CC14B_HUMAN
ID CC14B_HUMAN Reviewed; 498 AA.
AC O60729; A6N5X8; A8MQ20; B1AL31; B1AL32; O43183; O60730; Q5JU08;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Dual specificity protein phosphatase CDC14B;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDC14 cell division cycle 14 homolog B;
GN Name=CDC14B;
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] (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 [3]
RP SEQUENCE REVISION (ISOFORM 3).
RA Hao L., Baskerville C., Charbonneau H.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Rosso L., Marques A.C., Kaessmann H.;
RT "Subcellular adaptation of a hominoid cell cycle protein expressed in the
RT brain.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-302 AND THR-341.
RG NIEHS SNPs program;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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 [10]
RP SUBCELLULAR LOCATION.
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 [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FZR1.
RX PubMed=18662541; DOI=10.1016/j.cell.2008.05.043;
RA Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A.,
RA Pagano M.;
RT "The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
RT checkpoint.";
RL Cell 134:256-267(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-386.
RX PubMed=12853468; DOI=10.1093/emboj/cdg348;
RA Gray C.H., Good V.M., Tonks N.K., Barford D.;
RT "The structure of the cell cycle protein Cdc14 reveals a proline-directed
RT protein phosphatase.";
RL EMBO J. 22:3524-3535(2003).
CC -!- FUNCTION: Dual-specificity phosphatase involved in DNA damage response.
CC Essential regulator of the G2 DNA damage checkpoint: following DNA
CC damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a
CC key activator of the anaphase promoting complex/cyclosome (APC/C).
CC Dephosphorylates SIRT2 around early anaphase. Dephosphorylation of
CC FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1,
CC preventing entry into mitosis. Preferentially dephosphorylates proteins
CC modified by proline-directed kinases. {ECO:0000269|PubMed:17488717,
CC ECO:0000269|PubMed:18662541, 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, ECO:0000269|PubMed:12134069};
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 Evidence={ECO:0000269|PubMed:12134069};
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 Evidence={ECO:0000269|PubMed:12134069};
CC -!- SUBUNIT: Interacts with FZR1/CDH1. {ECO:0000269|PubMed:18662541}.
CC -!- INTERACTION:
CC O60729; P55081: MFAP1; NbExp=3; IntAct=EBI-970231, EBI-1048159;
CC O60729; O43741: PRKAB2; NbExp=3; IntAct=EBI-970231, EBI-1053424;
CC O60729; P20618: PSMB1; NbExp=3; IntAct=EBI-970231, EBI-372273;
CC O60729; Q8IXJ6: SIRT2; NbExp=2; IntAct=EBI-970231, EBI-477232;
CC O60729; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-970231, EBI-12023934;
CC O60729; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-970231, EBI-11090299;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC Note=Following DNA damage, translocates from the nucleolus to the
CC nucleoplasm and interacts with FZR1/CDH1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2; Synonyms=CDC14B2;
CC IsoId=O60729-1; Sequence=Displayed;
CC Name=1; Synonyms=CDC14B1;
CC IsoId=O60729-2; Sequence=VSP_012038;
CC Name=3; Synonyms=CDC14B3;
CC IsoId=O60729-3; Sequence=VSP_012039;
CC Name=4;
CC IsoId=O60729-4; Sequence=VSP_030720;
CC Name=5;
CC IsoId=O60729-5; Sequence=VSP_043576;
CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that
CC adopt a dual specificity protein phosphatase (DSP) fold.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc14b/";
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DR EMBL; AF023158; AAB88293.1; -; mRNA.
DR EMBL; AF064104; AAC16661.1; -; mRNA.
DR EMBL; AF064105; AAC16662.2; -; mRNA.
DR EMBL; AK126388; BAG54321.1; -; mRNA.
DR EMBL; EF611343; ABR12627.1; -; mRNA.
DR EMBL; AY675321; AAT70726.1; -; Genomic_DNA.
DR EMBL; AL133477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471174; EAW92658.1; -; Genomic_DNA.
DR EMBL; CH471174; EAW92659.1; -; Genomic_DNA.
DR CCDS; CCDS43853.1; -. [O60729-5]
DR CCDS; CCDS6721.1; -. [O60729-2]
DR CCDS; CCDS6722.1; -. [O60729-1]
DR CCDS; CCDS87662.1; -. [O60729-4]
DR RefSeq; NP_001070649.1; NM_001077181.1. [O60729-5]
DR RefSeq; NP_003662.1; NM_003671.3. [O60729-2]
DR RefSeq; NP_201588.1; NM_033331.2. [O60729-1]
DR RefSeq; XP_011517460.1; XM_011519158.1.
DR RefSeq; XP_016870732.1; XM_017015243.1.
DR PDB; 1OHC; X-ray; 2.50 A; A=39-386.
DR PDB; 1OHD; X-ray; 2.60 A; A=39-386.
DR PDB; 1OHE; X-ray; 2.20 A; A=39-386.
DR PDBsum; 1OHC; -.
DR PDBsum; 1OHD; -.
DR PDBsum; 1OHE; -.
DR AlphaFoldDB; O60729; -.
DR SMR; O60729; -.
DR BioGRID; 114125; 159.
DR IntAct; O60729; 92.
DR MINT; O60729; -.
DR STRING; 9606.ENSP00000364389; -.
DR DEPOD; CDC14B; -.
DR iPTMnet; O60729; -.
DR PhosphoSitePlus; O60729; -.
DR BioMuta; CDC14B; -.
DR EPD; O60729; -.
DR jPOST; O60729; -.
DR MassIVE; O60729; -.
DR PaxDb; O60729; -.
DR PeptideAtlas; O60729; -.
DR PRIDE; O60729; -.
DR ProteomicsDB; 49572; -. [O60729-1]
DR ProteomicsDB; 49573; -. [O60729-2]
DR ProteomicsDB; 49574; -. [O60729-3]
DR ProteomicsDB; 49575; -. [O60729-4]
DR ProteomicsDB; 49576; -. [O60729-5]
DR Antibodypedia; 14207; 128 antibodies from 25 providers.
DR DNASU; 8555; -.
DR Ensembl; ENST00000375240.7; ENSP00000364388.3; ENSG00000081377.17. [O60729-2]
DR Ensembl; ENST00000375241.6; ENSP00000364389.1; ENSG00000081377.17. [O60729-1]
DR Ensembl; ENST00000375242.7; ENSP00000364390.3; ENSG00000081377.17. [O60729-5]
DR Ensembl; ENST00000463569.5; ENSP00000420572.1; ENSG00000081377.17. [O60729-4]
DR Ensembl; ENST00000474602.5; ENSP00000417897.1; ENSG00000081377.17. [O60729-3]
DR GeneID; 8555; -.
DR KEGG; hsa:8555; -.
DR MANE-Select; ENST00000375241.6; ENSP00000364389.1; NM_033331.4; NP_201588.1.
DR UCSC; uc004awi.4; human. [O60729-1]
DR CTD; 8555; -.
DR DisGeNET; 8555; -.
DR GeneCards; CDC14B; -.
DR HGNC; HGNC:1719; CDC14B.
DR HPA; ENSG00000081377; Tissue enhanced (brain).
DR MIM; 603505; gene.
DR neXtProt; NX_O60729; -.
DR OpenTargets; ENSG00000081377; -.
DR PharmGKB; PA26255; -.
DR VEuPathDB; HostDB:ENSG00000081377; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00940000155950; -.
DR HOGENOM; CLU_017787_2_0_1; -.
DR InParanoid; O60729; -.
DR OMA; TFDLHEF; -.
DR OrthoDB; 1357618at2759; -.
DR PhylomeDB; O60729; -.
DR TreeFam; TF101053; -.
DR PathwayCommons; O60729; -.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR SignaLink; O60729; -.
DR SIGNOR; O60729; -.
DR BioGRID-ORCS; 8555; 11 hits in 1087 CRISPR screens.
DR ChiTaRS; CDC14B; human.
DR EvolutionaryTrace; O60729; -.
DR GeneWiki; CDC14B; -.
DR GenomeRNAi; 8555; -.
DR Pharos; O60729; Tbio.
DR PRO; PR:O60729; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O60729; protein.
DR Bgee; ENSG00000081377; Expressed in corpus callosum and 197 other tissues.
DR ExpressionAtlas; O60729; baseline and differential.
DR Genevisible; O60729; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair; Hydrolase;
KW Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..498
FT /note="Dual specificity protein phosphatase CDC14B"
FT /id="PRO_0000094878"
FT DOMAIN 214..374
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..198
FT /note="A"
FT REGION 199..212
FT /note="Linker"
FT REGION 213..379
FT /note="B"
FT REGION 459..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..54
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..53
FT /note="MKRKSERRSSWAAAPPCSRRCSSTSPGVKKIRSSTQQDPRRRDPQDDVYLDI
FT T -> MSREGAGAALVAEVIK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043576"
FT VAR_SEQ 449..498
FT /note="VILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR
FT -> DGWLSQAVTFLDRLLIWLGIHKD (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012039"
FT VAR_SEQ 449..498
FT /note="VILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR
FT -> CPLAVLTSALCSVVIWWIVCDYILPILLFCLDGFRTQ (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_030720"
FT VAR_SEQ 449..487
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9367992"
FT /id="VSP_012038"
FT VARIANT 302
FT /note="I -> T (in dbSNP:rs16911114)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_019959"
FT VARIANT 341
FT /note="I -> T (in dbSNP:rs16911075)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_019960"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 48..60
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1OHE"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1OHE"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1OHC"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1OHE"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1OHC"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:1OHE"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1OHE"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:1OHE"
FT HELIX 355..377
FT /evidence="ECO:0007829|PDB:1OHE"
SQ SEQUENCE 498 AA; 56802 MW; CEE15EC4DC3B1DC7 CRC64;
MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL DITDRLCFAI
LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIVH
FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE AYRILIFGET SYIPFRDAAY GSCNFYITLL
DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY
HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL
DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG SVIGPQQQFL
VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI SINGVENQDQ QEPEPYSDDD
EINGVTQGDR LRALKSRRQS KTNAIPLTVI LQSSVQSCKT SEPNISGSAG ITKRTTRSAS
RKSSVKSLSI SRTKTVLR
