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Q64455 (PTPRJ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=Protein-tyrosine phosphatase eta
Short name=R-PTP-eta
EC=3.1.3.48
Alternative name(s):
HPTP beta-like tyrosine phosphatase
Protein-tyrosine phosphatase receptor type J
Short name=R-PTP-J
Susceptibility to colon cancer 1
CD_antigen=CD148
Gene names
Name:Ptprj
Synonyms:Byp, Scc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1238 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. May be involved in the mechanism of contact inhibition of cell growth. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell projectionruffle membrane. Cell junction. Note: After T-cell stimulation, it is temporarily excluded from immunological synapses. Found at cell borders. Ref.8 Ref.13

Tissue specificity

Expressed at high levels in brain, kidney, spleen and intestine, and at lower levels in liver, lung, thymus and heart. Expressed at a high level in the myeloid cell line FDC-P2, and at a lower level in the pre-B lymphoid cell line WEHI-231 and the T hybridoma cell line HB21.7.31. Not expressed in the fibroblast cell line NIH3T3 or the erythroid cell line F5-5. Expressed in macrophages. Ref.1 Ref.5 Ref.6

Developmental stage

Expressed at 11.5 dpc in presumptive macrophages concentrated in the liver and scattered throughout the embryonic mesenchyme. Expressed at 11.5 and 12.5 dpc in the developing eye and in the ganglia and processes of cranial and spinal nerves constituting the PNS. Ref.6

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.

Contains 8 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

heart development

Inferred from mutant phenotype Ref.9. Source: MGI

negative regulation of MAP kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of T cell receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of platelet-derived growth factor receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of receptor activity

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

platelet-derived growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-matrix adhesion

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of macrophage chemotaxis

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of platelet activation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

vasculogenesis

Inferred from mutant phenotype Ref.9. Source: MGI

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

immunological synapse

Inferred from direct assay Ref.8. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

ruffle membrane

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from mutant phenotype Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 12381210Receptor-type tyrosine-protein phosphatase eta
PRO_0000025445

Regions

Topological domain29 – 876848Extracellular Potential
Transmembrane877 – 89721Helical; Potential
Topological domain898 – 1238341Cytoplasmic Potential
Domain39 – 12284Fibronectin type-III 1
Domain170 – 26697Fibronectin type-III 2
Domain270 – 35889Fibronectin type-III 3
Domain359 – 44385Fibronectin type-III 4
Domain444 – 52784Fibronectin type-III 5
Domain528 – 62194Fibronectin type-III 6
Domain622 – 71897Fibronectin type-III 7
Domain717 – 80387Fibronectin type-III 8
Domain942 – 1199258Tyrosine-protein phosphatase
Region1140 – 11467Substrate binding By similarity

Sites

Active site11401Phosphocysteine intermediate By similarity
Binding site11061Substrate By similarity
Binding site11841Substrate By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Ref.14
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Ref.14
Glycosylation3171N-linked (GlcNAc...) Ref.14
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Glycosylation5381N-linked (GlcNAc...) Ref.14
Glycosylation5721N-linked (GlcNAc...) Potential
Glycosylation5761N-linked (GlcNAc...) Potential
Glycosylation6621N-linked (GlcNAc...) Potential
Glycosylation6681N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Glycosylation6911N-linked (GlcNAc...) Potential
Glycosylation7251N-linked (GlcNAc...) Potential
Glycosylation8111N-linked (GlcNAc...) Potential
Glycosylation8381N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis11061D → A: Substrate trapping with much higher affinity for substrate. Ref.7
Mutagenesis11401C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. Ref.7 Ref.10
Sequence conflict1751S → T in BAA08146. Ref.1
Sequence conflict1751S → T in AAK96030. Ref.2
Sequence conflict1751S → T in AAK98640. Ref.2
Sequence conflict2111L → P in AAK98640. Ref.2
Sequence conflict2171V → A in AAK98640. Ref.2
Sequence conflict4631Q → H in BAE27842. Ref.4
Sequence conflict5531A → T in AAK98640. Ref.2
Sequence conflict6221P → S in AAK98640. Ref.2
Sequence conflict10611D → E in AAK98640. Ref.2
Sequence conflict11261Y → D in AAN11409. Ref.2
Sequence conflict11331E → K in AAN11409. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q64455 [UniParc].

Last modified December 15, 2009. Version 2.
Checksum: E525D346A2C60335

FASTA1,238136,769
        10         20         30         40         50         60 
MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV SPTSVLLTWK 

        70         80         90        100        110        120 
HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY TFSIISVTTN ETLNKTITTE 

       130        140        150        160        170        180 
PWPVSDLHVT SVGVTQARLT WSNANGTASY RMLIEELTTH SSVNISGLKP GTNNSFAFPE 

       190        200        210        220        230        240 
SNETQADFAV AEEVPDANGT KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD 

       250        260        270        280        290        300 
TQYNATIYSQ AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV 

       310        320        330        340        350        360 
YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL QVYTSPDQVS 

       370        380        390        400        410        420 
DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS TGNQSYMVED LKPGTSYHFE 

       430        440        450        460        470        480 
IIPRGPDGTE GLSSTVNGST DPSAVTDIRV VNISTTEMQL EWQNTDDASG YTYHLVLESK 

       490        500        510        520        530        540 
SGSIIRTNSS QKWITVGSLT PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT 

       550        560        570        580        590        600 
TTTAAIRWKN EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT 

       610        620        630        640        650        660 
QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG FELGVRSDSW 

       670        680        690        700        710        720 
DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG KMALPAQNIC TTGITDPPTP 

       730        740        750        760        770        780 
DGSPNITSVS HNSVKVKFSG FEASHGPIKA YAVILTTGEA AQPSADVLKY TYEDFKRGAS 

       790        800        810        820        830        840 
DTYVTYLIRI EEKGQSQGLS EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT 

       850        860        870        880        890        900 
YNLQNDGLIN GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK 

       910        920        930        940        950        960 
RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK LIGISLPKYT 

       970        980        990       1000       1010       1020 
AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY MPGYHSKKDF IATQGPLPNT 

      1030       1040       1050       1060       1070       1080 
LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI 

      1090       1100       1110       1120       1130       1140 
RDFVVKNMQN SESHPLRQFH FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC 

      1150       1160       1170       1180       1190       1200 
SAGVGRTGTF IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII 

      1210       1220       1230 
RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1."
Kuramochi S., Matsuda S., Matsuda Y., Saitoh T., Ohsugi M., Yamamoto T.
FEBS Lett. 378:7-14(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: MRL-LPR/LPR.
Tissue: Lymph node.
[2]"Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers."
Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C., Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L., Groot P.C., Lindeman J., Mooi W.J., Meijjer G.A., Scholten G., Dauwerse H., Paces V., van Zandwijk N., van Ommen G.J.B., Demant P.
Nat. Genet. 31:295-300(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvSl and BALB/c.
[3]"Phenotypic consequences of the germ-line loss of the putative tumor suppressor Ptprj (Scc1)."
Csikos T., Snoek M., de Boer T., Drenth T., Krimpenfort P., van Amerongen R., Zevenhoven J., van der Valk M., Hellberg C., Ostman A., Demant P., Berns A.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129P2.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and C57BL/6J.
Tissue: Brain.
[5]"Identification of novel protein-tyrosine phosphatases in a human leukemia cell line, F-36P."
Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.
Leukemia 7:742-746(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed in macrophages and is regulated by CSF-1 and LPS."
Osborne J.M., den Elzen N., Lichanska A.M., Costelloe E.O., Yamada T., Cassady A.I., Hume D.A.
J. Leukoc. Biol. 64:692-701(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148."
Grazia Lampugnani M., Zanetti A., Corada M., Takahashi T., Balconi G., Breviario F., Orsenigo F., Cattelino A., Kemler R., Daniel T.O., Dejana E.
J. Cell Biol. 161:793-804(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-1106 AND CYS-1140.
[8]"The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
Lin J., Weiss A.
J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"A mutant receptor tyrosine phosphatase, CD148, causes defects in vascular development."
Takahashi T., Takahashi K., St John P.L., Fleming P.A., Tomemori T., Watanabe T., Abrahamson D.R., Drake C.J., Shirasawa T., Daniel T.O.
Mol. Cell. Biol. 23:1817-1831(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion."
Jandt E., Denner K., Kovalenko M., Ostman A., Bohmer F.D.
Oncogene 22:4175-4185(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-1140.
[11]"Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling."
Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., Weiss A.
Immunity 28:183-196(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis."
Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y., Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N., Zhu J.W., Weiss A., Watson S.P.
Blood 113:4942-4954(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"CD148/DEP-1 association with areas of cytoskeletal organisation in macrophages."
Dave R.K., Hume D.A., Elsegood C., Kellie S.
Exp. Cell Res. 315:1734-1744(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-313; ASN-317 AND ASN-538.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45212 mRNA. Translation: BAA08146.1.
AY038877, AY038861 Genomic DNA. Translation: AAN11409.1.
AY038891 mRNA. Translation: AAK96030.1.
AY039232 mRNA. Translation: AAK98640.1.
DQ133576 mRNA. Translation: ABA07808.1.
AK147318 mRNA. Translation: BAE27842.1.
AK147556 mRNA. Translation: BAE27993.1.
PIRS68700.
RefSeqNP_033008.3. NM_008982.5.
UniGeneMm.330393.

3D structure databases

ProteinModelPortalQ64455.
SMRQ64455. Positions 42-145, 217-607, 919-1204.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ64455.

Proteomic databases

PaxDbQ64455.
PRIDEQ64455.

Protocols and materials databases

DNASU19271.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID19271.
KEGGmmu:19271.

Organism-specific databases

CTD5795.
MGIMGI:104574. Ptprj.

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000232054.
HOVERGENHBG053761.
InParanoidQ541R5.
KOK05698.

Gene expression databases

ArrayExpressQ64455.
BgeeQ64455.
CleanExMM_PTPRJ.
GenevestigatorQ64455.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 5 hits.
PROSITEPS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296158.
PROQ64455.
SOURCESearch...

Entry information

Entry namePTPRJ_MOUSE
AccessionPrimary (citable) accession number: Q64455
Secondary accession number(s): Q3UH64 expand/collapse secondary AC list , Q3UHL5, Q541R5, Q8CIW9, Q8K3Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 2009
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot