CENPJ_PANTR
ID CENPJ_PANTR Reviewed; 1338 AA.
AC Q5BQN8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Centromere protein J;
DE Short=CENP-J;
GN Name=CENPJ;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Springell K., Bond J., Woods C.G.;
RT "Chimpanzee CENPJ gene.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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-590 and Ser-596 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-596
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; AY917123; AAX30073.1; -; mRNA.
DR RefSeq; NP_001029343.1; NM_001034171.1.
DR BMRB; Q5BQN8; -.
DR STRING; 9598.ENSPTRP00000009739; -.
DR PaxDb; Q5BQN8; -.
DR GeneID; 467235; -.
DR KEGG; ptr:467235; -.
DR CTD; 55835; -.
DR eggNOG; ENOG502QQR0; Eukaryota.
DR InParanoid; Q5BQN8; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0061511; P:centriole elongation; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
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..1338
FT /note="Centromere protein J"
FT /id="PRO_0000089481"
FT REGION 77..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..395
FT /note="Alpha/beta-tubulin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT REGION 387..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..1338
FT /note="Interaction with STIL"
FT REGION 1088..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 590
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 596
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC77"
SQ SEQUENCE 1338 AA; 152895 MW; 97B94DC1CD7320E5 CRC64;
MFLMPTSSEL NSGQNFLTQW MTNPSRAGVI LNRGFPILEA DKEKRAAVDI STSFPIKGTH
FSDSFSFINE EDSLLEEQKL ESNSPYKPQS DKSETHTGFP CIKKGPQVAA CHSAPGHQEE
NKNDFIPHLA SEFKEGAYKD PLFKKLEQLK EVQQKKQEQL KRQQLEQLQR LMEEQEKLLT
MVSGQCTLPG LSLLPDDQSQ KHRSPGNTTT GERATCCFPS YVYPDPTQEE TYASNILSHE
QSNFCRTAHG DFVLTSKRAS PNLFSEAQYQ EAPVEKNNLK EENRNHPTGE SILSCWEKVT
EQIQEANDKN LQKHDDSSEV ANIEERPIKA AIGERKQTFE DYLEEQIQLE EQELKQKQLK
EAEGPLPIKA KPKQPFLKRG EGLARFTNAK SKFQKGKESK LVTNQSTSED QPLFKMDRQQ
LQRKTALKNK ELCADNPILK KDSKARTKSG SVTLSQKPKM LKCSNRKSLS PSGLKIQTGK
KCDGQFRDQI KFEKKVTSNN KENVPECPKP CDTGCTGWNK TQGKDRLPLS TGPASRLAAK
SPIRETMKES ESSLDVSLQK KLETWEREKE KENLELDEFL FLEQAADEIS FSSNSSFVLK
ILERDQQICK GHRMSSTPVK AVPQKTNPAD PISHCNRSED LDHTAREKES ECEVAPKQLH
SLSSADELRE QPCKIRKAVQ KSTSENQTEW NARDDEGVPN SDSSTNSEEQ LDVTIKPSTE
DRERGISSRE DSPQVCDDKG PFKDTRTQED KRRDVDLDLS DKDYSSDESS MESIKHKVSE
PSRSSSLSMS KMDFDDERTW TDLEENLCNH DVVLGNESTY GTPQTCYPNN EIGILDKTIK
RKIAPVKRGE DLSKSRRSRS PPTSELMMKF FPSLKPKPKS DSHLGNEPKL NINQDQPPGD
NARSQVLREK IIELETEIEK FKAENASLAK LRIERESALE KLRKEIADFE QQKAKELARI
EEFKKEEMRK LQKERKVFEK YTTAARTFPD KKEREEIQTL KQQIADLRED LKRKETKWSS
THSRLRSQIE MLVRENTDLR EEIKVMERFR LDAWKRAEAI ESSLEVEKKD KLANTXVRFQ
NSQISSGTQV EKYKKNYLPM QGNPPRRSKS APPRDLGSLD KGQAASPREP PEPLNFPDPE
YKEEEDQDIQ GEISHPDGKV EKVYKNGCRV ILFPNGTRKE VSADGKTITV TFFNGDVKQV
MPDQRVIYYY AAAQTTHTTY PEGLEVLHFS SGQIEKHYPD GRKEITFPDQ TVKNLFPDGQ
EESIFPDGTT VRVQRDGNKL IEFNNGQREL HTAQFKRREY PDGTVKTVYA NGHQETKYRS
GRIRVKDKEG NVLMDTEL
