SGO1_HUMAN
ID SGO1_HUMAN Reviewed; 561 AA.
AC Q5FBB7; Q588H5; Q5FBB4; Q5FBB5; Q5FBB6; Q5FBB8; Q8N579; Q8WVL0; Q9BVA8;
AC Q9H275;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Shugoshin 1 {ECO:0000312|HGNC:HGNC:25088};
DE AltName: Full=Serologically defined breast cancer antigen NY-BR-85;
DE AltName: Full=Shugoshin-like 1;
GN Name=SGO1 {ECO:0000312|HGNC:HGNC:25088}; Synonyms=SGOL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), FUNCTION, AND
RP SUBCELLULAR LOCATION.
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 [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RA Suzuki H., Akiyama N., Tsuji M., Saito S., Eto Y.;
RT "Human SgoL1 inhibits precocious separation of sister centromere in early
RT mitosis.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 25-561 (ISOFORM 6).
RC TISSUE=Cervix, Lung, and Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 250-527 (ISOFORM 6), AND TISSUE SPECIFICITY.
RC TISSUE=Mammary gland;
RX PubMed=12747765;
RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O.,
RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
RT "Humoral immunity to human breast cancer: antigen definition and
RT quantitative analysis of mRNA expression.";
RL Cancer Immun. 1:4-4(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15723797; DOI=10.1016/j.cub.2004.12.044;
RA Kitajima T.S., Hauf S., Ohsugi M., Yamamoto T., Watanabe Y.;
RT "Human Bub1 defines the persistent cohesion site along the mitotic
RT chromosome by affecting Shugoshin localization.";
RL Curr. Biol. 15:353-359(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15604152; DOI=10.1073/pnas.0408600102;
RA Tang Z., Sun Y., Harley S.E., Zou H., Yu H.;
RT "Human Bub1 protects centromeric sister-chromatid cohesion through
RT Shugoshin during mitosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18012-18017(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=16582621;
RA Wang X., Yang Y., Dai W.;
RT "Differential subcellular localizations of two human Sgo1 isoforms:
RT implications in regulation of sister chromatid cohesion and microtubule
RT dynamics.";
RL Cell Cycle 5:635-640(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA; PPP2R1A AND
RP PPP2R5C, AND MUTAGENESIS OF ASN-61 AND LYS-492.
RX PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010;
RA Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.;
RT "PP2A is required for centromeric localization of Sgo1 and proper
RT chromosome segregation.";
RL Dev. Cell 10:575-585(2006).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PPP2CA/PPP2CB; PPP2R1B; PPP2R5A;
RP PPP2R5B; PPP2R5C; PPP2R5D; PPP2R5E; SET; LRRC59; RBM10/RBM5; RPL10A; RPL28;
RP RPL7; RPL7A AND RPLP1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=17617734; DOI=10.4161/cc.6.13.4442;
RA Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T.,
RA Kallio M.J.;
RT "Shugoshin 1 plays a central role in kinetochore assembly and is required
RT for kinetochore targeting of Plk1.";
RL Cell Cycle 6:1579-1585(2007).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEK2, PHOSPHORYLATION AT
RP SER-14 AND SER-507, AND MUTAGENESIS OF SER-14 AND SER-507.
RX PubMed=17621308; DOI=10.1038/cr.2007.55;
RA Fu G., Ding X., Yuan K., Aikhionbare F., Yao J., Cai X., Jiang K., Yao X.;
RT "Phosphorylation of human Sgo1 by NEK2A is essential for chromosome
RT congression in mitosis.";
RL Cell Res. 17:608-618(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1, AND MUTAGENESIS OF
RP SER-73 AND THR-146.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP UBIQUITINATION, AND DOMAIN KEN BOX AND D-BOX.
RX PubMed=19015261; DOI=10.1074/jbc.m807083200;
RA Karamysheva Z., Diaz-Martinez L.A., Crow S.E., Li B., Yu H.;
RT "Multiple anaphase-promoting complex/cyclosome degrons mediate the
RT degradation of human Sgo1.";
RL J. Biol. Chem. 284:1772-1780(2009).
RN [16]
RP INTERACTION WITH CDCA8, AND FUNCTION.
RX PubMed=20739936; DOI=10.1038/nature09390;
RA Tsukahara T., Tanno Y., Watanabe Y.;
RT "Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation.";
RL Nature 467:719-723(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-507, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-436, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP INVOLVEMENT IN CAID, VARIANT CAID GLU-23, AND CHARACTERIZATION OF VARIANT
RP CAID GLU-23.
RX PubMed=25282101; DOI=10.1038/ng.3113;
RG FORGE Canada Consortium;
RA Chetaille P., Preuss C., Burkhard S., Cote J.M., Houde C., Castilloux J.,
RA Piche J., Gosset N., Leclerc S., Wuennemann F., Thibeault M., Gagnon C.,
RA Galli A., Tuck E., Hickson G.R., El Amine N., Boufaied I., Lemyre E.,
RA de Santa Barbara P., Faure S., Jonzon A., Cameron M., Dietz H.C.,
RA Gallo-McFarlane E., Benson D.W., Moreau C., Labuda D., Zhan S.H., Shen Y.,
RA Jomphe M., Jones S.J., Bakkers J., Andelfinger G.;
RT "Mutations in SGOL1 cause a novel cohesinopathy affecting heart and gut
RT rhythm.";
RL Nat. Genet. 46:1245-1249(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 445-463 IN COMPLEX WITH CBX1,
RP INTERACTION WITH CBX5, MUTAGENESIS OF PRO-451; VAL-453 AND ILE-455, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21346195; DOI=10.1091/mbc.e11-01-0009;
RA Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.;
RT "Mitotic centromeric targeting of HP1 and its binding to Sgo1 are
RT dispensable for sister-chromatid cohesion in human cells.";
RL Mol. Biol. Cell 22:1181-1190(2011).
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. Isoform 3 plays a role in
CC maintaining centriole cohesion involved in controlling spindle pole
CC integrity. Involved in centromeric enrichment of AUKRB in prometaphase.
CC {ECO:0000269|PubMed:15604152, ECO:0000269|PubMed:15723797,
CC ECO:0000269|PubMed:15737064, ECO:0000269|PubMed:16580887,
CC ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:17621308,
CC ECO:0000269|PubMed:18331714, ECO:0000269|PubMed:20739936}.
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. Isoform 3 interacts with PLK1. Interacts with CDCA8.
CC {ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16580887,
CC ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:18331714,
CC ECO:0000269|PubMed:20739936}.
CC -!- INTERACTION:
CC Q5FBB7; P83916: CBX1; NbExp=2; IntAct=EBI-989069, EBI-78129;
CC Q5FBB7; P45973: CBX5; NbExp=4; IntAct=EBI-989069, EBI-78219;
CC Q5FBB7; Q96FF9: CDCA5; NbExp=4; IntAct=EBI-989069, EBI-718805;
CC Q5FBB7; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-989069, EBI-979174;
CC Q5FBB7; P67775: PPP2CA; NbExp=4; IntAct=EBI-989069, EBI-712311;
CC Q5FBB7; Q15172: PPP2R5A; NbExp=3; IntAct=EBI-989069, EBI-641666;
CC Q5FBB7; Q14683: SMC1A; NbExp=9; IntAct=EBI-989069, EBI-80690;
CC Q5FBB7; Q8N3U4: STAG2; NbExp=7; IntAct=EBI-989069, EBI-1057252;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:16582621}.
CC Chromosome, centromere {ECO:0000269|PubMed:15604152,
CC ECO:0000269|PubMed:15723797, ECO:0000269|PubMed:16541025,
CC ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:21346195}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:16582621,
CC ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:17621308}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:16582621,
CC ECO:0000269|PubMed:18331714}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:18331714}.
CC Note=Localizes to the inner centromere throughout prophase until
CC metaphase and disappears at anaphase (PubMed:16541025). Centromeric
CC localization requires the presence of BUB1 and the interaction with
CC PPP2R1A (PubMed:16580887)(PubMed:16541025)(PubMed:15604152).
CC Colocalizes with NEK2 at the kinetochore (PubMed:17621308). Colocalizes
CC with and SS18L1 at the kinetochore (PubMed:16582621). Phosphorylation
CC by AUKRB and the presence of BUB1 are required for localization to the
CC kinetochore (PubMed:17617734). Isoform 1 primarily localizes to
CC kinetochores during G2 phase and mitotic prophase, metaphase, and
CC anaphase and does not appear to be associated with kinetochores during
CC late mitosis (PubMed:16582621). Isoform 3 is found at the centrosome in
CC interphase and at spindle poles in mitosis and its spindle pole
CC localization is PLK1 dependent (PubMed:16582621). Isoform 3 does not
CC localize to kinetochores during any stages of the cell cycle
CC (PubMed:16582621). {ECO:0000269|PubMed:15604152,
CC ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16580887,
CC ECO:0000269|PubMed:16582621, ECO:0000269|PubMed:17617734,
CC ECO:0000269|PubMed:17621308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=1EF, SgoL1-A2;
CC IsoId=Q5FBB7-1; Sequence=Displayed;
CC Name=2; Synonyms=1GH, SgoL1-B2;
CC IsoId=Q5FBB7-2; Sequence=VSP_016792, VSP_016794;
CC Name=3; Synonyms=1KL, sSGO1, SgoL1-C2;
CC IsoId=Q5FBB7-3; Sequence=VSP_016790, VSP_016791;
CC Name=4; Synonyms=1CD, SgoL1-B1;
CC IsoId=Q5FBB7-4; Sequence=VSP_016792, VSP_016794, VSP_016795;
CC Name=5; Synonyms=1AB, SgoL1-C1;
CC IsoId=Q5FBB7-5; Sequence=VSP_016790, VSP_016791, VSP_016795;
CC Name=6; Synonyms=1AB, SgoL1-A1;
CC IsoId=Q5FBB7-6; Sequence=VSP_016795;
CC Name=7; Synonyms=1J;
CC IsoId=Q5FBB7-7; Sequence=VSP_016793;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis.
CC Expressed in lung, small intestine, breast, liver and placenta.
CC Strongly overexpressed in 90% of breast cancers tested.
CC {ECO:0000269|PubMed:12747765}.
CC -!- DEVELOPMENTAL STAGE: Appears in prophase cells and remains present
CC until metaphase. Strongly decreases at the onset of anaphase and
CC completely disappears at telophase. Not present in interphase cells (at
CC protein level). {ECO:0000269|PubMed:15723797}.
CC -!- DOMAIN: The KEN box and D-box 3 are required for its ubiquitination and
CC degradation. {ECO:0000269|PubMed:19015261}.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1.
CC {ECO:0000269|PubMed:19015261}.
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.
CC {ECO:0000269|PubMed:16582621, ECO:0000269|PubMed:17617734,
CC ECO:0000269|PubMed:17621308}.
CC -!- DISEASE: Chronic atrial and intestinal dysrhythmia (CAID) [MIM:616201]:
CC A disease characterized by dysregulation of the cardiac sinus node
CC resulting in sick sinus syndrome, in association with chronic
CC intestinal pseudo-obstruction, a disorder of gastrointestinal motility
CC in which intestinal obstruction occurs in the absence of a mechanical
CC obstacle. {ECO:0000269|PubMed:25282101}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
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=AAH01339.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH32696.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB190994; BAD91318.1; -; mRNA.
DR EMBL; AB193056; BAD95529.1; -; mRNA.
DR EMBL; AB193057; BAD95530.1; -; mRNA.
DR EMBL; AB193058; BAD95531.1; -; mRNA.
DR EMBL; AB193059; BAD95532.1; -; mRNA.
DR EMBL; AB193060; BAD95533.1; -; mRNA.
DR EMBL; AB193061; BAD95534.1; -; mRNA.
DR EMBL; AB193062; BAD95535.1; -; mRNA.
DR EMBL; AB193063; BAD95536.1; -; mRNA.
DR EMBL; AB193064; BAD95537.1; -; mRNA.
DR EMBL; AB193065; BAD95538.1; -; mRNA.
DR EMBL; AB193066; BAD95539.1; -; mRNA.
DR EMBL; AB187577; BAD89587.1; -; mRNA.
DR EMBL; AB187578; BAD89588.1; -; mRNA.
DR EMBL; AB187579; BAD89589.1; -; mRNA.
DR EMBL; AB187580; BAD89590.1; -; mRNA.
DR EMBL; AB187581; BAD89591.1; -; mRNA.
DR EMBL; AB187582; BAD89592.1; -; mRNA.
DR EMBL; BC001339; AAH01339.2; ALT_INIT; mRNA.
DR EMBL; BC017867; AAH17867.1; -; mRNA.
DR EMBL; BC032696; AAH32696.1; ALT_INIT; mRNA.
DR EMBL; AF308299; AAG48266.1; -; mRNA.
DR CCDS; CCDS2635.1; -. [Q5FBB7-3]
DR CCDS; CCDS33716.1; -. [Q5FBB7-1]
DR CCDS; CCDS46771.1; -. [Q5FBB7-2]
DR CCDS; CCDS46772.1; -. [Q5FBB7-5]
DR CCDS; CCDS46773.1; -. [Q5FBB7-6]
DR CCDS; CCDS46774.1; -. [Q5FBB7-4]
DR CCDS; CCDS56243.1; -. [Q5FBB7-7]
DR RefSeq; NP_001012409.1; NM_001012409.3. [Q5FBB7-6]
DR RefSeq; NP_001012410.1; NM_001012410.4. [Q5FBB7-1]
DR RefSeq; NP_001012411.1; NM_001012411.3. [Q5FBB7-4]
DR RefSeq; NP_001012412.1; NM_001012412.4. [Q5FBB7-2]
DR RefSeq; NP_001012413.1; NM_001012413.3. [Q5FBB7-5]
DR RefSeq; NP_001186180.1; NM_001199251.2. [Q5FBB7-6]
DR RefSeq; NP_001186181.1; NM_001199252.2. [Q5FBB7-1]
DR RefSeq; NP_001186182.1; NM_001199253.2. [Q5FBB7-4]
DR RefSeq; NP_001186183.1; NM_001199254.2. [Q5FBB7-2]
DR RefSeq; NP_001186184.1; NM_001199255.2. [Q5FBB7-5]
DR RefSeq; NP_001186185.1; NM_001199256.2. [Q5FBB7-3]
DR RefSeq; NP_001186186.1; NM_001199257.2. [Q5FBB7-7]
DR RefSeq; NP_612493.1; NM_138484.4. [Q5FBB7-3]
DR RefSeq; XP_011531675.1; XM_011533373.2. [Q5FBB7-1]
DR RefSeq; XP_011531677.1; XM_011533375.2. [Q5FBB7-1]
DR RefSeq; XP_011531678.1; XM_011533376.2. [Q5FBB7-1]
DR RefSeq; XP_011531679.1; XM_011533377.2. [Q5FBB7-1]
DR PDB; 3FGA; X-ray; 2.70 A; D=51-96.
DR PDB; 3Q6S; X-ray; 1.93 A; E/F=445-463.
DR PDB; 4A0I; X-ray; 2.60 A; C/D=2-6.
DR PDBsum; 3FGA; -.
DR PDBsum; 3Q6S; -.
DR PDBsum; 4A0I; -.
DR AlphaFoldDB; Q5FBB7; -.
DR SMR; Q5FBB7; -.
DR BioGRID; 127395; 105.
DR DIP; DIP-36614N; -.
DR IntAct; Q5FBB7; 51.
DR MINT; Q5FBB7; -.
DR STRING; 9606.ENSP00000263753; -.
DR iPTMnet; Q5FBB7; -.
DR PhosphoSitePlus; Q5FBB7; -.
DR BioMuta; SGO1; -.
DR DMDM; 74741474; -.
DR EPD; Q5FBB7; -.
DR jPOST; Q5FBB7; -.
DR MassIVE; Q5FBB7; -.
DR MaxQB; Q5FBB7; -.
DR PaxDb; Q5FBB7; -.
DR PeptideAtlas; Q5FBB7; -.
DR PRIDE; Q5FBB7; -.
DR ProteomicsDB; 62781; -. [Q5FBB7-1]
DR ProteomicsDB; 62782; -. [Q5FBB7-2]
DR ProteomicsDB; 62783; -. [Q5FBB7-3]
DR ProteomicsDB; 62784; -. [Q5FBB7-4]
DR ProteomicsDB; 62785; -. [Q5FBB7-5]
DR ProteomicsDB; 62786; -. [Q5FBB7-6]
DR ProteomicsDB; 62787; -. [Q5FBB7-7]
DR Antibodypedia; 27089; 246 antibodies from 27 providers.
DR DNASU; 151648; -.
DR Ensembl; ENST00000263753.8; ENSP00000263753.4; ENSG00000129810.15. [Q5FBB7-1]
DR Ensembl; ENST00000306698.6; ENSP00000306581.2; ENSG00000129810.15. [Q5FBB7-3]
DR Ensembl; ENST00000412997.6; ENSP00000410458.1; ENSG00000129810.15. [Q5FBB7-6]
DR Ensembl; ENST00000417364.1; ENSP00000394613.1; ENSG00000129810.15. [Q5FBB7-4]
DR Ensembl; ENST00000419233.6; ENSP00000394625.2; ENSG00000129810.15. [Q5FBB7-2]
DR Ensembl; ENST00000421451.5; ENSP00000414129.1; ENSG00000129810.15. [Q5FBB7-1]
DR Ensembl; ENST00000425061.5; ENSP00000414960.1; ENSG00000129810.15. [Q5FBB7-2]
DR Ensembl; ENST00000437051.5; ENSP00000389034.1; ENSG00000129810.15. [Q5FBB7-4]
DR Ensembl; ENST00000442720.5; ENSP00000394957.1; ENSG00000129810.15. [Q5FBB7-5]
DR Ensembl; ENST00000443724.5; ENSP00000413070.1; ENSG00000129810.15. [Q5FBB7-7]
DR Ensembl; ENST00000452020.5; ENSP00000411200.1; ENSG00000129810.15. [Q5FBB7-3]
DR GeneID; 151648; -.
DR KEGG; hsa:151648; -.
DR MANE-Select; ENST00000412997.6; ENSP00000410458.1; NM_001199251.3; NP_001186180.1. [Q5FBB7-6]
DR UCSC; uc003cbr.4; human. [Q5FBB7-1]
DR CTD; 151648; -.
DR DisGeNET; 151648; -.
DR GeneCards; SGO1; -.
DR HGNC; HGNC:25088; SGO1.
DR HPA; ENSG00000129810; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MalaCards; SGO1; -.
DR MIM; 609168; gene.
DR MIM; 616201; phenotype.
DR neXtProt; NX_Q5FBB7; -.
DR OpenTargets; ENSG00000129810; -.
DR Orphanet; 435988; Chronic atrial and intestinal dysrhythmia syndrome.
DR PharmGKB; PA134988556; -.
DR VEuPathDB; HostDB:ENSG00000129810; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000154107; -.
DR HOGENOM; CLU_1015500_0_0_1; -.
DR InParanoid; Q5FBB7; -.
DR OMA; CQWNKDQ; -.
DR OrthoDB; 1414582at2759; -.
DR PhylomeDB; Q5FBB7; -.
DR TreeFam; TF334213; -.
DR PathwayCommons; Q5FBB7; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q5FBB7; -.
DR SIGNOR; Q5FBB7; -.
DR BioGRID-ORCS; 151648; 696 hits in 1029 CRISPR screens.
DR ChiTaRS; SGO1; human.
DR EvolutionaryTrace; Q5FBB7; -.
DR GeneWiki; SGOL1; -.
DR GenomeRNAi; 151648; -.
DR Pharos; Q5FBB7; Tbio.
DR PRO; PR:Q5FBB7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q5FBB7; protein.
DR Bgee; ENSG00000129810; Expressed in ventricular zone and 104 other tissues.
DR ExpressionAtlas; Q5FBB7; baseline and differential.
DR Genevisible; Q5FBB7; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IDA:MGI.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010457; P:centriole-centriole cohesion; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:MGI.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; IMP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..561
FT /note="Shugoshin 1"
FT /id="PRO_0000055436"
FT REGION 1..176
FT /note="Necessary for interaction with PPP2CA and PPP2R1A"
FT /evidence="ECO:0000269|PubMed:16580887"
FT REGION 260..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..89
FT /evidence="ECO:0000255"
FT COILED 273..313
FT /evidence="ECO:0000255"
FT MOTIF 192..200
FT /note="D-box 1"
FT MOTIF 310..312
FT /note="KEN box"
FT MOTIF 438..446
FT /note="D-box 2"
FT MOTIF 451..455
FT /note="PXVXL/I motif"
FT /evidence="ECO:0000305|PubMed:21346195"
FT MOTIF 457..465
FT /note="D-box 3"
FT COMPBIAS 269..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000269|PubMed:17621308"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 507
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000269|PubMed:17621308,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 159
FT /note="D -> A (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15737064, ECO:0000303|Ref.2"
FT /id="VSP_016790"
FT VAR_SEQ 160..428
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15737064, ECO:0000303|Ref.2"
FT /id="VSP_016791"
FT VAR_SEQ 176
FT /note="G -> A (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15737064, ECO:0000303|Ref.2"
FT /id="VSP_016792"
FT VAR_SEQ 177..522
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15737064"
FT /id="VSP_016793"
FT VAR_SEQ 177..428
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15737064, ECO:0000303|Ref.2"
FT /id="VSP_016794"
FT VAR_SEQ 522..561
FT /note="RALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR -> SMKQIQ
FT (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12747765,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15737064,
FT ECO:0000303|Ref.2"
FT /id="VSP_016795"
FT VARIANT 23
FT /note="K -> E (in CAID; patient fibroblasts exhibit
FT significantly faster cell proliferation than controls;
FT during mitosis the mutant protein is localized in an
FT ordered fashion around the centromeres but display a rather
FT homogeneous cytoplasmic localization pattern;
FT dbSNP:rs199815268)"
FT /evidence="ECO:0000269|PubMed:25282101"
FT /id="VAR_072709"
FT VARIANT 171
FT /note="V -> A (in dbSNP:rs6806241)"
FT /id="VAR_051968"
FT VARIANT 322
FT /note="Q -> P (in dbSNP:rs9868701)"
FT /id="VAR_051969"
FT MUTAGEN 14
FT /note="S->A: Loss of phosphorylation and presence of
FT misaligned chromosomes; when associated with A-507."
FT /evidence="ECO:0000269|PubMed:17621308"
FT MUTAGEN 61
FT /note="N->I: Loss of interaction with PPP2CA and PPP2R1A
FT and loss of centromeric localization."
FT /evidence="ECO:0000269|PubMed:16580887"
FT MUTAGEN 73
FT /note="S->A: Loss of proper localization to spindle pole
FT and mitotic spindle. Significant increase in split spindle
FT poles."
FT /evidence="ECO:0000269|PubMed:18331714"
FT MUTAGEN 146
FT /note="T->A: Loss of proper localization to spindle pole
FT and mitotic spindle. Significant increase in split spindle
FT poles."
FT /evidence="ECO:0000269|PubMed:18331714"
FT MUTAGEN 451
FT /note="P->A: Disrupts interaction with CBX5, loss of
FT localization to centromeres in interphase, no effect on
FT localization to centromeres in mitosis; when associated
FT with A-453 and A-455."
FT /evidence="ECO:0000269|PubMed:21346195"
FT MUTAGEN 453
FT /note="V->A: Disrupts interaction with CBX5, loss of
FT localization to centromeres in interphase, no effect on
FT localization to centromeres in mitosis; when associated
FT with A-451 and A-455."
FT /evidence="ECO:0000269|PubMed:21346195"
FT MUTAGEN 455
FT /note="I->A: Disrupts interaction with CBX5, loss of
FT localization to centromeres in interphase, no effect on
FT localization to centromeres in mitosis; when associated
FT with A-451 and A-453."
FT /evidence="ECO:0000269|PubMed:21346195"
FT MUTAGEN 492
FT /note="K->A: Loss of centromeric localization."
FT /evidence="ECO:0000269|PubMed:16580887"
FT MUTAGEN 507
FT /note="S->A: Loss of phosphorylation; and presence of
FT misaligned chromosomes; when associated with A-14."
FT /evidence="ECO:0000269|PubMed:17621308"
FT HELIX 51..93
FT /evidence="ECO:0007829|PDB:3FGA"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:3Q6S"
SQ SEQUENCE 561 AA; 64190 MW; 90CEE0FD2B40CD9C CRC64;
MAKERCLKKS FQDSLEDIKK RMKEKRNKNL AEIGKRRSFI AAPCQIITNT STLLKNYQDN
NKMLVLALEN EKSKVKEAQD IILQLRKECY YLTCQLYALK GKLTSQQTVE PAQNQEICSS
GMDPNSDDSS RNLFVKDLPQ IPLEETELPG QGESFQIEDQ IPTIPQDTLG VDFDSGEAKS
TDNVLPRTVS VRSSLKKHCN SICQFDSLDD FETSHLAGKS FEFERVGFLD PLVNMHIPEN
VQHNACQWSK DQVNLSPKLI QPGTFTKTKE DILESKSEQT KSKQRDTQER KREEKRKANR
RKSKRMSKYK ENKSENKKTV PQKKMHKSVS SNDAYNFNLE EGVHLTPFRQ KVSNDSNREE
NNESEVSLCE SSGSGDDSDD LYLPTCKYIQ NPTSNSDRPV TRPLAKRALK YTDEKETEGS
KPTKTPTTTP PETQQSPHLS LKDITNVSLY PVVKIRRLSL SPKKNKASPA VALPKRRCTA
SVNYKEPTLA SKLRRGDPFT DLCFLNSPIF KQKKDLRRSK KRALEVSPAK EAIFILYYVR
EFVSRFPDCR KCKLETHICL R
