Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q12913

- PTPRJ_HUMAN

UniProt

Q12913 - PTPRJ_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase eta

Gene

PTPRJ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (05 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1205 – 12051SubstrateBy similarity
    Active sitei1239 – 12391Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1283 – 12831SubstrateBy similarity

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. delta-catenin binding Source: UniProtKB
    3. gamma-catenin binding Source: UniProtKB
    4. mitogen-activated protein kinase binding Source: UniProtKB
    5. phosphatase activity Source: UniProtKB
    6. platelet-derived growth factor receptor binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein kinase binding Source: UniProtKB
    9. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Ensembl
    2. contact inhibition Source: UniProtKB
    3. heart development Source: Ensembl
    4. negative regulation of cell growth Source: UniProtKB
    5. negative regulation of cell migration Source: UniProtKB
    6. negative regulation of cell proliferation Source: UniProtKB
    7. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    8. negative regulation of MAP kinase activity Source: UniProtKB
    9. negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    10. negative regulation of protein kinase B signaling Source: UniProtKB
    11. negative regulation of receptor activity Source: Ensembl
    12. negative regulation of T cell receptor signaling pathway Source: UniProtKB
    13. negative regulation of vascular permeability Source: UniProtKB
    14. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    15. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    16. positive chemotaxis Source: UniProtKB
    17. positive regulation of cell adhesion Source: UniProtKB
    18. positive regulation of focal adhesion assembly Source: UniProtKB
    19. positive regulation of macrophage chemotaxis Source: Ensembl
    20. positive regulation of platelet activation Source: Ensembl
    21. positive regulation of protein kinase B signaling Source: UniProtKB
    22. regulation of cell adhesion Source: UniProtKB
    23. vasculogenesis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiQ12913.

    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
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9673. PTPRJ.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cell projectionruffle membrane By similarity. Cell junction
    Note: After T-cell stimulation, it is temporarily excluded from immunological synapses.

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cell surface Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. immunological synapse Source: UniProtKB
    5. integral component of plasma membrane Source: ProtInc
    6. plasma membrane Source: UniProtKB
    7. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1016 – 10161K → A: 80% decrease in interaction with MAPK1 and MAPK3. 1 Publication
    Mutagenesisi1205 – 12051D → A: Substrate trapping with much higher affinity for substrate. 9 Publications
    Mutagenesisi1239 – 12391C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 6 Publications

    Organism-specific databases

    PharmGKBiPA34018.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 13371302Receptor-type tyrosine-protein phosphatase etaPRO_0000025444Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi342 – 3421N-linked (GlcNAc...)2 Publications
    Glycosylationi351 – 3511N-linked (GlcNAc...)2 Publications
    Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi391 – 3911N-linked (GlcNAc...)2 Publications
    Glycosylationi396 – 3961N-linked (GlcNAc...)2 Publications
    Glycosylationi413 – 4131N-linked (GlcNAc...)2 Publications
    Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi618 – 6181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi628 – 6281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi784 – 7841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi824 – 8241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi910 – 9101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi937 – 9371N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    N- and O-glycosylated.3 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ12913.
    PaxDbiQ12913.
    PRIDEiQ12913.

    PTM databases

    PhosphoSiteiQ12913.

    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

    ArrayExpressiQ12913.
    BgeeiQ12913.
    CleanExiHS_PTPRJ.
    GenevestigatoriQ12913.

    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
    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

    Protein-protein interaction databases

    BioGridi111759. 10 interactions.
    IntActiQ12913. 38 interactions.
    MINTiMINT-1349281.
    STRINGi9606.ENSP00000400010.

    Structurei

    Secondary structure

    1
    1337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi368 – 37710
    Beta strandi382 – 3898
    Beta strandi398 – 4047
    Beta strandi409 – 42012
    Beta strandi429 – 44012
    Beta strandi446 – 4516
    Helixi1023 – 104725
    Turni1048 – 10547
    Turni1058 – 10614
    Helixi1063 – 10686
    Turni1078 – 10803
    Beta strandi1087 – 10893
    Helixi1090 – 10934
    Beta strandi1096 – 11005
    Beta strandi1108 – 11136
    Turni1117 – 11193
    Helixi1120 – 112910
    Beta strandi1134 – 11385
    Beta strandi1155 – 11573
    Beta strandi1159 – 11613
    Beta strandi1164 – 117310
    Beta strandi1175 – 118612
    Turni1187 – 11893
    Beta strandi1192 – 12009
    Helixi1212 – 122514
    Beta strandi1235 – 12439
    Helixi1244 – 126118
    Beta strandi1262 – 12654
    Helixi1267 – 12759
    Helixi1285 – 130218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CFVX-ray2.50A1019-1311[»]
    2DLENMR-A366-456[»]
    2NZ6X-ray2.30A1019-1311[»]
    ProteinModelPortaliQ12913.
    SMRiQ12913. Positions 169-195, 210-279, 319-714, 721-812, 1018-1303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12913.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 975940ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini997 – 1337341CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei976 – 99621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini121 – 20989Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini207 – 29185Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 36494Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini368 – 45689Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini457 – 54185Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini542 – 62382Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini625 – 72096Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini721 – 81797Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini816 – 90287Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1041 – 1298258Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1239 – 12457Substrate bindingBy similarity

    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

    eggNOGiCOG5599.
    HOGENOMiHOG000232054.
    HOVERGENiHBG053761.
    InParanoidiQ12913.
    KOiK05698.
    OMAiSYVSFSR.
    OrthoDBiEOG7PCJFZ.
    PhylomeDBiQ12913.
    TreeFamiTF351926.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    3.90.190.10. 1 hit.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 4 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 8 hits.
    SM00194. PTPc. 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. Align

    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

    MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT     50
    VATGENGITQ ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE 100
    QGSNGTDGAS QKTPSSTGPS PVFDIKAVSI SPTNVILTWK SNDTAASEYK 150
    YVVKHKMENE KTITVVHQPW CNITGLRPAT SYVFSITPGI GNETWGDPRV 200
    IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL ESIGSHEELT 250
    QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR 300
    AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA 350
    NGTEGQPQAI EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK 400
    IHVAGETDSS NLNVSEPRAV IPGLRSSTFY NITVCPVLGD IEGTPGFLQV 450
    HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE SFQMHITQEG AGNSRVEITT 500
    NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP SAVFDIHVVY 550
    VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT 600
    LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD 650
    ASPTYSYCLL IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ 700
    VGDGIKSLEP GRKSFCTDPA SMASFDCEVV PKEPALVLKW TCPPGANAGF 750
    ELEVSSGAWN NATHLESCSS ENGTEYRTEV TYLNFSTSYN ISITTVSCGK 800
    MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF EASHGPIKAY 850
    AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE 900
    VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG 950
    AESYVSFSRY SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR 1000
    KDAKNNEVSF SQIKPKKSKL IRVENFEAYF KKQQADSNCG FAEEYEDLKL 1050
    VGISQPKYAA ELAENRGKNR YNNVLPYDIS RVKLSVQTHS TDDYINANYM 1100
    PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK CVEQGRTKCE 1150
    EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF 1200
    TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI 1250
    AIDRLIYQIE NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR 1300
    SQKDSKVDLI YQNTTAMTIY ENLAPVTTFG KTNGYIA 1337
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611G → D in AAB36687. (PubMed:7937872)Curated
    Sequence conflicti918 – 92912YNGKL…LGSYR → LQWEAGTSGLLP in BAA07035. (PubMed:7994032)CuratedAdd
    BLAST
    Sequence conflicti1130 – 11301K → Q no nucleotide entry (PubMed:8483328)Curated
    Sequence conflicti1234 – 12341P → E no nucleotide entry (PubMed:8483328)Curated
    Sequence conflicti1243 – 12431V → I no nucleotide entry (PubMed:8483328)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141R → C in a colon cancer sample; somatic mutation. 1 Publication
    VAR_015905
    Natural varianti276 – 2761Q → P in a colon cancer sample; somatic mutation. 2 Publications
    Corresponds to variant rs1566734 [ dbSNP | Ensembl ].
    VAR_015906
    Natural varianti293 – 2931A → T.
    Corresponds to variant rs2229701 [ dbSNP | Ensembl ].
    VAR_038414
    Natural varianti326 – 3261R → Q.1 Publication
    Corresponds to variant rs1503185 [ dbSNP | Ensembl ].
    VAR_024582
    Natural varianti372 – 3721V → I.
    Corresponds to variant rs2229703 [ dbSNP | Ensembl ].
    VAR_038415
    Natural varianti872 – 8721E → D.4 Publications
    Corresponds to variant rs4752904 [ dbSNP | Ensembl ].
    VAR_038416
    Natural varianti1235 – 12351I → T.
    Corresponds to variant rs11039554 [ dbSNP | Ensembl ].
    VAR_038417

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei539 – 5391V → G in isoform 2. 1 PublicationVSP_043652
    Alternative sequencei540 – 1337798Missing in isoform 2. 1 PublicationVSP_043653Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.4. human. [Q12913-2]
    uc001ngp.4. human. [Q12913-1]

    Polymorphism databases

    DMDMi166899088.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS44596.1. [Q12913-2 ]
    CCDS7945.1. [Q12913-1 ]
    PIRi I38670.
    RefSeqi NP_001091973.1. NM_001098503.1. [Q12913-2 ]
    NP_002834.3. NM_002843.3. [Q12913-1 ]
    UniGenei Hs.318547.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CFV X-ray 2.50 A 1019-1311 [» ]
    2DLE NMR - A 366-456 [» ]
    2NZ6 X-ray 2.30 A 1019-1311 [» ]
    ProteinModelPortali Q12913.
    SMRi Q12913. Positions 169-195, 210-279, 319-714, 721-812, 1018-1303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111759. 10 interactions.
    IntActi Q12913. 38 interactions.
    MINTi MINT-1349281.
    STRINGi 9606.ENSP00000400010.

    Chemistry

    BindingDBi Q12913.
    ChEMBLi CHEMBL3692.

    PTM databases

    PhosphoSitei Q12913.

    Polymorphism databases

    DMDMi 166899088.

    Proteomic databases

    MaxQBi Q12913.
    PaxDbi Q12913.
    PRIDEi Q12913.

    Protocols and materials databases

    DNASUi 5795.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000418331 ; ENSP00000400010 ; ENSG00000149177 . [Q12913-1 ]
    ENST00000440289 ; ENSP00000409733 ; ENSG00000149177 . [Q12913-2 ]
    GeneIDi 5795.
    KEGGi hsa:5795.
    UCSCi uc001ngo.4. human. [Q12913-2 ]
    uc001ngp.4. human. [Q12913-1 ]

    Organism-specific databases

    CTDi 5795.
    GeneCardsi GC11P047958.
    H-InvDB HIX0035923.
    HGNCi HGNC:9673. PTPRJ.
    HPAi HPA006026.
    MIMi 600925. gene.
    neXtProti NX_Q12913.
    PharmGKBi PA34018.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000232054.
    HOVERGENi HBG053761.
    InParanoidi Q12913.
    KOi K05698.
    OMAi SYVSFSR.
    OrthoDBi EOG7PCJFZ.
    PhylomeDBi Q12913.
    TreeFami TF351926.

    Enzyme and pathway databases

    SignaLinki Q12913.

    Miscellaneous databases

    ChiTaRSi PTPRJ. human.
    EvolutionaryTracei Q12913.
    GeneWikii PTPRJ.
    GenomeRNAii 5795.
    NextBioi 22564.
    PROi Q12913.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12913.
    Bgeei Q12913.
    CleanExi HS_PTPRJ.
    Genevestigatori Q12913.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    3.90.190.10. 1 hit.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00041. fn3. 4 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 8 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 4 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50853. FN3. 6 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density."
      Oestman A., Yang Q., Tonks N.K.
      Proc. Natl. Acad. Sci. U.S.A. 91:9680-9684(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-872.
    2. "Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta."
      Honda H., Inazawa J., Nishida J., Yazaki Y., Hirai H.
      Blood 84:4186-4194(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-872.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2).
      Tissue: Pancreas.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-1337, VARIANTS CYS-214; PRO-276 AND ASP-872.
      Tissue: Colon.
    6. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 1124-1245 (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Leukemia.
    7. "CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes."
      de la Fuente-Garcia M.A., Nicolas J.M., Freed J.H., Palou E., Thomas A.P., Vilella R., Vives J., Gaya A.
      Blood 91:2800-2809(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-49; 485-502 AND 723-739, FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
    8. "Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148."
      Tangye S.G., Wu J., Aversa G., de Vries J.E., Lanier L.L., Phillips J.H.
      J. Immunol. 161:3803-3807(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1."
      Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., Ostman A.
      J. Biol. Chem. 275:16219-16226(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
      Baker J.E., Majeti R., Tangye S.G., Weiss A.
      Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1."
      Persson C., Engstrom U., Mowbray S.L., Ostman A.
      FEBS Lett. 517:27-31(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
      Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
      Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTNNB1 AND JUP, MUTAGENESIS OF ASP-1205 AND CYS-1239, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    13. "Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
      Palka H.L., Park M., Tonks N.K.
      J. Biol. Chem. 278:5728-5735(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTNNB1; GRB2; GAB1 AND JUP, MUTAGENESIS OF ASP-1205 AND CYS-1239.
    14. "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.
    15. "The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation."
      Kellie S., Craggs G., Bird I.N., Jones G.E.
      J. Cell Sci. 117:609-618(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 AND ASN-396.
      Tissue: Plasma.
    17. "The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins."
      Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M., Carlomagno F., Santoro M., Fusco A.
      Cancer Res. 66:6280-6287(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-1205.
    18. "DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients."
      Balavenkatraman K.K., Jandt E., Friedrich K., Kautenburger T., Pool-Zobel B.L., Ostman A., Bohmer F.D.
      Oncogene 25:6319-6324(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase."
      Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M., Takahashi T.
      Biochem. J. 413:193-200(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-1205, SUBCELLULAR LOCATION.
    20. "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: SUBUNIT.
    21. "An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
      Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
      Curr. Biol. 19:1788-1798(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EGFR REGULATION, MUTAGENESIS OF ASP-1205 AND CYS-1239, SUBCELLULAR LOCATION.
    22. "Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells."
      Sallee J.L., Burridge K.
      J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239, SUBCELLULAR LOCATION.
    23. "Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases."
      Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P., Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.
      J. Biol. Chem. 284:22048-22058(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-1016 AND ASP-1205.
    24. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937.
      Tissue: Liver.
    25. "New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival."
      Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.
      Mol. Cell. Biol. 29:241-253(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239.
    26. "Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility."
      Petermann A., Haase D., Wetzel A., Balavenkatraman K.K., Tenev T., Guhrs K.H., Friedrich S., Nakamura M., Mawrin C., Bohmer F.D.
      Brain Pathol. 21:405-418(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells."
      Omerovic J., Clague M.J., Prior I.A.
      Biochem. J. 426:65-72(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. Cited for: FUNCTION, INTERACTION WITH FLT3, MUTAGENESIS OF ASP-1205 AND CYS-1239.
    29. "Solution structure of the fourth FN3 domain of human receptor-type tyrosine-protein phosphatase eta."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 366-456.
    30. "The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid carcinogenesis."
      Iuliano R., Le Pera I., Cristofaro C., Baudi F., Arturi F., Pallante P., Martelli M.L., Trapasso F., Chiariotti L., Fusco A.
      Oncogene 23:8432-8438(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PRO-276; GLN-326 AND ASP-872.

    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: October 1, 2014
    This is version 153 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

    External Data

    Dasty 3