CATAC_HUMAN
ID CATAC_HUMAN Reviewed; 332 AA.
AC Q86UT8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Centrosomal AT-AC splicing factor {ECO:0000305};
DE AltName: Full=Coiled-coil domain-containing protein 84;
GN Name=CENATAC {ECO:0000312|HGNC:HGNC:30460}; ORFNames=CCDC84, DLNB14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT "Identification of a 500-kb region of common allelic loss in chromosome
RT 11q23 in non-MYCN amplified type of neuroblastoma.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-31, INTERACTION WITH
RP SASS6, AND MUTAGENESIS OF LYS-31.
RX PubMed=31722219; DOI=10.1016/j.celrep.2019.10.028;
RA Wang T., Zou Y., Huang N., Teng J., Chen J.;
RT "CCDC84 Acetylation Oscillation Regulates Centrosome Duplication by
RT Modulating HsSAS-6 Degradation.";
RL Cell Rep. 29:2078-2091.e5(2019).
CC -!- FUNCTION: Negative regulator of centrosome duplication
CC (PubMed:31722219). Constrains centriole number by modulating the
CC degradation of the centrosome-duplication-associated protein SASS6 in
CC an acetylation-dependent manner. SIRT1 deacetylates CENATAC in G1
CC phase, allowing for SASS6 accumulation on the centrosome and subsequent
CC procentriole assembly. The CENATAC acetylation level is restored in
CC mitosis by NAT10, promoting SASS6 proteasome degradation by
CC facilitating SASS6 binding to APC/C E3 ubiquitin-protein ligase
CC complex/FZR1 (PubMed:31722219). {ECO:0000269|PubMed:31722219}.
CC -!- SUBUNIT: Interacts with SASS6; the interaction increases with CENATAC
CC acetylation. {ECO:0000269|PubMed:31722219}.
CC -!- INTERACTION:
CC Q86UT8; Q14696: MESD; NbExp=3; IntAct=EBI-11028020, EBI-6165891;
CC Q86UT8; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-11028020, EBI-720441;
CC Q86UT8; Q9UHB4: NDOR1; NbExp=3; IntAct=EBI-11028020, EBI-10249760;
CC Q86UT8; Q9H2H8: PPIL3; NbExp=3; IntAct=EBI-11028020, EBI-751051;
CC Q86UT8; Q9NX01: TXNL4B; NbExp=6; IntAct=EBI-11028020, EBI-10309345;
CC Q86UT8; Q8NC26: ZNF114; NbExp=3; IntAct=EBI-11028020, EBI-10265237;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:31722219}. Note=Localizes to the
CC proximal end of the mother centriole. During the cell cycle, from G1 to
CC metaphase, gradually accumulates on the centrosome and then decreased
CC significantly upon entry into anaphase. {ECO:0000269|PubMed:31722219}.
CC -!- PTM: Acetylated. Acetylation oscillates throughout the cell cycle, and
CC the acetylation state at Lys-31 is regulated by the deacetylase SIRT1
CC and the acetyltransferase NAT10. Deacetylated CENATAC is responsible
CC for its centrosome targeting, and acetylated CENATAC promotes SASS6
CC degradation by enhancing the binding affinity of SASS6 for APC/C E3
CC ubiquitin-protein ligase complex/FZR1. {ECO:0000269|PubMed:31722219}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB094093; BAC76047.1; -; mRNA.
DR EMBL; BC126469; AAI26470.1; -; mRNA.
DR EMBL; BC126471; AAI26472.1; -; mRNA.
DR CCDS; CCDS8405.1; -.
DR RefSeq; NP_940891.1; NM_198489.2.
DR AlphaFoldDB; Q86UT8; -.
DR BioGRID; 130775; 45.
DR IntAct; Q86UT8; 24.
DR STRING; 9606.ENSP00000334767; -.
DR iPTMnet; Q86UT8; -.
DR PhosphoSitePlus; Q86UT8; -.
DR BioMuta; CCDC84; -.
DR DMDM; 74714025; -.
DR EPD; Q86UT8; -.
DR jPOST; Q86UT8; -.
DR MassIVE; Q86UT8; -.
DR MaxQB; Q86UT8; -.
DR PaxDb; Q86UT8; -.
DR PeptideAtlas; Q86UT8; -.
DR PRIDE; Q86UT8; -.
DR ProteomicsDB; 69889; -.
DR Antibodypedia; 54439; 87 antibodies from 17 providers.
DR DNASU; 338657; -.
DR Ensembl; ENST00000334418.6; ENSP00000334767.1; ENSG00000186166.9.
DR Ensembl; ENST00000625528.3; ENSP00000487197.1; ENSG00000280975.3.
DR GeneID; 338657; -.
DR KEGG; hsa:338657; -.
DR MANE-Select; ENST00000334418.6; ENSP00000334767.1; NM_198489.3; NP_940891.1.
DR UCSC; uc001pul.5; human.
DR CTD; 338657; -.
DR DisGeNET; 338657; -.
DR GeneCards; CENATAC; -.
DR HGNC; HGNC:30460; CENATAC.
DR HPA; ENSG00000186166; Low tissue specificity.
DR neXtProt; NX_Q86UT8; -.
DR OpenTargets; ENSG00000186166; -.
DR VEuPathDB; HostDB:ENSG00000186166; -.
DR eggNOG; ENOG502QS8B; Eukaryota.
DR GeneTree; ENSGT00390000007799; -.
DR HOGENOM; CLU_041370_1_0_1; -.
DR InParanoid; Q86UT8; -.
DR OMA; YFPNHKK; -.
DR OrthoDB; 1213548at2759; -.
DR PhylomeDB; Q86UT8; -.
DR TreeFam; TF324670; -.
DR PathwayCommons; Q86UT8; -.
DR SignaLink; Q86UT8; -.
DR BioGRID-ORCS; 338657; 600 hits in 1093 CRISPR screens.
DR ChiTaRS; CCDC84; human.
DR GenomeRNAi; 338657; -.
DR Pharos; Q86UT8; Tdark.
DR PRO; PR:Q86UT8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86UT8; protein.
DR Bgee; ENSG00000186166; Expressed in cerebellar cortex and 93 other tissues.
DR ExpressionAtlas; Q86UT8; baseline and differential.
DR Genevisible; Q86UT8; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IDA:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR028015; CCDC84-like.
DR PANTHER; PTHR31198; PTHR31198; 1.
DR Pfam; PF14968; CCDC84; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..332
FT /note="Centrosomal AT-AC splicing factor"
FT /id="PRO_0000271022"
FT REGION 1..169
FT /note="Required for centrosome location"
FT /evidence="ECO:0000269|PubMed:31722219"
FT REGION 169..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 137..168
FT /evidence="ECO:0000255"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="N6-acetyllysine; by NAT10"
FT /evidence="ECO:0000269|PubMed:31722219"
FT VARIANT 244
FT /note="W -> G (in dbSNP:rs600648)"
FT /id="VAR_029848"
FT MUTAGEN 31
FT /note="K->Q: Increases interaction with SASS6."
FT /evidence="ECO:0000269|PubMed:31722219"
FT MUTAGEN 31
FT /note="K->R: Strongly reduces acetylation. No effect on
FT interaction with SASS6."
FT /evidence="ECO:0000269|PubMed:31722219"
SQ SEQUENCE 332 AA; 37974 MW; 341209B75BE56349 CRC64;
MAPAQRCPLC RQTFFCGRGH VYSRKHQRQL KEALERLLPQ VEAARKAIRA AQVERYVPEH
ERCCWCLCCG CEVREHLSHG NLTVLYGGLL EHLASPEHKK ATNKFWWENK AEVQMKEKFL
VTPQDYARFK KSMVKGLDSY EEKEDKVIKE MAAQIREVEQ SRQEVVRSVL EPQAVPDPEE
GSSAPRSWKG MNSQVASSLQ QPSNLDLPPA PELDWMETGP SLTFIGHQDI PGVGNIHSGA
TPPWMIQDEE YIAGNQEIGP SYEEFLKEKE KQKLKKLPPD RVGANFDHSS RTSAGWLPSF
GRVWNNGRRW QSRHQFKTEA AAMKKQSHTE KS
