158W; -.
DR   iPTMnet; P38285; -.
DR   MaxQB; P38285; -.
DR   PaxDb; P38285; -.
DR   PRIDE; P38285; -.
DR   EnsemblFungi; YBR158W_mRNA; YBR158W; YBR158W.
DR   GeneID; 852455; -.
DR   KEGG; sce:YBR158W; -.
DR   SGD; S000000362; AMN1.
DR   VEuPathDB; FungiDB:YBR158W; -.
DR   eggNOG; KOG1947; Eukaryota.
DR   HOGENOM; CLU_031725_1_0_1; -.
DR   InParanoid; P38285; -.
DR   OMA; NCLLVNK; -.
DR   BioCyc; YEAST:G3O-29108-MON; -.
DR   PRO; PR:P38285; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38285; protein.
DR   GO; GO:0005933; C:cellular bud; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; IPI:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR   GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IMP:SGD.
DR   GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR   GO; GO:2001042; P:negative regulation of septum digestion after cytokinesis; IMP:SGD.
DR   GO; GO:0032984; P:protein-containing complex disassembly; IMP:SGD.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   SMART; SM00367; LRR_CC; 5.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..549
FT                   /note="Antagonist of mitotic exit network protein 1"
FT                   /id="PRO_0000202500"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  62686 MW;  EA1EC675D6A84F20 CRC64;
     MKLERVSSNG SFKRGRDIQS LESPCTRPLK KMSPSPSFTS LKMEKPFKDI VRKYGGHLHQ
     SSYNPGSSKV ELVRPDLSLK TDQSFLQSSV QTTPNKKSCN EYLSTPEATP LKNTATENAW
     ATSRVVSASS LSIVTPTEIK NILVDEFSEL KLGQPLTAQH QRSHAVFEIP EIVENIIKMI
     VSLESANIPK ERPCLRRNPQ SYEHSLLMYK DEERAKKAWS AAQQLRDPPL VGHKEKKQGA
     LFSCMMVNRL WLNVTRPFLF KSLHFKSVHN FKEFLRTSQE TTQVMRPSHF ILHKLHQVTQ
     PDIERLSRME CQNLKWLEFY VCPRITPPLS WFDNLHKLEK LIIPGNKNID DNFLLRLSQS
     IPNLKHLVLR ACDNVSDSGV VCIALNCPKL KTFNIGRHRR GNLITSVSLV ALGKYTQVET
     VGFAGCDVDD AGIWEFARLN GKNVERLSLN SCRLLTDYSL PILFALNSFP NLAVLEIRNL
     DKITDVRHFV KYNLWKKSLD APILIEACER ITKLIDQEEN RVKRINSLVA LKDMTAWVNA
     DDEIENNVD
 
 
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