ID PTPRT_HUMAN Reviewed; 1441 AA. AC O14522; A8E4R6; O43655; O75664; Q5W0X9; Q5W0Y1; Q9BR24; Q9BR28; AC Q9H0Y8; Q9NTL1; Q9NU72; Q9UBD2; Q9UJL7; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 6. DT 13-FEB-2019, entry version 171. DE RecName: Full=Receptor-type tyrosine-protein phosphatase T; DE Short=R-PTP-T; DE EC=3.1.3.48; DE AltName: Full=Receptor-type tyrosine-protein phosphatase rho; DE Short=RPTP-rho; DE Flags: Precursor; GN Name=PTPRT; Synonyms=KIAA0283; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND VARIANT RP PRO-29. RX PubMed=9602027; DOI=10.1016/S0169-328X(98)00014-X; RA McAndrew P.E., Frostholm A., White R.A., Rotter A., Burghes A.H.M.; RT "Identification and characterization of RPTP rho, a novel RPTP RT mu/kappa-like receptor protein tyrosine phosphatase whose expression RT is restricted to the central nervous system."; RL Brain Res. Mol. Brain Res. 56:9-21(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP PRO-29. RC TISSUE=Brain; RX PubMed=9179496; DOI=10.1093/dnares/4.1.53; RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., RA Nomura N.; RT "Construction and characterization of human brain cDNA libraries RT suitable for analysis of cDNA clones encoding relatively large RT proteins."; RL DNA Res. 4:53-59(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP PRO-29. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ALTERNATIVE SPLICING. RX PubMed=11423001; DOI=10.1186/1471-2164-2-1; RA Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.; RT "Genomic organization and alternative splicing of the human and mouse RT RPTPrho genes."; RL BMC Genomics 2:1-1(2001). RN [6] RP ERRATUM. RX PubMed=11814386; DOI=10.1186/1471-2164-2-5; RA Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.; RL BMC Genomics 2:5-5(2001). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 868-1151. 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 RT tyrosine phosphatome."; RL Cell 136:352-363(2009). RN [8] RP VARIANTS SER-74; THR-209; THR-218; SER-248; HIS-280; VAL-395; PHE-412; RP CYS-453; LYS-510; MET-605; GLY-648; THR-707; VAL-707; PRO-708; RP ILE-771; GLY-905; LYS-965; PRO-1096; ILE-1106; TRP-1190; LEU-1237; RP MET-1247; LEU-1324; PHE-1329 AND MET-1346, AND TISSUE SPECIFICITY. RX PubMed=15155950; DOI=10.1126/science.1096096; RA Wang Z., Shen D., Parsons D.W., Bardelli A., Sager J., Szabo S., RA Ptak J., Silliman N., Peters B.A., van der Heijden M.S., RA Parmigiani G., Yan H., Wang T.-L., Riggins G., Powell S.M., RA Willson J.K.V., Markowitz S., Kinzler K.W., Vogelstein B., RA Velculescu V.E.; RT "Mutational analysis of the tyrosine phosphatome in colorectal RT cancers."; RL Science 304:1164-1166(2004). RN [9] RP VARIANT [LARGE SCALE ANALYSIS] LEU-1213. RX PubMed=18987736; DOI=10.1038/nature07485; RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., RA Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., RA Graubert T.A., DiPersio J.F., Wilson R.K.; RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia RT genome."; RL Nature 456:66-72(2008). RN [10] RP VARIANT MET-1346. RX PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644; RA Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E., RA van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C., RA Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S., RA Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T., RA Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., RA Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A., RA van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.; RT "Identification of pathogenic gene variants in small families with RT intellectually disabled siblings by exome sequencing."; RL J. Med. Genet. 50:802-811(2013). CC -!- FUNCTION: May be involved in both signal transduction and cellular CC adhesion in the CNS. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] CC + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CC -!- INTERACTION: CC P62993:GRB2; NbExp=2; IntAct=EBI-728180, EBI-401755; CC Q99K10:Nlgn1 (xeno); NbExp=2; IntAct=EBI-728180, EBI-775037; CC Q69ZK9:Nlgn2 (xeno); NbExp=2; IntAct=EBI-728180, EBI-775065; CC Q9CS84:Nrxn1 (xeno); NbExp=2; IntAct=EBI-728180, EBI-399696; CC Q6P9K9:Nrxn3 (xeno); NbExp=2; IntAct=EBI-728180, EBI-7281557; CC Q16849:PTPRN; NbExp=3; IntAct=EBI-728180, EBI-728153; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=3; CC IsoId=O14522-3; Sequence=Displayed; CC Name=1; CC IsoId=O14522-1; Sequence=VSP_040385, VSP_040386; CC -!- TISSUE SPECIFICITY: Expressed in colon, lung, heart and testis, as CC well as in fetal and adult brain. Not detected in muscle and CC peripheral blood leukocytes. {ECO:0000269|PubMed:15155950}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 2B subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA22952.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={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; AF043644; AAD09421.2; -; mRNA. DR EMBL; AB006621; BAA22952.2; ALT_INIT; mRNA. DR EMBL; AL021395; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL022239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL024473; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031656; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035459; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049812; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121763; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136461; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z93942; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035666; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL109826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL117374; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359695; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC153300; AAI53301.1; -; mRNA. DR CCDS; CCDS42874.1; -. [O14522-3] DR RefSeq; NP_008981.4; NM_007050.5. [O14522-3] DR RefSeq; NP_573400.3; NM_133170.3. DR UniGene; Hs.526879; -. DR PDB; 2OOQ; X-ray; 1.80 A; A/B=868-1151. DR PDBsum; 2OOQ; -. DR ProteinModelPortal; O14522; -. DR SMR; O14522; -. DR BioGrid; 116296; 7. DR DIP; DIP-33967N; -. DR IntAct; O14522; 14. DR MINT; O14522; -. DR STRING; 9606.ENSP00000362283; -. DR DEPOD; O14522; -. DR iPTMnet; O14522; -. DR PhosphoSitePlus; O14522; -. DR BioMuta; PTPRT; -. DR EPD; O14522; -. DR jPOST; O14522; -. DR MaxQB; O14522; -. DR PaxDb; O14522; -. DR PeptideAtlas; O14522; -. DR PRIDE; O14522; -. DR ProteomicsDB; 48065; -. DR ProteomicsDB; 48066; -. [O14522-1] DR DNASU; 11122; -. DR Ensembl; ENST00000373187; ENSP00000362283; ENSG00000196090. [O14522-3] DR Ensembl; ENST00000373193; ENSP00000362289; ENSG00000196090. [O14522-1] DR GeneID; 11122; -. DR KEGG; hsa:11122; -. DR UCSC; uc002xkg.4; human. [O14522-3] DR CTD; 11122; -. DR DisGeNET; 11122; -. DR EuPathDB; HostDB:ENSG00000196090.12; -. DR GeneCards; PTPRT; -. DR HGNC; HGNC:9682; PTPRT. DR HPA; CAB069423; -. DR HPA; HPA017336; -. DR MIM; 608712; gene. DR neXtProt; NX_O14522; -. DR OpenTargets; ENSG00000196090; -. DR PharmGKB; PA34027; -. DR eggNOG; KOG4228; Eukaryota. DR eggNOG; COG5599; LUCA. DR GeneTree; ENSGT00940000155326; -. DR HOVERGEN; HBG062785; -. DR InParanoid; O14522; -. DR KO; K13297; -. DR OMA; CTAGGKW; -. DR OrthoDB; 411281at2759; -. DR PhylomeDB; O14522; -. DR TreeFam; TF312900; -. DR BRENDA; 3.1.3.48; 2681. DR SignaLink; O14522; -. DR ChiTaRS; PTPRT; human. DR EvolutionaryTrace; O14522; -. DR GeneWiki; PTPRT; -. DR GenomeRNAi; 11122; -. DR PRO; PR:O14522; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000196090; Expressed in 82 organ(s), highest expression level in middle temporal gyrus. DR ExpressionAtlas; O14522; baseline and differential. DR Genevisible; O14522; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045294; F:alpha-catenin binding; IDA:UniProtKB. DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB. DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB. DR GO; GO:0070097; F:delta-catenin binding; IPI:UniProtKB. DR GO; GO:0045295; F:gamma-catenin binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:ARUK-UCL. DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB. DR GO; GO:0097677; F:STAT family protein binding; IPI:ARUK-UCL. DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:ARUK-UCL. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:ARUK-UCL. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL. DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; IDA:ARUK-UCL. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:ARUK-UCL. DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IDA:ARUK-UCL. DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IMP:UniProtKB. DR CDD; cd00063; FN3; 3. DR CDD; cd06263; MAM; 1. DR Gene3D; 2.60.40.10; -; 4. DR Gene3D; 3.90.190.10; -; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR000998; MAM_dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTPase_domain. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR Pfam; PF00041; fn3; 2. DR Pfam; PF00629; MAM; 1. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00020; MAMDOMAIN. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 3. DR SMART; SM00137; MAM; 1. DR SMART; SM00194; PTPc; 2. DR SMART; SM00404; PTPc_motif; 2. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF49265; SSF49265; 2. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF52799; SSF52799; 2. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00740; MAM_1; 1. DR PROSITE; PS50060; MAM_2; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; KW Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; KW Phosphoprotein; Polymorphism; Protein phosphatase; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 1441 Receptor-type tyrosine-protein FT phosphatase T. FT /FTId=PRO_0000025463. FT TOPO_DOM 26 747 Extracellular. {ECO:0000255}. FT TRANSMEM 748 768 Helical. {ECO:0000255}. FT TOPO_DOM 769 1441 Cytoplasmic. {ECO:0000255}. FT DOMAIN 30 191 MAM. {ECO:0000255|PROSITE- FT ProRule:PRU00128}. FT DOMAIN 193 284 Ig-like C2-type. FT DOMAIN 291 384 Fibronectin type-III 1. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 389 483 Fibronectin type-III 2. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 484 590 Fibronectin type-III 3. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 591 726 Fibronectin type-III 4. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 889 1143 Tyrosine-protein phosphatase 1. FT {ECO:0000255|PROSITE-ProRule:PRU00160}. FT DOMAIN 1175 1437 Tyrosine-protein phosphatase 2. FT {ECO:0000255|PROSITE-ProRule:PRU00160}. FT REGION 1084 1090 Substrate binding. {ECO:0000250}. FT ACT_SITE 1084 1084 Phosphocysteine intermediate. FT {ECO:0000250}. FT ACT_SITE 1378 1378 Phosphocysteine intermediate. FT {ECO:0000250}. FT BINDING 1052 1052 Substrate. {ECO:0000250}. FT BINDING 1128 1128 Substrate. {ECO:0000250}. FT MOD_RES 1208 1208 Phosphoserine. FT {ECO:0000250|UniProtKB:Q99M80}. FT CARBOHYD 78 78 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 98 98 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 137 137 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 208 208 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 421 421 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 510 510 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 547 547 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 601 601 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 654 654 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 684 684 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 213 267 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 725 725 K -> KAPMGSAQVTPGTPLCLLTT (in isoform 1). FT {ECO:0000303|PubMed:9602027}. FT /FTId=VSP_040385. FT VAR_SEQ 781 781 L -> LSQR (in isoform 1). FT {ECO:0000303|PubMed:9602027}. FT /FTId=VSP_040386. FT VARIANT 29 29 A -> P (in dbSNP:rs2867655). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9179496, FT ECO:0000269|PubMed:9602027}. FT /FTId=VAR_028795. FT VARIANT 74 74 F -> S (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020746. FT VARIANT 76 76 M -> V (in dbSNP:rs17811401). FT /FTId=VAR_028796. FT VARIANT 209 209 A -> T (in some colorectal cancers). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020747. FT VARIANT 218 218 K -> T (in a gastric cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020748. FT VARIANT 248 248 F -> S (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020749. FT VARIANT 280 280 Y -> H (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020750. FT VARIANT 395 395 I -> V (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020751. FT VARIANT 412 412 Y -> F (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020752. FT VARIANT 453 453 R -> C (in a gastric cancer; FT dbSNP:rs1371429276). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020753. FT VARIANT 510 510 N -> K (in a colorectal cancer; FT dbSNP:rs749647294). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020754. FT VARIANT 605 605 T -> M (in a colorectal cancer; FT dbSNP:rs1217327426). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020755. FT VARIANT 648 648 V -> G (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020756. FT VARIANT 707 707 A -> T (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020757. FT VARIANT 707 707 A -> V (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020758. FT VARIANT 708 708 L -> P (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020759. FT VARIANT 771 771 R -> I (in a lung cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020760. FT VARIANT 905 905 D -> G (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020761. FT VARIANT 965 965 Q -> K (in a colorectal cancer; reduced FT phosphatase activity). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020762. FT VARIANT 1096 1096 A -> P (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020763. FT VARIANT 1106 1106 N -> I (in a colorectal cancer; reduced FT phosphatase activity). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020764. FT VARIANT 1190 1190 R -> W (in a colorectal cancer; reduced FT phosphatase activity; dbSNP:rs370873414). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020765. FT VARIANT 1213 1213 P -> L (in an acute myeloid leukemia FT sample; somatic mutation). FT {ECO:0000269|PubMed:18987736}. FT /FTId=VAR_054144. FT VARIANT 1237 1237 M -> L (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020766. FT VARIANT 1247 1247 V -> M (in a colorectal cancer; FT dbSNP:rs761148007). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020767. FT VARIANT 1324 1324 R -> L (in a lung cancer; reduced FT phosphatase activity). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020768. FT VARIANT 1329 1329 Y -> F (in a colorectal cancer). FT {ECO:0000269|PubMed:15155950}. FT /FTId=VAR_020769. FT VARIANT 1346 1346 T -> M (found in a patient with severe FT intellectual disability, behavioral FT problems, microcephaly, congenital FT cardiac defect and herniation of the FT abdominal diaphragm; also observed in FT some colorectal cancers; reduced FT phosphatase activity; unknown FT pathological significance; FT dbSNP:rs199947379). FT {ECO:0000269|PubMed:15155950, FT ECO:0000269|PubMed:24123876}. FT /FTId=VAR_020770. FT CONFLICT 60 60 W -> T (in Ref. 1; AAD09421). FT {ECO:0000305}. FT CONFLICT 375 375 P -> A (in Ref. 1; AAD09421). FT {ECO:0000305}. FT CONFLICT 867 867 P -> L (in Ref. 1; AAD09421). FT {ECO:0000305}. FT HELIX 871 873 {ECO:0000244|PDB:2OOQ}. FT HELIX 874 882 {ECO:0000244|PDB:2OOQ}. FT HELIX 889 895 {ECO:0000244|PDB:2OOQ}. FT TURN 905 908 {ECO:0000244|PDB:2OOQ}. FT HELIX 910 915 {ECO:0000244|PDB:2OOQ}. FT HELIX 925 927 {ECO:0000244|PDB:2OOQ}. FT HELIX 938 941 {ECO:0000244|PDB:2OOQ}. FT STRAND 944 948 {ECO:0000244|PDB:2OOQ}. FT STRAND 951 953 {ECO:0000244|PDB:2OOQ}. FT STRAND 957 960 {ECO:0000244|PDB:2OOQ}. FT TURN 965 967 {ECO:0000244|PDB:2OOQ}. FT HELIX 968 978 {ECO:0000244|PDB:2OOQ}. FT STRAND 982 985 {ECO:0000244|PDB:2OOQ}. FT STRAND 989 991 {ECO:0000244|PDB:2OOQ}. FT STRAND 1003 1009 {ECO:0000244|PDB:2OOQ}. FT STRAND 1011 1020 {ECO:0000244|PDB:2OOQ}. FT STRAND 1022 1033 {ECO:0000244|PDB:2OOQ}. FT STRAND 1040 1047 {ECO:0000244|PDB:2OOQ}. FT HELIX 1060 1072 {ECO:0000244|PDB:2OOQ}. FT STRAND 1080 1083 {ECO:0000244|PDB:2OOQ}. FT STRAND 1085 1088 {ECO:0000244|PDB:2OOQ}. FT HELIX 1089 1107 {ECO:0000244|PDB:2OOQ}. FT STRAND 1108 1110 {ECO:0000244|PDB:2OOQ}. FT HELIX 1112 1122 {ECO:0000244|PDB:2OOQ}. FT HELIX 1130 1145 {ECO:0000244|PDB:2OOQ}. SQ SEQUENCE 1441 AA; 162134 MW; BE60F3DB2CE13539 CRC64; MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDEHYSN CGYSVALGTN GFTWEQINTW EKPMLDQAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL NVYVKVNGGP QGNPVWNVSG VVTEGWVKAE LAISTFWPHF YQVIFESVSL KGHPGYIAVD EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT RVVNHRRFSA TVSVADTAQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY NLTVQYQYVF NQQQYEAEEV IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEELVVQT EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYRNASSLDS LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV RLATKGASTQ NSNTVEPEKQ VDNTVKMAGV IAGLLMFIII LLGVMLTIKR RRNAYSYSYY LKLAKKQKET QSGAQREMGP VASADKPTTK LSASRNDEGF SSSSQDVNGF TDGSRGELSQ PTLTIQTHPY RTCDPVEMSY PRDQFQPAIR VADLLQHITQ MKRGQGYGFK EEYEALPEGQ TASWDTAKED ENRNKNRYGN IISYDHSRVR LLVLDGDPHS DYINANYIDG YHRPRHYIAT QGPMQETVKD FWRMIWQENS ASIVMVTNLV EVGRVKCVRY WPDDTEVYGD IKVTLIETEP LAEYVIRTFT VQKKGYHEIR ELRLFHFTSW PDHGVPCYAT GLLGFVRQVK FLNPPEAGPI VVHCSAGAGR TGCFIAIDTM LDMAENEGVV DIFNCVRELR AQRVNLVQTE EQYVFVHDAI LEACLCGNTA IPVCEFRSLY YNISRLDPQT NSSQIKDEFQ TLNIVTPRVR PEDCSIGLLP RNHDKNRSMD VLPLDRCLPF LISVDGESSN YINAALMDSH KQPAAFVVTQ HPLPNTVADF WRLVFDYNCS SVVMLNEMDT AQFCMQYWPE KTSGCYGPIQ VEFVSADIDE DIIHRIFRIC NMARPQDGYR IVQHLQYIGW PAYRDTPPSK RSLLKVVRRL EKWQEQYDGR EGRTVVHCLN GGGRSGTFCA ICSVCEMIQQ QNIIDVFHIV KTLRNNKSNM VETLEQYKFV YEVALEYLSS F //