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 27-MAR-2024, entry version 163. 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}; 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; 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 PDB; 7ZJS; X-ray; 3.24 A; E/F=331-341. DR PDBsum; 3FGA; -. DR PDBsum; 3Q6S; -. DR PDBsum; 4A0I; -. DR PDBsum; 7ZJS; -. DR AlphaFoldDB; Q5FBB7; -. DR SMR; Q5FBB7; -. DR BioGRID; 127395; 116. 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; 9606-ENSP00000263753; -. DR PeptideAtlas; 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 Pumba; Q5FBB7; -. DR Antibodypedia; 27089; 277 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 AGR; HGNC:25088; -. 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; 5320947at2759; -. 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; 712 hits in 1072 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 primordial germ cell in gonad and 105 other cell types or tissues. DR ExpressionAtlas; Q5FBB7; baseline and differential. 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:HPA. 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:0045132; P:meiotic chromosome segregation; IMP:MGI. DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; IMP:UniProtKB. 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; Q5FBB7; HS. 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 333..335 FT /evidence="ECO:0007829|PDB:7ZJS" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:7ZJS" 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 //