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MDM1_DANRE
ID   MDM1_DANRE              Reviewed;         656 AA.
AC   Q5RHU7; A3KNZ6; Q5RHU8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nuclear protein MDM1;
GN   Name=mdm1; ORFNames=si:ch211-266a5.6;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Microtubule-binding protein that negatively regulates
CC       centriole duplication. Binds to and stabilizes microtubules.
CC       {ECO:0000250|UniProtKB:Q8TC05}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TC05}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q8TC05}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q8TC05}. Note=Localizes to the centriole lumen.
CC       {ECO:0000250|UniProtKB:Q8TC05}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5RHU7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RHU7-2; Sequence=VSP_027553;
CC   -!- SIMILARITY: Belongs to the MDM1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI11945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX465210; CAI11945.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX465210; CAI11946.1; -; Genomic_DNA.
DR   EMBL; BC134090; AAI34091.1; -; mRNA.
DR   RefSeq; NP_001038285.1; NM_001044820.1. [Q5RHU7-1]
DR   AlphaFoldDB; Q5RHU7; -.
DR   STRING; 7955.ENSDARP00000116078; -.
DR   PaxDb; Q5RHU7; -.
DR   Ensembl; ENSDART00000102010; ENSDARP00000092786; ENSDARG00000045675. [Q5RHU7-1]
DR   GeneID; 557148; -.
DR   KEGG; dre:557148; -.
DR   CTD; 56890; -.
DR   ZFIN; ZDB-GENE-041210-117; mdm1.
DR   eggNOG; ENOG502QVRV; Eukaryota.
DR   GeneTree; ENSGT00390000004106; -.
DR   HOGENOM; CLU_023835_0_0_1; -.
DR   InParanoid; Q5RHU7; -.
DR   OMA; KVNTEYR; -.
DR   OrthoDB; 350018at2759; -.
DR   PhylomeDB; Q5RHU7; -.
DR   TreeFam; TF331015; -.
DR   PRO; PR:Q5RHU7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 4.
DR   Bgee; ENSDARG00000045675; Expressed in testis and 29 other tissues.
DR   ExpressionAtlas; Q5RHU7; baseline.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR   InterPro; IPR029136; MDM1.
DR   PANTHER; PTHR32078; PTHR32078; 2.
DR   Pfam; PF15501; MDM1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..656
FT                   /note="Nuclear protein MDM1"
FT                   /id="PRO_0000299064"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          309..337
FT                   /evidence="ECO:0000255"
FT   MOTIF           161..167
FT                   /note="ST]-E-Y-X(3)-F motif 1; required for efficient
FT                   microtubule binding and stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT   MOTIF           204..210
FT                   /note="ST]-E-Y-X(3)-F motif 2; required for efficient
FT                   microtubule binding and stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT   MOTIF           291..297
FT                   /note="ST]-E-Y-X(3)-F motif 3; required for efficient
FT                   microtubule binding and stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT   COMPBIAS        9..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         289..449
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_027553"
FT   CONFLICT        42
FT                   /note="G -> R (in Ref. 2; AAI34091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="S -> T (in Ref. 2; AAI34091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="Q -> K (in Ref. 2; AAI34091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="V -> L (in Ref. 2; AAI34091)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   656 AA;  74293 MW;  431F6961AABFF89C CRC64;
     MPVRFKGISE YRSKYKGRTS RSRSDSPHRR MRLAGLRSDQ SGITQEPQFI SKRRVPFYPS
     QVSSSFRWEG RDHSQQQLEK SRSPAVSPVL RATSAERQVT PLAPRDPPEG TTAPSQPPQA
     EAAQTSTFAV QKQKQALNGI NHALRMKAGL RSEHQRNGLN SEYQRQFMWK TPVAESPLLA
     AHQMLYSNNR AIPPFKTNPV IMESEYKRSF KGSPLPRPPR LRRDVEQYEV PEFLTESKTP
     EKSKRKKKKK ERPHSRKSSP EQEVAYLQQQ EVKSPHNLKD PSPKVMRKGK TEYRSNFHSP
     LQYSYKDGAW LKIKSAKEEV KELRERAEAY KKRAWGTHFS RQHLNQILSD QNWMWEPSSG
     TSSSSIESEA CRSTSHIIEA LDLARAGSVR ESSSPGHSAS VVVSRRSSSG EVGLPEEPTL
     PVQRKLAWDE EEQLGEREEI VQDRLTDKEG KTRNENGMER NERLNSLESE SLSSAEEGSE
     ASVNGGRLPT PKLKTMQTVQ RTHHDRTTPS IDFNLHYIAK AANGSLPRSS PVAGLTTVDV
     LPMREDVWSD EEVTDYRSLK PPKPSRKQQS SQRHKANAAP PANRIQGTMR NAEFQHNGNL
     GIFRPELFVL PQSDSALSDN DDKMSQISSR SAASCSMASE VLGRAQRRKQ EFWGKS
 
 
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