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Q5FBB7

- SGOL1_HUMAN

UniProt

Q5FBB7 - SGOL1_HUMAN

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Protein

Shugoshin-like 1

Gene

SGOL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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 nuclear chromosome, centromeric region Source: Ensembl
  5. cytoplasm Source: HPA
  6. cytosol Source: Reactome
  7. kinetochore Source: UniProtKB
  8. mitotic cohesin complex Source: MGI
  9. nucleus Source: HPA
  10. spindle pole Source: UniProtKB
Complete GO annotation...

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

BgeeiQ5FBB7.
ExpressionAtlasiQ5FBB7. baseline and differential.
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 – 9343Combined sources
Beta strandi448 – 4558Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000014987.
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

        10         20         30         40         50
MAKERCLKKS FQDSLEDIKK RMKEKRNKNL AEIGKRRSFI AAPCQIITNT
60 70 80 90 100
STLLKNYQDN NKMLVLALEN EKSKVKEAQD IILQLRKECY YLTCQLYALK
110 120 130 140 150
GKLTSQQTVE PAQNQEICSS GMDPNSDDSS RNLFVKDLPQ IPLEETELPG
160 170 180 190 200
QGESFQIEDQ IPTIPQDTLG VDFDSGEAKS TDNVLPRTVS VRSSLKKHCN
210 220 230 240 250
SICQFDSLDD FETSHLAGKS FEFERVGFLD PLVNMHIPEN VQHNACQWSK
260 270 280 290 300
DQVNLSPKLI QPGTFTKTKE DILESKSEQT KSKQRDTQER KREEKRKANR
310 320 330 340 350
RKSKRMSKYK ENKSENKKTV PQKKMHKSVS SNDAYNFNLE EGVHLTPFRQ
360 370 380 390 400
KVSNDSNREE NNESEVSLCE SSGSGDDSDD LYLPTCKYIQ NPTSNSDRPV
410 420 430 440 450
TRPLAKRALK YTDEKETEGS KPTKTPTTTP PETQQSPHLS LKDITNVSLY
460 470 480 490 500
PVVKIRRLSL SPKKNKASPA VALPKRRCTA SVNYKEPTLA SKLRRGDPFT
510 520 530 540 550
DLCFLNSPIF KQKKDLRRSK KRALEVSPAK EAIFILYYVR EFVSRFPDCR
560
KCKLETHICL R
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. Curated
The sequence AAH32696.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00390000014987.
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

Bgeei Q5FBB7.
ExpressionAtlasi Q5FBB7. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 100 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