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 24-JAN-2024, entry version 149. 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}. 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; 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. 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; 10090-ENSMUSP00000024736; -. DR PeptideAtlas; Q9CXH7; -. DR ProteomicsDB; 261339; -. [Q9CXH7-1] DR ProteomicsDB; 261340; -. [Q9CXH7-2] DR Pumba; Q9CXH7; -. DR Antibodypedia; 27089; 277 antibodies from 27 providers. DR DNASU; 72415; -. DR Ensembl; ENSMUST00000024736.14; ENSMUSP00000024736.8; ENSMUSG00000023940.15. [Q9CXH7-1] DR GeneID; 72415; -. DR KEGG; mmu:72415; -. DR UCSC; uc008czq.2; mouse. [Q9CXH7-1] DR UCSC; uc008czr.2; mouse. [Q9CXH7-2] DR AGR; MGI:1919665; -. 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; 5320947at2759; -. 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 81 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 119 other cell types or tissues. 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:0045132; P:meiotic chromosome segregation; ISO:MGI. DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; ISO:MGI. DR Gene3D; 1.20.5.730; Single helix bin; 1. DR InterPro; IPR038889; Shugoshin1/2. DR InterPro; IPR011515; Shugoshin_C. DR InterPro; IPR011516; Shugoshin_N. DR PANTHER; PTHR21577; SHUGOSHIN; 1. DR PANTHER; PTHR21577:SF3; SHUGOSHIN 1-RELATED; 1. DR Pfam; PF07557; Shugoshin_C; 1. DR Pfam; PF07558; Shugoshin_N; 1. DR Genevisible; Q9CXH7; MM. 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 //