UniProtKB - Q64455 (PTPRJ_MOUSE)
Protein
Receptor-type tyrosine-protein phosphatase eta
Gene
Ptprj
Organism
Mus musculus (Mouse)
Status
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
- EC:3.1.3.48PROSITE-ProRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 1106 | SubstrateBy similarity | 1 | |
Active sitei | 1140 | Phosphocysteine intermediatePROSITE-ProRule annotation | 1 | |
Binding sitei | 1184 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- beta-catenin binding Source: MGI
- cadherin binding Source: MGI
- delta-catenin binding Source: MGI
- gamma-catenin binding Source: MGI
- mitogen-activated protein kinase binding Source: MGI
- phosphatase activity Source: UniProtKB
- platelet-derived growth factor receptor binding Source: MGI
- protein kinase binding Source: MGI
- protein tyrosine phosphatase activity Source: UniProtKB
GO - Biological processi
- B cell differentiation Source: ARUK-UCL
- blood coagulation Source: UniProtKB
- calcium-mediated signaling using intracellular calcium source Source: ARUK-UCL
- glucose homeostasis Source: CACAO
- heart development Source: MGI
- negative regulation of cell growth Source: MGI
- negative regulation of cell migration Source: UniProtKB
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
- negative regulation of insulin receptor signaling pathway Source: CACAO
- 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 signaling 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
- peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: CACAO
- 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 Fc-gamma receptor signaling pathway involved in phagocytosis Source: ARUK-UCL
- positive regulation of focal adhesion assembly Source: UniProtKB
- positive regulation of macrophage chemotaxis Source: UniProtKB
- positive regulation of MAPK cascade Source: ARUK-UCL
- positive regulation of peptidyl-tyrosine phosphorylation Source: ARUK-UCL
- positive regulation of platelet activation Source: UniProtKB
- positive regulation of protein kinase B signaling Source: MGI
- positive regulation of tumor necrosis factor production Source: ARUK-UCL
- protein dephosphorylation Source: GO_Central
- regulation of cell adhesion Source: MGI
- vasculogenesis Source: MGI
Keywordsi
Molecular function | Hydrolase, Protein phosphatase |
Enzyme and pathway databases
Reactomei | R-MMU-202427, Phosphorylation of CD3 and TCR zeta chains R-MMU-6798695, Neutrophil degranulation R-MMU-6807004, Negative regulation of MET activity R-MMU-9706369, Negative regulation of FLT3 |
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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:104574, Ptprj |
Subcellular locationi
Plasma membrane
Other locations
Note: After T-cell stimulation, it is temporarily excluded from immunological synapses. Found at cell borders.
Plasma Membrane
- immunological synapse Source: UniProtKB
- plasma membrane Source: UniProtKB
- ruffle membrane Source: UniProtKB
Other locations
- cell surface Source: MGI
- cell-cell junction Source: UniProtKB
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 29 – 876 | ExtracellularSequence analysisAdd BLAST | 848 | |
Transmembranei | 877 – 897 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 898 – 1238 | CytoplasmicSequence analysisAdd BLAST | 341 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1106 | D → A: Substrate trapping with much higher affinity for substrate. 1 Publication | 1 | |
Mutagenesisi | 1140 | C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | Sequence analysisAdd BLAST | 28 | |
ChainiPRO_0000025445 | 29 – 1238 | Receptor-type tyrosine-protein phosphatase etaAdd BLAST | 1210 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 62 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 78 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 85 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 90 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 110 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 114 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 145 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 164 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 173 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 182 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 198 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 207 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 244 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 253 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 267 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 278 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 313 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 317 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 333 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 366 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 379 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 398 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 403 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 437 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 452 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 488 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 506 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 538 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 572 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 576 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 662 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 668 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 685 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 691 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 725 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 811 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 838 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 910 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Glycoprotein, PhosphoproteinProteomic databases
EPDi | Q64455 |
MaxQBi | Q64455 |
PaxDbi | Q64455 |
PRIDEi | Q64455 |
ProteomicsDBi | 302014 |
PTM databases
GlyConnecti | 2668, 5 N-Linked glycans (4 sites) |
GlyGeni | Q64455, 37 sites |
iPTMneti | Q64455 |
PhosphoSitePlusi | Q64455 |
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
Interactioni
Subunit structurei
Monomer.
Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated).
Interacts with FLT3 (phosphorylated).
Interacts with GAB1 and GRB2 (By similarity).
By similarityGO - Molecular functioni
- beta-catenin binding Source: MGI
- cadherin binding Source: MGI
- delta-catenin binding Source: MGI
- gamma-catenin binding Source: MGI
- mitogen-activated protein kinase binding Source: MGI
- platelet-derived growth factor receptor binding Source: MGI
- protein kinase binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 202499, 8 interactors |
IntActi | Q64455, 1 interactor |
STRINGi | 10090.ENSMUSP00000107121 |
Miscellaneous databases
RNActi | Q64455, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 39 – 122 | Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST | 84 | |
Domaini | 170 – 266 | Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST | 97 | |
Domaini | 270 – 358 | Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST | 89 | |
Domaini | 359 – 443 | Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST | 85 | |
Domaini | 444 – 527 | Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST | 84 | |
Domaini | 528 – 621 | Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST | 94 | |
Domaini | 622 – 718 | Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST | 97 | |
Domaini | 717 – 803 | Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST | 87 | |
Domaini | 942 – 1199 | Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST | 258 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1140 – 1146 | Substrate bindingBy similarity | 7 |
Sequence similaritiesi
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0791, Eukaryota |
InParanoidi | Q64455 |
OrthoDBi | 411281at2759 |
Family and domain databases
CDDi | cd00063, FN3, 5 hits |
Gene3Di | 2.60.40.10, 5 hits 3.90.190.10, 1 hit |
InterProi | View protein in InterPro IPR003961, FN3_dom IPR036116, FN3_sf IPR013783, Ig-like_fold IPR029021, Prot-tyrosine_phosphatase-like IPR000242, PTPase_domain IPR041201, PTPRJ_TM IPR016130, Tyr_Pase_AS IPR003595, Tyr_Pase_cat IPR000387, TYR_PHOSPHATASE_dom |
Pfami | View protein in Pfam PF00041, fn3, 3 hits PF18861, PTP_tm, 1 hit PF00102, Y_phosphatase, 1 hit |
PRINTSi | PR00700, PRTYPHPHTASE |
SMARTi | View protein in SMART SM00060, FN3, 8 hits SM00194, PTPc, 1 hit SM00404, PTPc_motif, 1 hit |
SUPFAMi | SSF49265, SSF49265, 4 hits SSF52799, SSF52799, 1 hit |
PROSITEi | View protein in PROSITE PS50853, FN3, 6 hits PS00383, TYR_PHOSPHATASE_1, 1 hit PS50056, TYR_PHOSPHATASE_2, 1 hit PS50055, TYR_PHOSPHATASE_PTP, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
Q64455-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9Q4S7 | E9Q4S7_MOUSE | Protein-tyrosine-phosphatase | Ptprj | 1,350 | Annotation score: | ||
A2AWF8 | A2AWF8_MOUSE | Protein-tyrosine-phosphatase | Ptprj | 1,164 | Annotation score: | ||
A2AWF9 | A2AWF9_MOUSE | Protein-tyrosine-phosphatase | Ptprj | 1,299 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 175 | S → T in BAA08146 (PubMed:8549806).Curated | 1 | |
Sequence conflicti | 175 | S → T in AAK96030 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 175 | S → T in AAK98640 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 211 | L → P in AAK98640 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 217 | V → A in AAK98640 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 463 | Q → H in BAE27842 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 553 | A → T in AAK98640 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 622 | P → S in AAK98640 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 1061 | D → E in AAK98640 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 1126 | Y → D in AAN11409 (PubMed:12089527).Curated | 1 | |
Sequence conflicti | 1133 | E → K in AAN11409 (PubMed:12089527).Curated | 1 |
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 |
CCDSi | CCDS50630.1 |
PIRi | S68700 |
RefSeqi | NP_033008.3, NM_008982.5 |
Genome annotation databases
GeneIDi | 19271 |
KEGGi | mmu:19271 |
Similar proteinsi
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 |
CCDSi | CCDS50630.1 |
PIRi | S68700 |
RefSeqi | NP_033008.3, NM_008982.5 |
3D structure databases
SMRi | Q64455 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 202499, 8 interactors |
IntActi | Q64455, 1 interactor |
STRINGi | 10090.ENSMUSP00000107121 |
PTM databases
GlyConnecti | 2668, 5 N-Linked glycans (4 sites) |
GlyGeni | Q64455, 37 sites |
iPTMneti | Q64455 |
PhosphoSitePlusi | Q64455 |
Proteomic databases
EPDi | Q64455 |
MaxQBi | Q64455 |
PaxDbi | Q64455 |
PRIDEi | Q64455 |
ProteomicsDBi | 302014 |
Protocols and materials databases
DNASUi | 19271 |
Genome annotation databases
GeneIDi | 19271 |
KEGGi | mmu:19271 |
Organism-specific databases
CTDi | 5795 |
MGIi | MGI:104574, Ptprj |
Phylogenomic databases
eggNOGi | KOG0791, Eukaryota |
InParanoidi | Q64455 |
OrthoDBi | 411281at2759 |
Enzyme and pathway databases
Reactomei | R-MMU-202427, Phosphorylation of CD3 and TCR zeta chains R-MMU-6798695, Neutrophil degranulation R-MMU-6807004, Negative regulation of MET activity R-MMU-9706369, Negative regulation of FLT3 |
Miscellaneous databases
BioGRID-ORCSi | 19271, 2 hits in 53 CRISPR screens |
ChiTaRSi | Ptprj, mouse |
PROi | PR:Q64455 |
RNActi | Q64455, protein |
SOURCEi | Search... |
Family and domain databases
CDDi | cd00063, FN3, 5 hits |
Gene3Di | 2.60.40.10, 5 hits 3.90.190.10, 1 hit |
InterProi | View protein in InterPro IPR003961, FN3_dom IPR036116, FN3_sf IPR013783, Ig-like_fold IPR029021, Prot-tyrosine_phosphatase-like IPR000242, PTPase_domain IPR041201, PTPRJ_TM IPR016130, Tyr_Pase_AS IPR003595, Tyr_Pase_cat IPR000387, TYR_PHOSPHATASE_dom |
Pfami | View protein in Pfam PF00041, fn3, 3 hits PF18861, PTP_tm, 1 hit PF00102, Y_phosphatase, 1 hit |
PRINTSi | PR00700, PRTYPHPHTASE |
SMARTi | View protein in SMART SM00060, FN3, 8 hits SM00194, PTPc, 1 hit SM00404, PTPc_motif, 1 hit |
SUPFAMi | SSF49265, SSF49265, 4 hits SSF52799, SSF52799, 1 hit |
PROSITEi | View protein in PROSITE PS50853, FN3, 6 hits PS00383, TYR_PHOSPHATASE_1, 1 hit PS50056, TYR_PHOSPHATASE_2, 1 hit PS50055, TYR_PHOSPHATASE_PTP, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PTPRJ_MOUSE | |
Accessioni | Q64455Primary (citable) accession number: Q64455 Secondary accession number(s): Q3UH64 Q8K3Q2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | December 15, 2009 | |
Last modified: | April 7, 2021 | |
This is version 174 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families