ID   CEP68_PONAB             Reviewed;         751 AA.
AC   Q5RCQ2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Centrosomal protein of 68 kDa;
DE            Short=Cep68;
GN   Name=CEP68;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in maintenance of centrosome cohesion, probably as
CC       part of a linker structure which prevents centrosome splitting.
CC       Required for localization of CDK5RAP2 to the centrosome during
CC       interphase. {ECO:0000250|UniProtKB:Q76N32}.
CC   -!- SUBUNIT: Interacts with CNTLN; the interaction recruits CEP68 to the
CC       centrosome. Interacts with the SCF(FBXW11) complex which contains SKP1,
CC       CUL1 and FBXW11; the interaction is probably mediated by FBXW11 and the
CC       complex also contains CDK5RAP2 and PCNT. Also interacts with F-box
CC       protein BTRC. Interacts with serine/threonine-protein kinase PLK1; the
CC       interaction leads to phosphorylation of CEP68 and its subsequent
CC       degradation. Interacts with NEK2; the interaction leads to
CC       phosphorylation of CEP68. {ECO:0000250|UniProtKB:Q76N32}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250}. Note=Localizes to thin fibers
CC       protruding away from the proximal ends of the two centrioles.
CC       Dissociates from interphase centrosomes at the onset of mitosis.
CC       {ECO:0000250|UniProtKB:Q76N32}.
CC   -!- PTM: Phosphorylation by PLK1 is required for binding to BTRC in
CC       prometaphase. Phosphorylated directly or indirectly by NEK2. NEK2-
CC       mediated phosphorylation promotes CEP68 dissociation from the
CC       centrosome and its degradation at the onset of mitosis.
CC       {ECO:0000250|UniProtKB:Q76N32}.
CC   -!- PTM: Ubiquitinated and targeted for proteasomal degradation in early
CC       mitosis by the SCF(BTRC) and/or SCF(FBXW11) E3 ubiquitin-protein ligase
CC       complexes. Degradation is complete by prometaphase and is required for
CC       removal of CDK5RAP2 from the peripheral pericentriolar material and
CC       subsequent centriole separation. {ECO:0000250|UniProtKB:Q76N32}.
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DR   EMBL; CR858217; CAH90455.1; -; mRNA.
DR   RefSeq; NP_001125234.1; NM_001131762.1.
DR   AlphaFoldDB; Q5RCQ2; -.
DR   SMR; Q5RCQ2; -.
DR   STRING; 9601.ENSPPYP00000013784; -.
DR   GeneID; 100172127; -.
DR   KEGG; pon:100172127; -.
DR   CTD; 23177; -.
DR   eggNOG; ENOG502RK93; Eukaryota.
DR   InParanoid; Q5RCQ2; -.
DR   OrthoDB; 1235573at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   InterPro; IPR030265; CEP68.
DR   PANTHER; PTHR14514:SF3; PTHR14514:SF3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..751
FT                   /note="Centrosomal protein of 68 kDa"
FT                   /id="PRO_0000089496"
FT   REGION          1..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q76N32"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C0D9"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q76N32"
SQ   SEQUENCE   751 AA;  80211 MW;  FF8362B7BEC079B8 CRC64;
     MALGEEKAEA EASEDTKAQS YGRGSCGERE LDTPGPMSGE QPPRLEAEGG LTSPVWGAEG
     IPAPTCWIGT DPGGPSRAHQ PQASDASREP VAERSEPALS GLPPATMGSG DLLLSRESQV
     EKTKLSASEE LPQTPSLPRT TTICSGHDAD TEDDPSLADL PQAPSSGLSC LSQWKSMPSP
     GSAAPQPSSC SVSASSTGSS LQGHQERTEP RGGSLAKVSS SLELVVPQEP SSVVGLGPRP
     QWSPQPVFSG GDASGLGRRR LSFQAEYWAC VLPDSLPPSP DRHSPLWNPN KEYEDLLDYT
     YPLRPGPQLP KHLDSRVPAD PVLQDSGVDL DSFSVSPAST LKSPTNVFPN CPPAEATALP
     LSGPREPSLK QWPSGVPQKQ GGMGLASWSQ LTSTPRAPGS RDARWECREP ALRGAKDWLP
     IGKPLDMGSP QLRTRDRGWP SPRPEREKRT SQSARRPTCT ESRWKSEEEV ESDDEYLALP
     ARLTQVSSLV SYIGSISTLV TLPAGDIKGQ SPLEVSDTDG PASLPSSSSQ SQLPPGAALR
     GSGDPEGQNP CFLRSFVRAQ DSAGEGSLGS SQALGVSSGL LKTRPSLPAR LDRWPFSDPD
     AEGQLPRKGG EQGKESLVQC VKTFCCQLEE LICWLYNVAD VTDHGTAARS NLTSLKSSLQ
     LYRQFKKDID EHQSLTESVL QKGEILLQCL LENTPVLEDV LGRIAKQSGE LESHADRLYD
     SILASLDMLA GCTLIPDKKP MAAMERPREG V