CENPJ_MOUSE
ID CENPJ_MOUSE Reviewed; 1344 AA.
AC Q569L8; E9QLP3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Centromere protein J;
DE Short=CENP-J;
GN Name=Cenpj;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
CC -!- FUNCTION: Plays an important role in cell division and centrosome
CC function by participating in centriole duplication. Inhibits
CC microtubule nucleation from the centrosome. Involved in the regulation
CC of slow processive growth of centriolar microtubules. Acts as
CC microtubule plus-end tracking protein that stabilizes centriolar
CC microtubules and inhibits microtubule polymerization and extension from
CC the distal ends of centrioles. Required for centriole elongation and
CC for STIL-mediated centriole amplification. Required for the recruitment
CC of CEP295 to the proximal end of new-born centrioles at the centriolar
CC microtubule wall during early S phase in a PLK4-dependent manner. May
CC be involved in the control of centriolar-microtubule growth by acting
CC as a regulator of tubulin release (By similarity).
CC {ECO:0000250|UniProtKB:Q9HC77}.
CC -!- SUBUNIT: Forms homodimers. Associates with microtubules plus ends;
CC binds to beta-tubulin subunits exposed on microtubule outer surface at
CC its distal tip; also associates with microtubule lattice. Associated
CC with the gamma-tubulin complex. Interacts with the head domain of
CC EPB41. Interacts with LYST. Interacts with CEP152 (via C-terminus).
CC Interacts with STIL. Forms a complex with STIL and SASS6 (By
CC similarity). {ECO:0000250|UniProtKB:Q9HC77}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9HC77}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9HC77}. Note=Localized within the center of
CC microtubule asters. During centriole biogenesis, it is concentrated
CC within the proximal lumen of both parental centrioles and procentrioles
CC (By similarity). {ECO:0000250|UniProtKB:Q9HC77}.
CC -!- PTM: Phosphorylation at Ser-577 and Ser-583 by PLK2 is required for
CC procentriole formation and centriole elongation. Phosphorylation by
CC PLK2 oscillates during the cell cycle: it increases at G1/S transition
CC and decreases during the exit from mitosis. Phosphorylation at Ser-583
CC is also mediated by PLK4 but is not a critical step in PLK4 function in
CC procentriole assembly. {ECO:0000250|UniProtKB:Q9HC77}.
CC -!- SIMILARITY: Belongs to the TCP10 family. {ECO:0000305}.
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DR EMBL; AC154837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092399; AAH92399.1; -; mRNA.
DR CCDS; CCDS27150.1; -.
DR RefSeq; NP_001014996.2; NM_001014996.2.
DR AlphaFoldDB; Q569L8; -.
DR SMR; Q569L8; -.
DR BioGRID; 230108; 5.
DR ComplexPortal; CPX-1297; CPAP-STIL complex.
DR IntAct; Q569L8; 1.
DR STRING; 10090.ENSMUSP00000065949; -.
DR iPTMnet; Q569L8; -.
DR PhosphoSitePlus; Q569L8; -.
DR EPD; Q569L8; -.
DR jPOST; Q569L8; -.
DR MaxQB; Q569L8; -.
DR PaxDb; Q569L8; -.
DR PeptideAtlas; Q569L8; -.
DR PRIDE; Q569L8; -.
DR ProteomicsDB; 283881; -.
DR Antibodypedia; 22520; 201 antibodies from 26 providers.
DR DNASU; 219103; -.
DR Ensembl; ENSMUST00000065302; ENSMUSP00000065949; ENSMUSG00000064128.
DR Ensembl; ENSMUST00000225951; ENSMUSP00000153013; ENSMUSG00000064128.
DR GeneID; 219103; -.
DR KEGG; mmu:219103; -.
DR UCSC; uc007ucb.2; mouse.
DR CTD; 55835; -.
DR MGI; MGI:2684927; Cenpj.
DR VEuPathDB; HostDB:ENSMUSG00000064128; -.
DR eggNOG; ENOG502QQR0; Eukaryota.
DR GeneTree; ENSGT00530000063927; -.
DR HOGENOM; CLU_008072_0_0_1; -.
DR InParanoid; Q569L8; -.
DR OMA; EPLNFPD; -.
DR OrthoDB; 122802at2759; -.
DR PhylomeDB; Q569L8; -.
DR TreeFam; TF343156; -.
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-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 219103; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Cenpj; mouse.
DR PRO; PR:Q569L8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q569L8; protein.
DR Bgee; ENSMUSG00000064128; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; Q569L8; baseline and differential.
DR Genevisible; Q569L8; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0120099; C:procentriole replication complex; ISO:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0030954; P:astral microtubule nucleation; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0098534; P:centriole assembly; IMP:MGI.
DR GO; GO:0061511; P:centriole elongation; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:MGI.
DR GO; GO:0051298; P:centrosome duplication; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0046785; P:microtubule polymerization; ISO:MGI.
DR GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISO:MGI.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR InterPro; IPR033068; CENP-J.
DR InterPro; IPR009852; Tcp10_C_dom.
DR InterPro; IPR026581; TCP10_fam.
DR PANTHER; PTHR10331; PTHR10331; 1.
DR PANTHER; PTHR10331:SF23; PTHR10331:SF23; 1.
DR Pfam; PF07202; Tcp10_C; 4.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1344
FT /note="Centromere protein J"
FT /id="PRO_0000286053"
FT REGION 67..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..382
FT /note="Alpha/beta-tubulin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT REGION 347..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..1344
FT /note="Interaction with STIL"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT REGION 1105..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 577
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 583
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT CONFLICT 716
FT /note="N -> S (in Ref. 2; AAH92399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1344 AA; 153079 MW; 0C7596B79161C2C6 CRC64;
MFLMPTSSEL NSGQNFLTQW MTSPSRAGVI LNRGFPILEA DDKQAATNVS TSFPAKATHF
SNSFSISSEE DSFHEEQKLE AGGPYKPWSE NPEAPPVFPS VRKEPIASRQ DAPGCQEDNN
NDLTPHLESE FKEVANKNPL FKKLEQLKEI QQKKQEQLKR QQLEQLQRLM EEQEKLLTMV
SAQHAFPGTL LPDDQSQKHR SPGDLTLPPH SYSNPTQENS CASNVLPDEQ SNFCRATQDS
VLTSKNASDL FYESQYQEAH VKRNDLKEES PAHPSGEGAL PRWEKKMGRS QEGKDVNLQK
CGDSSEVVNI DERPIKAAVR EKQQTFEDYL EEQIQLEERE LRQKQLQEAE GPLLAKTKPK
QPFLKRGEGL ARFTNAKSKF QKGKESKLAS TQSPSEDQPG SKVDRQHLQR KTALINKDLC
AETPTVKKDS KARPKAGFAS LRQKPKVTKT NMRESLSPPG LKVQTGKKRD GQFRHQVKGE
RNAHASNKEN VPACIKPWDA GCKMWSKTQG RERLPLSTGP VGCVVSRSPI RETDRETESS
LDFSLQKKLE IWEREKEKEN LELDEFLFLE RAADEISFSS NSSFVLRILE RDQQICDGHR
LSSTPVKAVQ QREAQQADPR GQSNCSEIPR YGVAHENESE CEAMLLSWGS GSPDGLRELS
CKRSMKAFQT STSEIQSQWD ARDDGVANSD SSTESEEQHD ITIKPSTEVG DRVFSNREDS
PQVCDAKGPI RDTGAQEDKW RDADLDLSDK ECSSDESVIV ESLNNKVLEP LRLPSSQAGS
KIDFDDERSW TDLEENPYEH GVIHREEAIY GTPQTQCHSK SEGCVLDKTI KRKIAPVKKG
EDFKCDRRIS PPPPSDLMVK FFPSLKPKPK LDSHLENESK LNLSQDQPPE FMVCFIGDSV
RSQVLREKVT ELESEIEKFK AENTSLAKLR IERESALEKL RKEIADFEQQ KARELARIEE
YRKEETRKLQ KERKVFEKYT AAARTFPDKK EREEIQALKQ QIADLQEDLK RKETKWSSTQ
SRLRSQIEML VKENTDLREE IKVMERFRLD AWKRAEAMEN SPKACQYMMA TKKDESMNSS
FQFQKSHVSS GVQVEKYKKK YLPAQGNLSR RIKSAPPRDL GSSDKGQAAL PREPLQQVNF
PDLEYKNKEE KEEEIQGEIS HPDGKVEKIY KNGRRVVLFP NGTRKEVSAD GKSVTVTFFN
GDVKQVMPDE RVVYYYAAAQ TTHTTYPEGL EVLHFSSGQI EKHFPDGRKE ITFPDQTIKT
LFADGQEESI FPDGTIVRVQ RDGNKIIEFN NGQRELHTAQ FKRREYPDGT VKTVYANGHQ
ETKYTSGRVR VKDKDGNVLM DTEM
