ID CC14A_HUMAN Reviewed; 594 AA. AC Q9UNH5; A6MA65; B1AQ14; B1AQ15; O43171; O60727; O60728; Q52LH9; Q8IXX0; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 184. DE RecName: Full=Dual specificity protein phosphatase CDC14A; DE EC=3.1.3.16; DE EC=3.1.3.48; DE AltName: Full=CDC14 cell division cycle 14 homolog A; GN Name=CDC14A; 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] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9367992; DOI=10.1074/jbc.272.47.29403; RA Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E.; RT "A family of putative tumor suppressors is structurally and functionally RT conserved in humans and yeast."; RL J. Biol. Chem. 272:29403-29406(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10409437; DOI=10.1006/geno.1999.5863; RA Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K., Carillo A., RA Emerson M., Heichman K., Gupte J., Tavtigian S.V., Teng D.H.-F.; RT "Genomic structure, chromosomal location, and mutation analysis of the RT human CDC14A gene."; RL Genomics 59:248-251(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Placenta; RA Hao L., Baskerville C., Charbonneau H.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RA Belyaev A.S., Kolokithas A., Monell C.R.; RT "Human CDC14A splice variant."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-345 AND PHE-589. RG NIEHS SNPs program; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). 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 [9] RP DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP CYS-278. RX PubMed=11598127; DOI=10.1074/jbc.m108126200; RA Bembenek J., Yu H.; RT "Regulation of the anaphase-promoting complex by the dual specificity RT phosphatase human Cdc14a."; RL J. Biol. Chem. 276:48237-48242(2001). RN [10] RP SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ASP-251; CYS-278 AND ARG-284. RX PubMed=12134069; DOI=10.1091/mbc.01-11-0535; RA Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K.; RT "Disruption of centrosome structure, chromosome segregation, and RT cytokinesis by misexpression of human Cdc14A phosphatase."; RL Mol. Biol. Cell 13:2289-2300(2002). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF MET-362 AND ILE-364. RX PubMed=11901424; DOI=10.1038/ncb777; RA Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J.; RT "Deregulated human Cdc14A phosphatase disrupts centrosome separation and RT chromosome segregation."; RL Nat. Cell Biol. 4:317-322(2002). RN [12] RP INTERACTION WITH KIF20A, AND SUBCELLULAR LOCATION. RX PubMed=15263015; DOI=10.1083/jcb.200403084; RA Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A.; RT "Relocation of Aurora B from centromeres to the central spindle at the RT metaphase to anaphase transition requires MKlp2."; RL J. Cell Biol. 166:167-172(2004). RN [13] RP FUNCTION AS SIRT2 PHOSPHATASE. RX PubMed=17488717; DOI=10.1074/jbc.m702990200; RA North B.J., Verdin E.; RT "Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent RT phosphorylation."; RL J. Biol. Chem. 282:19546-19555(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP INVOLVEMENT IN DFNB32, AND VARIANTS DFNB32 339-ARG--TYR-594 DEL AND RP 376-ARG--TYR-594 DEL. RX PubMed=27259055; DOI=10.1016/j.ajhg.2016.04.015; RA Delmaghani S., Aghaie A., Bouyacoub Y., El Hachmi H., Bonnet C., Riahi Z., RA Chardenoux S., Perfettini I., Hardelin J.P., Houmeida A., Herbomel P., RA Petit C.; RT "Mutations in CDC14A, encoding a protein phosphatase involved in hair cell RT ciliogenesis, cause autosomal-recessive severe to profound deafness."; RL Am. J. Hum. Genet. 98:1266-1270(2016). RN [16] RP FUNCTION, VARIANTS DFNB32 139-TYR--TYR-594 DEL; GLN-312; GLY-312; PRO-320; RP 345-ARG--TYR-594 DEL AND 376-ARG--TYR-594 DEL, AND INVOLVEMENT IN DFNB32. RX PubMed=29293958; DOI=10.1093/hmg/ddx440; RA Imtiaz A., Belyantseva I.A., Beirl A.J., Fenollar-Ferrer C., Bashir R., RA Bukhari I., Bouzid A., Shaukat U., Azaiez H., Booth K.T., Kahrizi K., RA Najmabadi H., Maqsood A., Wilson E.A., Fitzgerald T.S., Tlili A., RA Olszewski R., Lund M., Chaudhry T., Rehman A.U., Starost M.F., Waryah A.M., RA Hoa M., Dong L., Morell R.J., Smith R.J.H., Riazuddin S., Masmoudi S., RA Kindt K.S., Naz S., Friedman T.B.; RT "CDC14A phosphatase is essential for hearing and male fertility in mouse RT and human."; RL Hum. Mol. Genet. 27:780-798(2018). RN [17] RP VARIANT [LARGE SCALE ANALYSIS] TYR-493. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Dual-specificity phosphatase. Required for centrosome CC separation and productive cytokinesis during cell division. CC Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the CC APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation CC of mitotic cyclins and subsequent exit from mitosis. Required for CC normal hearing (PubMed:29293958). {ECO:0000269|PubMed:11901424, CC ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:17488717, CC ECO:0000269|PubMed:29293958, ECO:0000269|PubMed:9367992}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- SUBUNIT: Interacts with KIF20A, which is required to localize CDC14 to CC the midzone of the mitotic spindle. {ECO:0000269|PubMed:15263015}. CC -!- INTERACTION: CC Q9UNH5; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-7851002, EBI-1166928; CC Q9UNH5; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-7851002, EBI-725606; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9367992}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069}. Cytoplasm, CC cytoskeleton, spindle pole {ECO:0000269|PubMed:11901424, CC ECO:0000269|PubMed:15263015}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:15263015}. Cell projection, kinocilium CC {ECO:0000250|UniProtKB:Q6GQT0}. Cell projection, stereocilium CC {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase, CC released into the cytoplasm at the onset of mitosis. Subsequently CC localizes to the mitotic spindle pole and at the central spindle CC (PubMed:12134069, PubMed:11901424, PubMed:15263015). Present along both CC the transient kinocilia of developing cochlear hair cells and the CC persistent kinocilia of vestibular hair cells (By similarity). CC {ECO:0000250|UniProtKB:Q6GQT0, ECO:0000269|PubMed:11901424, CC ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:15263015}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=CDC14A1; CC IsoId=Q9UNH5-1; Sequence=Displayed; CC Name=2; Synonyms=CDC14A2; CC IsoId=Q9UNH5-2; Sequence=VSP_012037; CC Name=3; Synonyms=CDC14A3; CC IsoId=Q9UNH5-3; Sequence=VSP_012035, VSP_012036; CC Name=4; Synonyms=CDC14A4; CC IsoId=Q9UNH5-4; Sequence=VSP_012322, VSP_012323; CC Name=5; CC IsoId=Q9UNH5-5; Sequence=VSP_047597; CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that CC adopt a dual specificity protein phosphatase (DSP) fold. {ECO:0000250}. CC -!- DISEASE: Deafness, autosomal recessive, 32, with or without immotile CC sperm (DFNB32) [MIM:608653]: A form of non-syndromic sensorineural CC hearing loss. Sensorineural deafness results from damage to the neural CC receptors of the inner ear, the nerve pathways to the brain, or the CC area of the brain that receives sound information. DFNB32 is CC characterized by prelingual, progressive, moderate to profound CC sensorineural deafness. Some affected men are infertile. CC {ECO:0000269|PubMed:27259055, ECO:0000269|PubMed:29293958}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class CDC14 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB88277.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdc14a/"; 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; AF000367; AAB88277.1; ALT_FRAME; mRNA. DR EMBL; AF122013; AAD49217.1; -; mRNA. DR EMBL; AF064102; AAC16659.1; -; mRNA. DR EMBL; AF064103; AAC16660.1; -; mRNA. DR EMBL; DQ530256; ABF74568.1; -; mRNA. DR EMBL; AY623111; AAT38107.1; -; Genomic_DNA. DR EMBL; AC104457; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL589990; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW72956.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72958.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72959.1; -; Genomic_DNA. DR EMBL; BC038979; AAH38979.1; -; mRNA. DR EMBL; BC093916; AAH93916.1; -; mRNA. DR EMBL; BC093918; AAH93918.1; -; mRNA. DR CCDS; CCDS769.1; -. [Q9UNH5-1] DR CCDS; CCDS770.1; -. [Q9UNH5-2] DR CCDS; CCDS771.1; -. [Q9UNH5-3] DR CCDS; CCDS86000.1; -. [Q9UNH5-5] DR RefSeq; NP_001306139.1; NM_001319210.1. [Q9UNH5-5] DR RefSeq; NP_001306140.1; NM_001319211.1. DR RefSeq; NP_001306141.1; NM_001319212.1. DR RefSeq; NP_003663.2; NM_003672.3. [Q9UNH5-1] DR RefSeq; NP_201569.1; NM_033312.2. [Q9UNH5-2] DR RefSeq; NP_201570.1; NM_033313.2. [Q9UNH5-3] DR AlphaFoldDB; Q9UNH5; -. DR SMR; Q9UNH5; -. DR BioGRID; 114126; 112. DR IntAct; Q9UNH5; 50. DR MINT; Q9UNH5; -. DR STRING; 9606.ENSP00000354916; -. DR BindingDB; Q9UNH5; -. DR ChEMBL; CHEMBL1772926; -. DR DEPOD; CDC14A; -. DR iPTMnet; Q9UNH5; -. DR PhosphoSitePlus; Q9UNH5; -. DR BioMuta; CDC14A; -. DR DMDM; 55976620; -. DR EPD; Q9UNH5; -. DR jPOST; Q9UNH5; -. DR MassIVE; Q9UNH5; -. DR PaxDb; 9606-ENSP00000354916; -. DR PeptideAtlas; Q9UNH5; -. DR ProteomicsDB; 792; -. DR ProteomicsDB; 85289; -. [Q9UNH5-1] DR ProteomicsDB; 85290; -. [Q9UNH5-2] DR ProteomicsDB; 85291; -. [Q9UNH5-3] DR Pumba; Q9UNH5; -. DR Antibodypedia; 19991; 361 antibodies from 32 providers. DR DNASU; 8556; -. DR Ensembl; ENST00000336454.5; ENSP00000336739.3; ENSG00000079335.20. [Q9UNH5-1] DR Ensembl; ENST00000361544.11; ENSP00000354916.6; ENSG00000079335.20. [Q9UNH5-2] DR Ensembl; ENST00000370124.8; ENSP00000359142.3; ENSG00000079335.20. [Q9UNH5-3] DR Ensembl; ENST00000644813.1; ENSP00000496374.1; ENSG00000079335.20. [Q9UNH5-5] DR GeneID; 8556; -. DR KEGG; hsa:8556; -. DR MANE-Select; ENST00000336454.5; ENSP00000336739.3; NM_003672.4; NP_003663.2. DR UCSC; uc001dte.5; human. [Q9UNH5-1] DR AGR; HGNC:1718; -. DR CTD; 8556; -. DR DisGeNET; 8556; -. DR GeneCards; CDC14A; -. DR HGNC; HGNC:1718; CDC14A. DR HPA; ENSG00000079335; Tissue enhanced (testis). DR MalaCards; CDC14A; -. DR MIM; 603504; gene. DR MIM; 608653; phenotype. DR neXtProt; NX_Q9UNH5; -. DR OpenTargets; ENSG00000079335; -. DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB. DR PharmGKB; PA26254; -. DR VEuPathDB; HostDB:ENSG00000079335; -. DR eggNOG; KOG1720; Eukaryota. DR GeneTree; ENSGT00940000155899; -. DR HOGENOM; CLU_017787_0_2_1; -. DR InParanoid; Q9UNH5; -. DR OMA; EDMKLHT; -. DR OrthoDB; 9871at2759; -. DR PhylomeDB; Q9UNH5; -. DR TreeFam; TF101053; -. DR PathwayCommons; Q9UNH5; -. DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR SignaLink; Q9UNH5; -. DR SIGNOR; Q9UNH5; -. DR BioGRID-ORCS; 8556; 13 hits in 1188 CRISPR screens. DR ChiTaRS; CDC14A; human. DR GeneWiki; CDC14A; -. DR GenomeRNAi; 8556; -. DR Pharos; Q9UNH5; Tbio. DR PRO; PR:Q9UNH5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UNH5; Protein. DR Bgee; ENSG00000079335; Expressed in sperm and 147 other cell types or tissues. DR ExpressionAtlas; Q9UNH5; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:1902636; C:kinociliary basal body; ISS:UniProtKB. DR GO; GO:0060091; C:kinocilium; ISS:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000922; C:spindle pole; IBA:GO_Central. DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central. DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR CDD; cd14499; CDC14_C; 1. DR CDD; cd17657; CDC14_N; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2. DR InterPro; IPR044506; CDC14_C. DR InterPro; IPR029260; DSPn. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR23339:SF77; DUAL SPECIFICITY PROTEIN PHOSPHATASE CDC14A; 1. DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR Pfam; PF00782; DSPc; 1. DR Pfam; PF14671; DSPn; 1. DR SMART; SM00195; DSPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q9UNH5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Cell projection; KW Cytoplasm; Cytoskeleton; Deafness; Disease variant; Hearing; Hydrolase; KW Non-syndromic deafness; Nucleus; Phosphoprotein; Protein phosphatase; KW Reference proteome. FT CHAIN 1..594 FT /note="Dual specificity protein phosphatase CDC14A" FT /id="PRO_0000094876" FT DOMAIN 179..336 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 7..162 FT /note="A" FT REGION 163..176 FT /note="Linker" FT REGION 177..343 FT /note="B" FT REGION 396..435 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 487..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 398..417 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 278 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 583 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 174..191 FT /note="RVENGDFNWIVPGKFLAF -> VILFTPLKPTFLISKSIM (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012322" FT VAR_SEQ 192..594 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012323" FT VAR_SEQ 380..383 FT /note="DNLE -> VSFP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_012035" FT VAR_SEQ 384..594 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_012036" FT VAR_SEQ 586..594 FT /note="SLQSEYVHY -> VSAQTPPPGPQNPECNFCALPSQPRLPPKKFNSAKEAF FT (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_012037" FT VAR_SEQ 586..594 FT /note="SLQSEYVHY -> CSCLLLVFRKPFLGSPLLSLPISHL (in isoform FT 5)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047597" FT VARIANT 139..594 FT /note="Missing (in DFNB32)" FT /evidence="ECO:0000269|PubMed:29293958" FT /id="VAR_081127" FT VARIANT 312 FT /note="R -> G (in DFNB32; dbSNP:rs148737918)" FT /evidence="ECO:0000269|PubMed:29293958" FT /id="VAR_081128" FT VARIANT 312 FT /note="R -> Q (in DFNB32; dbSNP:rs369245990)" FT /evidence="ECO:0000269|PubMed:29293958" FT /id="VAR_081129" FT VARIANT 320 FT /note="Q -> P (in DFNB32; dbSNP:rs1339709390)" FT /evidence="ECO:0000269|PubMed:29293958" FT /id="VAR_081130" FT VARIANT 339..594 FT /note="Missing (in DFNB32)" FT /evidence="ECO:0000269|PubMed:27259055" FT /id="VAR_081131" FT VARIANT 345..594 FT /note="Missing (in DFNB32)" FT /evidence="ECO:0000269|PubMed:29293958" FT /id="VAR_081132" FT VARIANT 345 FT /note="R -> Q (in dbSNP:rs28364897)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_019957" FT VARIANT 376..594 FT /note="Missing (in DFNB32)" FT /evidence="ECO:0000269|PubMed:27259055, FT ECO:0000269|PubMed:29293958" FT /id="VAR_081133" FT VARIANT 493 FT /note="D -> Y (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035655" FT VARIANT 589 FT /note="S -> F (in dbSNP:rs28364923)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_019958" FT MUTAGEN 251 FT /note="D->A: Loss of phosphatase activity." FT /evidence="ECO:0000269|PubMed:12134069" FT MUTAGEN 278 FT /note="C->S: Loss of phosphatase activity." FT /evidence="ECO:0000269|PubMed:11598127, FT ECO:0000269|PubMed:12134069" FT MUTAGEN 284 FT /note="R->A: Loss of phosphatase activity." FT /evidence="ECO:0000269|PubMed:12134069" FT MUTAGEN 362 FT /note="M->A: Inappropriate nucleolar localization; when FT associated with A-364." FT /evidence="ECO:0000269|PubMed:11901424" FT MUTAGEN 364 FT /note="I->A: Inappropriate nucleolar localization; when FT associated with A-362." FT /evidence="ECO:0000269|PubMed:11901424" FT CONFLICT 164 FT /note="F -> I (in Ref. 1; AAB88277)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="W -> C (in Ref. 1; AAB88277)" FT /evidence="ECO:0000305" SQ SEQUENCE 594 AA; 66574 MW; D5552E2BAEEA84DF CRC64; MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY //