SGO2_SCHPO
ID SGO2_SCHPO Reviewed; 647 AA.
AC O13734; Q9UU02;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Shugoshin-2;
GN Name=sgo2; ORFNames=SPAC15A10.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 315-492, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14730319; DOI=10.1038/nature02312;
RA Kitajima T.S., Kawashima S.A., Watanabe Y.;
RT "The conserved kinetochore protein shugoshin protects centromeric cohesion
RT during meiosis.";
RL Nature 427:510-517(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14972679; DOI=10.1016/j.cub.2004.01.051;
RA Rabitsch K.P., Gregan J., Schleiffer A., Javerzat J.-P., Eisenhaber F.,
RA Nasmyth K.;
RT "Two fission yeast homologs of Drosophila Mei-S332 are required for
RT chromosome segregation during meiosis I and II.";
RL Curr. Biol. 14:287-301(2004).
RN [5]
RP FUNCTION.
RX PubMed=16229998; DOI=10.1016/j.ceb.2005.10.003;
RA Watanabe Y.;
RT "Shugoshin: guardian spirit at the centromere.";
RL Curr. Opin. Cell Biol. 17:590-595(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-240; THR-292; SER-332
RP AND SER-335, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in chromosome cohesion during mitosis and meiosis by
CC preventing premature dissociation of cohesin complex from centromeres
CC after prophase, when most of cohesin complex dissociates from
CC chromosomes arms. Required for faithful mitotic chromosome segregation
CC and proper kinetochore orientation during meiosis I. In contrast to
CC sgo1, it is dispensable for centromeric protection of rec8 during
CC meiosis I as well as protection of rad21 during mitosis. Required to
CC sense the lack of tension at centromeres during mitosis.
CC {ECO:0000269|PubMed:14730319, ECO:0000269|PubMed:14972679,
CC ECO:0000269|PubMed:16229998}.
CC -!- INTERACTION:
CC O13734; O14064: bir1; NbExp=3; IntAct=EBI-15872428, EBI-15872259;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:14730319, ECO:0000269|PubMed:14972679}.
CC Note=Localizes to the centromere. Bub1 is required for centromeric
CC localization (PubMed:14730319). At the onset of anaphase I, Sgo1
CC decreases markedly (PubMed:14730319). {ECO:0000269|PubMed:14730319}.
CC -!- DEVELOPMENTAL STAGE: Present throughout the mitotic and meiotic cell
CC cycle. {ECO:0000269|PubMed:14730319}.
CC -!- MISCELLANEOUS: 'Shugoshin' means 'guardian spirit' in Japanese.
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR EMBL; CU329670; CAB10111.1; -; Genomic_DNA.
DR EMBL; AB027892; BAA87196.1; -; Genomic_DNA.
DR PIR; T37714; T37714.
DR RefSeq; NP_594301.1; NM_001019724.2.
DR AlphaFoldDB; O13734; -.
DR SMR; O13734; -.
DR BioGRID; 279237; 27.
DR DIP; DIP-59226N; -.
DR IntAct; O13734; 1.
DR STRING; 4896.SPAC15A10.15.1; -.
DR iPTMnet; O13734; -.
DR MaxQB; O13734; -.
DR PaxDb; O13734; -.
DR PRIDE; O13734; -.
DR EnsemblFungi; SPAC15A10.15.1; SPAC15A10.15.1:pep; SPAC15A10.15.
DR GeneID; 2542788; -.
DR KEGG; spo:SPAC15A10.15; -.
DR PomBase; SPAC15A10.15; sgo2.
DR VEuPathDB; FungiDB:SPAC15A10.15; -.
DR HOGENOM; CLU_455727_0_0_1; -.
DR InParanoid; O13734; -.
DR OMA; TKMRRDF; -.
DR PhylomeDB; O13734; -.
DR PRO; PR:O13734; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0140463; F:chromatin-protein adaptor; IPI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:PomBase.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:1903467; P:negative regulation of mitotic DNA replication initiation; IMP:CACAO.
DR InterPro; IPR038889; Shugoshin.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR PANTHER; PTHR21577; PTHR21577; 1.
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; Meiosis; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..647
FT /note="Shugoshin-2"
FT /id="PRO_0000055452"
FT REGION 171..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..87
FT /evidence="ECO:0000255"
FT COILED 125..145
FT /evidence="ECO:0000255"
FT COMPBIAS 197..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 647 AA; 72485 MW; 23E909737AFA4B2B CRC64;
MSKASLSPNV EDLKKKQIRQ YKEIIRISKA QSIRIKELQL ENERLLSENI DLRTTAINLE
EQLETVQNEN EENKTKLAAL LNRFHEETDN FLSKLSLCQQ EIQDTFKPVE ANLAYDVDTD
SEDLDEESVV KDTEEIIEQA QHDVSLRNLS GIEDENIIDD GETAINEQKK REANVFSDTQ
SAPQLKSGKA LPADFENPYN LSNSKPVNNN NEDRVEAVTS ENKSIDSAPQ EKNHEYEIVS
PKSLSNKINN QAAAQRRTEE DNANGVAQEE NEGSQEAHFH SRIQSDTVIQ STPTKRKWDV
DIQNKQINLA SAATNVTGYV SETDSRPNRA NSLDSAVLLV QSSNKSNRNG HHISDPNLNS
SISLKFAPED TAHNSLTSQE NVGPQVTTTS LSNMTVAESP RTDTPREING LVDSSVTNGN
EKFSVEIMND SNKIGLNPKS FTDEEREILT LFRNPPMRLS SEPPSSNGFS IAHPNNSPLR
PPSLQGILNA EDRPYEIEPS RSSFATNDTG SYNNLELLSS VTNLKSPNEN DRVTKTQSRR
ETKVKRRRKA RIQETSEEST VVNEPNEKPD GRSRRERKKV NYALPGLRTK LRRNFDLPSD
HVKAKKTRRA PKNSENDSAT KTETANITSE APTTSEVTLE NSETLNL
