Q562F6 · SGO2_HUMAN
- ProteinShugoshin 2
- GeneSGO2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1265 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation (By similarity).
Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Involved in centromeric enrichment of AUKRB in prometaphase
Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Involved in centromeric enrichment of AUKRB in prometaphase
Miscellaneous
Shugoshin is Japanese for guardian spirit (as it is known to be a protector of centromeric cohesin).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome, centromeric region | |
Cellular Component | cytosol | |
Cellular Component | kinetochore | |
Cellular Component | mitotic cohesin complex | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Biological Process | cell division | |
Biological Process | chromosome segregation | |
Biological Process | meiotic cell cycle | |
Biological Process | meiotic sister chromatid cohesion |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameShugoshin 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ562F6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: During meiosis I, accumulates at centromeres during diplotene, and colocalizes differentially with the cohesin subunits RAD21 and REC8 at metaphase I centromeres (By similarity).
SGO2 and RAD21 change their relative distributions during telophase I when sister-kinetochore association is lost (By similarity).
During meiosis II, it shows a striking tension-dependent redistribution within centromeres throughout chromosome congression during prometaphase II, as it does during mitosis (By similarity).
In Hela cells, localizes at centromeres throughout prophase until metaphase and disappears at anaphase (PubMed:17485487).
Centromeric localization requires the presence of BUB1 and AUKRB (PubMed:17485487).
SGO2 and RAD21 change their relative distributions during telophase I when sister-kinetochore association is lost (By similarity).
During meiosis II, it shows a striking tension-dependent redistribution within centromeres throughout chromosome congression during prometaphase II, as it does during mitosis (By similarity).
In Hela cells, localizes at centromeres throughout prophase until metaphase and disappears at anaphase (PubMed:17485487).
Centromeric localization requires the presence of BUB1 and AUKRB (PubMed:17485487).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_024784 | 9 | in dbSNP:rs1036533 | |||
Sequence: G → D | ||||||
Natural variant | VAR_057178 | 343 | in dbSNP:rs13417812 | |||
Sequence: E → A | ||||||
Natural variant | VAR_024785 | 496 | in dbSNP:rs17448235 | |||
Sequence: I → V | ||||||
Natural variant | VAR_057179 | 660 | in dbSNP:rs17532665 | |||
Sequence: N → S | ||||||
Natural variant | VAR_057180 | 1099 | in dbSNP:rs11896759 | |||
Sequence: I → T | ||||||
Natural variant | VAR_057181 | 1143 | in dbSNP:rs16833776 | |||
Sequence: H → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,333 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000055439 | 1-1265 | UniProt | Shugoshin 2 | |||
Sequence: MECPVMETGSLFTSGIKRHLKDKRISKTTKLNVSLASKIKTKILNNSSIFKISLKHNNRALAQALSREKENSRRITTEKMLLQKEVEKLNFENTFLRLKLNNLNKKLIDIEALMNNNLITAIEMSSLSEFHQSSFLLSASKKKRISKQCKLMRLPFARVPLTSNDDEDEDKEKMQCDNNIKSKTLPDIPSSGSTTQPLSTQDNSEVLFLKENNQNVYGLDDSEHISSIVDVPPRESHSHSDQSSKTSLMSEMRNAQSIGRRWEKPSPSNVTERKKRGSSWESNNLSADTPCATVLDKQHISSPELNCNNEINGHTNETNTEMQRNKQDLPGLSSESAREPNAECMNQIEDNDDFQLQKTVYDADMDLTASEVSKIVTVSTGIKKKSNKKTNEHGMKTFRKVKDSSSEKKRERSKRQFKNSSDVDIGEKIENRTERSDVLDGKRGAEDPGFIFNNEQLAQMNEQLAQVNELKKMTLQTGFEQGDRENVLCNKKEKRITNEQEETYSLSQSSGKFHQESKFDKGQNSLTCNKSKASRQTFVIHKLEKDNLLPNQKDKVTIYENLDVTNEFHTANLSTKDNGNLCDYGTHNILDLKKYVTDIQPSEQNESNINKLRKKVNRKTEIISGMNHMYEDNDKDVVHGLKKGNFFFKTQEDKEPISENIEVSKELQIPALSTRDNENQCDYRTQNVLGLQKQITNMYPVQQNESKVNKKLRQKVNRKTEIISEVNHLDNDKSIEYTVKSHSLFLTQKDKEIIPGNLEDPSEFETPALSTKDSGNLYDSEIQNVLGVKHGHDMQPACQNDSKIGKKPRLNVCQKSEIIPETNQIYENDNKGVHDLEKDNFFSLTPKDKETISENLQVTNEFQTVDLLIKDNGNLCDYDTQNILELKKYVTDRKSAEQNESKINKLRNKVNWKTEIISEMNQIYEDNDKDAHVQESYTKDLDFKVNKSKQKLECQDIINKHYMEVNSNEKESCDQILDSYKVVKKRKKESSCKAKNILTKAKNKLASQLTESSQTSISLESDLKHITSEADSDPGNPVELCKTQKQSTTTLNKKDLPFVEEIKEGECQVKKVNKMTSKSKKRKTSIDPSPESHEVMERILDSVQGKSTVSEQADKENNLENEKMVKNKPDFYTKAFRSLSEIHSPNIQDSSFDSVREGLVPLSVSSGKNVIIKENFALECSPAFQVSDDEHEKMNKMKFKVNRRTQKSGIGDRPLQDLSNTSFVSNNTAESENKSEDLSSERTSRRRRCTPFYFKEPSLRDKMRR | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 436 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 497 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 845 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1032 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1085 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1089 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1144 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1163 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1187 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1222 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Directly interacts with PPP2CA. Part of an astrin (SPAG5) -kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with CDCA8.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q562F6 | CDCA8 Q53HL2 | 3 | EBI-989213, EBI-979174 | |
BINARY | Q562F6 | MAD2L1 Q13257 | 11 | EBI-989213, EBI-78203 | |
BINARY | Q562F6 | MAD2L1BP Q15013 | 2 | EBI-989213, EBI-712181 | |
BINARY | Q562F6 | PPP1CA P62136 | 4 | EBI-989213, EBI-357253 | |
BINARY | Q562F6 | PPP2CA P67775 | 2 | EBI-989213, EBI-712311 | |
BINARY | Q562F6 | PPP2R5A Q15172 | 3 | EBI-989213, EBI-641666 | |
BINARY | Q562F6-3 | SET Q01105-2 | 3 | EBI-12111430, EBI-7481343 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 69-116 | |||||
Sequence: KENSRRITTEKMLLQKEVEKLNFENTFLRLKLNNLNKKLIDIEALMNN | ||||||
Region | 161-202 | Disordered | ||||
Sequence: LTSNDDEDEDKEKMQCDNNIKSKTLPDIPSSGSTTQPLSTQD | ||||||
Compositional bias | 162-178 | Basic and acidic residues | ||||
Sequence: TSNDDEDEDKEKMQCDN | ||||||
Compositional bias | 179-202 | Polar residues | ||||
Sequence: NIKSKTLPDIPSSGSTTQPLSTQD | ||||||
Region | 230-287 | Disordered | ||||
Sequence: DVPPRESHSHSDQSSKTSLMSEMRNAQSIGRRWEKPSPSNVTERKKRGSSWESNNLSA | ||||||
Compositional bias | 305-334 | Polar residues | ||||
Sequence: LNCNNEINGHTNETNTEMQRNKQDLPGLSS | ||||||
Region | 305-339 | Disordered | ||||
Sequence: LNCNNEINGHTNETNTEMQRNKQDLPGLSSESARE | ||||||
Region | 381-447 | Disordered | ||||
Sequence: GIKKKSNKKTNEHGMKTFRKVKDSSSEKKRERSKRQFKNSSDVDIGEKIENRTERSDVLDGKRGAED | ||||||
Compositional bias | 385-444 | Basic and acidic residues | ||||
Sequence: KSNKKTNEHGMKTFRKVKDSSSEKKRERSKRQFKNSSDVDIGEKIENRTERSDVLDGKRG | ||||||
Coiled coil | 452-476 | |||||
Sequence: FNNEQLAQMNEQLAQVNELKKMTLQ | ||||||
Region | 499-526 | Disordered | ||||
Sequence: EQEETYSLSQSSGKFHQESKFDKGQNSL | ||||||
Coiled coil | 603-626 | |||||
Sequence: EQNESNINKLRKKVNRKTEIISGM | ||||||
Region | 1073-1093 | Disordered | ||||
Sequence: NKMTSKSKKRKTSIDPSPESH | ||||||
Region | 1200-1265 | Disordered | ||||
Sequence: KVNRRTQKSGIGDRPLQDLSNTSFVSNNTAESENKSEDLSSERTSRRRRCTPFYFKEPSLRDKMRR | ||||||
Compositional bias | 1212-1233 | Polar residues | ||||
Sequence: DRPLQDLSNTSFVSNNTAESEN | ||||||
Compositional bias | 1234-1265 | Basic and acidic residues | ||||
Sequence: KSEDLSSERTSRRRRCTPFYFKEPSLRDKMRR |
Sequence similarities
Belongs to the shugoshin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q562F6-1
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.
- Name1
- Length1,265
- Mass (Da)144,739
- Last updated2006-01-10 v2
- Checksum6A678CB3E6DF72D7
Q562F6-2
- Name2
- Differences from canonical
- 1261-1265: DKMRR → E
Q562F6-3
- Name3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JW92 | C9JW92_HUMAN | SGO2 | 87 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 122 | in Ref. 3; BX647433 | ||||
Sequence: I → T | ||||||
Sequence conflict | 145 | in Ref. 3; BX647433 | ||||
Sequence: I → V | ||||||
Compositional bias | 162-178 | Basic and acidic residues | ||||
Sequence: TSNDDEDEDKEKMQCDN | ||||||
Compositional bias | 179-202 | Polar residues | ||||
Sequence: NIKSKTLPDIPSSGSTTQPLSTQD | ||||||
Sequence conflict | 193 | in Ref. 1; AAM21971 | ||||
Sequence: S → R | ||||||
Sequence conflict | 205 | in Ref. 1; AAM21971 | ||||
Sequence: E → G | ||||||
Sequence conflict | 215 | in Ref. 1; AAM21971 | ||||
Sequence: N → H | ||||||
Alternative sequence | VSP_016798 | 235-247 | in isoform 3 | |||
Sequence: ESHSHSDQSSKTS → GEIVLKIHFEYLY | ||||||
Alternative sequence | VSP_016799 | 248-1265 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 305-334 | Polar residues | ||||
Sequence: LNCNNEINGHTNETNTEMQRNKQDLPGLSS | ||||||
Compositional bias | 385-444 | Basic and acidic residues | ||||
Sequence: KSNKKTNEHGMKTFRKVKDSSSEKKRERSKRQFKNSSDVDIGEKIENRTERSDVLDGKRG | ||||||
Sequence conflict | 450-451 | in Ref. 1; AAM21971 | ||||
Sequence: FI → LF | ||||||
Compositional bias | 1212-1233 | Polar residues | ||||
Sequence: DRPLQDLSNTSFVSNNTAESEN | ||||||
Compositional bias | 1234-1265 | Basic and acidic residues | ||||
Sequence: KSEDLSSERTSRRRRCTPFYFKEPSLRDKMRR | ||||||
Sequence conflict | 1243 | in Ref. 2; BAB71617 | ||||
Sequence: T → A | ||||||
Alternative sequence | VSP_016800 | 1261-1265 | in isoform 2 | |||
Sequence: DKMRR → E |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY094614 EMBL· GenBank· DDBJ | AAM21971.1 EMBL· GenBank· DDBJ | mRNA | ||
AK057940 EMBL· GenBank· DDBJ | BAB71617.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK095291 EMBL· GenBank· DDBJ | BAC04524.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BX647433 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AC012459 EMBL· GenBank· DDBJ | AAY24310.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC080164 EMBL· GenBank· DDBJ | AAY24264.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC035764 EMBL· GenBank· DDBJ | AAH35764.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC048349 EMBL· GenBank· DDBJ | AAH48349.1 EMBL· GenBank· DDBJ | mRNA | ||
BC092412 EMBL· GenBank· DDBJ | AAH92412.1 EMBL· GenBank· DDBJ | mRNA |