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Receptor-type tyrosine-protein phosphatase U (R-PTP-U) (EC 3.1.3.48) (Pancreatic carcinoma phosphatase 2) (PCP-2) (Protein-tyrosine phosphatase J) (PTP-J) (hPTP-J) (Protein-tyrosine phosphatase pi) (PTP pi) (Protein-tyrosine phosphatase receptor omicron) (PTP-RO) (Receptor-type protein-tyrosine phosphatase psi) (R-PTP-psi)

 PTPRU_HUMAN             Reviewed;        1446 AA.
Q92729; A6H8L1; O00197; P78399; Q59HA4; Q5SYU4; Q5SYU5; Q92735;
Q92850;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
10-OCT-2018, entry version 180.
RecName: Full=Receptor-type tyrosine-protein phosphatase U;
Short=R-PTP-U;
EC=3.1.3.48;
AltName: Full=Pancreatic carcinoma phosphatase 2;
Short=PCP-2;
AltName: Full=Protein-tyrosine phosphatase J;
Short=PTP-J;
Short=hPTP-J;
AltName: Full=Protein-tyrosine phosphatase pi;
Short=PTP pi;
AltName: Full=Protein-tyrosine phosphatase receptor omicron;
Short=PTP-RO;
AltName: Full=Receptor-type protein-tyrosine phosphatase psi;
Short=R-PTP-psi;
Flags: Precursor;
Name=PTPRU; Synonyms=FMI, PCP2, PTPRO;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Mammary gland;
PubMed=8870675; DOI=10.1042/bj3190249;
Crossland S., Smith P.D., Crompton M.R.;
"Molecular cloning and characterization of PTP pi, a novel receptor-
like protein-tyrosine phosphatase.";
Biochem. J. 319:249-254(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY,
GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Pancreas;
PubMed=8700514;
Wang H.-Y., Lian Z., Lerch M.M., Chen Z., Xie W., Ullrich A.;
"Characterization of PCP-2, a novel receptor protein tyrosine
phosphatase of the MAM domain family.";
Oncogene 12:2555-2562(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Skeletal muscle;
PubMed=9070223; DOI=10.1006/bbrc.1997.6004;
Wang B., Kishihara K., Zhang D., Hara H., Nomoto K.;
"Molecular cloning and characterization of a novel human receptor
protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene
expression by PMA and calcium ionophore in Jurkat T lymphoma cells.";
Biochem. Biophys. Res. Commun. 231:77-81(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Brain;
PubMed=9434160; DOI=10.1016/S0378-1119(97)00420-4;
Avraham S., London R., Tulloch G.A., Ellis M., Fu Y., Jiang S.,
White R.A., Painter C., Steinberger A.A., Avraham H.;
"Characterization and chromosomal localization of PTPRO, a novel
receptor protein tyrosine phosphatase, expressed in hematopoietic stem
cells.";
Gene 204:5-16(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
Banville D., Masson S., L'Abbe D., Stocco R., Shen S.-H.;
"Cloning and expression of R-PTP-psi, a novel receptor protein
tyrosine phosphatase related to the homophilic binding R-PTP-kappa and
-mu.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1446 (ISOFORM 2).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
INDUCTION.
PubMed=10395944; DOI=10.1016/S0167-4889(99)00064-6;
Wang B., Kishihara K., Zhang D., Sakamoto T., Nomoto K.;
"Transcriptional regulation of a receptor protein tyrosine phosphatase
gene hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T
lymphoma cells.";
Biochim. Biophys. Acta 1450:331-340(1999).
[11]
FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, PROTEOLYTIC
PROCESSING, AND INDUCTION BY PHORBOL ESTER.
PubMed=10397721;
Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H.;
"The receptor protein tyrosine phosphatase, PTP-RO, is upregulated
during megakaryocyte differentiation and is associated with the c-Kit
receptor.";
Blood 94:539-549(1999).
[12]
FUNCTION, INTERACTION WITH CTNNB1, INDUCTION, AND MUTAGENESIS OF
CYS-1085 AND CYS-1380.
PubMed=12501215; DOI=10.1021/bi026095u;
Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F.,
Wu M.-C., Wang H.-Y.;
"Physical and functional interaction between receptor-like protein
tyrosine phosphatase PCP-2 and beta-catenin.";
Biochemistry 41:15854-15860(2002).
[13]
FUNCTION, INTERACTION WITH CTNNB1, AND MUTAGENESIS OF CYS-1085 AND
CYS-1380.
PubMed=16574648; DOI=10.1074/jbc.M602607200;
Yan H.-X., Yang W., Zhang R., Chen L., Tang L., Zhai B., Liu S.-Q.,
Cao H.-F., Man X.-B., Wu H.-P., Wu M.-C., Wang H.-Y.;
"Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling
and increases E-cadherin-dependent cell adhesion.";
J. Biol. Chem. 281:15423-15433(2006).
[14]
INTERACTION WITH AP3B1.
PubMed=17622474; DOI=10.1111/j.1745-7270.2007.00303.x;
Dong H., Yuan H., Jin W., Shen Y., Xu X., Wang H.-Y.;
"Involvement of beta3A subunit of adaptor protein-3 in intracellular
trafficking of receptor-like protein tyrosine phosphatase PCP-2.";
Acta Biochim. Biophys. Sin. 39:540-546(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848 AND SER-853, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
VARIANTS [LARGE SCALE ANALYSIS] TYR-830; TRP-835 AND CYS-856.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Tyrosine-protein phosphatase which dephosphorylates
CTNNB1. Regulates CTNNB1 function both in cell adhesion and
signaling. May function in cell proliferation and migration and
play a role in the maintenance of epithelial integrity. May play a
role in megakaryocytopoiesis. {ECO:0000269|PubMed:10397721,
ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:16574648}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:8700514}.
-!- SUBUNIT: Forms homooligomeric complexes which mediate cell
homotypic adhesion (Probable). Interacts (via the cytoplasmic
juxtamembrane domain) with CTNNB1; may mediate interaction with
the cadherin/catenin adhesion complex. Interacts with KIT. May
interact with AP3B1. {ECO:0000269|PubMed:10397721,
ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:16574648,
ECO:0000269|PubMed:17622474, ECO:0000305}.
-!- INTERACTION:
P10721:KIT; NbExp=2; IntAct=EBI-7052301, EBI-1379503;
-!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:8700514}.
Cell membrane {ECO:0000269|PubMed:8700514}; Single-pass type I
membrane protein {ECO:0000269|PubMed:8700514}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q92729-1; Sequence=Displayed;
Name=2;
IsoId=Q92729-2; Sequence=VSP_037082;
Name=3;
IsoId=Q92729-3; Sequence=VSP_037082, VSP_037084;
Name=4; Synonyms=PTPRO;
IsoId=Q92729-4; Sequence=VSP_037082, VSP_037083, VSP_037085;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High levels in brain, pancreas, and skeletal
muscle; less in colon, kidney, liver, stomach, and uterus; not
expressed in placenta and spleen. Also detected in heart,
prostate, lung, thymus, testis and ovary. Ubiquitously expressed
in brain. Expressed by hematopoietic stem cells.
{ECO:0000269|PubMed:8700514, ECO:0000269|PubMed:8870675,
ECO:0000269|PubMed:9070223, ECO:0000269|PubMed:9434160}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung and kidney.
{ECO:0000269|PubMed:9434160}.
-!- INDUCTION: Up-regulated upon cell contact (at protein level).
Down-regulated by phorbol ester (at protein level) and calcium
ionophore but up-regulated by phorbol ester in megakaryocytic
cells (PubMed:10397721). {ECO:0000269|PubMed:10395944,
ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12501215,
ECO:0000269|PubMed:9070223}.
-!- PTM: The extracellular domain is proteolytically processed through
cleavage within the fibronectin type-III 4 domain (By similarity).
In addition to the 190 kDa full-length protein, proteolytic
products of 100 kDa, 80 kDa and 73 kDa are observed. {ECO:0000250,
ECO:0000269|PubMed:10397721}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8700514}.
-!- PTM: Phosphorylated on tyrosine residues upon activation of KIT
with stem cell factor (SCF). The 73 kDa proteolytic product is not
phosphorylated. {ECO:0000269|PubMed:10397721}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 2B subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA65016.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems.; Evidence={ECO:0000305};
Sequence=CAA65832.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems.; Evidence={ECO:0000305};
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EMBL; X95712; CAA65016.1; ALT_SEQ; mRNA.
EMBL; X97198; CAA65832.1; ALT_SEQ; mRNA.
EMBL; U73727; AAB51343.1; -; mRNA.
EMBL; U71075; AAC51938.1; -; mRNA.
EMBL; U60289; AAB07074.1; -; Genomic_DNA.
EMBL; AL645859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07651.1; -; Genomic_DNA.
EMBL; CH471059; EAX07652.1; -; Genomic_DNA.
EMBL; BC146655; AAI46656.1; -; mRNA.
EMBL; AB208855; BAD92092.1; -; mRNA.
CCDS; CCDS334.1; -. [Q92729-1]
CCDS; CCDS335.1; -. [Q92729-2]
CCDS; CCDS44098.2; -. [Q92729-4]
CCDS; CCDS53290.1; -. [Q92729-3]
PIR; JC5290; JC5290.
PIR; S72441; S72441.
RefSeq; NP_001181930.1; NM_001195001.1. [Q92729-3]
RefSeq; NP_005695.3; NM_005704.4. [Q92729-1]
RefSeq; NP_573438.3; NM_133177.3. [Q92729-4]
RefSeq; NP_573439.2; NM_133178.3. [Q92729-2]
UniGene; Hs.19718; -.
ProteinModelPortal; Q92729; -.
SMR; Q92729; -.
BioGrid; 115386; 27.
IntAct; Q92729; 1.
MINT; Q92729; -.
STRING; 9606.ENSP00000334941; -.
ChEMBL; CHEMBL1961785; -.
DEPOD; Q92729; -.
iPTMnet; Q92729; -.
PhosphoSitePlus; Q92729; -.
BioMuta; PTPRU; -.
DMDM; 229462800; -.
EPD; Q92729; -.
MaxQB; Q92729; -.
PaxDb; Q92729; -.
PeptideAtlas; Q92729; -.
PRIDE; Q92729; -.
ProteomicsDB; 75416; -.
ProteomicsDB; 75417; -. [Q92729-2]
ProteomicsDB; 75418; -. [Q92729-3]
ProteomicsDB; 75419; -. [Q92729-4]
DNASU; 10076; -.
Ensembl; ENST00000345512; ENSP00000334941; ENSG00000060656. [Q92729-1]
Ensembl; ENST00000373779; ENSP00000362884; ENSG00000060656. [Q92729-2]
Ensembl; ENST00000428026; ENSP00000392332; ENSG00000060656. [Q92729-3]
Ensembl; ENST00000460170; ENSP00000432906; ENSG00000060656. [Q92729-4]
GeneID; 10076; -.
KEGG; hsa:10076; -.
UCSC; uc001bru.4; human. [Q92729-1]
CTD; 10076; -.
DisGeNET; 10076; -.
EuPathDB; HostDB:ENSG00000060656.19; -.
GeneCards; PTPRU; -.
H-InvDB; HIX0000346; -.
HGNC; HGNC:9683; PTPRU.
HPA; CAB011476; -.
HPA; HPA039832; -.
MIM; 602454; gene.
neXtProt; NX_Q92729; -.
OpenTargets; ENSG00000060656; -.
PharmGKB; PA34028; -.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00760000118900; -.
HOVERGEN; HBG062785; -.
InParanoid; Q92729; -.
KO; K16662; -.
OMA; ASFQCMA; -.
OrthoDB; EOG091G00CK; -.
PhylomeDB; Q92729; -.
TreeFam; TF312900; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
ChiTaRS; PTPRU; human.
GeneWiki; PTPRU; -.
GenomeRNAi; 10076; -.
PRO; PR:Q92729; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000060656; Expressed in 199 organ(s), highest expression level in epithelium of bronchus.
CleanEx; HS_PCP2; -.
CleanEx; HS_PTPRU; -.
Genevisible; Q92729; HS.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; NAS:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; NAS:UniProtKB.
CDD; cd00063; FN3; 3.
CDD; cd06263; MAM; 1.
Gene3D; 2.60.40.10; -; 4.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR000998; MAM_dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 2.
Pfam; PF00629; MAM; 1.
Pfam; PF00102; Y_phosphatase; 2.
PRINTS; PR00020; MAMDOMAIN.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 3.
SMART; SM00137; MAM; 1.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS00740; MAM_1; 1.
PROSITE; PS50060; MAM_2; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Differentiation; Disulfide bond; Glycoprotein;
Hydrolase; Immunoglobulin domain; Membrane; Phosphoprotein;
Polymorphism; Protein phosphatase; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1446 Receptor-type tyrosine-protein
phosphatase U.
/FTId=PRO_0000371658.
TOPO_DOM 19 749 Extracellular. {ECO:0000255}.
TRANSMEM 750 770 Helical. {ECO:0000255}.
TOPO_DOM 771 1446 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 188 MAM. {ECO:0000255|PROSITE-
ProRule:PRU00128}.
DOMAIN 190 275 Ig-like C2-type.
DOMAIN 288 383 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 386 484 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 485 591 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 592 674 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 888 1144 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 1176 1439 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 771 887 Mediates interaction with CTNNB1.
{ECO:0000250}.
REGION 1085 1091 Substrate binding. {ECO:0000250}.
ACT_SITE 1085 1085 Phosphocysteine intermediate.
{ECO:0000250}.
ACT_SITE 1380 1380 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 1053 1053 Substrate. {ECO:0000255}.
BINDING 1129 1129 Substrate. {ECO:0000250}.
MOD_RES 848 848 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000250|UniProtKB:B1AUH1}.
MOD_RES 865 865 Phosphotyrosine.
{ECO:0000250|UniProtKB:B1AUH1}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 685 685 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 210 264 {ECO:0000255}.
VAR_SEQ 774 783 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8700514,
ECO:0000303|PubMed:9070223,
ECO:0000303|PubMed:9434160,
ECO:0000303|Ref.9}.
/FTId=VSP_037082.
VAR_SEQ 950 950 D -> DIRINRE (in isoform 4).
{ECO:0000303|PubMed:9434160}.
/FTId=VSP_037083.
VAR_SEQ 993 995 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037084.
VAR_SEQ 1329 1330 Missing (in isoform 4).
{ECO:0000303|PubMed:9434160}.
/FTId=VSP_037085.
VARIANT 60 60 T -> N (in dbSNP:rs35332573).
/FTId=VAR_055075.
VARIANT 471 471 R -> L (in dbSNP:rs35745442).
/FTId=VAR_055076.
VARIANT 830 830 H -> Y (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035650.
VARIANT 835 835 R -> W (in a colorectal cancer sample;
somatic mutation; dbSNP:rs558954146).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035651.
VARIANT 856 856 R -> C (in a colorectal cancer sample;
somatic mutation; dbSNP:rs763868325).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035652.
VARIANT 940 940 N -> S (in dbSNP:rs2235937).
/FTId=VAR_055077.
MUTAGEN 1085 1085 C->S: Loss of phosphatase activity toward
CTNNB1. Loss of the inhibitory effect on
CTNNB1 transcriptional activity without
effect on interaction with CTNNB1; when
associated with S-1380.
{ECO:0000269|PubMed:12501215,
ECO:0000269|PubMed:16574648}.
MUTAGEN 1380 1380 C->S: No effect on phosphatase activity
toward CTNNB1. Loss of the inhibitory
effect on CTNNB1 transcriptional activity
without effect on interaction with
CTNNB1; when associated with S-1085.
{ECO:0000269|PubMed:12501215,
ECO:0000269|PubMed:16574648}.
CONFLICT 359 360 LT -> S (in Ref. 4; AAC51938).
{ECO:0000305}.
CONFLICT 401 401 T -> A (in Ref. 4; AAC51938).
{ECO:0000305}.
CONFLICT 715 715 E -> D (in Ref. 3; AAB51343).
{ECO:0000305}.
CONFLICT 840 841 SG -> GW (in Ref. 4; AAC51938).
{ECO:0000305}.
CONFLICT 1215 1215 P -> A (in Ref. 5; AAB07074).
{ECO:0000305}.
CONFLICT 1245 1245 A -> R (in Ref. 4; AAC51938).
{ECO:0000305}.
CONFLICT 1399 1399 M -> I (in Ref. 4; AAC51938).
{ECO:0000305}.
CONFLICT 1436 1436 A -> V (in Ref. 5; AAB07074).
{ECO:0000305}.
SEQUENCE 1446 AA; 162423 MW; 76F9BD6EFABE8663 CRC64;
MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT
RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY
VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL
LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI
SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT
RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS
LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ
TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR
RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP
LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG
LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC
IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDHYAYS
YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS
GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES
FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA
TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR YWPEDSDTYG DIKIMLVKTE
TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP
IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA
ILEACLCGET TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL
PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT LHPLQSTTPD
FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFMSG TADEDLVARV
FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC
LNGGGRSGTF CACATVLEMI RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL
EGLESR


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