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Shugoshin 1 (Serologically defined breast cancer antigen NY-BR-85) (Shugoshin-like 1)

 SGO1_HUMAN              Reviewed;         561 AA.
Q5FBB7; Q588H5; Q5FBB4; Q5FBB5; Q5FBB6; Q5FBB8; Q8N579; Q8WVL0;
Q9BVA8; Q9H275;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
30-AUG-2017, entry version 125.
RecName: Full=Shugoshin 1 {ECO:0000312|HGNC:HGNC:25088};
AltName: Full=Serologically defined breast cancer antigen NY-BR-85;
AltName: Full=Shugoshin-like 1;
Name=SGO1 {ECO:0000312|HGNC:HGNC:25088}; Synonyms=SGOL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7),
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15737064; DOI=10.1371/journal.pbio.0030086;
McGuinness B.E., Hirota T., Kudo N.R., Peters J.-M., Nasmyth K.;
"Shugoshin prevents dissociation of cohesin from centromeres during
mitosis in vertebrate cells.";
PLoS Biol. 3:433-449(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
Suzuki H., Akiyama N., Tsuji M., Saito S., Eto Y.;
"Human SgoL1 inhibits precocious separation of sister centromere in
early mitosis.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 25-561 (ISOFORM 6).
TISSUE=Cervix, Lung, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 250-527 (ISOFORM 6), AND TISSUE
SPECIFICITY.
TISSUE=Mammary gland;
PubMed=12747765;
Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E.,
Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
"Humoral immunity to human breast cancer: antigen definition and
quantitative analysis of mRNA expression.";
Cancer Immun. 1:4-4(2001).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=15723797; DOI=10.1016/j.cub.2004.12.044;
Kitajima T.S., Hauf S., Ohsugi M., Yamamoto T., Watanabe Y.;
"Human Bub1 defines the persistent cohesion site along the mitotic
chromosome by affecting Shugoshin localization.";
Curr. Biol. 15:353-359(2005).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15604152; DOI=10.1073/pnas.0408600102;
Tang Z., Sun Y., Harley S.E., Zou H., Yu H.;
"Human Bub1 protects centromeric sister-chromatid cohesion through
Shugoshin during mitosis.";
Proc. Natl. Acad. Sci. U.S.A. 101:18012-18017(2004).
[7]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=16582621;
Wang X., Yang Y., Dai W.;
"Differential subcellular localizations of two human Sgo1 isoforms:
implications in regulation of sister chromatid cohesion and
microtubule dynamics.";
Cell Cycle 5:635-640(2006).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA; PPP2R1A AND
PPP2R5C, AND MUTAGENESIS OF ASN-61 AND LYS-492.
PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010;
Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.;
"PP2A is required for centromeric localization of Sgo1 and proper
chromosome segregation.";
Dev. Cell 10:575-585(2006).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH PPP2CA/PPP2CB; PPP2R1B;
PPP2R5A; PPP2R5B; PPP2R5C; PPP2R5D; PPP2R5E; SET; LRRC59; RBM10/RBM5;
RPL10A; RPL28; RPL7; RPL7A AND RPLP1.
PubMed=16541025; DOI=10.1038/nature04663;
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
Kawashima S.A., Watanabe Y.;
"Shugoshin collaborates with protein phosphatase 2A to protect
cohesin.";
Nature 441:46-52(2006).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=17617734; DOI=10.4161/cc.6.13.4442;
Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J.,
Stukenberg T., Kallio M.J.;
"Shugoshin 1 plays a central role in kinetochore assembly and is
required for kinetochore targeting of Plk1.";
Cell Cycle 6:1579-1585(2007).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEK2, PHOSPHORYLATION
AT SER-14 AND SER-507, AND MUTAGENESIS OF SER-14 AND SER-507.
PubMed=17621308; DOI=10.1038/cr.2007.55;
Fu G., Ding X., Yuan K., Aikhionbare F., Yao J., Cai X., Jiang K.,
Yao X.;
"Phosphorylation of human Sgo1 by NEK2A is essential for chromosome
congression in mitosis.";
Cell Res. 17:608-618(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1, AND MUTAGENESIS
OF SER-73 AND THR-146.
PubMed=18331714; DOI=10.1016/j.devcel.2007.12.007;
Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z.,
Dai W.;
"sSgo1, a major splice variant of Sgo1, functions in centriole
cohesion where it is regulated by Plk1.";
Dev. Cell 14:331-341(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
UBIQUITINATION, AND DOMAIN KEN BOX AND D-BOX.
PubMed=19015261; DOI=10.1074/jbc.M807083200;
Karamysheva Z., Diaz-Martinez L.A., Crow S.E., Li B., Yu H.;
"Multiple anaphase-promoting complex/cyclosome degrons mediate the
degradation of human Sgo1.";
J. Biol. Chem. 284:1772-1780(2009).
[16]
INTERACTION WITH CDCA8, AND FUNCTION.
PubMed=20739936; DOI=10.1038/nature09390;
Tsukahara T., Tanno Y., Watanabe Y.;
"Phosphorylation of the CPC by Cdk1 promotes chromosome bi-
orientation.";
Nature 467:719-723(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-507, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-436, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INVOLVEMENT IN CAID, VARIANT CAID GLU-23, AND CHARACTERIZATION OF
VARIANT CAID GLU-23.
PubMed=25282101; DOI=10.1038/ng.3113;
FORGE Canada Consortium;
Chetaille P., Preuss C., Burkhard S., Cote J.M., Houde C.,
Castilloux J., Piche J., Gosset N., Leclerc S., Wuennemann F.,
Thibeault M., Gagnon C., Galli A., Tuck E., Hickson G.R., El Amine N.,
Boufaied I., Lemyre E., de Santa Barbara P., Faure S., Jonzon A.,
Cameron M., Dietz H.C., Gallo-McFarlane E., Benson D.W., Moreau C.,
Labuda D., Zhan S.H., Shen Y., Jomphe M., Jones S.J., Bakkers J.,
Andelfinger G.;
"Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
gut rhythm.";
Nat. Genet. 46:1245-1249(2014).
[21]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 445-463 IN COMPLEX WITH
CBX1, INTERACTION WITH CBX5, MUTAGENESIS OF PRO-451; VAL-453 AND
ILE-455, AND SUBCELLULAR LOCATION.
PubMed=21346195; DOI=10.1091/mbc.E11-01-0009;
Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.;
"Mitotic centromeric targeting of HP1 and its binding to Sgo1 are
dispensable for sister-chromatid cohesion in human cells.";
Mol. Biol. Cell 22:1181-1190(2011).
-!- FUNCTION: Plays a central role in chromosome cohesion during
mitosis by preventing premature dissociation of cohesin complex
from centromeres after prophase, when most of cohesin complex
dissociates from chromosomes arms. May act by preventing
phosphorylation of the STAG2 subunit of cohesin complex at the
centromere, ensuring cohesin persistence at centromere until
cohesin cleavage by ESPL1/separase at anaphase. Essential for
proper chromosome segregation during mitosis and this function
requires interaction with PPP2R1A. Its phosphorylated form is
necessary for chromosome congression and for the proper attachment
of spindle microtubule to the kinetochore. Necessary for
kinetochore localization of PLK1 and CENPF. May play a role in the
tension sensing mechanism of the spindle-assembly checkpoint by
regulating PLK1 kinetochore affinity. Isoform 3 plays a role in
maintaining centriole cohesion involved in controlling spindle
pole integrity. Involved in centromeric enrichment of AUKRB in
prometaphase. {ECO:0000269|PubMed:15604152,
ECO:0000269|PubMed:15723797, ECO:0000269|PubMed:15737064,
ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:17617734,
ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:18331714,
ECO:0000269|PubMed:20739936}.
-!- SUBUNIT: Interacts with PPP2CA (or PPP2CB), PPP2R1B, PPP2R5A,
PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E, SET, LRRC59, RBM10 (or RBM5),
RPL10A, RPL28, RPL7, RPL7A and RPLP1. Interaction with protein
phosphatase 2A occurs most probably through direct binding to the
regulatory B56 subunits: PPP2R1B, PPP2R5A, PPP2R5B, PPP2R5C,
PPP2R5D, PPP2R5E. Interacts with PPP2R1A and NEK2. Isoform 3
interacts with PLK1. Interacts with CDCA8.
{ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16580887,
ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:18331714,
ECO:0000269|PubMed:20739936}.
-!- INTERACTION:
P83916:CBX1; NbExp=2; IntAct=EBI-989069, EBI-78129;
P45973:CBX5; NbExp=2; IntAct=EBI-989069, EBI-78219;
P67775:PPP2CA; NbExp=2; IntAct=EBI-989069, EBI-712311;
Q15172:PPP2R5A; NbExp=3; IntAct=EBI-989069, EBI-641666;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:16582621}.
Chromosome, centromere {ECO:0000269|PubMed:15604152,
ECO:0000269|PubMed:15723797, ECO:0000269|PubMed:16541025,
ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:21346195}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16582621,
ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:17621308}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:16582621, ECO:0000269|PubMed:18331714}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:18331714}. Note=Localizes to the inner
centromere throughout prophase until metaphase and disappears at
anaphase (PubMed:16541025). Centromeric localization requires the
presence of BUB1 and the interaction with PPP2R1A
(PubMed:16580887)(PubMed:16541025)(PubMed:15604152). Colocalizes
with NEK2 at the kinetochore (PubMed:17621308). Colocalizes with
and SS18L1 at the kinetochore (PubMed:16582621). Phosphorylation
by AUKRB and the presence of BUB1 are required for localization to
the kinetochore (PubMed:17617734). Isoform 1 primarily localizes
to kinetochores during G2 phase and mitotic prophase, metaphase,
and anaphase and does not appear to be associated with
kinetochores during late mitosis (PubMed:16582621). Isoform 3 is
found at the centrosome in interphase and at spindle poles in
mitosis and its spindle pole localization is PLK1 dependent
(PubMed:16582621). Isoform 3 does not localize to kinetochores
during any stages of the cell cycle (PubMed:16582621).
{ECO:0000269|PubMed:15604152, ECO:0000269|PubMed:16541025,
ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:16582621,
ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:17621308}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=1EF, SgoL1-A2;
IsoId=Q5FBB7-1; Sequence=Displayed;
Name=2; Synonyms=1GH, SgoL1-B2;
IsoId=Q5FBB7-2; Sequence=VSP_016792, VSP_016794;
Name=3; Synonyms=1KL, sSGO1, SgoL1-C2;
IsoId=Q5FBB7-3; Sequence=VSP_016790, VSP_016791;
Name=4; Synonyms=1CD, SgoL1-B1;
IsoId=Q5FBB7-4; Sequence=VSP_016792, VSP_016794, VSP_016795;
Name=5; Synonyms=1AB, SgoL1-C1;
IsoId=Q5FBB7-5; Sequence=VSP_016790, VSP_016791, VSP_016795;
Name=6; Synonyms=1AB, SgoL1-A1;
IsoId=Q5FBB7-6; Sequence=VSP_016795;
Name=7; Synonyms=1J;
IsoId=Q5FBB7-7; Sequence=VSP_016793;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis.
Expressed in lung, small intestine, breast, liver and placenta.
Strongly overexpressed in 90% of breast cancers tested.
{ECO:0000269|PubMed:12747765}.
-!- DEVELOPMENTAL STAGE: Appears in prophase cells and remains present
until metaphase. Strongly decreases at the onset of anaphase and
completely disappears at telophase. Not present in interphase
cells (at protein level). {ECO:0000269|PubMed:15723797}.
-!- DOMAIN: The KEN box and D-box 3 are required for its
ubiquitination and degradation. {ECO:0000269|PubMed:19015261}.
-!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1.
{ECO:0000269|PubMed:19015261}.
-!- PTM: Phosphorylation by NEK2 is essential for chromosome
congression in mitosis and for the proper attachment of spindle
microtubule to the kinetochore. Phosphorylated by PLK1 and AUKRB.
{ECO:0000269|PubMed:16582621, ECO:0000269|PubMed:17617734,
ECO:0000269|PubMed:17621308}.
-!- DISEASE: Chronic atrial and intestinal dysrhythmia (CAID)
[MIM:616201]: A disease characterized by dysregulation of the
cardiac sinus node resulting in sick sinus syndrome, in
association with chronic intestinal pseudo-obstruction, a disorder
of gastrointestinal motility in which intestinal obstruction
occurs in the absence of a mechanical obstacle.
{ECO:0000269|PubMed:25282101}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Shugoshin is Japanese for guardian spirit (as it is
known to be a protector of centromeric cohesin).
-!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH01339.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH32696.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB190994; BAD91318.1; -; mRNA.
EMBL; AB193056; BAD95529.1; -; mRNA.
EMBL; AB193057; BAD95530.1; -; mRNA.
EMBL; AB193058; BAD95531.1; -; mRNA.
EMBL; AB193059; BAD95532.1; -; mRNA.
EMBL; AB193060; BAD95533.1; -; mRNA.
EMBL; AB193061; BAD95534.1; -; mRNA.
EMBL; AB193062; BAD95535.1; -; mRNA.
EMBL; AB193063; BAD95536.1; -; mRNA.
EMBL; AB193064; BAD95537.1; -; mRNA.
EMBL; AB193065; BAD95538.1; -; mRNA.
EMBL; AB193066; BAD95539.1; -; mRNA.
EMBL; AB187577; BAD89587.1; -; mRNA.
EMBL; AB187578; BAD89588.1; -; mRNA.
EMBL; AB187579; BAD89589.1; -; mRNA.
EMBL; AB187580; BAD89590.1; -; mRNA.
EMBL; AB187581; BAD89591.1; -; mRNA.
EMBL; AB187582; BAD89592.1; -; mRNA.
EMBL; BC001339; AAH01339.2; ALT_INIT; mRNA.
EMBL; BC017867; AAH17867.1; -; mRNA.
EMBL; BC032696; AAH32696.1; ALT_INIT; mRNA.
EMBL; AF308299; AAG48266.1; -; mRNA.
CCDS; CCDS2635.1; -. [Q5FBB7-3]
CCDS; CCDS33716.1; -. [Q5FBB7-1]
CCDS; CCDS46771.1; -. [Q5FBB7-2]
CCDS; CCDS46772.1; -. [Q5FBB7-5]
CCDS; CCDS46773.1; -. [Q5FBB7-6]
CCDS; CCDS46774.1; -. [Q5FBB7-4]
CCDS; CCDS56243.1; -. [Q5FBB7-7]
RefSeq; NP_001012409.1; NM_001012409.3. [Q5FBB7-6]
RefSeq; NP_001012410.1; NM_001012410.4. [Q5FBB7-1]
RefSeq; NP_001012411.1; NM_001012411.3. [Q5FBB7-4]
RefSeq; NP_001012412.1; NM_001012412.4. [Q5FBB7-2]
RefSeq; NP_001012413.1; NM_001012413.3. [Q5FBB7-5]
RefSeq; NP_001186180.1; NM_001199251.2. [Q5FBB7-6]
RefSeq; NP_001186181.1; NM_001199252.2. [Q5FBB7-1]
RefSeq; NP_001186182.1; NM_001199253.2. [Q5FBB7-4]
RefSeq; NP_001186183.1; NM_001199254.2. [Q5FBB7-2]
RefSeq; NP_001186184.1; NM_001199255.2. [Q5FBB7-5]
RefSeq; NP_001186185.1; NM_001199256.2. [Q5FBB7-3]
RefSeq; NP_001186186.1; NM_001199257.2. [Q5FBB7-7]
RefSeq; NP_612493.1; NM_138484.4. [Q5FBB7-3]
RefSeq; XP_011531675.1; XM_011533373.2. [Q5FBB7-1]
RefSeq; XP_011531677.1; XM_011533375.2. [Q5FBB7-1]
RefSeq; XP_011531678.1; XM_011533376.2. [Q5FBB7-1]
RefSeq; XP_011531679.1; XM_011533377.2. [Q5FBB7-1]
UniGene; Hs.105153; -.
PDB; 3FGA; X-ray; 2.70 A; D=51-96.
PDB; 3Q6S; X-ray; 1.93 A; E/F=445-463.
PDB; 4A0I; X-ray; 2.60 A; C/D=2-6.
PDBsum; 3FGA; -.
PDBsum; 3Q6S; -.
PDBsum; 4A0I; -.
ProteinModelPortal; Q5FBB7; -.
SMR; Q5FBB7; -.
BioGrid; 127395; 57.
DIP; DIP-36614N; -.
IntAct; Q5FBB7; 38.
MINT; MINT-4989914; -.
STRING; 9606.ENSP00000263753; -.
iPTMnet; Q5FBB7; -.
PhosphoSitePlus; Q5FBB7; -.
BioMuta; SGOL1; -.
DMDM; 74741474; -.
EPD; Q5FBB7; -.
MaxQB; Q5FBB7; -.
PaxDb; Q5FBB7; -.
PeptideAtlas; Q5FBB7; -.
PRIDE; Q5FBB7; -.
Ensembl; ENST00000263753; ENSP00000263753; ENSG00000129810. [Q5FBB7-1]
Ensembl; ENST00000306698; ENSP00000306581; ENSG00000129810. [Q5FBB7-3]
Ensembl; ENST00000412997; ENSP00000410458; ENSG00000129810. [Q5FBB7-6]
Ensembl; ENST00000417364; ENSP00000394613; ENSG00000129810. [Q5FBB7-4]
Ensembl; ENST00000419233; ENSP00000394625; ENSG00000129810. [Q5FBB7-2]
Ensembl; ENST00000421451; ENSP00000414129; ENSG00000129810. [Q5FBB7-1]
Ensembl; ENST00000425061; ENSP00000414960; ENSG00000129810. [Q5FBB7-2]
Ensembl; ENST00000437051; ENSP00000389034; ENSG00000129810. [Q5FBB7-4]
Ensembl; ENST00000442720; ENSP00000394957; ENSG00000129810. [Q5FBB7-5]
Ensembl; ENST00000443724; ENSP00000413070; ENSG00000129810. [Q5FBB7-7]
Ensembl; ENST00000452020; ENSP00000411200; ENSG00000129810. [Q5FBB7-3]
GeneID; 151648; -.
KEGG; hsa:151648; -.
UCSC; uc003cbr.4; human. [Q5FBB7-1]
CTD; 151648; -.
DisGeNET; 151648; -.
GeneCards; SGO1; -.
HGNC; HGNC:25088; SGO1.
HPA; HPA069857; -.
MalaCards; SGO1; -.
MIM; 609168; gene.
MIM; 616201; phenotype.
neXtProt; NX_Q5FBB7; -.
OpenTargets; ENSG00000129810; -.
PharmGKB; PA134988556; -.
eggNOG; ENOG410IPKX; Eukaryota.
eggNOG; ENOG4111FBS; LUCA.
GeneTree; ENSGT00390000014987; -.
HOVERGEN; HBG080777; -.
InParanoid; Q5FBB7; -.
KO; K11580; -.
OMA; TPFRQKM; -.
OrthoDB; EOG091G0AX7; -.
PhylomeDB; Q5FBB7; -.
TreeFam; TF334213; -.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SIGNOR; Q5FBB7; -.
ChiTaRS; SGOL1; human.
EvolutionaryTrace; Q5FBB7; -.
GeneWiki; SGOL1; -.
GenomeRNAi; 151648; -.
PRO; PR:Q5FBB7; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000129810; -.
ExpressionAtlas; Q5FBB7; baseline and differential.
Genevisible; Q5FBB7; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IDA:MGI.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0010457; P:centriole-centriole cohesion; IDA:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
GO; GO:0045132; P:meiotic chromosome segregation; IMP:MGI.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
InterPro; IPR011515; Shugoshin_C.
InterPro; IPR011516; Shugoshin_N.
Pfam; PF07557; Shugoshin_C; 1.
Pfam; PF07558; Shugoshin_N; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Centromere; Chromosome; Chromosome partition; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
Kinetochore; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 561 Shugoshin 1.
/FTId=PRO_0000055436.
REGION 1 176 Necessary for interaction with PPP2CA and
PPP2R1A. {ECO:0000269|PubMed:16580887}.
COILED 7 89 {ECO:0000255}.
COILED 273 313 {ECO:0000255}.
MOTIF 192 200 D-box 1.
MOTIF 310 312 KEN box.
MOTIF 438 446 D-box 2.
MOTIF 451 455 PXVXL/I motif.
{ECO:0000305|PubMed:21346195}.
MOTIF 457 465 D-box 3.
MOD_RES 14 14 Phosphoserine; by NEK2.
{ECO:0000269|PubMed:17621308}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
MOD_RES 507 507 Phosphoserine; by NEK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:17621308}.
VAR_SEQ 159 159 D -> A (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15737064,
ECO:0000303|Ref.2}.
/FTId=VSP_016790.
VAR_SEQ 160 428 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15737064,
ECO:0000303|Ref.2}.
/FTId=VSP_016791.
VAR_SEQ 176 176 G -> A (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15737064,
ECO:0000303|Ref.2}.
/FTId=VSP_016792.
VAR_SEQ 177 522 Missing (in isoform 7).
{ECO:0000303|PubMed:15737064}.
/FTId=VSP_016793.
VAR_SEQ 177 428 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15737064,
ECO:0000303|Ref.2}.
/FTId=VSP_016794.
VAR_SEQ 522 561 RALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR
-> SMKQIQ (in isoform 4, isoform 5 and
isoform 6). {ECO:0000303|PubMed:12747765,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15737064,
ECO:0000303|Ref.2}.
/FTId=VSP_016795.
VARIANT 23 23 K -> E (in CAID; patient fibroblasts
exhibit significantly faster cell
proliferation than controls; during
mitosis the mutant protein is localized
in an ordered fashion around the
centromeres but display a rather
homogeneous cytoplasmic localization
pattern; dbSNP:rs199815268).
{ECO:0000269|PubMed:25282101}.
/FTId=VAR_072709.
VARIANT 171 171 V -> A (in dbSNP:rs6806241).
/FTId=VAR_051968.
VARIANT 322 322 Q -> P (in dbSNP:rs9868701).
/FTId=VAR_051969.
MUTAGEN 14 14 S->A: Loss of phosphorylation and
presence of misaligned chromosomes; when
associated with A-507.
{ECO:0000269|PubMed:17621308}.
MUTAGEN 61 61 N->I: Loss of interaction with PPP2CA and
PPP2R1A and loss of centromeric
localization.
{ECO:0000269|PubMed:16580887}.
MUTAGEN 73 73 S->A: Loss of proper localization to
spindle pole and mitotic spindle.
Significant increase in split spindle
poles. {ECO:0000269|PubMed:18331714}.
MUTAGEN 146 146 T->A: Loss of proper localization to
spindle pole and mitotic spindle.
Significant increase in split spindle
poles. {ECO:0000269|PubMed:18331714}.
MUTAGEN 451 451 P->A: Disrupts interaction with CBX5,
loss of localization to centromeres in
interphase, no effect on localization to
centromeres in mitosis; when associated
with A-453 and A-455.
{ECO:0000269|PubMed:21346195}.
MUTAGEN 453 453 V->A: Disrupts interaction with CBX5,
loss of localization to centromeres in
interphase, no effect on localization to
centromeres in mitosis; when associated
with A-451 and A-455.
{ECO:0000269|PubMed:21346195}.
MUTAGEN 455 455 I->A: Disrupts interaction with CBX5,
loss of localization to centromeres in
interphase, no effect on localization to
centromeres in mitosis; when associated
with A-451 and A-453.
{ECO:0000269|PubMed:21346195}.
MUTAGEN 492 492 K->A: Loss of centromeric localization.
{ECO:0000269|PubMed:16580887}.
MUTAGEN 507 507 S->A: Loss of phosphorylation; and
presence of misaligned chromosomes; when
associated with A-14.
{ECO:0000269|PubMed:17621308}.
HELIX 51 93 {ECO:0000244|PDB:3FGA}.
STRAND 448 455 {ECO:0000244|PDB:3Q6S}.
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


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