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Protein

Centrosomal protein of 68 kDa

Gene

Cep68

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting. Required for localization of CDK5RAP2 to the centrosome during interphase.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein of 68 kDa
Short name:
Cep68
Gene namesi
Name:Cep68
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2667663. Cep68.

Subcellular locationi

  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity

  • Note: Localizes to thin fibers protruding away from the proximal ends of the two centrioles. Dissociates from interphase centrosomes at the onset of mitosis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Centrosomal protein of 68 kDaPRO_0000089495Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei453 – 4531PhosphoserineCombined sources
Modified residuei459 – 4591PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation by PLK1 is required for binding to BTRC in prometaphase. Phosphorylated directly or indirectly by NEK2. NEK2-mediated phosphorylation promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis.By similarity
Ubiquitinated and targeted for proteasomal degradation in early mitosis by the SCF(BTRC) and/or SCF(FBXW11) E3 ubiquitin-protein ligase complexes. Degradation is complete by prometaphase and is required for removal of CDK5RAP2 from the peripheral pericentriolar material and subsequent centriole separation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8C0D9.
PaxDbiQ8C0D9.
PRIDEiQ8C0D9.

PTM databases

PhosphoSiteiQ8C0D9.

Expressioni

Gene expression databases

BgeeiQ8C0D9.
CleanExiMM_CEP68.
ExpressionAtlasiQ8C0D9. baseline and differential.
GenevisibleiQ8C0D9. MM.

Interactioni

Subunit structurei

Interacts with CNTLN; the interaction recruits CEP68 to the centrosome. Interacts with the SCF(FBXW11) complex which contains SKP1, CUL1 and FBXW11; the interaction is probably mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT. Also interacts with F-box protein BTRC. Interacts with serine/threonine-protein kinase PLK1; the interaction leads to phosphorylation of CEP68 and its subsequent degradation. Interacts with NEK2; the interaction leads to phosphorylation of CEP68.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054943.

Structurei

3D structure databases

ProteinModelPortaliQ8C0D9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IIDK. Eukaryota.
ENOG41129RE. LUCA.
GeneTreeiENSGT00810000125473.
HOGENOMiHOG000070069.
HOVERGENiHBG050898.
InParanoidiQ8C0D9.
KOiK16764.
OMAiQAEYWAC.
OrthoDBiEOG7NW68J.
PhylomeDBiQ8C0D9.
TreeFamiTF333570.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C0D9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALSEDEAEA EVSVNTKVPS CGRWNSGKLL PSGLEPDQPL HLGVEGGPLW
60 70 80 90 100
RAEADPGCIS GVFLSRVHTA SKEPVADRSK PPLRGPLPSA SVGTGEVLHS
110 120 130 140 150
MGSQMEEDRL PASQDLLPAL QVFGTITVCS GQEADSEDFQ ATLDPSQVLG
160 170 180 190 200
LSQQPHTSGL PLPPQWKSTV SPGAPQLSSR SISASSVGSS LQDHQEKAGP
210 220 230 240 250
QRASFANVSS PELTVPQAAH SVVGAGPPLQ GSAQPLTSGS DATGLGKRHL
260 270 280 290 300
SFQAEYWACA LPNSLPPSPN RHSALWDPNK EYEDLLDYTY PLRPGPQLPK
310 320 330 340 350
QPESHVLTEP VLQDSGVDLD SLSVSPASTL KSPTNVSHNC SSAEVPTLPF
360 370 380 390 400
SGARESCLKR WPLGIFQKQG GTSLSSWNQL ASTPRAPGTE DASWENREAA
410 420 430 440 450
LRGTAEDCLP IGEDLRMGSP QLKTKEKEPP FPRQKRGRQH VSCPACVTPG
460 470 480 490 500
WPSEEEVGSD EEYLALPTRL TQVSSLVSYS GARPSFVNLH TGAAEEHSSL
510 520 530 540 550
QVSDSDKPAS PTLDSSHRKH PSGTSFQGPV GQNPCFRHSI QPQDSRGKSS
560 570 580 590 600
LMSNQTLGVS SKPLKTQPAS KAMTDRRLFS ELVAGETLPR TTDEQEKASL
610 620 630 640 650
VQCVQTFCCR LEELICWLYN VTDVADLSAP PRTSLTGLKS SLQLYRQFKK
660 670 680 690 700
DVDEHQSLTE SVLEKGEILL QCLLDNTPVL KDVLERIAKQ SGELESRADH
710 720 730
LYDSILASLD MLAGCTLIPD NRPTAAEHPH EGL
Length:733
Mass (Da):78,749
Last modified:April 26, 2005 - v2
Checksum:i15D93FCECDDC92A9
GO
Isoform 2 (identifier: Q8C0D9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     647-733: QFKKDVDEHQ...TAAEHPHEGL → VICSPGLFIHGDGS

Note: No experimental confirmation available.
Show »
Length:660
Mass (Da):70,487
Checksum:i4076BCB810C66E65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281P → Q in BAC27484 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei647 – 73387QFKKD…PHEGL → VICSPGLFIHGDGS in isoform 2. 1 PublicationVSP_013477Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031622 mRNA. Translation: BAC27484.1.
AK140820 mRNA. Translation: BAE24488.1.
AL606522 Genomic DNA. Translation: CAI24452.1.
AL606522 Genomic DNA. Translation: CAI24453.1.
BC027174 mRNA. Translation: AAH27174.1.
CCDSiCCDS24456.1. [Q8C0D9-1]
RefSeqiNP_758464.2. NM_172260.3. [Q8C0D9-1]
UniGeneiMm.260314.

Genome annotation databases

EnsembliENSMUST00000050611; ENSMUSP00000054943; ENSMUSG00000044066. [Q8C0D9-1]
ENSMUST00000109596; ENSMUSP00000105225; ENSMUSG00000044066. [Q8C0D9-2]
GeneIDi216543.
KEGGimmu:216543.
UCSCiuc007icw.1. mouse. [Q8C0D9-1]
uc007icx.1. mouse. [Q8C0D9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031622 mRNA. Translation: BAC27484.1.
AK140820 mRNA. Translation: BAE24488.1.
AL606522 Genomic DNA. Translation: CAI24452.1.
AL606522 Genomic DNA. Translation: CAI24453.1.
BC027174 mRNA. Translation: AAH27174.1.
CCDSiCCDS24456.1. [Q8C0D9-1]
RefSeqiNP_758464.2. NM_172260.3. [Q8C0D9-1]
UniGeneiMm.260314.

3D structure databases

ProteinModelPortaliQ8C0D9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054943.

PTM databases

PhosphoSiteiQ8C0D9.

Proteomic databases

MaxQBiQ8C0D9.
PaxDbiQ8C0D9.
PRIDEiQ8C0D9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050611; ENSMUSP00000054943; ENSMUSG00000044066. [Q8C0D9-1]
ENSMUST00000109596; ENSMUSP00000105225; ENSMUSG00000044066. [Q8C0D9-2]
GeneIDi216543.
KEGGimmu:216543.
UCSCiuc007icw.1. mouse. [Q8C0D9-1]
uc007icx.1. mouse. [Q8C0D9-2]

Organism-specific databases

CTDi23177.
MGIiMGI:2667663. Cep68.

Phylogenomic databases

eggNOGiENOG410IIDK. Eukaryota.
ENOG41129RE. LUCA.
GeneTreeiENSGT00810000125473.
HOGENOMiHOG000070069.
HOVERGENiHBG050898.
InParanoidiQ8C0D9.
KOiK16764.
OMAiQAEYWAC.
OrthoDBiEOG7NW68J.
PhylomeDBiQ8C0D9.
TreeFamiTF333570.

Miscellaneous databases

NextBioi375198.
PROiQ8C0D9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0D9.
CleanExiMM_CEP68.
ExpressionAtlasiQ8C0D9. baseline and differential.
GenevisibleiQ8C0D9. MM.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Head and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: 129.
    Tissue: Mammary gland.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.

Entry informationi

Entry nameiCEP68_MOUSE
AccessioniPrimary (citable) accession number: Q8C0D9
Secondary accession number(s): Q3US49, Q5SW85, Q8R2V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: May 11, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.