PTN14_HUMAN
ID PTN14_HUMAN Reviewed; 1187 AA.
AC Q15678; Q5VSI0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 14;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase pez;
GN Name=PTPN14; Synonyms=PEZ, PTPD2;
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].
RC TISSUE=Mammary carcinoma;
RX PubMed=7733990; DOI=10.1006/bbrc.1995.1591;
RA Smith A.L., Mitchell P.J., Shipley J., Gusterson B.A., Rogers M.V.,
RA Crompton M.R.;
RT "Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-
RT like domains.";
RL Biochem. Biophys. Res. Commun. 209:959-965(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10934049; DOI=10.1242/jcs.113.17.3117;
RA Wadham C., Gamble J.R., Vadas M.A., Khew-Goodall Y.;
RT "Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the
RT nucleus is associated with induction of cell proliferation.";
RL J. Cell Sci. 113:3117-3123(2000).
RN [6]
RP FUNCTION.
RX PubMed=12808048; DOI=10.1091/mbc.e02-09-0577;
RA Wadham C., Gamble J.R., Vadas M.A., Khew-Goodall Y.;
RT "The protein tyrosine phosphatase Pez is a major phosphatase of adherens
RT junctions and dephosphorylates beta-catenin.";
RL Mol. Biol. Cell 14:2520-2529(2003).
RN [7]
RP FUNCTION.
RX PubMed=17893246; DOI=10.1083/jcb.200705035;
RA Wyatt L., Wadham C., Crocker L.A., Lardelli M., Khew-Goodall Y.;
RT "The protein tyrosine phosphatase Pez regulates TGFbeta, epithelial-
RT mesenchymal transition, and organ development.";
RL J. Cell Biol. 178:1223-1235(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP FUNCTION, INTERACTION WITH FLT4, AND INVOLVEMENT IN CATLPH.
RX PubMed=20826270; DOI=10.1016/j.ajhg.2010.08.008;
RA Au A.C., Hernandez P.A., Lieber E., Nadroo A.M., Shen Y.M., Kelley K.A.,
RA Gelb B.D., Diaz G.A.;
RT "Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function
RT and choanal development in humans.";
RL Am. J. Hum. Genet. 87:436-444(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591; SER-594 AND SER-642, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP SUBCELLULAR LOCATION, INDUCTION, FUNCTION, INTERACTION WITH YAP1; CUL2 AND
RP LRR1, AND UBIQUITINATION.
RX PubMed=22948661; DOI=10.1101/gad.192955.112;
RA Wang W., Huang J., Wang X., Yuan J., Li X., Feng L., Park J.I., Chen J.;
RT "PTPN14 is required for the density-dependent control of YAP1.";
RL Genes Dev. 26:1959-1971(2012).
RN [14]
RP INVOLVEMENT IN HTT, AND FUNCTION.
RX PubMed=22233626; DOI=10.1038/ncomms1633;
RA Benzinou M., Clermont F.F., Letteboer T.G., Kim J.H., Espejel S.,
RA Harradine K.A., Arbelaez J., Luu M.T., Roy R., Quigley D., Higgins M.N.,
RA Zaid M., Aouizerat B.E., van Amstel J.K., Giraud S., Dupuis-Girod S.,
RA Lesca G., Plauchu H., Hughes C.C., Westermann C.J., Akhurst R.J.;
RT "Mouse and human strategies identify PTPN14 as a modifier of angiogenesis
RT and hereditary haemorrhagic telangiectasia.";
RL Nat. Commun. 3:616-616(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [16]
RP INTERACTION WITH YAP1, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22525271; DOI=10.1038/onc.2012.147;
RA Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H.,
RA Zhang J.;
RT "PTPN14 interacts with and negatively regulates the oncogenic function of
RT YAP.";
RL Oncogene 32:1266-1273(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 886-1187.
RX PubMed=16534812; DOI=10.1002/prot.20958;
RA Barr A.J., Debreczeni J.E., Eswaran J., Knapp S.;
RT "Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at
RT 1.65-A resolution.";
RL Proteins 63:1132-1136(2006).
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-159 AND PRO-360.
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: Protein tyrosine phosphatase which may play a role in the
CC regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix
CC adhesion, cell migration, cell growth and also regulates TGF-beta gene
CC expression, thereby modulating epithelial-mesenchymal transition.
CC Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as
CC a negative regulator of the oncogenic property of YAP, a downstream
CC target of the hippo pathway, in a cell density-dependent manner. May
CC function as a tumor suppressor. {ECO:0000269|PubMed:10934049,
CC ECO:0000269|PubMed:12808048, ECO:0000269|PubMed:17893246,
CC ECO:0000269|PubMed:20826270, ECO:0000269|PubMed:22233626,
CC ECO:0000269|PubMed:22525271, ECO:0000269|PubMed:22948661}.
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 -!- SUBUNIT: Interacts with FLT4; the interaction is enhanced by
CC stimulation with VEGFC. Interacts (via PPxY motifs) with YAP1 (via WW
CC domains); this interaction leads to the cytoplasmic sequestration of
CC YAP1 and inhibits its transcriptional co-activator activity.
CC {ECO:0000269|PubMed:20826270, ECO:0000269|PubMed:22525271,
CC ECO:0000269|PubMed:22948661}.
CC -!- INTERACTION:
CC Q15678; A2BDD9: AMOT; NbExp=3; IntAct=EBI-1237156, EBI-17286414;
CC Q15678; Q15654: TRIP6; NbExp=3; IntAct=EBI-1237156, EBI-742327;
CC Q15678; P46937: YAP1; NbExp=7; IntAct=EBI-1237156, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Nucleus. Note=Translocation into the nucleus is associated with
CC induction of cell proliferation. Partially colocalized with actin
CC filaments at the plasma membrane.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: Up-regulated at protein level by cell density. However, at
CC the mRNA level remains the same regardless of the status of cell
CC density. {ECO:0000269|PubMed:22948661}.
CC -!- PTM: Ubiquitinated by the ECS (Elongin BC-CUL2/5-SOCS-box protein)/LRR1
CC E3 ligase complex and subsequently targeted to proteasomal degradation.
CC {ECO:0000269|PubMed:22948661}.
CC -!- DISEASE: Choanal atresia and lymphedema (CATLPH) [MIM:613611]: A
CC disease characterized by posterior choanal atresia and lymphedema.
CC Additional features are a high-arched palate, hypoplastic nipples, and
CC mild pectus excavatum. {ECO:0000269|PubMed:20826270}. Note=The disease
CC is caused by variants affecting the gene represented in this entry. A
CC homozygous deletion in PTPN14 predicted to result in frameshift and
CC premature truncation, has been shown to be the cause of choanal atresia
CC and lymphedema in one family.
CC -!- DISEASE: Note=Influence clinical severity of hereditary haemorragic
CC telagiectasia (HHT). {ECO:0000269|PubMed:22233626}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPN14ID41913ch1q32.html";
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; X82676; CAA57993.1; -; mRNA.
DR EMBL; AL929236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93351.1; -; Genomic_DNA.
DR EMBL; BC101754; AAI01755.1; -; mRNA.
DR EMBL; BC104803; AAI04804.1; -; mRNA.
DR CCDS; CCDS1514.1; -.
DR PIR; JC4155; JC4155.
DR RefSeq; NP_005392.2; NM_005401.4.
DR RefSeq; XP_016857430.1; XM_017001941.1.
DR PDB; 2BZL; X-ray; 1.65 A; A=886-1187.
DR PDB; 6IWD; X-ray; 1.80 A; A=886-1187.
DR PDB; 6JJW; X-ray; 2.40 A; U=428-455.
DR PDBsum; 2BZL; -.
DR PDBsum; 6IWD; -.
DR PDBsum; 6JJW; -.
DR AlphaFoldDB; Q15678; -.
DR SMR; Q15678; -.
DR BioGRID; 111748; 154.
DR DIP; DIP-38131N; -.
DR IntAct; Q15678; 34.
DR MINT; Q15678; -.
DR STRING; 9606.ENSP00000355923; -.
DR BindingDB; Q15678; -.
DR ChEMBL; CHEMBL3317332; -.
DR DEPOD; PTPN14; -.
DR iPTMnet; Q15678; -.
DR PhosphoSitePlus; Q15678; -.
DR BioMuta; PTPN14; -.
DR DMDM; 209572662; -.
DR EPD; Q15678; -.
DR jPOST; Q15678; -.
DR MassIVE; Q15678; -.
DR MaxQB; Q15678; -.
DR PaxDb; Q15678; -.
DR PeptideAtlas; Q15678; -.
DR PRIDE; Q15678; -.
DR ProteomicsDB; 60701; -.
DR Antibodypedia; 34618; 168 antibodies from 28 providers.
DR DNASU; 5784; -.
DR Ensembl; ENST00000366956.10; ENSP00000355923.4; ENSG00000152104.12.
DR GeneID; 5784; -.
DR KEGG; hsa:5784; -.
DR MANE-Select; ENST00000366956.10; ENSP00000355923.4; NM_005401.5; NP_005392.2.
DR UCSC; uc001hkk.3; human.
DR CTD; 5784; -.
DR DisGeNET; 5784; -.
DR GeneCards; PTPN14; -.
DR HGNC; HGNC:9647; PTPN14.
DR HPA; ENSG00000152104; Low tissue specificity.
DR MalaCards; PTPN14; -.
DR MIM; 603155; gene.
DR MIM; 613611; phenotype.
DR neXtProt; NX_Q15678; -.
DR OpenTargets; ENSG00000152104; -.
DR Orphanet; 99141; Lymphedema-posterior choanal atresia syndrome.
DR PharmGKB; PA33989; -.
DR VEuPathDB; HostDB:ENSG00000152104; -.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000156874; -.
DR HOGENOM; CLU_006456_1_0_1; -.
DR InParanoid; Q15678; -.
DR OMA; HYTETHN; -.
DR OrthoDB; 144506at2759; -.
DR PhylomeDB; Q15678; -.
DR TreeFam; TF315900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q15678; -.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR SignaLink; Q15678; -.
DR SIGNOR; Q15678; -.
DR BioGRID-ORCS; 5784; 30 hits in 1083 CRISPR screens.
DR ChiTaRS; PTPN14; human.
DR EvolutionaryTrace; Q15678; -.
DR GeneWiki; PTPN14; -.
DR GenomeRNAi; 5784; -.
DR Pharos; Q15678; Tbio.
DR PRO; PR:Q15678; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15678; protein.
DR Bgee; ENSG00000152104; Expressed in buccal mucosa cell and 181 other tissues.
DR ExpressionAtlas; Q15678; baseline and differential.
DR Genevisible; Q15678; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IDA:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR IDEAL; IID00476; -.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR014392; PTP_non-rcpt_14/21.
DR InterPro; IPR041782; PTPN14/21_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1187
FT /note="Tyrosine-protein phosphatase non-receptor type 14"
FT /id="PRO_0000219437"
FT DOMAIN 21..306
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 909..1180
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 510..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1121
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1079
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1121..1127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62130"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62130"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62130"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62130"
FT VARIANT 159
FT /note="Q -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035849"
FT VARIANT 360
FT /note="H -> P (in a breast cancer sample; somatic mutation;
FT dbSNP:rs112523432)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035850"
FT VARIANT 505
FT /note="V -> F (in dbSNP:rs12239356)"
FT /id="VAR_046995"
FT CONFLICT 392
FT /note="H -> D (in Ref. 1; CAA57993)"
FT /evidence="ECO:0000305"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:6JJW"
FT HELIX 896..903
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 909..914
FT /evidence="ECO:0007829|PDB:2BZL"
FT TURN 926..929
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 946..948
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:6IWD"
FT STRAND 956..958
FT /evidence="ECO:0007829|PDB:6IWD"
FT STRAND 964..972
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 975..982
FT /evidence="ECO:0007829|PDB:2BZL"
FT TURN 987..989
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 990..999
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1004..1007
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1011..1013
FT /evidence="ECO:0007829|PDB:2BZL"
FT TURN 1029..1031
FT /evidence="ECO:0007829|PDB:6IWD"
FT STRAND 1032..1035
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1038..1047
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1049..1060
FT /evidence="ECO:0007829|PDB:2BZL"
FT TURN 1061..1063
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1066..1074
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 1086..1103
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 1105..1107
FT /evidence="ECO:0007829|PDB:2BZL"
FT STRAND 1117..1125
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 1126..1142
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 1149..1157
FT /evidence="ECO:0007829|PDB:2BZL"
FT HELIX 1167..1183
FT /evidence="ECO:0007829|PDB:2BZL"
SQ SEQUENCE 1187 AA; 135261 MW; 1D22F1C8ED06C096 CRC64;
MPFGLKLRRT RRYNVLSKNC FVTRIRLLDS NVIECTLSVE STGQECLEAV AQRLELRETH
YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM FYVPNVSWLQ QEATRYQYYL
QVKKDVLEGR LRCTLDQVIR LAGLAVQADF GDYNQFDSQD FLREYVLFPM DLALEEAVLE
ELTQKVAQEH KAHSGILPAE AELMYINEVE RLDGFGQEIF PVKDNHGNCV HLGIFFMGIF
VRNRIGRQAV IYRWNDMGNI THNKSTILVE LINKEETALF HTDDIENAKY ISRLFATRHK
FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPV HVQCGEHYSE THTSQDSIFH
GNEEALYCNS HNSLDLNYLN GTVTNGSVCS VHSVNSLNCS QSFIQASPVS SNLSIPGSDI
MRADYIPSHR HSAIIVPSYR PTPDYETVMR QMKRGILHTD SQSQSLRNLN IINTHAYNQP
EDLVYSQPEM RERHPYTVPY GPQGVYSNKL VSPSDQRNPK NNVVPSKPGA SAISHTVSTP
ELANMQLQGS HNYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR
KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGTVNKR HSLEVMNSMV RGMEAMTLKS
LHLPMARRNT LREQGPPEEG SGSHEVPQLP QYHHKKTFSD ATMLIHSSES EEEEEEAPES
VPQIPMLREK MEYSAQLQAA LARIPNKPPP EYPGPRKSVS NGALRQDQAS LPPAMARARV
LRHGPAKAIS MSRTDPPAVN GASLGPSISE PDLTSVKERV KKEPVKERPV SEMFSLEDSI
IEREMMIRNL EKQKMAGLEA QKRPLMLAAL NGLSVARVSG REENRVDATR VPMDERFRTL
KKKLEEGMVF TEYEQIPKKK ANGIFSTAAL PENAERSRIR EVVPYEENRV ELIPTKENNT
GYINASHIKV VVGGAEWHYI ATQGPLPHTC HDFWQMVWEQ GVNVIAMVTA EEEGGRTKSH
RYWPKLGSKH SSATYGKFKV TTKFRTDSVC YATTGLKVKH LLSGQERTVW HLQYTDWPDH
GCPEDVQGFL SYLEEIQSVR RHTNSMLEGT KNRHPPIVVH CSAGVGRTGV LILSELMIYC
LEHNEKVEVP MMLRLLREQR MFMIQTIAQY KFVYQVLIQF LQNSRLI
