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Protein

Receptor-type tyrosine-protein phosphatase eta

Gene

PTPRJ

Organism
Homo sapiens (Human)
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 (variant MEN2A), 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. 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.19 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1205SubstrateBy similarity1
Active sitei1239Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei1283SubstrateBy similarity1

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • delta-catenin binding Source: UniProtKB
  • gamma-catenin binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: UniProtKB
  • phosphatase activity Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • contact inhibition Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • 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 T cell receptor signaling pathway Source: UniProtKB
  • negative regulation of vascular permeability Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  • positive chemotaxis Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS07590-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807004. Negative regulation of MET activity.
SignaLinkiQ12913.
SIGNORiQ12913.

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):
Density-enhanced phosphatase 1
Short name:
DEP-1
HPTP eta
Protein-tyrosine phosphatase receptor type J
Short name:
R-PTP-J
CD_antigen: CD148
Gene namesi
Name:PTPRJ
Synonyms:DEP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9673. PTPRJ.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini36 – 975ExtracellularSequence analysisAdd BLAST940
Transmembranei976 – 996HelicalSequence analysisAdd BLAST21
Topological domaini997 – 1337CytoplasmicSequence analysisAdd BLAST341

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1016K → A: 80% decrease in interaction with MAPK1 and MAPK3. 1 Publication1
Mutagenesisi1205D → A: Substrate trapping with much higher affinity for substrate. 9 Publications1
Mutagenesisi1239C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 6 Publications1

Organism-specific databases

DisGeNETi5795.
MalaCardsiPTPRJ.
OpenTargetsiENSG00000149177.
PharmGKBiPA34018.

Chemistry databases

ChEMBLiCHEMBL3692.

Polymorphism and mutation databases

BioMutaiPTPRJ.
DMDMi166899088.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
ChainiPRO_000002544436 – 1337Receptor-type tyrosine-protein phosphatase etaAdd BLAST1302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi72N-linked (GlcNAc...)Sequence analysis1
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Glycosylationi93N-linked (GlcNAc...)Sequence analysis1
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi142N-linked (GlcNAc...)Sequence analysis1
Glycosylationi172N-linked (GlcNAc...)Sequence analysis1
Glycosylationi192N-linked (GlcNAc...)Sequence analysis1
Glycosylationi231N-linked (GlcNAc...)Sequence analysis1
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Glycosylationi342N-linked (GlcNAc...)1 Publication1
Glycosylationi351N-linked (GlcNAc...)1 Publication1
Glycosylationi376N-linked (GlcNAc...)Sequence analysis1
Glycosylationi391N-linked (GlcNAc...)1 Publication1
Glycosylationi396N-linked (GlcNAc...)1 Publication1
Glycosylationi413N-linked (GlcNAc...)1 Publication1
Glycosylationi431N-linked (GlcNAc...)Sequence analysis1
Glycosylationi501N-linked (GlcNAc...)Sequence analysis1
Glycosylationi525N-linked (GlcNAc...)Sequence analysis1
Glycosylationi536N-linked (GlcNAc...)Sequence analysis1
Glycosylationi582N-linked (GlcNAc...)Sequence analysis1
Glycosylationi603N-linked (GlcNAc...)Sequence analysis1
Glycosylationi618N-linked (GlcNAc...)Sequence analysis1
Glycosylationi628N-linked (GlcNAc...)Sequence analysis1
Glycosylationi637N-linked (GlcNAc...)Sequence analysis1
Glycosylationi666N-linked (GlcNAc...)Sequence analysis1
Glycosylationi669N-linked (GlcNAc...)Sequence analysis1
Glycosylationi761N-linked (GlcNAc...)Sequence analysis1
Glycosylationi772N-linked (GlcNAc...)Sequence analysis1
Glycosylationi784N-linked (GlcNAc...)Sequence analysis1
Glycosylationi790N-linked (GlcNAc...)Sequence analysis1
Glycosylationi824N-linked (GlcNAc...)Sequence analysis1
Glycosylationi910N-linked (GlcNAc...)Sequence analysis1
Glycosylationi937N-linked (GlcNAc...)1 Publication1
Modified residuei1009PhosphoserineCombined sources1

Post-translational modificationi

N- and O-glycosylated.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ12913.
MaxQBiQ12913.
PaxDbiQ12913.
PeptideAtlasiQ12913.
PRIDEiQ12913.

PTM databases

DEPODiQ12913.
iPTMnetiQ12913.
PhosphoSitePlusiQ12913.

Expressioni

Tissue specificityi

Expressed in the promyelocytic cell line HL-60, the granulocyte-macrophage colony-stimulating factor-dependent leukemic cell line F-36P, and the IL3 and erythropoietin-dependent leukemic cell line F-36E. Expressed predominantly in epithelial cells and lymphocytes. Enhanced expression at high cell density.3 Publications

Gene expression databases

BgeeiENSG00000149177.
CleanExiHS_PTPRJ.
ExpressionAtlasiQ12913. baseline and differential.
GenevisibleiQ12913. HS.

Organism-specific databases

HPAiHPA006026.

Interactioni

Subunit structurei

Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352222EBI-2264500,EBI-491549
CTNND1O607165EBI-2264500,EBI-701927
ERBB2P046262EBI-2264500,EBI-641062
FLT1P179482EBI-2264500,EBI-1026718
FLT3P368883EBI-2264500,EBI-3946257
GAB1Q134802EBI-2264500,EBI-517684
GHRP109122EBI-2264500,EBI-286316
KDRP359684EBI-2264500,EBI-1005487
MAPK1P284827EBI-2264500,EBI-959949
MAPK3P273615EBI-2264500,EBI-73995
METP085815EBI-2264500,EBI-1039152
PDGFRBP096194EBI-2264500,EBI-641237
TEKQ027632EBI-2264500,EBI-2257090

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • delta-catenin binding Source: UniProtKB
  • gamma-catenin binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111759. 22 interactors.
IntActiQ12913. 65 interactors.
MINTiMINT-1349281.
STRINGi9606.ENSP00000400010.

Chemistry databases

BindingDBiQ12913.

Structurei

Secondary structure

11337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi368 – 377Combined sources10
Beta strandi382 – 389Combined sources8
Beta strandi398 – 404Combined sources7
Beta strandi409 – 420Combined sources12
Beta strandi429 – 440Combined sources12
Beta strandi446 – 451Combined sources6
Helixi1023 – 1047Combined sources25
Turni1048 – 1054Combined sources7
Turni1058 – 1061Combined sources4
Helixi1063 – 1068Combined sources6
Turni1078 – 1080Combined sources3
Beta strandi1087 – 1089Combined sources3
Helixi1090 – 1093Combined sources4
Beta strandi1096 – 1100Combined sources5
Beta strandi1108 – 1113Combined sources6
Turni1117 – 1119Combined sources3
Helixi1120 – 1129Combined sources10
Beta strandi1134 – 1138Combined sources5
Beta strandi1155 – 1157Combined sources3
Beta strandi1159 – 1161Combined sources3
Beta strandi1164 – 1173Combined sources10
Beta strandi1175 – 1186Combined sources12
Turni1187 – 1189Combined sources3
Beta strandi1192 – 1200Combined sources9
Helixi1212 – 1225Combined sources14
Beta strandi1235 – 1243Combined sources9
Helixi1244 – 1261Combined sources18
Beta strandi1262 – 1265Combined sources4
Helixi1267 – 1275Combined sources9
Helixi1285 – 1302Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CFVX-ray2.50A1019-1311[»]
2DLENMR-A366-456[»]
2NZ6X-ray2.30A1019-1311[»]
ProteinModelPortaliQ12913.
SMRiQ12913.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12913.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini121 – 209Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST89
Domaini207 – 291Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST85
Domaini271 – 364Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST94
Domaini368 – 456Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST89
Domaini457 – 541Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST85
Domaini542 – 623Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST82
Domaini625 – 720Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST96
Domaini721 – 817Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST97
Domaini816 – 902Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST87
Domaini1041 – 1298Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST258

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1239 – 1245Substrate bindingBy similarity7

Sequence similaritiesi

Contains 9 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.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000232054.
HOVERGENiHBG053761.
InParanoidiQ12913.
KOiK05698.
PhylomeDBiQ12913.
TreeFamiTF351926.

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. 2 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. 4 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12913-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT
60 70 80 90 100
VATGENGITQ ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE
110 120 130 140 150
QGSNGTDGAS QKTPSSTGPS PVFDIKAVSI SPTNVILTWK SNDTAASEYK
160 170 180 190 200
YVVKHKMENE KTITVVHQPW CNITGLRPAT SYVFSITPGI GNETWGDPRV
210 220 230 240 250
IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL ESIGSHEELT
260 270 280 290 300
QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR
310 320 330 340 350
AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA
360 370 380 390 400
NGTEGQPQAI EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK
410 420 430 440 450
IHVAGETDSS NLNVSEPRAV IPGLRSSTFY NITVCPVLGD IEGTPGFLQV
460 470 480 490 500
HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE SFQMHITQEG AGNSRVEITT
510 520 530 540 550
NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP SAVFDIHVVY
560 570 580 590 600
VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT
610 620 630 640 650
LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD
660 670 680 690 700
ASPTYSYCLL IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ
710 720 730 740 750
VGDGIKSLEP GRKSFCTDPA SMASFDCEVV PKEPALVLKW TCPPGANAGF
760 770 780 790 800
ELEVSSGAWN NATHLESCSS ENGTEYRTEV TYLNFSTSYN ISITTVSCGK
810 820 830 840 850
MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF EASHGPIKAY
860 870 880 890 900
AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE
910 920 930 940 950
VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG
960 970 980 990 1000
AESYVSFSRY SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR
1010 1020 1030 1040 1050
KDAKNNEVSF SQIKPKKSKL IRVENFEAYF KKQQADSNCG FAEEYEDLKL
1060 1070 1080 1090 1100
VGISQPKYAA ELAENRGKNR YNNVLPYDIS RVKLSVQTHS TDDYINANYM
1110 1120 1130 1140 1150
PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK CVEQGRTKCE
1160 1170 1180 1190 1200
EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF
1210 1220 1230 1240 1250
TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI
1260 1270 1280 1290 1300
AIDRLIYQIE NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR
1310 1320 1330
SQKDSKVDLI YQNTTAMTIY ENLAPVTTFG KTNGYIA
Length:1,337
Mass (Da):145,941
Last modified:February 5, 2008 - v3
Checksum:iB44F4343FC8FD1B4
GO
Isoform 2 (identifier: Q12913-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-539: V → G
     540-1337: Missing.

Note: No experimental confirmation available.
Show »
Length:539
Mass (Da):57,190
Checksum:iE970DA55A6B2E38D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti261G → D in AAB36687 (PubMed:7937872).Curated1
Sequence conflicti918 – 929YNGKL…LGSYR → LQWEAGTSGLLP in BAA07035 (PubMed:7994032).CuratedAdd BLAST12
Sequence conflicti1130K → Q no nucleotide entry (PubMed:8483328).Curated1
Sequence conflicti1234P → E no nucleotide entry (PubMed:8483328).Curated1
Sequence conflicti1243V → I no nucleotide entry (PubMed:8483328).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015905214R → C in a colon cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs121434507dbSNPEnsembl.1
Natural variantiVAR_015906276Q → P in a colon cancer sample; somatic mutation. 2 PublicationsCorresponds to variant rs1566734dbSNPEnsembl.1
Natural variantiVAR_038414293A → T.Corresponds to variant rs2229701dbSNPEnsembl.1
Natural variantiVAR_024582326R → Q.1 PublicationCorresponds to variant rs1503185dbSNPEnsembl.1
Natural variantiVAR_038415372V → I.Corresponds to variant rs2229703dbSNPEnsembl.1
Natural variantiVAR_038416872E → D.4 PublicationsCorresponds to variant rs4752904dbSNPEnsembl.1
Natural variantiVAR_0384171235I → T.Corresponds to variant rs11039554dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_043652539V → G in isoform 2. 1 Publication1
Alternative sequenceiVSP_043653540 – 1337Missing in isoform 2. 1 PublicationAdd BLAST798

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10886 mRNA. Translation: AAB36687.1.
D37781 mRNA. Translation: BAA07035.1.
AC026975 Genomic DNA. No translation available.
AC103828 Genomic DNA. No translation available.
BC063417 mRNA. Translation: AAH63417.1.
AH011675 Genomic DNA. Translation: AAM69432.1.
CCDSiCCDS44596.1. [Q12913-2]
CCDS7945.1. [Q12913-1]
PIRiI38670.
RefSeqiNP_001091973.1. NM_001098503.1. [Q12913-2]
NP_002834.3. NM_002843.3. [Q12913-1]
UniGeneiHs.318547.

Genome annotation databases

EnsembliENST00000418331; ENSP00000400010; ENSG00000149177. [Q12913-1]
ENST00000440289; ENSP00000409733; ENSG00000149177. [Q12913-2]
GeneIDi5795.
KEGGihsa:5795.
UCSCiuc001ngo.5. human. [Q12913-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10886 mRNA. Translation: AAB36687.1.
D37781 mRNA. Translation: BAA07035.1.
AC026975 Genomic DNA. No translation available.
AC103828 Genomic DNA. No translation available.
BC063417 mRNA. Translation: AAH63417.1.
AH011675 Genomic DNA. Translation: AAM69432.1.
CCDSiCCDS44596.1. [Q12913-2]
CCDS7945.1. [Q12913-1]
PIRiI38670.
RefSeqiNP_001091973.1. NM_001098503.1. [Q12913-2]
NP_002834.3. NM_002843.3. [Q12913-1]
UniGeneiHs.318547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CFVX-ray2.50A1019-1311[»]
2DLENMR-A366-456[»]
2NZ6X-ray2.30A1019-1311[»]
ProteinModelPortaliQ12913.
SMRiQ12913.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111759. 22 interactors.
IntActiQ12913. 65 interactors.
MINTiMINT-1349281.
STRINGi9606.ENSP00000400010.

Chemistry databases

BindingDBiQ12913.
ChEMBLiCHEMBL3692.

PTM databases

DEPODiQ12913.
iPTMnetiQ12913.
PhosphoSitePlusiQ12913.

Polymorphism and mutation databases

BioMutaiPTPRJ.
DMDMi166899088.

Proteomic databases

EPDiQ12913.
MaxQBiQ12913.
PaxDbiQ12913.
PeptideAtlasiQ12913.
PRIDEiQ12913.

Protocols and materials databases

DNASUi5795.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418331; ENSP00000400010; ENSG00000149177. [Q12913-1]
ENST00000440289; ENSP00000409733; ENSG00000149177. [Q12913-2]
GeneIDi5795.
KEGGihsa:5795.
UCSCiuc001ngo.5. human. [Q12913-1]

Organism-specific databases

CTDi5795.
DisGeNETi5795.
GeneCardsiPTPRJ.
H-InvDBHIX0035923.
HGNCiHGNC:9673. PTPRJ.
HPAiHPA006026.
MalaCardsiPTPRJ.
MIMi600925. gene.
neXtProtiNX_Q12913.
OpenTargetsiENSG00000149177.
PharmGKBiPA34018.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0791. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000232054.
HOVERGENiHBG053761.
InParanoidiQ12913.
KOiK05698.
PhylomeDBiQ12913.
TreeFamiTF351926.

Enzyme and pathway databases

BioCyciZFISH:HS07590-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807004. Negative regulation of MET activity.
SignaLinkiQ12913.
SIGNORiQ12913.

Miscellaneous databases

ChiTaRSiPTPRJ. human.
EvolutionaryTraceiQ12913.
GeneWikiiPTPRJ.
GenomeRNAii5795.
PROiQ12913.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149177.
CleanExiHS_PTPRJ.
ExpressionAtlasiQ12913. baseline and differential.
GenevisibleiQ12913. HS.

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. 2 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. 4 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_HUMAN
AccessioniPrimary (citable) accession number: Q12913
Secondary accession number(s): Q15255
, Q6P4H4, Q8NHM2, Q9UDA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: November 30, 2016
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.