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CE152_MOUSE
ID   CE152_MOUSE             Reviewed;        1736 AA.
AC   A2AUM9; Q69ZV8; Q8R0X1;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Centrosomal protein of 152 kDa;
DE            Short=Cep152;
GN   Name=Cep152; Synonyms=Kiaa0912;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1010-1736.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1714, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   INTERACTION WITH CEP63 AND DEUP1, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=24240477; DOI=10.1038/ncb2880;
RA   Zhao H., Zhu L., Zhu Y., Cao J., Li S., Huang Q., Xu T., Huang X., Yan X.,
RA   Zhu X.;
RT   "The Cep63 paralogue Deup1 enables massive de novo centriole biogenesis for
RT   vertebrate multiciliogenesis.";
RL   Nat. Cell Biol. 15:1434-1444(2013).
CC   -!- FUNCTION: Necessary for centrosome duplication; the function seems also
CC       to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled
CC       complex at the centrosome that recruits CDK2 required for centriole
CC       duplication (By similarity). Acts as a molecular scaffold facilitating
CC       the interaction of PLK4 and CENPJ, 2 molecules involved in centriole
CC       formation (By similarity). Proposed to snatch PLK4 away from PLK4:CEP92
CC       complexes in early G1 daughter centriole and to reposition PLK4 at the
CC       outer boundary of a newly forming CEP152 ring structure (By
CC       similarity). Also plays a key role in deuterosome-mediated centriole
CC       amplification in multiciliated that can generate more than 100
CC       centrioles (PubMed:24240477). Overexpression of cep152 can drive
CC       amplification of centrioles. {ECO:0000250|UniProtKB:O94986,
CC       ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:24240477}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with PLK4; the interaction is
CC       mutally exclusive with a PLK4:CEP192 interaction. Interacts (via C-
CC       terminus) with CENPJ (via-N-terminus). Interacts with CINP. Interacts
CC       with CDK5RAP2, WDR62, CEP63 and CEP131. CEP63, CDK5RAP2, CEP152, WDR62
CC       are proposed to form a stepwise assembled complex at the centrosome
CC       forming a ring near parental centrioles (By similarity). Interacts with
CC       DEUP1; this interaction recruits CEP152 to the deuterosome. The
CC       interactions with CEP63 and DEUP1 are mutually exclusive
CC       (PubMed:24240477). {ECO:0000250|UniProtKB:O94986,
CC       ECO:0000269|PubMed:24240477}.
CC   -!- INTERACTION:
CC       A2AUM9; Q3UPP8: Cep63; NbExp=2; IntAct=EBI-2554268, EBI-16081652;
CC       A2AUM9; Q7M6Y5: Deup1; NbExp=2; IntAct=EBI-2554268, EBI-16081624;
CC       A2AUM9; Q96MT8: CEP63; Xeno; NbExp=3; IntAct=EBI-2554268, EBI-741977;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:O94986}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:O94986}. Note=Colocalizes with CDK5RAP2, WDR62
CC       and CEP63 in a discrete ring around the proximal end of the parental
CC       centriole (By similarity). At this site, a cohesive structure is
CC       predicted to engage parental centrioles and procentrioles (By
CC       similarity). Localizes to the deuterosome (PubMed:24240477). Localizes
CC       to pericentriolar material (PCM) (By similarity).
CC       {ECO:0000250|UniProtKB:O94986, ECO:0000269|PubMed:24240477}.
CC   -!- SIMILARITY: Belongs to the CEP152 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32338.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK173060; BAD32338.1; ALT_INIT; mRNA.
DR   EMBL; AL928930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX321866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026366; AAH26366.1; -; mRNA.
DR   CCDS; CCDS38229.1; -.
DR   RefSeq; NP_001074560.1; NM_001081091.1.
DR   AlphaFoldDB; A2AUM9; -.
DR   SMR; A2AUM9; -.
DR   BioGRID; 221186; 86.
DR   ComplexPortal; CPX-1160; CEP152-PLK4 complex.
DR   DIP; DIP-56915N; -.
DR   IntAct; A2AUM9; 85.
DR   STRING; 10090.ENSMUSP00000087208; -.
DR   iPTMnet; A2AUM9; -.
DR   PhosphoSitePlus; A2AUM9; -.
DR   EPD; A2AUM9; -.
DR   jPOST; A2AUM9; -.
DR   MaxQB; A2AUM9; -.
DR   PaxDb; A2AUM9; -.
DR   PeptideAtlas; A2AUM9; -.
DR   PRIDE; A2AUM9; -.
DR   ProteomicsDB; 281444; -.
DR   Antibodypedia; 50528; 188 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000089776; ENSMUSP00000087208; ENSMUSG00000068394.
DR   GeneID; 99100; -.
DR   KEGG; mmu:99100; -.
DR   UCSC; uc008mcs.1; mouse.
DR   CTD; 22995; -.
DR   MGI; MGI:2139083; Cep152.
DR   VEuPathDB; HostDB:ENSMUSG00000068394; -.
DR   eggNOG; ENOG502QT0E; Eukaryota.
DR   GeneTree; ENSGT00950000182870; -.
DR   HOGENOM; CLU_003346_0_0_1; -.
DR   InParanoid; A2AUM9; -.
DR   OMA; HHKADIL; -.
DR   OrthoDB; 243447at2759; -.
DR   PhylomeDB; A2AUM9; -.
DR   TreeFam; TF332017; -.
DR   Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR   BioGRID-ORCS; 99100; 6 hits in 77 CRISPR screens.
DR   PRO; PR:A2AUM9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AUM9; protein.
DR   Bgee; ENSMUSG00000068394; Expressed in ventricular system choroidal fissure and 196 other tissues.
DR   Genevisible; A2AUM9; MM.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR   GO; GO:0120098; C:procentriole; ISO:MGI.
DR   GO; GO:0120099; C:procentriole replication complex; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR   GO; GO:0051298; P:centrosome duplication; ISO:MGI.
DR   GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IMP:UniProtKB.
DR   InterPro; IPR029598; Cep152.
DR   PANTHER; PTHR10337:SF6; PTHR10337:SF6; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1736
FT                   /note="Centrosomal protein of 152 kDa"
FT                   /id="PRO_0000424820"
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..60
FT                   /note="Interaction with PLK4"
FT                   /evidence="ECO:0000250|UniProtKB:O94986"
FT   REGION          571..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1416..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1543..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1574..1614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1677..1736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          228..481
FT                   /evidence="ECO:0000255"
FT   COILED          552..651
FT                   /evidence="ECO:0000255"
FT   COILED          692..776
FT                   /evidence="ECO:0000255"
FT   COILED          835..868
FT                   /evidence="ECO:0000255"
FT   COILED          950..1075
FT                   /evidence="ECO:0000255"
FT   COILED          1205..1315
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        24..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1456..1473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1547..1561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1577..1613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1677..1713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1720..1736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1277
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O94986"
FT   MOD_RES         1714
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   1736 AA;  196534 MW;  16D6433AFFDEBA14 CRC64;
     MSLEFGSVAL QTQNEDEEFD KEDFEREKEL QQLLTDLPHD MLDDELSSPE RHDSDCSMDG
     RAAEPHPSEH LERKWIERDI LPKPHSMNCG NGWEENRSKT EDQHLGYHPG EGGDEGGSGY
     SPPGKREQAD LYRLPEDFRP YTGGSKQAAS VITFSDPQRD NFQQFGLSRG PSCGALEPYK
     AVYKPYRNSS VQKNSSPAQE VAASDMFEGL QQQFLGANET DSAENIHIIQ LQVLNKAKER
     QLDSLVEKLK DSERQVRYLS HQLLIVQDEK DGLALSLRES QQLFQNGKER EMQLEAQIAA
     LEAQVEAFRV SEEKLTKKLR TTEITLESLK QQLVELHHSE SLQRAREHHE SIVASLTQKH
     EEQVSSLQKN LDATITALQE QESICTRLKD HVQQLERNQE AVRLEKTELI NRLTRSLEDS
     QKQCAHLLQS GSVQEVAQLQ LQLQQAQKAH VLSESMNKAL QEELTELKDE ISLYESAAEL
     GVLPGDSEGD LSIELTESCV DLGIKKVNWK QSKANRVTQQ ESPDEDPSKD ELILKLKTQV
     QRLLTSNSVK RHLVSQLQSD LRECRETMEA FQQSKDGDSG METKTDTSEK TTKQLWLESS
     EAINREDILQ LKNEVQVLQK QNQELKEAEE KLRSTNQDLC NQMRQMVQEF DHDKQEAVAR
     CERTYQQHHE AMKAQIRESL LAKHAVEKQH LLEVYEGTQS QLRSDLDKMN KEMAAVQECY
     LEVCREKDGL ESTLRKTMEK AQEQKRQLLE AREEYVRKLK LELEEKYQET LKTERQSWLQ
     EQAAGATQQA EKESRQKLIQ QLEKEWQSKL DDSLAAWRKT TSDRGSQTEQ VACPAAVSKA
     EAAAVLAEEQ ARQVQQEKEL ATKEALRKPE VELELKYCEI IAQKVETAVQ NARSRWIQEL
     PMLAEYKALL RAQQQEWAKQ QELAVAHRLS LALSEAKEKW KSELENMKPN VMSVKELEEK
     VHSLQKELEL KDEEVPVIVR AEVAKARTEW NKEKQEEIHK IQEQNEEDYR QFLEDHRNKI
     NEVLAAAKED FVKQKAELLL QKETEFQACL DQSRKEWTLQ EAQQTQVEIR QYEEDTLTVL
     AYLLKDTQLE YGGDSQDKQL LEAMSACSSK WISVQYFEKV KACIQKALHD MLSLLTDSVA
     SEQEKRKVVK SSADTVSWTS SEGDSAVPVP LPDSTSVRCA QSSAWLKAEA ETDKKICEIK
     GLRCGHCFQE LEKEKQECQD LRRKLEKCRR HLQHLERTHR AAVEKLGEEN SRVVEELIEE
     NHDMKNKLEA LRALCRTPPR SLSAGAAESA GPSCSRQALE ELRGQYIKAV RKIKRDMLRY
     IQESKERAAE MVKAEVLRER QETARKMRNY YLSCLQQILQ DNGKEEGAEK KIMSAASKLA
     TMAELLGTIA ESDCRVRCAQ AGRSVALPLA SEMLTGTERS ERSGVNHNIP HYVESKPNSG
     KTLPRSVCEQ LPGRKAAPRS QRRLEESKHR EMRPMASTAL PSDCRCGDAS CRHSGVLAKD
     VAPEFVPCQG EGGFDLHEKR DALGAGSEPL LYSAAHSFLG GAEKNSSPRC ISESRHTTLR
     SPSEMPRLKA LMCGSPTETD SIASEKSQGV GSQDSPVKDG VGPSSSPAWP SDSTLPCGSP
     AVLFLGDGSQ RTQEMLGDSV QWKQFSATSC HPDAQKSNMV CRSSHTLDLP KETLHSQQGK
     MGATLGHPSP QSTDMLKTDF KRLSGTGPSS LCQKPLIKLT APMPSQQDSG FDSPLE
 
 
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