SGO1_YEAST
ID SGO1_YEAST Reviewed; 590 AA.
AC Q08490; D6W2D6; O00031;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Shugoshin;
GN Name=SGO1; OrderedLocusNames=YOR073W; ORFNames=YOR29-24;
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=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15062096; DOI=10.1016/j.cub.2004.03.001;
RA Katis V.L., Galova M., Rabitsch K.P., Gregan J., Nasmyth K.;
RT "Maintenance of cohesin at centromeres after meiosis I in budding yeast
RT requires a kinetochore-associated protein related to MEI-S332.";
RL Curr. Biol. 14:560-572(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROBABLE
RP UBIQUITINATION.
RX PubMed=14752166; DOI=10.1126/science.1094220;
RA Marston A.L., Tham W.-H., Shah H., Amon A.;
RT "A genome-wide screen identifies genes required for centromeric cohesion.";
RL Science 303:1367-1370(2004).
RN [7]
RP DEGRADATION.
RX PubMed=15797380; DOI=10.1016/j.cell.2005.01.017;
RA Penkner A.M., Prinz S., Ferscha S., Klein F.;
RT "Mnd2, an essential antagonist of the anaphase-promoting complex during
RT meiotic prophase.";
RL Cell 120:789-801(2005).
RN [8]
RP FUNCTION, PROBABLE UBIQUITINATION, AND MUTAGENESIS OF THR-379 AND PRO-390.
RX PubMed=15637284; DOI=10.1126/science.1101366;
RA Indjeian V.B., Stern B.M., Murray A.W.;
RT "The centromeric protein Sgo1 is required to sense lack of tension on
RT mitotic chromosomes.";
RL Science 307:130-133(2005).
CC -!- FUNCTION: Plays a central role in chromosome cohesion during mitosis
CC and meiosis divisions by preventing premature dissociation of cohesin
CC complex from centromeres after prophase, when most of cohesin complex
CC dissociates from chromosomes arms. Probably act by protecting REC8 and
CC RAD21 from separase degradation during anaphase. Also acts as a spindle
CC checkpoint component required for sensing tension between sister
CC chromatids during mitosis, its degradation when they separate
CC preventing cell cycle arrest and chromosome loss in anaphase, a time
CC when sister chromatids are no longer under tension.
CC {ECO:0000269|PubMed:14752166, ECO:0000269|PubMed:15062096,
CC ECO:0000269|PubMed:15637284}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:14752166, ECO:0000269|PubMed:15062096}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:15062096}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15062096}. Note=Localizes to the centromere during S
CC and M phases, dissociates at the onset of anaphase. Colocalizes with
CC kinetochores. Associates with the spindle pole.
CC {ECO:0000269|PubMed:15062096}.
CC -!- DEVELOPMENTAL STAGE: Appears in S phase cells and remains present
CC during mitosis until metaphase. Degraded at the onset of anaphase.
CC During meiosis it is present until anaphase II and is then degraded.
CC Not present in G1 cells. {ECO:0000269|PubMed:14752166}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset
CC of anaphase, conducting to its degradation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR EMBL; Z74981; CAA99266.1; -; Genomic_DNA.
DR EMBL; Z70678; CAA94558.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10852.1; -; Genomic_DNA.
DR PIR; S66956; S66956.
DR RefSeq; NP_014716.1; NM_001183492.1.
DR AlphaFoldDB; Q08490; -.
DR SMR; Q08490; -.
DR BioGRID; 34472; 132.
DR DIP; DIP-4161N; -.
DR IntAct; Q08490; 1.
DR STRING; 4932.YOR073W; -.
DR iPTMnet; Q08490; -.
DR PaxDb; Q08490; -.
DR PRIDE; Q08490; -.
DR EnsemblFungi; YOR073W_mRNA; YOR073W; YOR073W.
DR GeneID; 854240; -.
DR KEGG; sce:YOR073W; -.
DR SGD; S000005599; SGO1.
DR VEuPathDB; FungiDB:YOR073W; -.
DR eggNOG; ENOG502QSMK; Eukaryota.
DR HOGENOM; CLU_019322_0_0_1; -.
DR InParanoid; Q08490; -.
DR OMA; SKIKHSM; -.
DR BioCyc; YEAST:G3O-33611-MON; -.
DR PRO; PR:Q08490; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08490; protein.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034508; P:centromere complex assembly; IMP:SGD.
DR GO; GO:0045184; P:establishment of protein localization; IDA:SGD.
DR GO; GO:0070199; P:establishment of protein localization to chromosome; IMP:SGD.
DR GO; GO:0051383; P:kinetochore organization; IDA:SGD.
DR GO; GO:0034090; P:maintenance of meiotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0051757; P:meiotic sister chromatid separation; IMP:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0034096; P:positive regulation of maintenance of meiotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR Pfam; PF07557; Shugoshin_C; 1.
DR Pfam; PF07558; Shugoshin_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Meiosis; Mitosis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..590
FT /note="Shugoshin"
FT /id="PRO_0000055450"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..86
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 379
FT /note="T->I: In sgo1-100; induces a lack of response when
FT chromosomes that are not under tension."
FT /evidence="ECO:0000269|PubMed:15637284"
FT MUTAGEN 390
FT /note="P->H: In sgo1-700; induces a lack of response when
FT chromosomes that are not under tension."
FT /evidence="ECO:0000269|PubMed:15637284"
SQ SEQUENCE 590 AA; 66706 MW; EBC61416CD8E4263 CRC64;
MPKRKIAPNK ESSRRTVSHD DLTPQIQEFQ NLMDLESQKV ENIRQSYSRQ NSLLAKDNSI
LKIKVNSLEK KISQLVQENV TLRSKTSISE AIYRERLSNQ LQVIENGIIQ RFDEIFYMFE
NVRKNENLPS SSLRTMLKRT SSRSRSCSLS SPTYSKSYTR LSNHENNLSH ESSFNKDDGP
DLEPKAKKRK SSRRQSMFVS TSLEPEDETG ENEPMMENSS VEVPAESHES AQVEETIDAL
NPEEENSDSV SNFTNSIIEY SIPEENPTEP EHSSSKLEIF NDSTNMLSTV PSNPLPLPLP
GPSATLPTTT SDASTVYPSS SSSTNSHPKT KIKHSMKPPR IELKKKVIDE VMPVSNMSSN
SEISFTRTRR TRGKAVDYTL PSLRAKMRRP SEKLVDATTV IDIHDLQVSK RNRETSHKRK
SLSQDSIPDE PQLREVVVSK DYGTPKGKKT EDEIHEDTAH LMTTSNNNSN NKNEKKLTSN
NSPKKSSPLL DITNKSENKK KSTRTKKLFK NAIVNNLSDE NSTTRPSKSS KGTSNNNNNY
NNFDNNNSNI NNVNNKSVSF RLNEDDLAVF DLFGNGKAVK HQPKTYRTKK
