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Q92729 (PTPRU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase U

Short name=R-PTP-U
EC=3.1.3.48
Alternative name(s):
Pancreatic carcinoma phosphatase 2
Short name=PCP-2
Protein-tyrosine phosphatase J
Short name=PTP-J
Short name=hPTP-J
Protein-tyrosine phosphatase pi
Short name=PTP pi
Protein-tyrosine phosphatase receptor omicron
Short name=PTP-RO
Receptor-type protein-tyrosine phosphatase psi
Short name=R-PTP-psi
Gene names
Name:PTPRU
Synonyms:FMI, PCP2, PTPRO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.11 Ref.12 Ref.13

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.2

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cell junction. Cell membrane; Single-pass type I membrane protein Ref.2.

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. Ref.1 Ref.2 Ref.3 Ref.4

Developmental stage

Expressed in fetal brain, lung and kidney. Ref.4

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 (Ref.11). Ref.3 Ref.10 Ref.11 Ref.12

Post-translational modification

The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain By similarity. Beside the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed.

N-glycosylated. Ref.2

Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated. Ref.11

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily.

Contains 4 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 MAM domain.

Contains 2 tyrosine-protein phosphatase domains.

Sequence caution

The sequence CAA65016.1 differs from that shown. Reason: Several sequencing problems.

The sequence CAA65832.1 differs from that shown. Reason: Several sequencing problems.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcanonical Wnt signaling pathway

Inferred from direct assay Ref.13. Source: UniProtKB

cell adhesion

Non-traceable author statement Ref.2. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

homotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from direct assay Ref.12Ref.13. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.13. Source: UniProtKB

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.12. Source: GOC

protein dephosphorylation

Inferred from direct assay Ref.12. Source: UniProtKB

protein localization to cell surface

Inferred from direct assay Ref.13. Source: UniProtKB

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Inferred from direct assay Ref.13. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase signaling pathway

Non-traceable author statement Ref.2. Source: UniProtKB

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.12. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionbeta-catenin binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.12. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KITP107212EBI-7052301,EBI-1379503

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92729-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92729-2)

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.
Isoform 3 (identifier: Q92729-3)

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.
     993-995: Missing.
Isoform 4 (identifier: Q92729-4)

Also known as: PTPRO;

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.
     950-950: D → DIRINRE
     1329-1330: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 14461428Receptor-type tyrosine-protein phosphatase U
PRO_0000371658

Regions

Topological domain19 – 749731Extracellular Potential
Transmembrane750 – 77021Helical; Potential
Topological domain771 – 1446676Cytoplasmic Potential
Domain25 – 188164MAM
Domain190 – 27586Ig-like C2-type
Domain288 – 38396Fibronectin type-III 1
Domain386 – 48499Fibronectin type-III 2
Domain485 – 591107Fibronectin type-III 3
Domain592 – 67483Fibronectin type-III 4
Domain888 – 1144257Tyrosine-protein phosphatase 1
Domain1176 – 1439264Tyrosine-protein phosphatase 2
Region771 – 887117Mediates interaction with CTNNB1 By similarity
Region1085 – 10917Substrate binding By similarity

Sites

Active site10851Phosphocysteine intermediate By similarity
Active site13801Phosphocysteine intermediate By similarity
Binding site10531Substrate Potential
Binding site11291Substrate By similarity

Amino acid modifications

Modified residue8481Phosphoserine Ref.15
Modified residue8531Phosphoserine Ref.15
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Disulfide bond210 ↔ 264 Potential

Natural variations

Alternative sequence774 – 78310Missing in isoform 2, isoform 3 and isoform 4.
VSP_037082
Alternative sequence9501D → DIRINRE in isoform 4.
VSP_037083
Alternative sequence993 – 9953Missing in isoform 3.
VSP_037084
Alternative sequence1329 – 13302Missing in isoform 4.
VSP_037085
Natural variant601T → N.
Corresponds to variant rs35332573 [ dbSNP | Ensembl ].
VAR_055075
Natural variant4711R → L.
Corresponds to variant rs35745442 [ dbSNP | Ensembl ].
VAR_055076
Natural variant8301H → Y in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035650
Natural variant8351R → W in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035651
Natural variant8561R → C in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035652
Natural variant9401N → S.
Corresponds to variant rs2235937 [ dbSNP | Ensembl ].
VAR_055077

Experimental info

Mutagenesis10851C → 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. Ref.12 Ref.13
Mutagenesis13801C → 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. Ref.12 Ref.13
Sequence conflict359 – 3602LT → S in AAC51938. Ref.4
Sequence conflict4011T → A in AAC51938. Ref.4
Sequence conflict7151E → D in AAB51343. Ref.3
Sequence conflict840 – 8412SG → GW in AAC51938. Ref.4
Sequence conflict12151P → A in AAB07074. Ref.5
Sequence conflict12451A → R in AAC51938. Ref.4
Sequence conflict13991M → I in AAC51938. Ref.4
Sequence conflict14361A → V in AAB07074. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 76F9BD6EFABE8663

FASTA1,446162,423
        10         20         30         40         50         60 
MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT 

        70         80         90        100        110        120 
RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY 

       130        140        150        160        170        180 
VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL 

       190        200        210        220        230        240 
LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI 

       250        260        270        280        290        300 
SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 

       310        320        330        340        350        360 
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT 

       370        380        390        400        410        420 
RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS 

       430        440        450        460        470        480 
LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ 

       490        500        510        520        530        540 
TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 

       550        560        570        580        590        600 
RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 

       610        620        630        640        650        660 
LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG 

       670        680        690        700        710        720 
LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 

       730        740        750        760        770        780 
IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDHYAYS 

       790        800        810        820        830        840 
YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS 

       850        860        870        880        890        900 
GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES 

       910        920        930        940        950        960 
FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA 

       970        980        990       1000       1010       1020 
TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR YWPEDSDTYG DIKIMLVKTE 

      1030       1040       1050       1060       1070       1080 
TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP 

      1090       1100       1110       1120       1130       1140 
IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA 

      1150       1160       1170       1180       1190       1200 
ILEACLCGET TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL 

      1210       1220       1230       1240       1250       1260 
PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT LHPLQSTTPD 

      1270       1280       1290       1300       1310       1320 
FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFMSG TADEDLVARV 

      1330       1340       1350       1360       1370       1380 
FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC 

      1390       1400       1410       1420       1430       1440 
LNGGGRSGTF CACATVLEMI RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL 


EGLESR 

« Hide

Isoform 2 [UniParc].

Checksum: F88BB75170BF3676
Show »

FASTA1,436161,107
Isoform 3 [UniParc].

Checksum: BA085FF7C36BB2A8
Show »

FASTA1,433160,795
Isoform 4 (PTPRO) [UniParc].

Checksum: EDE5C3CF8C8C9DA0
Show »

FASTA1,440161,648

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase."
Crossland S., Smith P.D., Crompton M.R.
Biochem. J. 319:249-254(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Mammary gland.
[2]"Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family."
Wang H.-Y., Lian Z., Lerch M.M., Chen Z., Xie W., Ullrich A.
Oncogene 12:2555-2562(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Pancreas.
[3]"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."
Wang B., Kishihara K., Zhang D., Hara H., Nomoto K.
Biochem. Biophys. Res. Commun. 231:77-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION.
Tissue: Skeletal muscle.
[4]"Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells."
Avraham S., London R., Tulloch G.A., Ellis M., Fu Y., Jiang S., White R.A., Painter C., Steinberger A.A., Avraham H.
Gene 204:5-16(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Brain.
[5]"Cloning and expression of R-PTP-psi, a novel receptor protein tyrosine phosphatase related to the homophilic binding R-PTP-kappa and -mu."
Banville D., Masson S., L'Abbe D., Stocco R., Shen S.-H.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[6]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[9]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1446 (ISOFORM 2).
Tissue: Brain.
[10]"Transcriptional regulation of a receptor protein tyrosine phosphatase gene hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T lymphoma cells."
Wang B., Kishihara K., Zhang D., Sakamoto T., Nomoto K.
Biochim. Biophys. Acta 1450:331-340(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and is associated with the c-Kit receptor."
Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H.
Blood 94:539-549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, PROTEOLYTIC PROCESSING, INDUCTION BY PHORBOL ESTER.
[12]"Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin."
Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C., Wang H.-Y.
Biochemistry 41:15854-15860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1, INDUCTION, MUTAGENESIS OF CYS-1085 AND CYS-1380.
[13]"Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and increases E-cadherin-dependent cell adhesion."
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.
J. Biol. Chem. 281:15423-15433(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF CYS-1085 AND CYS-1380.
[14]"Involvement of beta3A subunit of adaptor protein-3 in intracellular trafficking of receptor-like protein tyrosine phosphatase PCP-2."
Dong H., Yuan H., Jin W., Shen Y., Xu X., Wang H.-Y.
Acta Biochim. Biophys. Sin. 39:540-546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP3B1.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848 AND SER-853, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-830; TRP-835 AND CYS-856.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95712 mRNA. Translation: CAA65016.1. Sequence problems.
X97198 mRNA. Translation: CAA65832.1. Sequence problems.
U73727 mRNA. Translation: AAB51343.1.
U71075 mRNA. Translation: AAC51938.1.
U60289 Genomic DNA. Translation: AAB07074.1.
AL645859, AL049570, AL590729 Genomic DNA. Translation: CAH72393.1.
AL645859, AL049570, AL590729 Genomic DNA. Translation: CAH72394.1.
AL590729, AL049570, AL645859 Genomic DNA. Translation: CAI14331.1.
AL590729, AL049570, AL645859 Genomic DNA. Translation: CAI14332.1.
AL049570, AL590729, AL645859 Genomic DNA. Translation: CAI20946.1.
AL049570, AL590729, AL645859 Genomic DNA. Translation: CAI20947.1.
CH471059 Genomic DNA. Translation: EAX07651.1.
CH471059 Genomic DNA. Translation: EAX07652.1.
BC146655 mRNA. Translation: AAI46656.1.
AB208855 mRNA. Translation: BAD92092.1.
CCDSCCDS334.1. [Q92729-1]
CCDS335.1. [Q92729-2]
CCDS44098.2. [Q92729-4]
CCDS53290.1. [Q92729-3]
PIRJC5290.
S72441.
RefSeqNP_001181930.1. NM_001195001.1. [Q92729-3]
NP_005695.3. NM_005704.4. [Q92729-1]
NP_573438.3. NM_133177.3. [Q92729-4]
NP_573439.2. NM_133178.3. [Q92729-2]
UniGeneHs.19718.

3D structure databases

ProteinModelPortalQ92729.
SMRQ92729. Positions 22-591, 871-1440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115386. 3 interactions.
IntActQ92729. 1 interaction.
MINTMINT-1349420.

Chemistry

ChEMBLCHEMBL1961785.

Polymorphism databases

DMDM229462800.

Proteomic databases

PaxDbQ92729.
PRIDEQ92729.

Protocols and materials databases

DNASU10076.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345512; ENSP00000334941; ENSG00000060656. [Q92729-1]
ENST00000373779; ENSP00000362884; ENSG00000060656. [Q92729-2]
ENST00000428026; ENSP00000392332; ENSG00000060656. [Q92729-3]
ENST00000460170; ENSP00000432906; ENSG00000060656. [Q92729-4]
GeneID10076.
KEGGhsa:10076.
UCSCuc001bru.3. human. [Q92729-1]
uc001brw.3. human. [Q92729-2]
uc009vtq.3. human. [Q92729-4]
uc009vtr.3. human. [Q92729-3]

Organism-specific databases

CTD10076.
GeneCardsGC01P029569.
H-InvDBHIX0000346.
HGNCHGNC:9683. PTPRU.
HPACAB011476.
HPA039832.
MIM602454. gene.
neXtProtNX_Q92729.
PharmGKBPA34028.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOVERGENHBG062785.
KOK16662.
OMALTDSYTR.
OrthoDBEOG70KGNP.
PhylomeDBQ92729.
TreeFamTF312900.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ92729.
BgeeQ92729.
CleanExHS_PCP2.
HS_PTPRU.
GenevestigatorQ92729.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEPS50853. FN3. 3 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRU. human.
GeneWikiPTPRU.
GenomeRNAi10076.
NextBio38089.
PROQ92729.
SOURCESearch...

Entry information

Entry namePTPRU_HUMAN
AccessionPrimary (citable) accession number: Q92729
Secondary accession number(s): A6H8L1 expand/collapse secondary AC list , O00197, P78399, Q59HA4, Q5SYU4, Q5SYU5, Q92735, Q92850
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM