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SGO1_CAEEL
ID   SGO1_CAEEL              Reviewed;         309 AA.
AC   Q18412; W6SBE3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Shugoshin;
GN   Name=sgo-1 {ECO:0000312|WormBase:C33H5.15b};
GN   ORFNames=C33H5.15 {ECO:0000312|WormBase:C33H5.15b};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 157-GLU--PHE-309.
RX   PubMed=18923084; DOI=10.1101/gad.1691208;
RA   de Carvalho C.E., Zaaijer S., Smolikov S., Gu Y., Schumacher J.M.,
RA   Colaiacovo M.P.;
RT   "LAB-1 antagonizes the Aurora B kinase in C. elegans.";
RL   Genes Dev. 22:2869-2885(2008).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF 157-GLU--PHE-309.
RX   PubMed=30293721; DOI=10.1016/j.cub.2018.08.026;
RA   Bohr T., Nelson C.R., Giacopazzi S., Lamelza P., Bhalla N.;
RT   "Shugoshin is essential for meiotic prophase checkpoints in C. elegans.";
RL   Curr. Biol. 28:3199-3211(2018).
CC   -!- FUNCTION: Component of cell cycle checkpoints, which ensures chromosome
CC       segregation during meiosis and mitosis (PubMed:18923084). During
CC       meiotic prophase, it is involved in the regulation of the synapsis
CC       checkpoint, which monitors whether homologous chromosomes have
CC       synapsed, and the DNA damage response (PubMed:30293721). Plays a
CC       central role in chromosome cohesion during cell division by preventing
CC       premature dissociation of cohesin complex after prophase, when most of
CC       cohesin complex dissociates from chromosomes arms (By similarity).
CC       {ECO:0000250|UniProtKB:Q5FBB7, ECO:0000269|PubMed:18923084,
CC       ECO:0000269|PubMed:30293721}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30293721}.
CC       Chromosome, centromere {ECO:0000269|PubMed:18923084}. Chromosome
CC       {ECO:0000269|PubMed:18923084}. Note=Localizes to nuclei prior to entry
CC       into meiotic prophase and late meiotic prophase (PubMed:30293721).
CC       Localizes to the short arms of bivalent chromosomes from late
CC       diakinesis until anaphase II (PubMed:18923084).
CC       {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:30293721}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b {ECO:0000312|WormBase:C33H5.15b};
CC         IsoId=Q18412-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:C33H5.15a};
CC         IsoId=Q18412-2; Sequence=VSP_060484;
CC   -!- TISSUE SPECIFICITY: Expressed in gonads. {ECO:0000269|PubMed:18923084,
CC       ECO:0000269|PubMed:30293721}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC       {ECO:0000269|PubMed:18923084}.
CC   -!- DISRUPTION PHENOTYPE: Viable with 100% of viable progeny
CC       (PubMed:30293721). Defects in the regulation of the synapsis checkpoint
CC       and DNA damage response in meiosis with an increased rate of
CC       synaptonemal complex disassembly in late pachytene meiotic nuclei and
CC       an increased number of rad-51 positive and hus-1 positive nuclei in
CC       meiotic prophase (PubMed:30293721). Reduces the number of apoptotic
CC       nuclei in the syp-1 mutant background, which is indicative of
CC       inactivation of the synapsis checkpoint or the DNA damage response
CC       (PubMed:30293721). RNAi-mediated knockdown results in chromosome
CC       segregation defects during meiosis and mitosis (PubMed:18923084).
CC       {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:30293721}.
CC   -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR   EMBL; BX284604; CCD66579.1; -; Genomic_DNA.
DR   EMBL; BX284604; CDM63523.1; -; Genomic_DNA.
DR   PIR; T34148; T34148.
DR   RefSeq; NP_001294168.1; NM_001307239.1. [Q18412-1]
DR   RefSeq; NP_501290.2; NM_068889.4. [Q18412-2]
DR   AlphaFoldDB; Q18412; -.
DR   SMR; Q18412; -.
DR   BioGRID; 48020; 2.
DR   IntAct; Q18412; 2.
DR   STRING; 6239.C33H5.15; -.
DR   EPD; Q18412; -.
DR   PaxDb; Q18412; -.
DR   PeptideAtlas; Q18412; -.
DR   EnsemblMetazoa; C33H5.15a.1; C33H5.15a.1; WBGene00016381. [Q18412-2]
DR   EnsemblMetazoa; C33H5.15b.1; C33H5.15b.1; WBGene00016381. [Q18412-1]
DR   EnsemblMetazoa; C33H5.15b.2; C33H5.15b.2; WBGene00016381. [Q18412-1]
DR   GeneID; 183189; -.
DR   KEGG; cel:CELE_C33H5.15; -.
DR   UCSC; C33H5.15; c. elegans. [Q18412-1]
DR   CTD; 183189; -.
DR   WormBase; C33H5.15a; CE34732; WBGene00016381; sgo-1. [Q18412-2]
DR   WormBase; C33H5.15b; CE49542; WBGene00016381; sgo-1. [Q18412-1]
DR   eggNOG; ENOG502RT7Z; Eukaryota.
DR   HOGENOM; CLU_858533_0_0_1; -.
DR   InParanoid; Q18412; -.
DR   OMA; DEPMPFI; -.
DR   OrthoDB; 1385559at2759; -.
DR   PRO; PR:Q18412; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00016381; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   InterPro; IPR011516; Shugoshin_N.
DR   Pfam; PF07558; Shugoshin_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW   Chromosome partition; Coiled coil; Nucleus; Reference proteome.
FT   CHAIN           1..309
FT                   /note="Shugoshin"
FT                   /id="PRO_0000055442"
FT   REGION          165..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          42..77
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        165..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..250
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         268..269
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060484"
FT   MUTAGEN         157..309
FT                   /note="Missing: In tm2443; chromosome segregation defects
FT                   during meiosis and mitosis."
FT                   /evidence="ECO:0000269|PubMed:18923084,
FT                   ECO:0000269|PubMed:30293721"
SQ   SEQUENCE   309 AA;  34567 MW;  D2951E740D04B447 CRC64;
     MDAKTAQSIF GGIVAAKKRP SKEVPEPTIN FKSANDSLVK KNLLLKQQVV QCTKTIEKLR
     NENVALRQKN QELIDGTLEQ RIELIVEQRL KFRLAHAAVL HKKLVQNIQQ TGLELDGLFK
     DLEPEPSGLN TRRPPKLELN LERVDEIPFC QSSMQGEIDE NEIRFDNNSS QSTSSIQNAV
     NGTPRKKQSV GKGRRSELFQ SFNADSSIVE EASTIPTNRR APMLIAPSST PAGPSKPTAR
     KPPTPRFKKP STPALAPQSD DTELSSTIQV RRQRSAKMNI KSLKEPSGKD KLRRPGKHDE
     PMPYINTFF
 
 
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