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P20417

- PTN1_RAT

UniProt

P20417 - PTN1_RAT

Protein

Tyrosine-protein phosphatase non-receptor type 1

Gene

Ptpn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei181 – 1811SubstrateBy similarity
    Active sitei215 – 2151Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei262 – 2621SubstrateBy similarity

    GO - Molecular functioni

    1. insulin receptor binding Source: RGD
    2. protein binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: RGD
    4. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. endoplasmic reticulum unfolded protein response Source: UniProtKB
    3. insulin receptor signaling pathway Source: Ensembl
    4. platelet-derived growth factor receptor-beta signaling pathway Source: Ensembl
    5. protein dephosphorylation Source: RGD
    6. regulation of endocytosis Source: UniProtKB
    7. regulation of hepatocyte growth factor receptor signaling pathway Source: Ensembl
    8. regulation of insulin receptor signaling pathway Source: RGD
    9. regulation of signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_196236. Regulation of IFNA signaling.
    REACT_196425. Growth hormone receptor signaling.
    REACT_196448. Regulation of IFNG signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 1 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase 1B
    Short name:
    PTP-1B
    Gene namesi
    Name:Ptpn1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi61965. Ptpn1.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Interacts with EPHA3 at the cell membrane.By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: RGD
    2. cytoplasmic vesicle Source: RGD
    3. cytosol Source: RGD
    4. early endosome Source: UniProtKB
    5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    6. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Tyrosine-protein phosphatase non-receptor type 1PRO_0000094750Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei20 – 201PhosphotyrosineBy similarity
    Modified residuei50 – 501Phosphoserine; by PKB/AKT1, CLK1 and CLK2By similarity
    Modified residuei66 – 661Phosphotyrosine; by EGFRBy similarity
    Modified residuei215 – 2151Cysteine persulfideBy similarity
    Modified residuei215 – 2151S-nitrosocysteine; in reversibly inhibited formBy similarity
    Modified residuei242 – 2421Phosphoserine; by CLK1 and CLK2By similarity
    Modified residuei243 – 2431Phosphoserine; by CLK1 and CLK2By similarity

    Post-translational modificationi

    Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50 By similarity.By similarity
    S-nitrosylation of Cys-215 inactivates the enzyme activity.By similarity
    Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    PaxDbiP20417.
    PRIDEiP20417.

    Expressioni

    Tissue specificityi

    Found in several tissues including central nervous system, liver and kidney. A high level of expression was found in the hippocampus.

    Gene expression databases

    ArrayExpressiP20417.
    GenevestigatoriP20417.

    Interactioni

    Subunit structurei

    Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts with MET.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP0053311EBI-916819,EBI-297353From a different organism.

    Protein-protein interaction databases

    IntActiP20417. 3 interactions.
    STRINGi10116.ENSRNOP00000014309.

    Structurei

    3D structure databases

    ProteinModelPortaliP20417.
    SMRiP20417. Positions 1-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 277275Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni215 – 2217Substrate bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00750000117312.
    HOGENOMiHOG000273908.
    HOVERGENiHBG008321.
    InParanoidiP20417.
    KOiK05696.
    OMAiMCMATVL.
    OrthoDBiEOG7RV9G4.
    PhylomeDBiP20417.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR012265. Ptpn1/Ptpn2.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
    PRINTSiPR00700. 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]

    Sequencei

    Sequence statusi: Complete.

    P20417-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMEKEFEQI DKAGNWAAIY QDIRHEASDF PCRIAKLPKN KNRNRYRDVS    50
    PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW 100
    EQKSRGVVML NRIMEKGSLK CAQYWPQKEE KEMVFDDTNL KLTLISEDVK 150
    SYYTVRQLEL ENLATQEARE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE 200
    SGSLSPEHGP IVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL 250
    LEMRRFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE 300
    PPPEHVPPPP RPPKRTLEPH NGKCKELFSN HQWVSEESCE DEDILAREES 350
    RAPSIAVHSM SSMSQDTEVR KRMVGGGLQS AQASVPTEEE LSPTEEEQKA 400
    HRPVHWKPFL VNVCMATALA TGAYLCYRVC FH 432
    Length:432
    Mass (Da):49,674
    Last modified:February 1, 1991 - v1
    Checksum:i0D5859A09B1885C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33962 mRNA. Translation: AAC79516.1.
    BC081829 mRNA. Translation: AAH81829.1.
    PIRiA34845.
    RefSeqiNP_036769.1. NM_012637.2.
    XP_006235700.1. XM_006235638.1.
    UniGeneiRn.11317.

    Genome annotation databases

    EnsembliENSRNOT00000014309; ENSRNOP00000014309; ENSRNOG00000010574.
    GeneIDi24697.
    KEGGirno:24697.
    UCSCiRGD:61965. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33962 mRNA. Translation: AAC79516.1 .
    BC081829 mRNA. Translation: AAH81829.1 .
    PIRi A34845.
    RefSeqi NP_036769.1. NM_012637.2.
    XP_006235700.1. XM_006235638.1.
    UniGenei Rn.11317.

    3D structure databases

    ProteinModelPortali P20417.
    SMRi P20417. Positions 1-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P20417. 3 interactions.
    STRINGi 10116.ENSRNOP00000014309.

    Chemistry

    BindingDBi P20417.
    ChEMBLi CHEMBL2371.

    Proteomic databases

    PaxDbi P20417.
    PRIDEi P20417.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014309 ; ENSRNOP00000014309 ; ENSRNOG00000010574 .
    GeneIDi 24697.
    KEGGi rno:24697.
    UCSCi RGD:61965. rat.

    Organism-specific databases

    CTDi 5770.
    RGDi 61965. Ptpn1.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00750000117312.
    HOGENOMi HOG000273908.
    HOVERGENi HBG008321.
    InParanoidi P20417.
    KOi K05696.
    OMAi MCMATVL.
    OrthoDBi EOG7RV9G4.
    PhylomeDBi P20417.

    Enzyme and pathway databases

    Reactomei REACT_196236. Regulation of IFNA signaling.
    REACT_196425. Growth hormone receptor signaling.
    REACT_196448. Regulation of IFNG signaling.

    Miscellaneous databases

    NextBioi 604151.
    PROi P20417.

    Gene expression databases

    ArrayExpressi P20417.
    Genevestigatori P20417.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR012265. Ptpn1/Ptpn2.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000926. Tyr-Ptase_nr1. 1 hit.
    PRINTSi 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "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].
      Tissue: Testis.
    3. "Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system."
      Hashimoto N., Zhang W.R., Goldstein B.J.
      Biochem. J. 284:569-576(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-283.

    Entry informationi

    Entry nameiPTN1_RAT
    AccessioniPrimary (citable) accession number: P20417
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3