位置:首页 > 蛋白库 > Z600_DROME
Z600_DROME
ID   Z600_DROME              Reviewed;          90 AA.
AC   P22469; A0JQ32; Q4V3M0; Q9VUP1;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Protein Z600 {ECO:0000303|PubMed:2497054};
DE   AltName: Full=Protein Fruhstart {ECO:0000303|PubMed:10850494};
GN   Name=Z600 {ECO:0000303|PubMed:2497054, ECO:0000312|FlyBase:FBgn0004052};
GN   Synonyms=frs {ECO:0000303|PubMed:10850494};
GN   ORFNames=CG17962 {ECO:0000312|FlyBase:FBgn0004052};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2497054; DOI=10.1101/gad.3.2.232;
RA   Schulz R.A., Butler B.A.;
RT   "Overlapping genes of Drosophila melanogaster: organization of the z600-
RT   gonadal-Eip28/29 gene cluster.";
RL   Genes Dev. 3:232-242(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=2478402; DOI=10.1016/0012-1606(89)90143-7;
RA   Schulz R.A., Miksch J.L.;
RT   "Dorsal expression of the Drosophila z600 gene during early
RT   embryogenesis.";
RL   Dev. Biol. 136:211-221(1989).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2125289; DOI=10.1016/0378-1119(90)90257-r;
RA   Galewsky S., Xie X.L., Schulz R.A.;
RT   "The Drosophila melanogaster z600 gene encodes a chromatin-associated
RT   protein synthesized in the syncytial blastoderm.";
RL   Gene 96:227-232(1990).
RN   [7]
RP   FUNCTION.
RX   PubMed=10850494; DOI=10.1016/s0092-8674(00)80862-4;
RA   Grosshans J., Wieschaus E.;
RT   "A genetic link between morphogenesis and cell division during formation of
RT   the ventral furrow in Drosophila.";
RL   Cell 101:523-531(2000).
RN   [8]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=12919679; DOI=10.1016/s1534-5807(03)00208-9;
RA   Grosshans J., Mueller H.A.J., Wieschaus E.;
RT   "Control of cleavage cycles in Drosophila embryos by fruhstart.";
RL   Dev. Cell 5:285-294(2003).
RN   [9]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH CYCA AND CDK1, INTERACTION WITH
RP   CYCE, PHOSPHORYLATION AT THR-22 AND THR-48, AND MUTAGENESIS OF LYS-86 AND
RP   LEU-88.
RX   PubMed=17431409; DOI=10.1038/sj.embor.7400948;
RA   Gawlinski P., Nikolay R., Goursot C., Lawo S., Chaurasia B., Herz H.M.,
RA   Kussler-Schneider Y., Ruppert T., Mayer M., Grosshans J.;
RT   "The Drosophila mitotic inhibitor Fruehstart specifically binds to the
RT   hydrophobic patch of cyclins.";
RL   EMBO Rep. 8:490-496(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Cell cycle regulator that is involved in modulating and
CC       adjusting cell proliferation according to the requirements of the
CC       developmental program (PubMed:10850494, PubMed:12919679,
CC       PubMed:17431409). Interacts with mitotic Cdk1-cyclin complexes to
CC       inhibit mitotic entry at the G2/M transition (PubMed:17431409). Likely
CC       to function by binding to the hydrophobic patch of cyclins to interfere
CC       with the interaction between the complex and certain Cdk1 substrates
CC       (PubMed:17431409). At the mid-blastula transition, involved in the cell
CC       cycle arrest in G2 of cycle 14 by delaying mitosis and thus reducing
CC       cell proliferation allowing cell fate specification and morphogenesis
CC       to take place (PubMed:12919679). Acts downstream or in parallel to the
CC       checkpoint regulator grp which is also required for the cell cycle
CC       pause at cycle 14 (PubMed:12919679). During gastrulation, delays
CC       mitosis in the ventral region of the embryonic mesoderm thus allowing
CC       invagination to be completed before cell division takes place
CC       (PubMed:10850494, PubMed:12919679, PubMed:17431409).
CC       {ECO:0000269|PubMed:10850494, ECO:0000269|PubMed:12919679,
CC       ECO:0000269|PubMed:17431409}.
CC   -!- SUBUNIT: Component of the Frs-CycA-Cdk1 complex composed of Z600, CycA
CC       and Cdk1. Interacts preferentially with CycA (via C-terminus) but is
CC       also able to interact (via C-terminus) with CycE (via C-terminus).
CC       {ECO:0000269|PubMed:17431409}.
CC   -!- INTERACTION:
CC       P22469; P14785: CycA; NbExp=4; IntAct=EBI-7376821, EBI-240333;
CC       P22469; P54733: CycE; NbExp=3; IntAct=EBI-7376821, EBI-203549;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2125289}.
CC       Note=Associates with chromatin in the syncytial blastoderm.
CC       {ECO:0000269|PubMed:2125289}.
CC   -!- DEVELOPMENTAL STAGE: Not detected until cycle 14 of embryogenesis when
CC       the cleavage cycles are completed (at protein level) (PubMed:12919679).
CC       Expression levels peak 15-30 min after cellularization and decrease
CC       during late cellularization and gastrulation (at protein level)
CC       (PubMed:12919679). Expressed until stage 9 in an area of dorsal cells
CC       that are probably the amnioserosa anlage (at protein level)
CC       (PubMed:12919679). At cycle 13, uniform expression throughout the
CC       cortex with expression levels increasing during stage 14
CC       (PubMed:2478402). During cellularization expression localizes dorsally
CC       and posteriorly (PubMed:2478402). During gastrulation expression
CC       persists in dorsal regions of the embryo and by germ band extension
CC       expression is concentrated anterior to the amnioproctodeal invagination
CC       and posterior to the forming cephalic furrow (PubMed:2478402).
CC       {ECO:0000269|PubMed:12919679, ECO:0000269|PubMed:2478402}.
CC   -!- DISRUPTION PHENOTYPE: Most embryos display premature mitosis resulting
CC       in defective invagination of the mesoderm during gastrulation. A small
CC       percentage of embryos also display an extra nuclear division prior to
CC       cellularization. {ECO:0000269|PubMed:12919679}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X58286; CAA41222.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF49634.1; -; Genomic_DNA.
DR   EMBL; BT023336; AAY55752.1; -; mRNA.
DR   EMBL; BT029402; ABK57059.1; -; mRNA.
DR   PIR; A30172; A30172.
DR   RefSeq; NP_524083.2; NM_079359.4.
DR   AlphaFoldDB; P22469; -.
DR   BioGRID; 64994; 11.
DR   IntAct; P22469; 13.
DR   MINT; P22469; -.
DR   STRING; 7227.FBpp0075304; -.
DR   iPTMnet; P22469; -.
DR   PaxDb; P22469; -.
DR   DNASU; 39673; -.
DR   EnsemblMetazoa; FBtr0075549; FBpp0075304; FBgn0004052.
DR   GeneID; 39673; -.
DR   KEGG; dme:Dmel_CG17962; -.
DR   UCSC; CG17962-RA; d. melanogaster.
DR   CTD; 39673; -.
DR   FlyBase; FBgn0004052; Z600.
DR   VEuPathDB; VectorBase:FBgn0004052; -.
DR   eggNOG; ENOG502TF3Q; Eukaryota.
DR   HOGENOM; CLU_2443232_0_0_1; -.
DR   InParanoid; P22469; -.
DR   OMA; KRECYSE; -.
DR   OrthoDB; 1606793at2759; -.
DR   PhylomeDB; P22469; -.
DR   SignaLink; P22469; -.
DR   BioGRID-ORCS; 39673; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Z600; fly.
DR   GenomeRNAi; 39673; -.
DR   PRO; PR:P22469; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004052; Expressed in amnioserosa primordium (Drosophila) and 7 other tissues.
DR   Genevisible; P22469; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030332; F:cyclin binding; IPI:FlyBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007369; P:gastrulation; NAS:FlyBase.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR   GO; GO:0045839; P:negative regulation of mitotic nuclear division; IMP:FlyBase.
DR   GO; GO:0007370; P:ventral furrow formation; IGI:FlyBase.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..90
FT                   /note="Protein Z600"
FT                   /id="PRO_0000066559"
FT   REGION          46..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17431409"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17431409,
FT                   ECO:0000269|PubMed:18327897"
FT   MUTAGEN         86
FT                   /note="K->A: No ventral furrow formation during
FT                   gastrulation and reduced binding to CycA; when associated
FT                   with A-88."
FT                   /evidence="ECO:0000269|PubMed:17431409"
FT   MUTAGEN         88
FT                   /note="L->A: No ventral furrow formation during
FT                   gastrulation and reduced binding to CycA; when associated
FT                   with A-86."
FT                   /evidence="ECO:0000269|PubMed:17431409"
FT   CONFLICT        27
FT                   /note="H -> N (in Ref. 1; CAA41222)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   90 AA;  10530 MW;  19054C5965EE9109 CRC64;
     MSSTNETNQV LQRLNSLKIV ETPKEQHEFG KRECYSLDSK KYSLVPATPS SSGHGKFQTE
     LKKRRKNKLN RMYTYEADKN FIKARKSLNF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024