SGO2_MOUSE
ID SGO2_MOUSE Reviewed; 1164 AA.
AC Q7TSY8; Q811I4; Q8C9C4; Q8CGJ4; Q9CS55;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Shugoshin 2 {ECO:0000250|UniProtKB:Q562F6};
DE AltName: Full=Shugoshin-2;
DE AltName: Full=Shugoshin-like 2;
GN Name=Sgo2 {ECO:0000250|UniProtKB:Q562F6};
GN Synonyms=Sgol2, Sgol2a {ECO:0000312|MGI:MGI:1098767};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-593.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 PROTEIN SEQUENCE OF 95-103; 259-269; 579-588 AND 1056-1065, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=17205076; DOI=10.1038/sj.embor.7400877;
RA Gomez R., Valdeolmillos A., Parra M.T., Viera A., Carreiro C., Roncal F.,
RA Rufas J.S., Barbero J.L., Suja J.A.;
RT "Mammalian SGO2 appears at the inner centromere domain and redistributes
RT depending on tension across centromeres during meiosis II and mitosis.";
RL EMBO Rep. 8:173-180(2007).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18765791; DOI=10.1101/gad.475308;
RA Llano E., Gomez R., Gutierrez-Caballero C., Herran Y., Sanchez-Martin M.,
RA Vazquez-Quinones L., Hernandez T., de Alava E., Cuadrado A., Barbero J.L.,
RA Suja J.A., Pendas A.M.;
RT "Shugoshin-2 is essential for the completion of meiosis but not for mitotic
RT cell division in mice.";
RL Genes Dev. 22:2400-2413(2008).
RN [6]
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: Cooperates with PPP2CA to protect centromeric cohesin from
CC separase-mediated cleavage in oocytes specifically during meiosis I.
CC Has a crucial role in protecting REC8 at centromeres from cleavage by
CC separase. During meiosis, protects centromeric cohesion complexes until
CC metaphase II/anaphase II transition, preventing premature release of
CC meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is
CC thus essential for an accurate gametogenesis. May act by targeting
CC PPP2CA to centromeres, thus leading to cohesin dephosphorylation.
CC Essential for recruiting KIF2C to the inner centromere and for
CC correcting defective kinetochore attachments. Involved in centromeric
CC enrichment of AUKRB in prometaphase. {ECO:0000250|UniProtKB:Q562F6,
CC ECO:0000269|PubMed:18084284, ECO:0000269|PubMed:18765791}.
CC -!- SUBUNIT: Interacts with PPP2CA. Part of an astrin (SPAG5)-kinastrin
CC (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2.
CC Interacts with CDCA8 (By similarity). {ECO:0000250|UniProtKB:Q562F6}.
CC -!- INTERACTION:
CC Q7TSY8; Q9Z1B5: Mad2l1; NbExp=3; IntAct=EBI-2552468, EBI-2552918;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q562F6}.
CC Chromosome, centromere {ECO:0000269|PubMed:17205076,
CC ECO:0000269|PubMed:18084284}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:17205076}. Note=Centromeric localization requires
CC the presence of BUB1 and AUKRB (By similarity). During meiosis I,
CC accumulates at centromeres during diplotene, and colocalizes
CC differentially with the cohesin subunits RAD21 and REC8 at metaphase I
CC centromeres (PubMed:17205076) (PubMed:18084284). SGO2 and RAD21 change
CC their relative distributions during telophase I when sister-kinetochore
CC association is lost (PubMed:17205076). During meiosis II, it shows a
CC striking tension-dependent redistribution within centromeres throughout
CC chromosome congression during prometaphase II, as it does during
CC mitosis (PubMed:17205076). {ECO:0000250|UniProtKB:Q562F6,
CC ECO:0000269|PubMed:17205076, ECO:0000269|PubMed:18084284}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in proliferating cells.
CC Highly expressed in the testis and oocytes.
CC {ECO:0000269|PubMed:18084284}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally and survive to adulthood
CC without any apparent alteration. However, both males and females are
CC infertile. This defect appears cytologically as complete loss of
CC centromere cohesion at metaphase II, leading to single chromatids, and
CC physiologically as formation of aneuploid gametes that gave rise to
CC infertility. {ECO:0000269|PubMed:18765791}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH23855.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC023855; AAH23855.1; ALT_SEQ; mRNA.
DR EMBL; BC044797; AAH44797.1; -; mRNA.
DR EMBL; BC052742; AAH52742.1; -; mRNA.
DR EMBL; AK017868; BAB30980.1; -; mRNA.
DR EMBL; AK042448; BAC31263.1; -; mRNA.
DR CCDS; CCDS35574.1; -.
DR RefSeq; NP_001171338.1; NM_001177867.1.
DR RefSeq; NP_950172.1; NM_199007.2.
DR AlphaFoldDB; Q7TSY8; -.
DR SMR; Q7TSY8; -.
DR BioGRID; 212920; 58.
DR IntAct; Q7TSY8; 59.
DR MINT; Q7TSY8; -.
DR STRING; 10090.ENSMUSP00000027202; -.
DR iPTMnet; Q7TSY8; -.
DR PhosphoSitePlus; Q7TSY8; -.
DR EPD; Q7TSY8; -.
DR MaxQB; Q7TSY8; -.
DR PaxDb; Q7TSY8; -.
DR PeptideAtlas; Q7TSY8; -.
DR PRIDE; Q7TSY8; -.
DR ProteomicsDB; 256987; -.
DR DNASU; 68549; -.
DR Ensembl; ENSMUST00000027202; ENSMUSP00000027202; ENSMUSG00000026039.
DR GeneID; 68549; -.
DR KEGG; mmu:68549; -.
DR UCSC; uc007bbk.2; mouse.
DR CTD; 68549; -.
DR MGI; MGI:1098767; Sgol2a.
DR VEuPathDB; HostDB:ENSMUSG00000026039; -.
DR eggNOG; ENOG502S9Y1; Eukaryota.
DR GeneTree; ENSGT00940000154107; -.
DR HOGENOM; CLU_264434_0_0_1; -.
DR InParanoid; Q7TSY8; -.
DR OMA; LNWNNEI; -.
DR OrthoDB; 290088at2759; -.
DR PhylomeDB; Q7TSY8; -.
DR TreeFam; TF350100; -.
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; 68549; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Sgo2a; mouse.
DR PRO; PR:Q7TSY8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q7TSY8; protein.
DR Bgee; ENSMUSG00000026039; Expressed in undifferentiated genital tubercle and 125 other tissues.
DR Genevisible; Q7TSY8; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0030892; C:mitotic cohesin complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0035875; P:maintenance of meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0010789; P:meiotic sister chromatid cohesion involved in meiosis I; IMP:MGI.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:2000711; P:positive regulation of maintenance of meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR InterPro; IPR026706; SGO2.
DR InterPro; IPR038889; Shugoshin.
DR PANTHER; PTHR21577; PTHR21577; 2.
DR PANTHER; PTHR21577:SF5; PTHR21577:SF5; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Direct protein sequencing; Kinetochore; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1164
FT /note="Shugoshin 2"
FT /id="PRO_0000055440"
FT REGION 160..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..113
FT /evidence="ECO:0000255"
FT COMPBIAS 174..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q562F6"
FT CONFLICT 78
FT /note="Q -> R (in Ref. 2; BAB30980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1164 AA; 130277 MW; 64BCDCE5738576D6 CRC64;
MEYPGIKVDT VTSGIQRRVK GRIAKTNLNV SLASKIKAKI LNNSSIFKIS LKHNNRALAR
ALSKEKENSR RITTEKMQLQ KEVEKLNFEN TFLRLKLNTL NKKLVEIESH VSNDLLTAIE
ISSLSEFHQG SFLLSATKKQ RNSKQCKPAH LPYARVLLTS ENDDDDGADD KWQTKCNNRT
ISKTSPDSTS SVSRQPSSLH QCNLKAFPPK EDNQKTCGSG HLEHTSSVDI LPNESHSDQS
PKSSLSEMKT APSPSLRREK LSHGNVTMRK KCVSSTPDIL YVTDLDHQPT SSPGSNWNNE
IHGHTNETSN NTQRNAECFL DLPSESSSEP DAKRMELVQK NTDSFHFQKT VYDAADMELT
ATDIGKIVAV SKSKKNQNKK KADCRKETFR KVKGASSDKK RESSKRECKD GSEVGAEEEA
DAARAERGAG VLDGRGDSEE PNCISSTEQP SQVNTQKKRT LQNSSDQENI QNTKRRQTYT
TDEQEETNPF SRHSVKFLQD GKFDLCQKTL HHNLSKPSRQ TFVIRKSEKD NLFPNQEDKD
TISENLEVTN EFHIDDLSIE ANENVCDHET QTMLDLKKSV SAQQNQTKIN KTKQKINRRT
KIISVMSQVY EDNDKDIHVL EKDNFPFHTQ ANKETTSGNL ESSKEFESPL LFTRDNGSLR
DCKTQNVLDL HKQIPDLYPD RNESQISKIP RQKVNRKTEV ISGVKCFSND QGVHCSEKDK
SLLLQKDKDF PGTLKDLSEF DTPAFCNKDS AKSCDYKSEM LLGLKKHDPN MQPACQDDSK
AGKKLRQKVN RKTEIISKIT QIHENDRGST HDSLNKKLCQ KVNISKIISQ MNQIYETINE
DGNGFKSSIK DCEDIKSCDF GEINSNKKEN YDPIQDPCTL VKKTKRKGSC KAGSSLAGAK
NRCGLQLTDS SQVQSVPLDS GLRHHPNEAD SGPGEQTNLP KMQKQSAGRS LGDAFSVSLG
KEGSRPAKAV SKMTPKSKKR KLPLGCSPET HGTVEITPNT DLAKAVDSQQ TEKENYLEKE
KIAKRKPDFC TKVLKPLSET CSSNIKNSSL DSMCKSSLPL SISSRKTLML EESSSLESTC
IFQVGDAAHE KITTGTRNPH HRTQKSTPGS RTSLVLVDTS SVSDTNPANP ENESEGQSSH
PMRRKRQCVP LNLTEPSLRS KMRR
