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
