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Q5FBB7

- SGOL1_HUMAN

UniProt

Q5FBB7 - SGOL1_HUMAN

Protein

Shugoshin-like 1

Gene

SGOL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
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    Functioni

    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.7 Publications

    GO - Molecular functioni

    1. kinase binding Source: MGI
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. attachment of spindle microtubules to kinetochore Source: UniProtKB
    2. centriole-centriole cohesion Source: UniProtKB
    3. chromosome segregation Source: UniProtKB
    4. meiotic chromosome segregation Source: MGI
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shugoshin-like 1
    Short name:
    hSgo1
    Alternative name(s):
    Serologically defined breast cancer antigen NY-BR-85
    Gene namesi
    Name:SGOL1
    Synonyms:SGO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:25088. SGOL1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. chromosome, centromeric region Source: UniProtKB
    3. condensed chromosome, centromeric region Source: UniProtKB
    4. condensed chromosome kinetochore Source: UniProtKB-SubCell
    5. condensed nuclear chromosome, centromeric region Source: Ensembl
    6. cytoplasm Source: HPA
    7. cytosol Source: Reactome
    8. kinetochore Source: UniProtKB
    9. mitotic cohesin complex Source: MGI
    10. nucleus Source: HPA
    11. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141S → A: Loss of phosphorylation and presence of misaligned chromosomes; when associated with A-507. 1 Publication
    Mutagenesisi61 – 611N → I: Loss of interaction with PPP2CA and PPP2R1A and loss of centromeric localization. 1 Publication
    Mutagenesisi73 – 731S → A: Loss of proper localization to spindle pole and mitotic spindle. Significant increase in split spindle poles. 1 Publication
    Mutagenesisi146 – 1461T → A: Loss of proper localization to spindle pole and mitotic spindle. Significant increase in split spindle poles. 1 Publication
    Mutagenesisi492 – 4921K → A: Loss of centromeric localization. 1 Publication
    Mutagenesisi507 – 5071S → A: Loss of phosphorylation; and presence of misaligned chromosomes; when associated with A-14. 1 Publication

    Organism-specific databases

    PharmGKBiPA134988556.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 561561Shugoshin-like 1PRO_0000055436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine; by NEK21 Publication
    Modified residuei256 – 2561Phosphoserine2 Publications
    Modified residuei436 – 4361Phosphoserine1 Publication
    Modified residuei507 – 5071Phosphoserine; by NEK23 Publications

    Post-translational modificationi

    Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1.1 Publication
    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.7 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ5FBB7.
    PaxDbiQ5FBB7.
    PRIDEiQ5FBB7.

    PTM databases

    PhosphoSiteiQ5FBB7.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in testis. Expressed in lung, small intestine, breast, liver and placenta. Strongly overexpressed in 90% of breast cancers tested.1 Publication

    Developmental stagei

    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).1 Publication

    Gene expression databases

    ArrayExpressiQ5FBB7.
    BgeeiQ5FBB7.
    GenevestigatoriQ5FBB7.

    Organism-specific databases

    HPAiCAB011569.
    HPA035501.

    Interactioni

    Subunit structurei

    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 PLK1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP2R5AQ151723EBI-989069,EBI-641666

    Protein-protein interaction databases

    BioGridi127395. 14 interactions.
    DIPiDIP-36614N.
    IntActiQ5FBB7. 10 interactions.
    MINTiMINT-4989914.

    Structurei

    Secondary structure

    1
    561
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi51 – 9343
    Beta strandi448 – 4558

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FGAX-ray2.70D51-96[»]
    3Q6SX-ray1.93E/F445-463[»]
    4A0IX-ray2.60C/D2-6[»]
    ProteinModelPortaliQ5FBB7.
    SMRiQ5FBB7. Positions 51-96.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5FBB7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 176176Necessary for interaction with PPP2CA and PPP2R1AAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili7 – 8983Sequence AnalysisAdd
    BLAST
    Coiled coili273 – 31341Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi192 – 2009D-box 1
    Motifi310 – 3123KEN box
    Motifi438 – 4469D-box 2
    Motifi457 – 4659D-box 3

    Domaini

    The KEN box and D-box 3 are required for its ubiquitination and degradation.1 Publication

    Sequence similaritiesi

    Belongs to the shugoshin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG47262.
    HOVERGENiHBG080777.
    InParanoidiQ5FBB7.
    KOiK11580.
    OMAiCYYLTCQ.
    OrthoDBiEOG7FXZZJ.
    PhylomeDBiQ5FBB7.
    TreeFamiTF334213.

    Family and domain databases

    InterProiIPR011515. Shugoshin_C.
    IPR011516. Shugoshin_N.
    [Graphical view]
    PfamiPF07557. Shugoshin_C. 1 hit.
    PF07558. Shugoshin_N. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5FBB7-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAKERCLKKS FQDSLEDIKK RMKEKRNKNL AEIGKRRSFI AAPCQIITNT    50
    STLLKNYQDN NKMLVLALEN EKSKVKEAQD IILQLRKECY YLTCQLYALK 100
    GKLTSQQTVE PAQNQEICSS GMDPNSDDSS RNLFVKDLPQ IPLEETELPG 150
    QGESFQIEDQ IPTIPQDTLG VDFDSGEAKS TDNVLPRTVS VRSSLKKHCN 200
    SICQFDSLDD FETSHLAGKS FEFERVGFLD PLVNMHIPEN VQHNACQWSK 250
    DQVNLSPKLI QPGTFTKTKE DILESKSEQT KSKQRDTQER KREEKRKANR 300
    RKSKRMSKYK ENKSENKKTV PQKKMHKSVS SNDAYNFNLE EGVHLTPFRQ 350
    KVSNDSNREE NNESEVSLCE SSGSGDDSDD LYLPTCKYIQ NPTSNSDRPV 400
    TRPLAKRALK YTDEKETEGS KPTKTPTTTP PETQQSPHLS LKDITNVSLY 450
    PVVKIRRLSL SPKKNKASPA VALPKRRCTA SVNYKEPTLA SKLRRGDPFT 500
    DLCFLNSPIF KQKKDLRRSK KRALEVSPAK EAIFILYYVR EFVSRFPDCR 550
    KCKLETHICL R 561
    Length:561
    Mass (Da):64,190
    Last modified:March 15, 2005 - v1
    Checksum:i90CEE0FD2B40CD9C
    GO
    Isoform 2 (identifier: Q5FBB7-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:309
    Mass (Da):35,344
    Checksum:iA8322EF03909112C
    GO
    Isoform 3 (identifier: Q5FBB7-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:292
    Mass (Da):33,501
    Checksum:i9E23E55D203774D7
    GO
    Isoform 4 (identifier: Q5FBB7-4) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:275
    Mass (Da):31,276
    Checksum:iFF0A4DC6D2F778D5
    GO
    Isoform 5 (identifier: Q5FBB7-5) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:258
    Mass (Da):29,433
    Checksum:i402AA77D4FDCAA74
    GO
    Isoform 6 (identifier: Q5FBB7-6) [UniParc]FASTAAdd to Basket

    Also known as: 1AB, SgoL1-A1

    The sequence of this isoform differs from the canonical sequence as follows:
         522-561: RALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR → SMKQIQ

    Show »
    Length:527
    Mass (Da):60,122
    Checksum:i7ADB8B2C0B960A92
    GO
    Isoform 7 (identifier: Q5FBB7-7) [UniParc]FASTAAdd to Basket

    Also known as: 1J

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

    Show »
    Length:215
    Mass (Da):24,646
    Checksum:i6FBC1BCA822DC3F4
    GO

    Sequence cautioni

    The sequence AAH01339.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH32696.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711V → A.
    Corresponds to variant rs6806241 [ dbSNP | Ensembl ].
    VAR_051968
    Natural varianti322 – 3221Q → P.
    Corresponds to variant rs9868701 [ dbSNP | Ensembl ].
    VAR_051969

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei159 – 1591D → A in isoform 3 and isoform 5. 3 PublicationsVSP_016790
    Alternative sequencei160 – 428269Missing in isoform 3 and isoform 5. 3 PublicationsVSP_016791Add
    BLAST
    Alternative sequencei176 – 1761G → A in isoform 2 and isoform 4. 2 PublicationsVSP_016792
    Alternative sequencei177 – 522346Missing in isoform 7. 1 PublicationVSP_016793Add
    BLAST
    Alternative sequencei177 – 428252Missing in isoform 2 and isoform 4. 2 PublicationsVSP_016794Add
    BLAST
    Alternative sequencei522 – 56140RALEV…HICLR → SMKQIQ in isoform 4, isoform 5 and isoform 6. 4 PublicationsVSP_016795Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2635.1. [Q5FBB7-3]
    CCDS33716.1. [Q5FBB7-1]
    CCDS46771.1. [Q5FBB7-2]
    CCDS46772.1. [Q5FBB7-5]
    CCDS46773.1. [Q5FBB7-6]
    CCDS46774.1. [Q5FBB7-4]
    CCDS56243.1. [Q5FBB7-7]
    RefSeqiNP_001012409.1. NM_001012409.2. [Q5FBB7-6]
    NP_001012410.1. NM_001012410.3. [Q5FBB7-1]
    NP_001012411.1. NM_001012411.2. [Q5FBB7-4]
    NP_001012412.1. NM_001012412.3. [Q5FBB7-2]
    NP_001012413.1. NM_001012413.2. [Q5FBB7-5]
    NP_001186180.1. NM_001199251.1. [Q5FBB7-6]
    NP_001186181.1. NM_001199252.1. [Q5FBB7-1]
    NP_001186182.1. NM_001199253.1. [Q5FBB7-4]
    NP_001186183.1. NM_001199254.1. [Q5FBB7-2]
    NP_001186184.1. NM_001199255.1. [Q5FBB7-5]
    NP_001186185.1. NM_001199256.1. [Q5FBB7-3]
    NP_001186186.1. NM_001199257.1. [Q5FBB7-7]
    NP_612493.1. NM_138484.3. [Q5FBB7-3]
    XP_006713049.1. XM_006712986.1. [Q5FBB7-6]
    XP_006713050.1. XM_006712987.1. [Q5FBB7-6]
    UniGeneiHs.105153.

    Genome annotation databases

    EnsembliENST00000263753; ENSP00000263753; ENSG00000129810. [Q5FBB7-1]
    ENST00000306698; ENSP00000306581; ENSG00000129810. [Q5FBB7-3]
    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]
    ENST00000437051; ENSP00000389034; ENSG00000129810. [Q5FBB7-4]
    ENST00000442720; ENSP00000394957; ENSG00000129810. [Q5FBB7-5]
    ENST00000443724; ENSP00000413070; ENSG00000129810. [Q5FBB7-7]
    ENST00000452020; ENSP00000411200; ENSG00000129810. [Q5FBB7-3]
    GeneIDi151648.
    KEGGihsa:151648.
    UCSCiuc003cbr.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]

    Polymorphism databases

    DMDMi74741474.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2635.1. [Q5FBB7-3 ]
    CCDS33716.1. [Q5FBB7-1 ]
    CCDS46771.1. [Q5FBB7-2 ]
    CCDS46772.1. [Q5FBB7-5 ]
    CCDS46773.1. [Q5FBB7-6 ]
    CCDS46774.1. [Q5FBB7-4 ]
    CCDS56243.1. [Q5FBB7-7 ]
    RefSeqi NP_001012409.1. NM_001012409.2. [Q5FBB7-6 ]
    NP_001012410.1. NM_001012410.3. [Q5FBB7-1 ]
    NP_001012411.1. NM_001012411.2. [Q5FBB7-4 ]
    NP_001012412.1. NM_001012412.3. [Q5FBB7-2 ]
    NP_001012413.1. NM_001012413.2. [Q5FBB7-5 ]
    NP_001186180.1. NM_001199251.1. [Q5FBB7-6 ]
    NP_001186181.1. NM_001199252.1. [Q5FBB7-1 ]
    NP_001186182.1. NM_001199253.1. [Q5FBB7-4 ]
    NP_001186183.1. NM_001199254.1. [Q5FBB7-2 ]
    NP_001186184.1. NM_001199255.1. [Q5FBB7-5 ]
    NP_001186185.1. NM_001199256.1. [Q5FBB7-3 ]
    NP_001186186.1. NM_001199257.1. [Q5FBB7-7 ]
    NP_612493.1. NM_138484.3. [Q5FBB7-3 ]
    XP_006713049.1. XM_006712986.1. [Q5FBB7-6 ]
    XP_006713050.1. XM_006712987.1. [Q5FBB7-6 ]
    UniGenei Hs.105153.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FGA X-ray 2.70 D 51-96 [» ]
    3Q6S X-ray 1.93 E/F 445-463 [» ]
    4A0I X-ray 2.60 C/D 2-6 [» ]
    ProteinModelPortali Q5FBB7.
    SMRi Q5FBB7. Positions 51-96.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127395. 14 interactions.
    DIPi DIP-36614N.
    IntActi Q5FBB7. 10 interactions.
    MINTi MINT-4989914.

    PTM databases

    PhosphoSitei Q5FBB7.

    Polymorphism databases

    DMDMi 74741474.

    Proteomic databases

    MaxQBi Q5FBB7.
    PaxDbi Q5FBB7.
    PRIDEi Q5FBB7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263753 ; ENSP00000263753 ; ENSG00000129810 . [Q5FBB7-1 ]
    ENST00000306698 ; ENSP00000306581 ; ENSG00000129810 . [Q5FBB7-3 ]
    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 ]
    ENST00000437051 ; ENSP00000389034 ; ENSG00000129810 . [Q5FBB7-4 ]
    ENST00000442720 ; ENSP00000394957 ; ENSG00000129810 . [Q5FBB7-5 ]
    ENST00000443724 ; ENSP00000413070 ; ENSG00000129810 . [Q5FBB7-7 ]
    ENST00000452020 ; ENSP00000411200 ; ENSG00000129810 . [Q5FBB7-3 ]
    GeneIDi 151648.
    KEGGi hsa:151648.
    UCSCi uc003cbr.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

    CTDi 151648.
    GeneCardsi GC03M020179.
    HGNCi HGNC:25088. SGOL1.
    HPAi CAB011569.
    HPA035501.
    MIMi 609168. gene.
    neXtProti NX_Q5FBB7.
    PharmGKBi PA134988556.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47262.
    HOVERGENi HBG080777.
    InParanoidi Q5FBB7.
    KOi K11580.
    OMAi CYYLTCQ.
    OrthoDBi EOG7FXZZJ.
    PhylomeDBi Q5FBB7.
    TreeFami TF334213.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi SGOL1. human.
    EvolutionaryTracei Q5FBB7.
    GeneWikii SGOL1.
    GenomeRNAii 151648.
    NextBioi 86755.
    PROi Q5FBB7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5FBB7.
    Bgeei Q5FBB7.
    Genevestigatori Q5FBB7.

    Family and domain databases

    InterProi IPR011515. Shugoshin_C.
    IPR011516. Shugoshin_N.
    [Graphical view ]
    Pfami PF07557. Shugoshin_C. 1 hit.
    PF07558. Shugoshin_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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].

    Entry informationi

    Entry nameiSGOL1_HUMAN
    AccessioniPrimary (citable) accession number: Q5FBB7
    Secondary accession number(s): Q588H5
    , Q5FBB4, Q5FBB5, Q5FBB6, Q5FBB8, Q8N579, Q8WVL0, Q9BVA8, Q9H275
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3