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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
 
 
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