PTN3_HUMAN
ID PTN3_HUMAN Reviewed; 913 AA.
AC P26045; A0AUW9; E7EN99; E9PGU7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 3;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase H1;
DE Short=PTP-H1;
GN Name=PTPN3; Synonyms=PTPH1;
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), AND VARIANT PRO-90.
RX PubMed=1648725; DOI=10.1073/pnas.88.14.5949;
RA Yang Q., Tonks N.K.;
RT "Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase
RT with homology to the cytoskeletal-associated proteins band 4.1, ezrin, and
RT talin.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5949-5953(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Fetal kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-896 (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=1626183; DOI=10.1159/000217763;
RA Arimura Y., Hinoda Y., Itoh F., Takekawa M., Tsujisaki M., Adachi M.,
RA Imai K., Yachi A.;
RT "cDNA cloning of new protein tyrosine phosphatases in the human colon.";
RL Tumor Biol. 13:180-186(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 899-913 (ISOFORM 1).
RX PubMed=7874267; DOI=10.1007/bf02349278;
RA Ikuta S., Itoh F., Hinoda Y., Toyota M., Makiguchi Y., Imai K., Yachi A.;
RT "Expression of cytoskeletal-associated protein tyrosine phosphatase PTPH1
RT mRNA in human hepatocellular carcinoma.";
RL J. Gastroenterol. 29:727-732(1994).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-367; THR-376 AND
RP SER-381, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-359, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 628-913.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein tyrosine
RT phosphatome.";
RL Cell 136:352-363(2009).
CC -!- FUNCTION: May act at junctions between the membrane and the
CC cytoskeleton. Possesses tyrosine phosphatase activity.
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 -!- INTERACTION:
CC P26045; Q04828: AKR1C1; NbExp=6; IntAct=EBI-1047946, EBI-2116455;
CC P26045; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-1047946, EBI-10233719;
CC P26045; P42566-1: EPS15; NbExp=4; IntAct=EBI-1047946, EBI-15895294;
CC P26045; P10912: GHR; NbExp=4; IntAct=EBI-1047946, EBI-286316;
CC P26045; P25800: LMO1; NbExp=6; IntAct=EBI-1047946, EBI-8639312;
CC P26045; P23508: MCC; NbExp=2; IntAct=EBI-1047946, EBI-307531;
CC P26045; P40692: MLH1; NbExp=3; IntAct=EBI-1047946, EBI-744248;
CC P26045; Q96QG7: MTMR9; NbExp=3; IntAct=EBI-1047946, EBI-744593;
CC P26045; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-1047946, EBI-752122;
CC P26045; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1047946, EBI-742388;
CC P26045; Q14524: SCN5A; NbExp=2; IntAct=EBI-1047946, EBI-726858;
CC P26045; P31040: SDHA; NbExp=2; IntAct=EBI-1047946, EBI-1057265;
CC P26045; Q6ZRS2-3: SRCAP; NbExp=3; IntAct=EBI-1047946, EBI-12029182;
CC P26045; Q8NEK8: TENT5D; NbExp=3; IntAct=EBI-1047946, EBI-744726;
CC P26045; Q01664: TFAP4; NbExp=3; IntAct=EBI-1047946, EBI-2514218;
CC P26045; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-1047946, EBI-725997;
CC P26045; Q8TAA9: VANGL1; NbExp=4; IntAct=EBI-1047946, EBI-682393;
CC P26045; Q9ULK5: VANGL2; NbExp=2; IntAct=EBI-1047946, EBI-1054279;
CC P26045; P55072: VCP; NbExp=2; IntAct=EBI-1047946, EBI-355164;
CC P26045; P11473: VDR; NbExp=4; IntAct=EBI-1047946, EBI-286357;
CC P26045; Q5GFL6-3: VWA2; NbExp=3; IntAct=EBI-1047946, EBI-13451145;
CC P26045; Q9NNW5: WDR6; NbExp=6; IntAct=EBI-1047946, EBI-1568315;
CC P26045; P31946: YWHAB; NbExp=5; IntAct=EBI-1047946, EBI-359815;
CC P26045; P61981: YWHAG; NbExp=5; IntAct=EBI-1047946, EBI-359832;
CC P26045; P63104: YWHAZ; NbExp=5; IntAct=EBI-1047946, EBI-347088;
CC P26045; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-1047946, EBI-597063;
CC P26045; P06463: E6; Xeno; NbExp=4; IntAct=EBI-1047946, EBI-1186926;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P26045-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26045-2; Sequence=VSP_046309;
CC Name=3;
CC IsoId=P26045-3; Sequence=VSP_046309, VSP_046310;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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; M64572; AAA35647.1; -; mRNA.
DR EMBL; BX648253; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX648735; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL359963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW59046.1; -; Genomic_DNA.
DR EMBL; BC126117; AAI26118.1; -; mRNA.
DR EMBL; S39392; AAB22439.2; -; mRNA.
DR EMBL; S76309; AAB33583.1; -; mRNA.
DR CCDS; CCDS48000.1; -. [P26045-3]
DR CCDS; CCDS48001.1; -. [P26045-2]
DR CCDS; CCDS6776.1; -. [P26045-1]
DR PIR; A41109; A41109.
DR RefSeq; NP_001138840.1; NM_001145368.1.
DR RefSeq; NP_001138841.1; NM_001145369.1. [P26045-2]
DR RefSeq; NP_001138842.1; NM_001145370.1. [P26045-3]
DR RefSeq; NP_001138843.1; NM_001145371.1.
DR RefSeq; NP_002820.3; NM_002829.3. [P26045-1]
DR RefSeq; XP_006717262.1; XM_006717199.3. [P26045-1]
DR RefSeq; XP_006717267.1; XM_006717204.3. [P26045-2]
DR RefSeq; XP_011517191.1; XM_011518889.2. [P26045-1]
DR RefSeq; XP_016870444.1; XM_017014955.1. [P26045-1]
DR RefSeq; XP_016870446.1; XM_017014957.1. [P26045-3]
DR PDB; 2B49; X-ray; 1.54 A; A=628-913.
DR PDB; 4QUM; X-ray; 2.52 A; A=628-909.
DR PDB; 4QUN; X-ray; 1.86 A; A/B=628-909.
DR PDB; 4RH5; X-ray; 1.60 A; A=628-909.
DR PDB; 4RH9; X-ray; 1.60 A; A=628-909.
DR PDB; 4RHG; X-ray; 1.58 A; A=628-909.
DR PDB; 4RI4; X-ray; 1.60 A; A/B=628-909.
DR PDB; 4RI5; X-ray; 1.26 A; A/B=628-909.
DR PDB; 4S0G; X-ray; 1.72 A; A=628-909.
DR PDB; 6HKS; X-ray; 2.19 A; A/B/C/D/E/F=489-597.
DR PDB; 6T36; X-ray; 1.86 A; A=1-913.
DR PDBsum; 2B49; -.
DR PDBsum; 4QUM; -.
DR PDBsum; 4QUN; -.
DR PDBsum; 4RH5; -.
DR PDBsum; 4RH9; -.
DR PDBsum; 4RHG; -.
DR PDBsum; 4RI4; -.
DR PDBsum; 4RI5; -.
DR PDBsum; 4S0G; -.
DR PDBsum; 6HKS; -.
DR PDBsum; 6T36; -.
DR AlphaFoldDB; P26045; -.
DR SMR; P26045; -.
DR BioGRID; 111740; 91.
DR DIP; DIP-38839N; -.
DR IntAct; P26045; 57.
DR MINT; P26045; -.
DR STRING; 9606.ENSP00000363667; -.
DR BindingDB; P26045; -.
DR ChEMBL; CHEMBL2396509; -.
DR DEPOD; PTPN3; -.
DR iPTMnet; P26045; -.
DR PhosphoSitePlus; P26045; -.
DR BioMuta; PTPN3; -.
DR DMDM; 229462761; -.
DR EPD; P26045; -.
DR jPOST; P26045; -.
DR MassIVE; P26045; -.
DR MaxQB; P26045; -.
DR PaxDb; P26045; -.
DR PeptideAtlas; P26045; -.
DR PRIDE; P26045; -.
DR ProteomicsDB; 17113; -.
DR ProteomicsDB; 20397; -.
DR ProteomicsDB; 54312; -. [P26045-1]
DR Antibodypedia; 29434; 247 antibodies from 33 providers.
DR DNASU; 5774; -.
DR Ensembl; ENST00000374541.4; ENSP00000363667.1; ENSG00000070159.14. [P26045-1]
DR Ensembl; ENST00000412145.5; ENSP00000416654.1; ENSG00000070159.14. [P26045-2]
DR Ensembl; ENST00000446349.5; ENSP00000395384.1; ENSG00000070159.14. [P26045-3]
DR GeneID; 5774; -.
DR KEGG; hsa:5774; -.
DR MANE-Select; ENST00000374541.4; ENSP00000363667.1; NM_002829.4; NP_002820.3.
DR UCSC; uc004beb.2; human. [P26045-1]
DR CTD; 5774; -.
DR DisGeNET; 5774; -.
DR GeneCards; PTPN3; -.
DR HGNC; HGNC:9655; PTPN3.
DR HPA; ENSG00000070159; Tissue enhanced (skeletal).
DR MalaCards; PTPN3; -.
DR MIM; 176877; gene.
DR neXtProt; NX_P26045; -.
DR OpenTargets; ENSG00000070159; -.
DR Orphanet; 70567; Cholangiocarcinoma.
DR PharmGKB; PA33999; -.
DR VEuPathDB; HostDB:ENSG00000070159; -.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000157888; -.
DR HOGENOM; CLU_001645_7_1_1; -.
DR InParanoid; P26045; -.
DR OMA; EHHSFFQ; -.
DR OrthoDB; 96595at2759; -.
DR PhylomeDB; P26045; -.
DR TreeFam; TF315900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P26045; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR SignaLink; P26045; -.
DR SIGNOR; P26045; -.
DR BioGRID-ORCS; 5774; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; PTPN3; human.
DR EvolutionaryTrace; P26045; -.
DR GeneWiki; PTPN3; -.
DR GenomeRNAi; 5774; -.
DR Pharos; P26045; Tbio.
DR PRO; PR:P26045; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P26045; protein.
DR Bgee; ENSG00000070159; Expressed in oocyte and 187 other tissues.
DR ExpressionAtlas; P26045; baseline and differential.
DR Genevisible; P26045; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:BHF-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0098902; P:regulation of membrane depolarization during action potential; IDA:BHF-UCL.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041783; PTPN3/4_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
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; PF00595; PDZ; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 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; PS50106; PDZ; 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; Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..913
FT /note="Tyrosine-protein phosphatase non-receptor type 3"
FT /id="PRO_0000219433"
FT DOMAIN 29..312
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 510..582
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 646..901
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 363..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 842
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 811
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 842..848
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 886
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046309"
FT VAR_SEQ 335..379
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046310"
FT VARIANT 77
FT /note="D -> N (in dbSNP:rs35285139)"
FT /id="VAR_055252"
FT VARIANT 90
FT /note="A -> P (in dbSNP:rs3793524)"
FT /evidence="ECO:0000269|PubMed:1648725"
FT /id="VAR_055253"
FT VARIANT 409
FT /note="T -> A (in dbSNP:rs10979858)"
FT /id="VAR_055254"
FT VARIANT 605
FT /note="F -> L (in dbSNP:rs7859962)"
FT /id="VAR_055255"
FT VARIANT 763
FT /note="D -> N (in dbSNP:rs10116806)"
FT /id="VAR_055256"
FT CONFLICT 814
FT /note="V -> I (in Ref. 1; AAA35647 and 6; AAB22439)"
FT /evidence="ECO:0000305"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:6T36"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:6T36"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:6T36"
FT STRAND 533..540
FT /evidence="ECO:0007829|PDB:6T36"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:6T36"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:6T36"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:6T36"
FT HELIX 572..581
FT /evidence="ECO:0007829|PDB:6T36"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:6T36"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:6T36"
FT HELIX 630..643
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 645..652
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 668..673
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:4RH9"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 695..705
FT /evidence="ECO:0007829|PDB:4RI5"
FT TURN 706..709
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 710..717
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 725..734
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 739..742
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 764..767
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 770..779
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 781..792
FT /evidence="ECO:0007829|PDB:4RI5"
FT TURN 793..795
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 798..806
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:2B49"
FT HELIX 818..831
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:4RI5"
FT STRAND 843..846
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 847..863
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 870..878
FT /evidence="ECO:0007829|PDB:4RI5"
FT HELIX 888..907
FT /evidence="ECO:0007829|PDB:4RI5"
SQ SEQUENCE 913 AA; 103990 MW; 44FBBFA35A5F2AFF CRC64;
MTSRLRALGG RINNIRTSEL PKEKTRSEVI CSIHFLDGVV QTFKVTKQDT GQVLLDMVHN
HLGVTEKEYF GLQHDDDSVD SPRWLEASKA IRKQLKGGFP CTLHFRVRFF IPDPNTLQQE
QTRHLYFLQL KMDICEGRLT CPLNSAVVLA SYAVQSHFGD YNSSIHHPGY LSDSHFIPDQ
NEDFLTKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHSGRDLHNL DLMIGIASAG
VAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS
CVEHHTFFQA KKLLPQEKNV LSQYWTMGSR NTKKSVNNQY CKKVIGGMVW NPAMRRSLSV
EHLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGSL
APQDSDSEVS QNRSPHQESL SENNPAQSYL TQKSSSSVSP SSNAPGSCSP DGVDQQLLDD
FHRVTKGGST EDASQYYCDK NDNGDSYLVL IRITPDEDGK FGFNLKGGVD QKMPLVVSRI
NPESPADTCI PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRRAVR
SFADFKSEDE LNQLFPEAIF PMCPEGGDTL EGSMAQLKKG LESGTVLIQF EQLYRKKPGL
AITFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEIPAANL VNKYIATQGP
LPHTCAQFWQ VVWDQKLSLI VMLTTLTERG RTKCHQYWPD PPDVMNHGGF HIQCQSEDCT
IAYVSREMLV TNTQTGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVNYVRS LRVDSEPVLV
HCSAGIGRTG VLVTMETAMC LTERNLPIYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR
VYEEGLVQML DPS
