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GeneE
10 sources retrieved Β· Most recent: April 2026 Β· Index updated 14 days ago
β“˜GeneE is for informational purposes only. It is not a substitute for professional medical advice, diagnosis, or treatment.
CEP63
centrosomal protein 63
Chromosome 3 Β· 3q22.2
NCBI Gene: 80254Ensembl: ENSG00000182923.20HGNC: HGNC:25815UniProt: A0A804HIX3
73PubMed Papers
21Diseases
0Drugs
35Pathogenic Variants
CLINICAL
OMIM Disease Gene
DATA QUALITY
βœ“ Experimental GO Evidenceβœ“ Swiss-Prot Reviewed
ciliary basal bodyprotein bindingnegative regulation of protein K63-linked ubiquitinationcentrosomeSeckel syndrome 6Seckel syndromegenetic disorderneurodegenerative disease
✦AI Summary

CEP63 is a centrosomal scaffolding protein essential for centriole duplication and spindle assembly. CEP63 functions as a key component of the pericentriolar matrix, interacting with CEP152, CEP57, and WDR62 to form a stepwise assembled complex that recruits CDK2 for centriole duplication 12. CEP63 also recruits CDK1 to centrosomes 3 and maintains proper spatial organization of centrosomal proteins, including anchoring CEP152 in ninefold symmetry during centriole maturation 4. Beyond cell cycle regulation, CEP63 plays a critical role in DNA damage response; following double-strand breaks, it is removed from centrosomes, leading to spindle assembly inactivation and mitotic delay 3. Recently identified functions include stabilization of the RNA-binding protein FXR1 through inhibition of its K63-linked ubiquitination 5, and regulation of innate immunity by modulating TBK1 centrosomal localization 6. Loss-of-function mutations in CEP63 cause Seckel syndrome 6, characterized by microcephaly, growth restriction, and intellectual disability 78, with disease pathology arising from centrosome-based mitotic errors and p53-dependent neural progenitor cell death rather than aberrant DNA damage response 8.

Sources cited
1
CEP63 plays key role in centriole duplication through complex with CEP152, CDK5RAP2, WDR62 recruiting CDK2
PMID: 21983783
2
CEP63 involved in stepwise assembled complex at centrosome for centriole duplication
PMID: 26297806
3
CEP63 recruits CDK1 to centrosomes and is removed following DNA damage to delay mitotic progression
PMID: 21406398
4
CEP63 anchors CEP152 in ninefold symmetry as component of centrosomal organization
PMID: 37707473
5
CEP63 stabilizes FXR1 protein by inhibiting K63-linked ubiquitination in cancer progression
PMID: 35989368
6
CEP63 regulates TBK1 centrosomal localization in innate immune response; required by ZIKV for centrosome disorganization
PMID: 35793002
7
Biallelic loss-of-function CEP63 variants cause Seckel syndrome with microcephaly and intellectual disability
PMID: 37017437
8
CEP63 deficiency causes Seckel syndrome-like microcephaly through centrosome-based mitotic errors and p53-dependent cell death
PMID: 26158450
Disease Associationsβ“˜21
Seckel syndrome 6Open Targets
0.66Moderate
Seckel syndromeOpen Targets
0.50Moderate
genetic disorderOpen Targets
0.47Moderate
neurodegenerative diseaseOpen Targets
0.36Weak
preeclampsiaOpen Targets
0.29Weak
smoking behaviorOpen Targets
0.27Weak
smoking initiationOpen Targets
0.20Weak
ThromboembolismOpen Targets
0.18Weak
cholelithiasisOpen Targets
0.10Weak
depressive disorderOpen Targets
0.10Weak
X-linked retinal dysplasiaOpen Targets
0.07Suggestive
age-related macular degenerationOpen Targets
0.07Suggestive
papillary thyroid carcinomaOpen Targets
0.06Suggestive
Familial exudative vitreoretinopathyOpen Targets
0.06Suggestive
choroidal dystrophy, central areolar, 1Open Targets
0.06Suggestive
azoospermiaOpen Targets
0.05Suggestive
severe early-childhood-onset retinal dystrophyOpen Targets
0.05Suggestive
Stargardt diseaseOpen Targets
0.05Suggestive
Familial drusenOpen Targets
0.04Suggestive
age related macular degeneration 6Open Targets
0.04Suggestive
Seckel syndrome 6UniProt
Pathogenic Variants35
NM_001353108.3(CEP63):c.1722C>A (p.Tyr574Ter)Pathogenic
not provided
β˜…β˜†β˜†β˜†2025β†’ Residue 574
NM_001353108.3(CEP63):c.555_555+1delinsCALikely pathogenic
not provided
β˜…β˜†β˜†β˜†2025
NM_001353108.3(CEP63):c.1154dup (p.Asn385fs)Pathogenic
not provided
β˜…β˜†β˜†β˜†2025β†’ Residue 385
NM_001353108.3(CEP63):c.990del (p.Asp330fs)Pathogenic
not provided
β˜…β˜†β˜†β˜†2025β†’ Residue 330
NM_001353108.3(CEP63):c.584T>G (p.Leu195Ter)Pathogenic
not provided
β˜…β˜†β˜†β˜†2025β†’ Residue 195
NM_001353108.3(CEP63):c.441+1G>ALikely pathogenic
not provided
β˜…β˜†β˜†β˜†2025
NM_001353108.3(CEP63):c.1627_1673+31delLikely pathogenic
not provided
β˜…β˜†β˜†β˜†2025
NM_001353108.3(CEP63):c.930-1G>ALikely pathogenic
not provided
β˜…β˜†β˜†β˜†2024
NM_001353108.3(CEP63):c.1191_1195del (p.Glu397fs)Pathogenic
not provided
β˜…β˜†β˜†β˜†2024β†’ Residue 397
NM_001353108.3(CEP63):c.1380+2T>GLikely pathogenic
not provided
β˜…β˜†β˜†β˜†2024
NM_001353108.3(CEP63):c.789+1G>TLikely pathogenic
not provided
β˜…β˜†β˜†β˜†2024
NM_001353108.3(CEP63):c.764T>A (p.Leu255Ter)Pathogenic
not provided
β˜…β˜†β˜†β˜†2024β†’ Residue 255
NM_001353108.3(CEP63):c.987dup (p.Asp330fs)Pathogenic
not provided
β˜…β˜†β˜†β˜†2024β†’ Residue 330
NM_001353108.3(CEP63):c.1068-2A>GLikely pathogenic
not provided|Papillary renal cell carcinoma type 1
β˜…β˜†β˜†β˜†2024
NM_001353108.3(CEP63):c.718del (p.Thr240fs)Pathogenic
not provided
β˜…β˜†β˜†β˜†2023β†’ Residue 240
NM_001353108.3(CEP63):c.1201C>T (p.Gln401Ter)Pathogenic
not provided
β˜…β˜†β˜†β˜†2023β†’ Residue 401
NM_001353108.3(CEP63):c.790-2A>GLikely pathogenic
Seckel syndrome 6|not provided
β˜…β˜†β˜†β˜†2023
NM_001353108.3(CEP63):c.1279C>T (p.Arg427Ter)Pathogenic
not provided
β˜…β˜†β˜†β˜†2023β†’ Residue 427
NM_001353108.3(CEP63):c.490C>T (p.Gln164Ter)Pathogenic
Seckel syndrome 6
β˜…β˜†β˜†β˜†2023β†’ Residue 164
NM_001353108.3(CEP63):c.1835del (p.Ser611_Leu612insTer)Likely pathogenic
Seckel syndrome 6
β˜…β˜†β˜†β˜†2023β†’ Residue 611
View on ClinVar β†—
Related Genes
PLK1Protein interaction91%PCNTProtein interaction85%STILProtein interaction82%CEP135Protein interaction82%KIAA0753Protein interaction82%PIBF1Protein interaction82%
Tissue Expression6 tissues
Heart
100%
Brain
88%
Bone Marrow
59%
Ovary
56%
Liver
49%
Lung
49%
Gene Interaction Network
Click a node to explore
CEP63PLK1PCNTSTILCEP135KIAA0753PIBF1
PROTEIN STRUCTURE
Preparing viewer…
PDB6CSU Β· 2.50 Γ… Β· X-ray
View on RCSB β†—
Constraintβ“˜
LOEUFβ“˜
1.13LoF Tolerant
pLIβ“˜
0.00Tolerant
Observed/Expected LoF0.90 [0.72–1.13]
RankingsWhere CEP63 stands among ~20K protein-coding genes
  • #6,452of 20,598
    Most Researched73
  • #1,678of 5,498
    Most Pathogenic Variants35
  • #11,647of 17,882
    Most Constrained (LOEUF)1.13
Genes detectedCEP63
Sources retrieved10 papers
Response timeβ€”
πŸ“„ Sources
10β–Ό
1
Centrosomal organization of Cep152 provides flexibility in Plk4 and procentriole positioning.
PMID: 37707473
J Cell Biol Β· 2023
1.00
2
Cep57 regulates human centrosomes through multivalent interactions.
PMID: 38857398
Proc Natl Acad Sci U S A Β· 2024
0.90
3
CEP63 upregulates YAP1 to promote colorectal cancer progression through stabilizing RNA binding protein FXR1.
PMID: 35989368
Oncogene Β· 2022
0.80
4
CCDC57 Cooperates with Microtubules and Microcephaly Protein CEP63 and Regulates Centriole Duplication and Mitotic Progression.
PMID: 32402286
Cell Rep Β· 2020
0.70
5
Requirement of the Cep57-Cep63 Interaction for Proper Cep152 Recruitment and Centriole Duplication.
PMID: 32152252
Mol Cell Biol Β· 2020
0.60