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Q5FBB7 (SGOL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Shugoshin-like 1

Short name=hSgo1
Alternative name(s):
Serologically defined breast cancer antigen NY-BR-85
Gene names
Name:SGOL1
Synonyms:SGO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12

Subunit structure

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. Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Nucleus. Chromosomecentromere. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle pole. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Localizes to the inner centromere throughout prophase until metaphase and disappears at anaphase. During prometaphase, it localizes to a single focus, while at metaphase, it localizes to 2 spots corresponding to the 2 centromeres. Centromeric localization requires the presence of BUB1 and the interaction with PPP2R1A. Localizes to the inner kinetochore from prophase to early metaphase. Colocalizes with NEK2 and SS18L1 at the kinetochore. Phosphorylation by AUKRB and the presence of BUB1 are required for localization to the kinetochore. 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. Isoform 3 is found at the centrosome in interphase and at spindle poles in mitosis and its spindle pole localization is PLK1 dependent. Isoform 3 does not localize to kinetochores during any stages of the cell cycle. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

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. Ref.4

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). Ref.5

Domain

The KEN box and D-box 3 are required for its ubiquitination and degradation. Ref.15

Post-translational modification

Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1. Ref.15

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. Ref.7 Ref.10 Ref.11

Miscellaneous

Shugoshin is Japanese for guardian spirit (as it is known to be a protector of centromeric cohesin).

Sequence similarities

Belongs to the shugoshin family.

Sequence caution

The sequence AAH01339.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH32696.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processattachment of spindle microtubules to kinetochore

Inferred from direct assay Ref.11. Source: UniProtKB

centriole-centriole cohesion

Inferred from direct assay Ref.12. Source: UniProtKB

chromosome segregation

Inferred from direct assay Ref.8. Source: UniProtKB

meiotic chromosome segregation

Inferred from electronic annotation. Source: InterPro

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from direct assay Ref.12. Source: UniProtKB

chromosome, centromeric region

Inferred from direct assay PubMed 16682347. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed chromosome, centromeric region

Inferred from direct assay PubMed 19465021. Source: UniProtKB

condensed nuclear chromosome, centromeric region

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.10Ref.12. Source: UniProtKB

mitotic cohesin complex

Inferred from direct assay PubMed 18084284. Source: MGI

nucleus

Inferred from direct assay. Source: HPA

spindle pole

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP2R5AQ151723EBI-989069,EBI-641666

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5FBB7-1)

Also known as: 1EF; SgoL1-A2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5FBB7-2)

Also known as: 1GH; SgoL1-B2;

The sequence of this isoform differs from the canonical sequence as follows:
     176-176: G → A
     177-428: Missing.
Isoform 3 (identifier: Q5FBB7-3)

Also known as: 1KL; sSGO1; SgoL1-C2;

The sequence of this isoform differs from the canonical sequence as follows:
     159-159: D → A
     160-428: Missing.
Isoform 4 (identifier: Q5FBB7-4)

Also known as: 1CD; SgoL1-B1;

The sequence of this isoform differs from the canonical sequence as follows:
     176-176: G → A
     177-428: Missing.
     522-561: RALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR → SMKQIQ
Isoform 5 (identifier: Q5FBB7-5)

Also known as: 1AB; SgoL1-C1;

The sequence of this isoform differs from the canonical sequence as follows:
     159-159: D → A
     160-428: Missing.
     522-561: RALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR → SMKQIQ
Isoform 6 (identifier: Q5FBB7-6)

Also known as: 1AB; SgoL1-A1;

The sequence of this isoform differs from the canonical sequence as follows:
     522-561: RALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR → SMKQIQ
Isoform 7 (identifier: Q5FBB7-7)

Also known as: 1J;

The sequence of this isoform differs from the canonical sequence as follows:
     177-522: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Shugoshin-like 1
PRO_0000055436

Regions

Region1 – 176176Necessary for interaction with PPP2CA and PPP2R1A
Coiled coil7 – 8983 Potential
Coiled coil273 – 31341 Potential
Motif192 – 2009D-box 1
Motif310 – 3123KEN box
Motif438 – 4469D-box 2
Motif457 – 4659D-box 3

Amino acid modifications

Modified residue141Phosphoserine; by NEK2 Ref.11
Modified residue2561Phosphoserine Ref.16 Ref.17
Modified residue4361Phosphoserine Ref.13
Modified residue5071Phosphoserine; by NEK2 Ref.11 Ref.14 Ref.16

Natural variations

Alternative sequence1591D → A in isoform 3 and isoform 5.
VSP_016790
Alternative sequence160 – 428269Missing in isoform 3 and isoform 5.
VSP_016791
Alternative sequence1761G → A in isoform 2 and isoform 4.
VSP_016792
Alternative sequence177 – 522346Missing in isoform 7.
VSP_016793
Alternative sequence177 – 428252Missing in isoform 2 and isoform 4.
VSP_016794
Alternative sequence522 – 56140RALEV…HICLR → SMKQIQ in isoform 4, isoform 5 and isoform 6.
VSP_016795
Natural variant1711V → A.
Corresponds to variant rs6806241 [ dbSNP | Ensembl ].
VAR_051968
Natural variant3221Q → P.
Corresponds to variant rs9868701 [ dbSNP | Ensembl ].
VAR_051969

Experimental info

Mutagenesis141S → A: Loss of phosphorylation and presence of misaligned chromosomes; when associated with A-507. Ref.11
Mutagenesis611N → I: Loss of interaction with PPP2CA and PPP2R1A and loss of centromeric localization. Ref.8
Mutagenesis731S → A: Loss of proper localization to spindle pole and mitotic spindle. Significant increase in split spindle poles. Ref.12
Mutagenesis1461T → A: Loss of proper localization to spindle pole and mitotic spindle. Significant increase in split spindle poles. Ref.12
Mutagenesis4921K → A: Loss of centromeric localization. Ref.8
Mutagenesis5071S → A: Loss of phosphorylation; and presence of misaligned chromosomes; when associated with A-14. Ref.11

Secondary structure

..... 561
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (1EF) (SgoL1-A2) [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 90CEE0FD2B40CD9C

FASTA56164,190
        10         20         30         40         50         60 
MAKERCLKKS FQDSLEDIKK RMKEKRNKNL AEIGKRRSFI AAPCQIITNT STLLKNYQDN 

        70         80         90        100        110        120 
NKMLVLALEN EKSKVKEAQD IILQLRKECY YLTCQLYALK GKLTSQQTVE PAQNQEICSS 

       130        140        150        160        170        180 
GMDPNSDDSS RNLFVKDLPQ IPLEETELPG QGESFQIEDQ IPTIPQDTLG VDFDSGEAKS 

       190        200        210        220        230        240 
TDNVLPRTVS VRSSLKKHCN SICQFDSLDD FETSHLAGKS FEFERVGFLD PLVNMHIPEN 

       250        260        270        280        290        300 
VQHNACQWSK DQVNLSPKLI QPGTFTKTKE DILESKSEQT KSKQRDTQER KREEKRKANR 

       310        320        330        340        350        360 
RKSKRMSKYK ENKSENKKTV PQKKMHKSVS SNDAYNFNLE EGVHLTPFRQ KVSNDSNREE 

       370        380        390        400        410        420 
NNESEVSLCE SSGSGDDSDD LYLPTCKYIQ NPTSNSDRPV TRPLAKRALK YTDEKETEGS 

       430        440        450        460        470        480 
KPTKTPTTTP PETQQSPHLS LKDITNVSLY PVVKIRRLSL SPKKNKASPA VALPKRRCTA 

       490        500        510        520        530        540 
SVNYKEPTLA SKLRRGDPFT DLCFLNSPIF KQKKDLRRSK KRALEVSPAK EAIFILYYVR 

       550        560 
EFVSRFPDCR KCKLETHICL R 

« Hide

Isoform 2 (1GH) (SgoL1-B2) [UniParc].

Checksum: A8322EF03909112C
Show »

FASTA30935,344
Isoform 3 (1KL) (sSGO1) (SgoL1-C2) [UniParc].

Checksum: 9E23E55D203774D7
Show »

FASTA29233,501
Isoform 4 (1CD) (SgoL1-B1) [UniParc].

Checksum: FF0A4DC6D2F778D5
Show »

FASTA27531,276
Isoform 5 (1AB) (SgoL1-C1) [UniParc].

Checksum: 402AA77D4FDCAA74
Show »

FASTA25829,433
Isoform 6 (1AB) (SgoL1-A1) [UniParc].

Checksum: 7ADB8B2C0B960A92
Show »

FASTA52760,122
Isoform 7 (1J) [UniParc].

Checksum: 6FBC1BCA822DC3F4
Show »

FASTA21524,646

References

« Hide 'large scale' references
[1]"Shugoshin prevents dissociation of cohesin from centromeres during mitosis in vertebrate cells."
McGuinness B.E., Hirota T., Kudo N.R., Peters J.-M., Nasmyth K.
PLoS Biol. 3:433-449(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), FUNCTION, SUBCELLULAR LOCATION.
[2]"Human SgoL1 inhibits precocious separation of sister centromere in early mitosis."
Suzuki H., Akiyama N., Tsuji M., Saito S., Eto Y.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-561 (ISOFORM 6).
Tissue: Cervix, Lung and Mammary gland.
[4]"Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression."
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.
Cancer Immun. 1:4-4(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 250-527 (ISOFORM 6), TISSUE SPECIFICITY.
Tissue: Mammary gland.
[5]"Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization."
Kitajima T.S., Hauf S., Ohsugi M., Yamamoto T., Watanabe Y.
Curr. Biol. 15:353-359(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[6]"Human Bub1 protects centromeric sister-chromatid cohesion through Shugoshin during mitosis."
Tang Z., Sun Y., Harley S.E., Zou H., Yu H.
Proc. Natl. Acad. Sci. U.S.A. 101:18012-18017(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Differential subcellular localizations of two human Sgo1 isoforms: implications in regulation of sister chromatid cohesion and microtubule dynamics."
Wang X., Yang Y., Dai W.
Cell Cycle 5:635-640(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[8]"PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation."
Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.
Dev. Cell 10:575-585(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA; PPP2R1A AND PPP2R5C, MUTAGENESIS OF ASN-61 AND LYS-492.
[9]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA/PPP2CB; PPP2R1B; PPP2R5A; PPP2R5B; PPP2R5C; PPP2R5D; PPP2R5E; SET; LRRC59; RBM10/RBM5; RPL10A; RPL28; RPL7; RPL7A AND RPLP1.
[10]"Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1."
Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., Kallio M.J.
Cell Cycle 6:1579-1585(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[11]"Phosphorylation of human Sgo1 by NEK2A is essential for chromosome congression in mitosis."
Fu G., Ding X., Yuan K., Aikhionbare F., Yao J., Cai X., Jiang K., Yao X.
Cell Res. 17:608-618(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEK2, PHOSPHORYLATION AT SER-14 AND SER-507, MUTAGENESIS OF SER-14 AND SER-507.
[12]"sSgo1, a major splice variant of Sgo1, functions in centriole cohesion where it is regulated by Plk1."
Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z., Dai W.
Dev. Cell 14:331-341(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1, MUTAGENESIS OF SER-73 AND THR-146.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Multiple anaphase-promoting complex/cyclosome degrons mediate the degradation of human Sgo1."
Karamysheva Z., Diaz-Martinez L.A., Crow S.E., Li B., Yu H.
J. Biol. Chem. 284:1772-1780(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DOMAIN KEN BOX AND D-BOX.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB190994 mRNA. Translation: BAD91318.1.
AB193056 mRNA. Translation: BAD95529.1.
AB193057 mRNA. Translation: BAD95530.1.
AB193058 mRNA. Translation: BAD95531.1.
AB193059 mRNA. Translation: BAD95532.1.
AB193060 mRNA. Translation: BAD95533.1.
AB193061 mRNA. Translation: BAD95534.1.
AB193062 mRNA. Translation: BAD95535.1.
AB193063 mRNA. Translation: BAD95536.1.
AB193064 mRNA. Translation: BAD95537.1.
AB193065 mRNA. Translation: BAD95538.1.
AB193066 mRNA. Translation: BAD95539.1.
AB187577 mRNA. Translation: BAD89587.1.
AB187578 mRNA. Translation: BAD89588.1.
AB187579 mRNA. Translation: BAD89589.1.
AB187580 mRNA. Translation: BAD89590.1.
AB187581 mRNA. Translation: BAD89591.1.
AB187582 mRNA. Translation: BAD89592.1.
BC001339 mRNA. Translation: AAH01339.2. Different initiation.
BC017867 mRNA. Translation: AAH17867.1.
BC032696 mRNA. Translation: AAH32696.1. Different initiation.
AF308299 mRNA. Translation: AAG48266.1.
RefSeqNP_001012409.1. NM_001012409.2.
NP_001012410.1. NM_001012410.3.
NP_001012411.1. NM_001012411.2.
NP_001012412.1. NM_001012412.3.
NP_001012413.1. NM_001012413.2.
NP_001186180.1. NM_001199251.1.
NP_001186181.1. NM_001199252.1.
NP_001186182.1. NM_001199253.1.
NP_001186183.1. NM_001199254.1.
NP_001186184.1. NM_001199255.1.
NP_001186185.1. NM_001199256.1.
NP_001186186.1. NM_001199257.1.
NP_612493.1. NM_138484.3.
UniGeneHs.105153.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FGAX-ray2.70D51-96[»]
3Q6SX-ray1.93E/F445-463[»]
4A0IX-ray2.60C/D2-6[»]
ProteinModelPortalQ5FBB7.
SMRQ5FBB7. Positions 51-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127395. 14 interactions.
DIPDIP-36614N.
IntActQ5FBB7. 10 interactions.
MINTMINT-4989914.

PTM databases

PhosphoSiteQ5FBB7.

Polymorphism databases

DMDM74741474.

Proteomic databases

PaxDbQ5FBB7.
PRIDEQ5FBB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263753; ENSP00000263753; ENSG00000129810. [Q5FBB7-1]
ENST00000306698; ENSP00000306581; ENSG00000129810. [Q5FBB7-3]
ENST00000383774; ENSP00000373284; ENSG00000129810. [Q5FBB7-7]
ENST00000412868; ENSP00000406880; ENSG00000129810. [Q5FBB7-6]
ENST00000412997; ENSP00000410458; ENSG00000129810. [Q5FBB7-6]
ENST00000417364; ENSP00000394613; ENSG00000129810. [Q5FBB7-4]
ENST00000419233; ENSP00000394625; ENSG00000129810. [Q5FBB7-2]
ENST00000421451; ENSP00000414129; ENSG00000129810. [Q5FBB7-1]
ENST00000425061; ENSP00000414960; ENSG00000129810. [Q5FBB7-2]
ENST00000429446; ENSP00000404562; ENSG00000129810. [Q5FBB7-5]
ENST00000437051; ENSP00000389034; ENSG00000129810. [Q5FBB7-4]
ENST00000442720; ENSP00000394957; ENSG00000129810. [Q5FBB7-5]
ENST00000443724; ENSP00000413070; ENSG00000129810. [Q5FBB7-7]
ENST00000452020; ENSP00000411200; ENSG00000129810. [Q5FBB7-3]
GeneID151648.
KEGGhsa:151648.
UCSCuc003cbr.3. human. [Q5FBB7-3]
uc003cbs.3. human. [Q5FBB7-1]
uc003cbt.3. human. [Q5FBB7-2]
uc003cbx.3. human. [Q5FBB7-4]
uc003cby.3. human. [Q5FBB7-5]
uc010hfa.3. human. [Q5FBB7-7]

Organism-specific databases

CTD151648.
GeneCardsGC03M020179.
HGNCHGNC:25088. SGOL1.
HPACAB011569.
HPA035501.
MIM609168. gene.
neXtProtNX_Q5FBB7.
PharmGKBPA134988556.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47262.
HOVERGENHBG080777.
InParanoidQ5FBB7.
KOK11580.
OMACYYLTCQ.
OrthoDBEOG7FXZZJ.
PhylomeDBQ5FBB7.
TreeFamTF334213.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ5FBB7.
BgeeQ5FBB7.
GenevestigatorQ5FBB7.

Family and domain databases

InterProIPR011515. Shugoshin_C.
IPR011516. Shugoshin_N.
[Graphical view]
PfamPF07557. Shugoshin_C. 1 hit.
PF07558. Shugoshin_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSGOL1. human.
EvolutionaryTraceQ5FBB7.
GeneWikiSGOL1.
GenomeRNAi151648.
NextBio86755.
PROQ5FBB7.
SOURCESearch...

Entry information

Entry nameSGOL1_HUMAN
AccessionPrimary (citable) accession number: Q5FBB7
Secondary accession number(s): Q588H5 expand/collapse secondary AC list , Q5FBB4, Q5FBB5, Q5FBB6, Q5FBB8, Q8N579, Q8WVL0, Q9BVA8, Q9H275
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM