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CSC1_CAEEL
ID   CSC1_CAEEL              Reviewed;         249 AA.
AC   O45952;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Chromosome segregation and cytokinesis defective protein 1;
GN   Name=csc-1; ORFNames=Y48E1B.12;
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, IDENTIFICATION IN THE CHROMOSOMAL PASSENGER COMPLEX, INTERACTION
RP   WITH AIR-2; BIR-1 AND ICP-1, AND SUBCELLULAR LOCATION.
RX   PubMed=12707312; DOI=10.1083/jcb.200207117;
RA   Romano A., Guse A., Krascenicova I., Schnabel H., Schnabel R., Glotzer M.;
RT   "CSC-1: a subunit of the Aurora B kinase complex that binds to the
RT   survivin-like protein BIR-1 and the incenp-like protein ICP-1.";
RL   J. Cell Biol. 161:229-236(2003).
CC   -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC       complex that acts as a key regulator of chromosome segregation and
CC       cytokinesis during mitosis. The CPC complex has essential functions at
CC       the centromere in ensuring correct chromosome alignment and
CC       segregation. In the complex, it may be required to direct the Aurora
CC       B/air-2 to centromeric DNA. {ECO:0000269|PubMed:12707312}.
CC   -!- SUBUNIT: Component of the CPC complex which consists of icp-1; csc-1;
CC       bir-1 and air-2. Within the complex interacts with Aurora B/air-2, bir-
CC       1 and icp-1. {ECO:0000269|PubMed:12707312}.
CC   -!- INTERACTION:
CC       O45952; Q9BIC1: afd-1; NbExp=2; IntAct=EBI-328477, EBI-317844;
CC       O45952; O17583: lin-10; NbExp=2; IntAct=EBI-328477, EBI-313389;
CC       O45952; C1P635: magi-1; NbExp=2; IntAct=EBI-328477, EBI-2917046;
CC       O45952; P90976; NbExp=2; IntAct=EBI-328477, EBI-2918984;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12707312}.
CC       Chromosome, centromere {ECO:0000269|PubMed:12707312}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:12707312}. Note=Localizes on
CC       chromosome arms and inner centromeres from prophase through metaphase
CC       and then transferring to the central spindle from anaphase through
CC       cytokinesis.
CC   -!- SIMILARITY: Belongs to the borealin family. Highly divergent.
CC       {ECO:0000305}.
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DR   EMBL; Z93393; CAB07696.1; -; Genomic_DNA.
DR   PIR; T27019; T27019.
DR   RefSeq; NP_496856.1; NM_064455.4.
DR   AlphaFoldDB; O45952; -.
DR   SMR; O45952; -.
DR   BioGRID; 40295; 5.
DR   ComplexPortal; CPX-3461; Chromosomal passenger complex.
DR   DIP; DIP-26942N; -.
DR   IntAct; O45952; 6.
DR   STRING; 6239.Y48E1B.12; -.
DR   iPTMnet; O45952; -.
DR   EPD; O45952; -.
DR   PaxDb; O45952; -.
DR   PeptideAtlas; O45952; -.
DR   EnsemblMetazoa; Y48E1B.12.1; Y48E1B.12.1; WBGene00000804.
DR   GeneID; 175006; -.
DR   KEGG; cel:CELE_Y48E1B.12; -.
DR   UCSC; Y48E1B.12.1; c. elegans.
DR   CTD; 175006; -.
DR   WormBase; Y48E1B.12; CE14874; WBGene00000804; csc-1.
DR   eggNOG; ENOG502R84G; Eukaryota.
DR   HOGENOM; CLU_116430_0_0_1; -.
DR   InParanoid; O45952; -.
DR   OMA; HRNEIIT; -.
DR   OrthoDB; 1592329at2759; -.
DR   SignaLink; O45952; -.
DR   PRO; PR:O45952; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000804; Expressed in embryo and 4 other tissues.
DR   GO; GO:0032133; C:chromosome passenger complex; IPI:ComplexPortal.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:1990385; C:meiotic spindle midzone; IDA:WormBase.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal.
DR   GO; GO:1990023; C:mitotic spindle midzone; IDA:WormBase.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR   GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR   GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:WormBase.
DR   GO; GO:1990386; P:mitotic cleavage furrow ingression; IMP:WormBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; IMP:WormBase.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; IC:ComplexPortal.
DR   GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR   GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..249
FT                   /note="Chromosome segregation and cytokinesis defective
FT                   protein 1"
FT                   /id="PRO_0000247084"
FT   REGION          70..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          12..48
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        111..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  26782 MW;  CAF155EB772416F5 CRC64;
     MPPRKIKKDP AVVAMADTLE TRVKDLLEEY KKKLREVALQ TAKAESDRII ATIKPKYRDM
     PIMEFLASPP DDFYIESGEE EEEGEAAVAV KQELPSEPDM EIDDAAAAQK TSIPIGQNSG
     RNTVQVKQEP EIDDDAAHET SIPIAPSGQN SGRNTAADEH RRNEIITPAG QVLPLPTLQP
     EKPFRAPHVD EEIAFSVNGS PLVLAGRTTA TAAGKENRKK SKKSGAASKK AAAAAGPLQP
     ETENAGTSV
 
 
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