CDCA8
entrez
55143
canonical
uniprot
Q53HL2
canonical
ensembl
ENSG00000134690
resolver
ensp
ENSP00000316121
resolver
ensp
ENSP00000362146
resolver
enst
ENST00000327331
resolver
enst
ENST00000373055
resolver
genesymbol
CDCA8
resolver
genesymbol_syn
PESCRG3
resolver
hgnc
HGNC:14629
resolver
uniprot
D3DPT4
resolver
uniprot
Q53HN1
resolver
uniprot
Q96AM3
resolver
uniprot
Q9NVW5
resolver
uniprot_entry
BOREA_HUMAN
resolver
uniprot_sec
D3DPT4
resolver
uniprot_sec
Q53HN1
resolver
uniprot_sec
Q96AM3
resolver
uniprot_sec
Q9NVW5
resolver
amino_acid_sequence
MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK
uniprot
proteins
function
FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. {ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:15260989, ECO:0000269|PubMed:16571674, ECO:0000269|PubMed:18243099}.
uniprot
proteins
mass_dalton
31323
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="R->E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 19; /note="R->E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 20; /note="K->E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 26; /note="K->R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells."; /evidence="ECO:0000269|PubMed:18946085"; MUTAGEN 35; /note="R->E: Loss of binding to INCENP; when associated with Y-46."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 46; /note="L->Y: Loss of binding to INCENP; when associated with E-35."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 70; /note="W->E: Loss of binding to BIRC5; when associated with E-74."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 74; /note="F->E: Loss of binding to BIRC5; when associated with E-70."; /evidence="ECO:0000269|PubMed:17956729"; MUTAGEN 88; /note="T->A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230."; /evidence="ECO:0000269|PubMed:19530738"; MUTAGEN 94; /note="T->A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230."; /evidence="ECO:0000269|PubMed:19530738"; MUTAGEN 106; /note="T->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-171, A-185, A-189, A-199, A-204 and A-219."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 165; /note="S->A: Results in reduction but not abolition of phosphorylation."; /evidence="ECO:0000269|PubMed:15249581"; MUTAGEN 169; /note="T->A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230."; /evidence="ECO:0000269|PubMed:19530738"; MUTAGEN 171; /note="T->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-185, A-189, A-199, A-204 and A-219."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 185; /note="T->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-189, A-199, A-204 and A-219."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 189; /note="T->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-199, A-204 and A-219."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 199; /note="T->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-204, A-219."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 204; /note="T->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-219."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 219; /note="S->A: Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-204."; /evidence="ECO:0000269|PubMed:20739936"; MUTAGEN 219; /note="S->D,K: No effect on the structure."; MUTAGEN 230; /note="T->A: Decrease in AURKB activity and dimer disruption. Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230."; /evidence="ECO:0000269|PubMed:19530738"; MUTAGEN 230; /note="T->D,K: Substantial loss of structure."; /evidence="ECO:0000269|PubMed:19530738"; MUTAGEN 230; /note="T->V: Decrease in AURKB activity and no effect on the structure."; /evidence="ECO:0000269|PubMed:19530738
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and Thr-230. Phosphorylation (probably by CDK1) promotes targeting of the CPC to centromeric DNA. {ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:19530738}.; PTM: Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. {ECO:0000269|PubMed:18946085}.
uniprot
proteins
protein_family
Borealin family
uniprot
proteins
pubmed
12188893
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15249581
uniprot
proteins
pubmed
15260989
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561729
uniprot
proteins
pubmed
16239925
uniprot
proteins
pubmed
16291752
uniprot
proteins
pubmed
16427043
uniprot
proteins
pubmed
16436504
uniprot
proteins
pubmed
16547492
uniprot
proteins
pubmed
16571674
uniprot
proteins
pubmed
17956729
uniprot
proteins
pubmed
18243099
uniprot
proteins
pubmed
18591255
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18946085
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19530738
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20739936
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
280
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18946085}. Cytoplasm {ECO:0000269|PubMed:18946085}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15561729}. Chromosome, centromere {ECO:0000269|PubMed:20739936}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalizes with SENP3 in the nucleolus in interphase cells. {ECO:0000269|PubMed:18946085}.
uniprot
proteins