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Protein

Receptor-type tyrosine-protein phosphatase eta

Gene

Ptprj

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1106SubstrateBy similarity1
Active sitei1140Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei1184SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: UniProtKB
  • heart development Source: MGI
  • negative regulation of cell growth Source: MGI
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • negative regulation of MAP kinase activity Source: UniProtKB
  • negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • negative regulation of receptor activity Source: UniProtKB
  • negative regulation of T cell receptor signaling pathway Source: UniProtKB
  • negative regulation of vascular permeability Source: MGI
  • oligodendrocyte differentiation Source: MGI
  • peptidyl-tyrosine dephosphorylation Source: MGI
  • platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  • positive chemotaxis Source: MGI
  • positive regulation of cell adhesion Source: MGI
  • positive regulation of cell-matrix adhesion Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of macrophage chemotaxis Source: UniProtKB
  • positive regulation of platelet activation Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: MGI
  • regulation of cell adhesion Source: MGI
  • vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase eta (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase eta
Short name:
R-PTP-eta
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 namesi
Name:Ptprj
Synonyms:Byp, Scc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:104574. Ptprj.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 876ExtracellularSequence analysisAdd BLAST848
Transmembranei877 – 897HelicalSequence analysisAdd BLAST21
Topological domaini898 – 1238CytoplasmicSequence analysisAdd BLAST341

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cell surface Source: MGI
  • extracellular exosome Source: MGI
  • immunological synapse Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1106D → A: Substrate trapping with much higher affinity for substrate. 1 Publication1
Mutagenesisi1140C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000002544529 – 1238Receptor-type tyrosine-protein phosphatase etaAdd BLAST1210

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Glycosylationi78N-linked (GlcNAc...)Sequence analysis1
Glycosylationi85N-linked (GlcNAc...)Sequence analysis1
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Glycosylationi110N-linked (GlcNAc...)Sequence analysis1
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Glycosylationi145N-linked (GlcNAc...)1 Publication1
Glycosylationi164N-linked (GlcNAc...)Sequence analysis1
Glycosylationi173N-linked (GlcNAc...)Sequence analysis1
Glycosylationi182N-linked (GlcNAc...)Sequence analysis1
Glycosylationi198N-linked (GlcNAc...)Sequence analysis1
Glycosylationi207N-linked (GlcNAc...)Sequence analysis1
Glycosylationi244N-linked (GlcNAc...)Sequence analysis1
Glycosylationi253N-linked (GlcNAc...)Sequence analysis1
Glycosylationi267N-linked (GlcNAc...)Sequence analysis1
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Glycosylationi313N-linked (GlcNAc...)1 Publication1
Glycosylationi317N-linked (GlcNAc...)1 Publication1
Glycosylationi333N-linked (GlcNAc...)Sequence analysis1
Glycosylationi366N-linked (GlcNAc...)Sequence analysis1
Glycosylationi379N-linked (GlcNAc...)Sequence analysis1
Glycosylationi398N-linked (GlcNAc...)Sequence analysis1
Glycosylationi403N-linked (GlcNAc...)Sequence analysis1
Glycosylationi437N-linked (GlcNAc...)Sequence analysis1
Glycosylationi452N-linked (GlcNAc...)Sequence analysis1
Glycosylationi488N-linked (GlcNAc...)Sequence analysis1
Glycosylationi506N-linked (GlcNAc...)Sequence analysis1
Glycosylationi538N-linked (GlcNAc...)1 Publication1
Glycosylationi572N-linked (GlcNAc...)Sequence analysis1
Glycosylationi576N-linked (GlcNAc...)Sequence analysis1
Glycosylationi662N-linked (GlcNAc...)Sequence analysis1
Glycosylationi668N-linked (GlcNAc...)Sequence analysis1
Glycosylationi685N-linked (GlcNAc...)Sequence analysis1
Glycosylationi691N-linked (GlcNAc...)Sequence analysis1
Glycosylationi725N-linked (GlcNAc...)Sequence analysis1
Glycosylationi811N-linked (GlcNAc...)Sequence analysis1
Glycosylationi838N-linked (GlcNAc...)Sequence analysis1
Modified residuei910PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ64455.
MaxQBiQ64455.
PaxDbiQ64455.
PRIDEiQ64455.

PTM databases

iPTMnetiQ64455.
PhosphoSitePlusiQ64455.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiENSMUSG00000025314.
CleanExiMM_PTPRJ.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ64455. 1 interactor.
STRINGi10090.ENSMUSP00000129592.

Structurei

3D structure databases

ProteinModelPortaliQ64455.
SMRiQ64455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 122Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST84
Domaini170 – 266Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST97
Domaini270 – 358Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST89
Domaini359 – 443Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST85
Domaini444 – 527Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST84
Domaini528 – 621Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST94
Domaini622 – 718Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST97
Domaini717 – 803Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST87
Domaini942 – 1199Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST258

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1140 – 1146Substrate bindingBy similarity7

Sequence similaritiesi

Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0791. Eukaryota.
COG5599. LUCA.
HOGENOMiHOG000232054.
HOVERGENiHBG053761.
InParanoidiQ64455.
KOiK05698.

Family and domain databases

CDDicd00063. FN3. 5 hits.
Gene3Di2.60.40.10. 7 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64455-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV
60 70 80 90 100
SPTSVLLTWK HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY
110 120 130 140 150
TFSIISVTTN ETLNKTITTE PWPVSDLHVT SVGVTQARLT WSNANGTASY
160 170 180 190 200
RMLIEELTTH SSVNISGLKP GTNNSFAFPE SNETQADFAV AEEVPDANGT
210 220 230 240 250
KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD TQYNATIYSQ
260 270 280 290 300
AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV
310 320 330 340 350
YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL
360 370 380 390 400
QVYTSPDQVS DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS
410 420 430 440 450
TGNQSYMVED LKPGTSYHFE IIPRGPDGTE GLSSTVNGST DPSAVTDIRV
460 470 480 490 500
VNISTTEMQL EWQNTDDASG YTYHLVLESK SGSIIRTNSS QKWITVGSLT
510 520 530 540 550
PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT TTTAAIRWKN
560 570 580 590 600
EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT
610 620 630 640 650
QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG
660 670 680 690 700
FELGVRSDSW DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG
710 720 730 740 750
KMALPAQNIC TTGITDPPTP DGSPNITSVS HNSVKVKFSG FEASHGPIKA
760 770 780 790 800
YAVILTTGEA AQPSADVLKY TYEDFKRGAS DTYVTYLIRI EEKGQSQGLS
810 820 830 840 850
EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT YNLQNDGLIN
860 870 880 890 900
GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK
910 920 930 940 950
RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK
960 970 980 990 1000
LIGISLPKYT AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY
1010 1020 1030 1040 1050
MPGYHSKKDF IATQGPLPNT LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC
1060 1070 1080 1090 1100
EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI RDFVVKNMQN SESHPLRQFH
1110 1120 1130 1140 1150
FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC SAGVGRTGTF
1160 1170 1180 1190 1200
IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII
1210 1220 1230
RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA
Length:1,238
Mass (Da):136,769
Last modified:December 15, 2009 - v2
Checksum:iE525D346A2C60335
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti175S → T in BAA08146 (PubMed:8549806).Curated1
Sequence conflicti175S → T in AAK96030 (PubMed:12089527).Curated1
Sequence conflicti175S → T in AAK98640 (PubMed:12089527).Curated1
Sequence conflicti211L → P in AAK98640 (PubMed:12089527).Curated1
Sequence conflicti217V → A in AAK98640 (PubMed:12089527).Curated1
Sequence conflicti463Q → H in BAE27842 (PubMed:16141072).Curated1
Sequence conflicti553A → T in AAK98640 (PubMed:12089527).Curated1
Sequence conflicti622P → S in AAK98640 (PubMed:12089527).Curated1
Sequence conflicti1061D → E in AAK98640 (PubMed:12089527).Curated1
Sequence conflicti1126Y → D in AAN11409 (PubMed:12089527).Curated1
Sequence conflicti1133E → K in AAN11409 (PubMed:12089527).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS68700.
RefSeqiNP_033008.3. NM_008982.5.
UniGeneiMm.330393.

Genome annotation databases

GeneIDi19271.
KEGGimmu:19271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS68700.
RefSeqiNP_033008.3. NM_008982.5.
UniGeneiMm.330393.

3D structure databases

ProteinModelPortaliQ64455.
SMRiQ64455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64455. 1 interactor.
STRINGi10090.ENSMUSP00000129592.

PTM databases

iPTMnetiQ64455.
PhosphoSitePlusiQ64455.

Proteomic databases

EPDiQ64455.
MaxQBiQ64455.
PaxDbiQ64455.
PRIDEiQ64455.

Protocols and materials databases

DNASUi19271.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi19271.
KEGGimmu:19271.

Organism-specific databases

CTDi5795.
MGIiMGI:104574. Ptprj.

Phylogenomic databases

eggNOGiKOG0791. Eukaryota.
COG5599. LUCA.
HOGENOMiHOG000232054.
HOVERGENiHBG053761.
InParanoidiQ64455.
KOiK05698.

Miscellaneous databases

ChiTaRSiPtprj. mouse.
PROiQ64455.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025314.
CleanExiMM_PTPRJ.

Family and domain databases

CDDicd00063. FN3. 5 hits.
Gene3Di2.60.40.10. 7 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTPRJ_MOUSE
AccessioniPrimary (citable) accession number: Q64455
Secondary accession number(s): Q3UH64
, Q3UHL5, Q541R5, Q8CIW9, Q8K3Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 2009
Last modified: November 30, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.