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CCNE_CAEBR
ID   CCNE_CAEBR              Reviewed;         518 AA.
AC   Q8MUK3; A8XGJ4; Q61CT3;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=G1/S-specific cyclin-E;
GN   Name=cye-1; ORFNames=CBG12774;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000312|EMBL:AAM78548.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12606285; DOI=10.1016/s0012-1606(02)00032-5;
RA   Brodigan T.M., Liu J., Park M., Kipreos E.T., Krause M.;
RT   "Cyclin E expression during development in Caenorhabditis elegans.";
RL   Dev. Biol. 254:102-115(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition. In association with cdk-2, regulates proliferation,
CC       quiescent state and cell fate during the development of several cell
CC       lineages. In the embryo, initiates the establishment of cell polarity
CC       through the recruitment of the centrosomal proteins spd-2 and spd-5
CC       during prophase. During the development of the vulva, controls the
CC       onset of vulval cell terminal differentiation by controlling the
CC       duration of G1 phase. During hypoderm development at early larval
CC       stages, controls syncytial fate of seam cell daughter cells. Involved
CC       in the progression of cell division in the intestinal lineage in
CC       larvae, and in particular in endoreplication, a specific growth pathway
CC       in the intestinal epithelium, required for feeding and gut development
CC       in growing larvae. By controlling the activity of translational
CC       repressor gld-1, regulates the pool of germline stem cells and the size
CC       of the mitotic zone by preventing entry into meiosis. In addition,
CC       repression of expression by gld-1 prevents mitosis re-entry in meiotic
CC       germline cells. {ECO:0000250|UniProtKB:O01501}.
CC   -!- SUBUNIT: Interacts with a member of the CDK2/CDK protein kinases to
CC       form a serine/threonine kinase holoenzyme complex. The cyclin subunit
CC       imparts substrate specificity to the complex (By similarity).
CC       {ECO:0000250|UniProtKB:P24864}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O01501}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC       centriole {ECO:0000250|UniProtKB:O01501}. Note=Co-localizes with cdk-2,
CC       in the sperm centrioles before the first embryonic mitosis and then to
CC       the male and female nuclei upon entry into mitosis.
CC       {ECO:0000250|UniProtKB:O01501}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF520617; AAM78548.1; -; mRNA.
DR   EMBL; HE600940; CAP31700.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MUK3; -.
DR   SMR; Q8MUK3; -.
DR   STRING; 6238.CBG12774; -.
DR   EnsemblMetazoa; CBG12774a.1; CBG12774a.1; WBGene00033670.
DR   WormBase; CBG12774a; CBP37596; WBGene00033670; Cbr-cye-1.
DR   eggNOG; KOG0655; Eukaryota.
DR   HOGENOM; CLU_522999_0_0_1; -.
DR   InParanoid; Q8MUK3; -.
DR   OMA; VLVDWMM; -.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0097134; C:cyclin E1-CDK2 complex; IBA:GO_Central.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0042023; P:DNA endoreduplication; IEA:EnsemblMetazoa.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0007281; P:germ cell development; IEA:EnsemblMetazoa.
DR   GO; GO:0051729; P:germline cell cycle switching, mitotic to meiotic cell cycle; IEA:EnsemblMetazoa.
DR   GO; GO:0048815; P:hermaphrodite genitalia morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0051782; P:negative regulation of cell division; IEA:EnsemblMetazoa.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:EnsemblMetazoa.
DR   GO; GO:1904781; P:positive regulation of protein localization to centrosome; IEA:EnsemblMetazoa.
DR   GO; GO:0040026; P:positive regulation of vulval development; IEA:EnsemblMetazoa.
DR   GO; GO:0009791; P:post-embryonic development; IEA:EnsemblMetazoa.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:EnsemblMetazoa.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:EnsemblMetazoa.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR   GO; GO:1904776; P:regulation of protein localization to cell cortex; IEA:EnsemblMetazoa.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Cytoplasm; Cytoskeleton; Meiosis;
KW   Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..518
FT                   /note="G1/S-specific cyclin-E"
FT                   /id="PRO_0000080457"
FT   REGION          1..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..193
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  59470 MW;  A084943B8E8891D3 CRC64;
     MAGRKSSRTT GEPVKKAERK SAILSPHDEL RERLLETSLD VKENIPERSS STRNESVGSQ
     RSDCSESRKR RSTEKGPVAK RPSTEKKGNG SRDDSFSSVF SEDRETESSV GSTSSRTRGQ
     PLPAMPEEEE SLDGSSDHNA ESEESRETPQ SDEHDGFEED GDVEDDVSSD VNDEEDEYDE
     YEEDEETEDE FDLPLQNDDF AVTKRLMNDR HMIDAPSLLS YGKCEGIGSP TKVWSLMVKR
     DDIPRATRQL LRNHPDMTIN MRRVLVDWMM ECCDVEKLHR ETFHLAVDYA DRFLESTREE
     VISENFQLVG TAALFIAAKY EEIYPPKCAD LAALTDGAFS CDDICRMESI VAKDLKWSFG
     PITSVQWLST YLQLLGTGKK NNDHFEEGNM YIPELLRSEY LRMVRILDYL LSDIDSFNFS
     YRTIAAAVLF VNYDPRSAVE KATGFIYEQL RNVIDYVTPI CRAYDRFTQE HVPKDIIPDY
     APAEDAHNIQ VHIKHYEVDP YVEKERERRH RRGPNRRL
 
 
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