SGO1_MOUSE
ID SGO1_MOUSE Reviewed; 517 AA.
AC Q9CXH7; Q3U4K4; Q588H1; Q8BKW2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Shugoshin 1 {ECO:0000250|UniProtKB:Q5FBB7};
DE AltName: Full=Shugoshin-like 1;
GN Name=Sgo1 {ECO:0000250|UniProtKB:Q5FBB7}; Synonyms=Sgol1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=15737064; DOI=10.1371/journal.pbio.0030086;
RA McGuinness B.E., Hirota T., Kudo N.R., Peters J.-M., Nasmyth K.;
RT "Shugoshin prevents dissociation of cohesin from centromeres during mitosis
RT in vertebrate cells.";
RL PLoS Biol. 3:433-449(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=18331714; DOI=10.1016/j.devcel.2007.12.007;
RA Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z., Dai W.;
RT "sSgo1, a major splice variant of Sgo1, functions in centriole cohesion
RT where it is regulated by Plk1.";
RL Dev. Cell 14:331-341(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18084284; DOI=10.1038/ncb1667;
RA Lee J., Kitajima T.S., Tanno Y., Yoshida K., Morita T., Miyano T.,
RA Miyake M., Watanabe Y.;
RT "Unified mode of centromeric protection by shugoshin in mammalian oocytes
RT and somatic cells.";
RL Nat. Cell Biol. 10:42-52(2008).
CC -!- FUNCTION: Plays a central role in chromosome cohesion during mitosis by
CC preventing premature dissociation of cohesin complex from centromeres
CC after prophase, when most of cohesin complex dissociates from
CC chromosomes arms. May act by preventing phosphorylation of the STAG2
CC subunit of cohesin complex at the centromere, ensuring cohesin
CC persistence at centromere until cohesin cleavage by ESPL1/separase at
CC anaphase. Essential for proper chromosome segregation during mitosis
CC and this function requires interaction with PPP2R1A. Its phosphorylated
CC form is necessary for chromosome congression and for the proper
CC attachment of spindle microtubule to the kinetochore. Necessary for
CC kinetochore localization of PLK1 and CENPF. May play a role in the
CC tension sensing mechanism of the spindle-assembly checkpoint by
CC regulating PLK1 kinetochore affinity. Involved in centromeric
CC enrichment of AUKRB in prometaphase. {ECO:0000250|UniProtKB:Q5FBB7,
CC ECO:0000269|PubMed:18084284, ECO:0000269|PubMed:18331714}.
CC -!- SUBUNIT: Interacts with PPP2CA (or PPP2CB), PPP2R1B, PPP2R5A, PPP2R5B,
CC PPP2R5C, PPP2R5D, PPP2R5E, SET, LRRC59, RBM10 (or RBM5), RPL10A, RPL28,
CC RPL7, RPL7A and RPLP1. Interaction with protein phosphatase 2A occurs
CC most probably through direct binding to the regulatory B56 subunits:
CC PPP2R1B, PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E. Interacts with
CC PPP2R1A and NEK2. Interacts with CDCA8 (By similarity).
CC {ECO:0000250|UniProtKB:Q5FBB7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FBB7}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q5FBB7}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q5FBB7}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5FBB7}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q5FBB7}. Note=Localizes to the inner centromere
CC throughout prophase until metaphase and disappears at anaphase.
CC Centromeric localization requires the presence of BUB1 and the
CC interaction with PPP2R1A. Colocalizes with NEK2 at the kinetochore.
CC Colocalizes with and SS18L1 at the kinetochore. Phosphorylation by
CC AUKRB and the presence of BUB1 are required for localization to the
CC kinetochore. Isoform 1 primarily localizes to kinetochores during G2
CC phase and mitotic prophase, metaphase, and anaphase and does not appear
CC to be associated with kinetochores during late mitosis. Isoform 3 is
CC found at the centrosome in interphase and at spindle poles in mitosis
CC and its spindle pole localization is PLK1 dependent. Isoform 3 does not
CC localize to kinetochores during any stages of the cell cycle.
CC {ECO:0000250|UniProtKB:Q5FBB7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=1A;
CC IsoId=Q9CXH7-1; Sequence=Displayed;
CC Name=2; Synonyms=1B;
CC IsoId=Q9CXH7-2; Sequence=VSP_016796, VSP_016797;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in proliferating cells.
CC Moderately expressed in the oocytes. {ECO:0000269|PubMed:18084284}.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation by NEK2 is essential for chromosome congression in
CC mitosis and for the proper attachment of spindle microtubule to the
CC kinetochore. Phosphorylated by PLK1 and AUKRB (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Shugoshin is Japanese for guardian spirit (as it is
CC known to be a protector of centromeric cohesin).
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR EMBL; AB193067; BAD95540.1; -; mRNA.
DR EMBL; AB193068; BAD95541.1; -; mRNA.
DR EMBL; AK014357; BAB29295.1; -; mRNA.
DR EMBL; AK049517; BAC33789.1; -; mRNA.
DR EMBL; AK154188; BAE32427.1; -; mRNA.
DR EMBL; BC089014; AAH89014.1; -; mRNA.
DR CCDS; CCDS28881.1; -. [Q9CXH7-1]
DR RefSeq; NP_082508.1; NM_028232.2. [Q9CXH7-1]
DR RefSeq; XP_011244944.1; XM_011246642.2. [Q9CXH7-1]
DR RefSeq; XP_017173147.1; XM_017317658.1. [Q9CXH7-2]
DR AlphaFoldDB; Q9CXH7; -.
DR SMR; Q9CXH7; -.
DR BioGRID; 215364; 28.
DR IntAct; Q9CXH7; 15.
DR STRING; 10090.ENSMUSP00000024736; -.
DR iPTMnet; Q9CXH7; -.
DR PhosphoSitePlus; Q9CXH7; -.
DR EPD; Q9CXH7; -.
DR MaxQB; Q9CXH7; -.
DR PaxDb; Q9CXH7; -.
DR PeptideAtlas; Q9CXH7; -.
DR PRIDE; Q9CXH7; -.
DR ProteomicsDB; 261339; -. [Q9CXH7-1]
DR ProteomicsDB; 261340; -. [Q9CXH7-2]
DR Antibodypedia; 27089; 246 antibodies from 27 providers.
DR DNASU; 72415; -.
DR Ensembl; ENSMUST00000024736; ENSMUSP00000024736; ENSMUSG00000023940. [Q9CXH7-1]
DR GeneID; 72415; -.
DR KEGG; mmu:72415; -.
DR UCSC; uc008czq.2; mouse. [Q9CXH7-1]
DR UCSC; uc008czr.2; mouse. [Q9CXH7-2]
DR CTD; 151648; -.
DR MGI; MGI:1919665; Sgo1.
DR VEuPathDB; HostDB:ENSMUSG00000023940; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000154107; -.
DR HOGENOM; CLU_022813_0_0_1; -.
DR InParanoid; Q9CXH7; -.
DR OMA; CQWNKDQ; -.
DR OrthoDB; 1414582at2759; -.
DR PhylomeDB; Q9CXH7; -.
DR TreeFam; TF334213; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 72415; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Sgo1; mouse.
DR PRO; PR:Q9CXH7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CXH7; protein.
DR Bgee; ENSMUSG00000023940; Expressed in yolk sac and 117 other tissues.
DR Genevisible; Q9CXH7; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; ISO:MGI.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; ISO:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR InterPro; IPR028321; Sgo1.
DR InterPro; IPR038889; Shugoshin.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR PANTHER; PTHR21577; PTHR21577; 1.
DR PANTHER; PTHR21577:SF3; PTHR21577:SF3; 1.
DR Pfam; PF07557; Shugoshin_C; 1.
DR Pfam; PF07558; Shugoshin_N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..517
FT /note="Shugoshin 1"
FT /id="PRO_0000055437"
FT REGION 1..176
FT /note="Necessary for interaction with PPP2CA and PPP2R1A"
FT /evidence="ECO:0000250"
FT REGION 107..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..89
FT /evidence="ECO:0000255"
FT COILED 268..291
FT /evidence="ECO:0000255"
FT MOTIF 441..445
FT /note="PXVXL/I motif"
FT /evidence="ECO:0000250|UniProtKB:Q5FBB7"
FT MOTIF 447..455
FT /note="D-box"
FT /evidence="ECO:0000250"
FT COMPBIAS 108..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..298
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FBB7"
FT MOD_RES 497
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:Q5FBB7"
FT VAR_SEQ 171..172
FT /note="GK -> ES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15737064"
FT /id="VSP_016796"
FT VAR_SEQ 173..517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15737064"
FT /id="VSP_016797"
FT CONFLICT 134
FT /note="S -> P (in Ref. 2; BAE32427)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="S -> T (in Ref. 2; BAE32427)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="A -> S (in Ref. 2; BAE32427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 58966 MW; 75E84B2C47833BCA CRC64;
MAKERCQKRS FQDTLEDIKN RMKEKRNKNL AGIGKRKSFI VAPGQVPTNT ATLLRYYQDN
NRLLVLALEN EKSKVREAQD VILQLRKECY YLTCQLYALK EKLTSRQSEE TTQNWKGRPS
DVVSSIDNTT RDLSGKSLQQ IAVEETDCPY QTTEPSPAVT PETQGCDFDS GKVESTDEVL
PRTISIRRHL RKDFSNISHS TTLEDCKASP RVAQSLEVKG SRCREVTVTL HRLENVCLWN
KDQISLCSRL INPAKITETE VILSSKPEQI ESKHKRARKR RAEQRRTKQR CKSKSSLRSK
GNKNKDKQGL PPTTLDGGIG SCDAYDFNLK GTVHPTPFRQ KMNNGCNKET DSSNSEVSDL
ECSTSEDESD DLYLPPSKRL RDYRESERAV TRPRSKRGLQ YPDGKERKEV LPSTAPTGIP
PETQESPRCS LKDVTNILQC PRVKIRKPSL PPKRREDSPA VALTKRRCST IKSYKEPTLA
SKLRRGDPFT DLCFLNSPIF KQKRGMRCPK RRTKQTQ
