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P35236

- PTN7_HUMAN

UniProt

P35236 - PTN7_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 7

Gene

PTPN7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction.6 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited in cells after FCER1A triggering.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei257 – 2571Substrate
    Active sitei291 – 2911Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation
    Binding sitei335 – 3351Substrate

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. peptidyl-tyrosine dephosphorylation Source: GOC
    2. protein dephosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BRENDAi3.1.3.48. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 7 (EC:3.1.3.48)
    Alternative name(s):
    Hematopoietic protein-tyrosine phosphatase
    Short name:
    HEPTP
    Protein-tyrosine phosphatase LC-PTP
    Gene namesi
    Name:PTPN7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9659. PTPN7.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic side of plasma membrane Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation. 1 Publication
    Mutagenesisi44 – 441S → D: Reduces binding of MAP kinase. 1 Publication
    Mutagenesisi66 – 661T → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93. 1 Publication
    Mutagenesisi93 – 931S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66. 1 Publication
    Mutagenesisi125 – 1251Y → A: Strongly reduced catalytic activity. 1 Publication
    Mutagenesisi257 – 2571D → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi291 – 2911C → S: Loss of catalytic activity. 1 Publication
    Mutagenesisi335 – 3351Q → A: Reduced catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34003.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 360360Tyrosine-protein phosphatase non-receptor type 7PRO_0000094761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441Phosphoserine3 Publications
    Modified residuei66 – 661Phosphothreonine2 Publications
    Modified residuei93 – 931Phosphoserine1 Publication
    Modified residuei143 – 1431Phosphoserine1 Publication
    Modified residuei291 – 2911Cysteine sulfenic acid (-SOH)By similarity

    Post-translational modificationi

    Phosphorylated on serine residues in resting T-cells. Phosphorylation increases upon exposure to stimuli that increase intracellular cAMP levels. Phosphorylation leads to dissociation of bound MAP kinases.5 Publications
    Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H2O2) or with antigen enhanced oxidation of active site cysteine By similarity.By similarity

    Keywords - PTMi

    Oxidation, Phosphoprotein

    Proteomic databases

    MaxQBiP35236.
    PaxDbiP35236.
    PRIDEiP35236.

    PTM databases

    PhosphoSiteiP35236.

    Expressioni

    Tissue specificityi

    Expressed exclusively in thymus and spleen.2 Publications

    Gene expression databases

    ArrayExpressiP35236.
    BgeeiP35236.
    CleanExiHS_PTPN7.
    GenevestigatoriP35236.

    Organism-specific databases

    HPAiCAB009530.
    HPA019118.

    Interactioni

    Subunit structurei

    Monomer. Interacts with MAPK1, MAPK3 and several other MAP kinases.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK1P284826EBI-2265723,EBI-959949
    MAPK14Q165392EBI-2265723,EBI-73946

    Protein-protein interaction databases

    BioGridi111743. 4 interactions.
    DIPiDIP-29118N.
    IntActiP35236. 4 interactions.
    MINTiMINT-8206881.
    STRINGi9606.ENSP00000356248.

    Structurei

    Secondary structure

    1
    360
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 414
    Helixi67 – 7711
    Beta strandi81 – 833
    Helixi84 – 896
    Helixi94 – 10310
    Helixi111 – 1133
    Helixi119 – 1224
    Helixi132 – 1343
    Beta strandi135 – 1373
    Beta strandi149 – 1557
    Helixi158 – 1603
    Beta strandi164 – 1696
    Helixi173 – 1753
    Helixi176 – 18510
    Beta strandi190 – 1945
    Beta strandi199 – 2013
    Beta strandi210 – 2156
    Beta strandi218 – 22710
    Beta strandi229 – 24012
    Beta strandi243 – 25210
    Helixi264 – 27512
    Beta strandi281 – 2833
    Beta strandi287 – 2959
    Helixi296 – 31419
    Beta strandi315 – 3173
    Helixi319 – 32911
    Helixi337 – 35317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZC0X-ray1.85A65-360[»]
    2A3KX-ray2.55A65-358[»]
    2GP0X-ray2.05A65-360[»]
    2GPHX-ray1.90B37-52[»]
    2HVLX-ray2.40A65-360[»]
    2QDCX-ray2.00A65-360[»]
    2QDMX-ray2.05A65-360[»]
    2QDPX-ray2.72A65-360[»]
    3D42X-ray2.46A65-360[»]
    3D44X-ray1.90A65-360[»]
    3O4SX-ray1.90A65-360[»]
    3O4TX-ray2.60A65-360[»]
    3O4UX-ray2.25A65-360[»]
    ProteinModelPortaliP35236.
    SMRiP35236. Positions 65-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35236.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 350254Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni38 – 5114Interaction with MAP kinasesAdd
    BLAST
    Regioni291 – 2977Substrate binding

    Sequence similaritiesi

    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000294188.
    HOVERGENiHBG001594.
    InParanoidiP35236.
    KOiK18019.
    OrthoDBiEOG7288QX.
    PhylomeDBiP35236.
    TreeFamiTF331016.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR008356. Tyr_Pase_KIM-con.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR01778. KIMPTPASE.
    PR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35236-1) [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

    MVQAHGGRSR AQPLTLSLGA AMTQPPPEKT PAKKHVRLQE RRGSNVALML    50
    DVRSLGAVEP ICSVNTPREV TLHFLRTAGH PLTRWALQRQ PPSPKQLEEE 100
    FLKIPSNFVS PEDLDIPGHA SKDRYKTILP NPQSRVCLGR AQSQEDGDYI 150
    NANYIRGYDG KEKVYIATQG PMPNTVSDFW EMVWQEEVSL IVMLTQLREG 200
    KEKCVHYWPT EEETYGPFQI RIQDMKECPE YTVRQLTIQY QEERRSVKHI 250
    LFSAWPDHQT PESAGPLLRL VAEVEESPET AAHPGPIVVH CSAGIGRTGC 300
    FIATRIGCQQ LKARGEVDIL GIVCQLRLDR GGMIQTAEQY QFLHHTLALY 350
    AGQLPEEPSP 360
    Length:360
    Mass (Da):40,529
    Last modified:January 23, 2002 - v3
    Checksum:i388A154CC55AC0EE
    GO
    Isoform 2 (identifier: P35236-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAPHLSM

    Show »
    Length:399
    Mass (Da):45,002
    Checksum:i16690FDF358E20C8
    GO
    Isoform 3 (identifier: P35236-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVGKAWPLTH...PLGPAPHLSM

    Show »
    Length:465
    Mass (Da):52,284
    Checksum:iAB2E025ECD392906
    GO

    Sequence cautioni

    The sequence AAA59531.1 differs from that shown. Reason: Frameshift at position 5.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti235 – 2362QL → HV in AAA59531. (PubMed:1530918)Curated
    Sequence conflicti337 – 3371A → D in BAA01946. (PubMed:1510684)Curated
    Isoform 3 (identifier: P35236-3)
    Sequence conflicti37 – 371Q → R in BAG54453. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGASFWPIRQAREQQRRALS FRQTSWLSEPPLGPAPHLSM in isoform 2. 1 PublicationVSP_026925
    Alternative sequencei1 – 11M → MVGKAWPLTHSQGTGPWAPE GHRREAADPWWQRQQAQEGR MQLGCAWVAARRGGGRKLAS WSLLSPQRQTDRQTDSWQEA AWGPQLLQQTSWLSEPPLGP APHLSM in isoform 3. 1 PublicationVSP_047275

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11327 mRNA. Translation: BAA01946.1.
    M64322 mRNA. Translation: AAA59531.1. Frameshift.
    BT009848 mRNA. Translation: AAP88850.1.
    AK127214 mRNA. Translation: BAG54453.1.
    AL592300 Genomic DNA. Translation: CAI13108.1.
    BC001746 mRNA. Translation: AAH01746.2.
    CCDSiCCDS1422.1. [P35236-2]
    CCDS1423.2. [P35236-3]
    PIRiJH0692.
    RefSeqiNP_002823.3. NM_002832.3.
    NP_542155.1. NM_080588.2. [P35236-2]
    UniGeneiHs.402773.

    Genome annotation databases

    EnsembliENST00000309017; ENSP00000309116; ENSG00000143851. [P35236-3]
    ENST00000367279; ENSP00000356248; ENSG00000143851. [P35236-2]
    ENST00000495688; ENSP00000420506; ENSG00000143851. [P35236-1]
    GeneIDi5778.
    KEGGihsa:5778.
    UCSCiuc001gxl.2. human. [P35236-2]
    uc001gxo.1. human. [P35236-1]

    Polymorphism databases

    DMDMi20141721.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11327 mRNA. Translation: BAA01946.1 .
    M64322 mRNA. Translation: AAA59531.1 . Frameshift.
    BT009848 mRNA. Translation: AAP88850.1 .
    AK127214 mRNA. Translation: BAG54453.1 .
    AL592300 Genomic DNA. Translation: CAI13108.1 .
    BC001746 mRNA. Translation: AAH01746.2 .
    CCDSi CCDS1422.1. [P35236-2 ]
    CCDS1423.2. [P35236-3 ]
    PIRi JH0692.
    RefSeqi NP_002823.3. NM_002832.3.
    NP_542155.1. NM_080588.2. [P35236-2 ]
    UniGenei Hs.402773.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZC0 X-ray 1.85 A 65-360 [» ]
    2A3K X-ray 2.55 A 65-358 [» ]
    2GP0 X-ray 2.05 A 65-360 [» ]
    2GPH X-ray 1.90 B 37-52 [» ]
    2HVL X-ray 2.40 A 65-360 [» ]
    2QDC X-ray 2.00 A 65-360 [» ]
    2QDM X-ray 2.05 A 65-360 [» ]
    2QDP X-ray 2.72 A 65-360 [» ]
    3D42 X-ray 2.46 A 65-360 [» ]
    3D44 X-ray 1.90 A 65-360 [» ]
    3O4S X-ray 1.90 A 65-360 [» ]
    3O4T X-ray 2.60 A 65-360 [» ]
    3O4U X-ray 2.25 A 65-360 [» ]
    ProteinModelPortali P35236.
    SMRi P35236. Positions 65-357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111743. 4 interactions.
    DIPi DIP-29118N.
    IntActi P35236. 4 interactions.
    MINTi MINT-8206881.
    STRINGi 9606.ENSP00000356248.

    Chemistry

    BindingDBi P35236.
    ChEMBLi CHEMBL2219.

    PTM databases

    PhosphoSitei P35236.

    Polymorphism databases

    DMDMi 20141721.

    Proteomic databases

    MaxQBi P35236.
    PaxDbi P35236.
    PRIDEi P35236.

    Protocols and materials databases

    DNASUi 5778.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309017 ; ENSP00000309116 ; ENSG00000143851 . [P35236-3 ]
    ENST00000367279 ; ENSP00000356248 ; ENSG00000143851 . [P35236-2 ]
    ENST00000495688 ; ENSP00000420506 ; ENSG00000143851 . [P35236-1 ]
    GeneIDi 5778.
    KEGGi hsa:5778.
    UCSCi uc001gxl.2. human. [P35236-2 ]
    uc001gxo.1. human. [P35236-1 ]

    Organism-specific databases

    CTDi 5778.
    GeneCardsi GC01M202116.
    H-InvDB HIX0001472.
    HGNCi HGNC:9659. PTPN7.
    HPAi CAB009530.
    HPA019118.
    MIMi 176889. gene.
    neXtProti NX_P35236.
    PharmGKBi PA34003.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000294188.
    HOVERGENi HBG001594.
    InParanoidi P35236.
    KOi K18019.
    OrthoDBi EOG7288QX.
    PhylomeDBi P35236.
    TreeFami TF331016.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.

    Miscellaneous databases

    ChiTaRSi PTPN7. human.
    EvolutionaryTracei P35236.
    GeneWikii PTPN7.
    GenomeRNAii 5778.
    NextBioi 22472.
    PROi P35236.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35236.
    Bgeei P35236.
    CleanExi HS_PTPN7.
    Genevestigatori P35236.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR008356. Tyr_Pase_KIM-con.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR01778. KIMPTPASE.
    PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTP."
      Adachi M., Sekiya M., Isobe M., Kumura Y., Ogita Z.I., Hinoda Y., Imai K., Yachi A.
      Biochem. Biophys. Res. Commun. 186:1607-1615(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
    2. "Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)."
      Zanke B., Suzuki H., Kishihara K., Mizzen L., Minden M., Pawson A., Mak T.W.
      Eur. J. Immunol. 22:235-239(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Lymphocyte.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Hippocampus.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    6. "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: Lymph.
    7. "Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP)."
      Saxena M., Williams S., Gilman J., Mustelin T.
      J. Biol. Chem. 273:15340-15344(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, MUTAGENESIS OF CYS-291.
    8. "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)."
      Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T.
      J. Biol. Chem. 274:11693-11700(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, PHOSPHORYLATION AT THR-66 AND SER-93, MUTAGENESIS OF THR-66 AND SER-93.
    9. "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase."
      Saxena M., Williams S., Tasken K., Mustelin T.
      Nat. Cell Biol. 1:305-311(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPK1, PHOSPHORYLATION AT SER-44.
    10. "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP."
      Pettiford S.M., Herbst R.
      Oncogene 19:858-869(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3.
    11. "Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T-cells: dynamics and subcellular location."
      Nika K., Hyunh H., Williams S., Paul S., Bottini N., Tasken K., Lombroso P.J., Mustelin T.
      Biochem. J. 378:335-342(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, MUTAGENESIS OF SER-44.
    12. "Molecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase."
      Huang Z., Zhou B., Zhang Z.-Y.
      J. Biol. Chem. 279:52150-52159(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-125; ASP-257 AND GLN-335.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic domain: structure of a KIM phosphatase with phosphate bound at the active site."
      Mustelin T., Tautz L., Page R.
      J. Mol. Biol. 354:150-163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 65-360 OF MUTANT ASP-246 IN COMPLEX WITH SUBSTRATE ANALOG.
    16. "Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases."
      Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E., Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.
      Biochem. J. 395:483-491(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
    17. "Docking interactions induce exposure of activation loop in the MAP kinase ERK2."
      Zhou T., Sun L., Humphreys J., Goldsmith E.J.
      Structure 14:1011-1019(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 37-52 IN COMPLEX WITH MAPK1.

    Entry informationi

    Entry nameiPTN7_HUMAN
    AccessioniPrimary (citable) accession number: P35236
    Secondary accession number(s): B3KXE1
    , Q53XK4, Q5SXQ0, Q5SXQ1, Q9BV05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 145 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3