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P18031

- PTN1_HUMAN

UniProt

P18031 - PTN1_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 1

Gene

PTPN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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.3 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei181 – 1811Substrate
    Active sitei215 – 2151Phosphocysteine intermediate
    Binding sitei262 – 2621SubstrateBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. ephrin receptor binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein kinase binding Source: UniProtKB
    6. protein tyrosine phosphatase activity Source: UniProtKB
    7. receptor tyrosine kinase binding Source: UniProtKB
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. blood coagulation Source: Reactome
    3. cytokine-mediated signaling pathway Source: Reactome
    4. endoplasmic reticulum unfolded protein response Source: UniProtKB
    5. insulin receptor signaling pathway Source: Ensembl
    6. interferon-gamma-mediated signaling pathway Source: Reactome
    7. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    8. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    9. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
    10. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    11. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    12. peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: BHF-UCL
    13. platelet activation Source: Reactome
    14. platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
    15. regulation of endocytosis Source: UniProtKB
    16. regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
    17. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    18. regulation of signal transduction Source: UniProtKB
    19. regulation of type I interferon-mediated signaling pathway Source: Reactome
    20. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BRENDAi3.1.3.48. 2681.
    ReactomeiREACT_111133. Growth hormone receptor signaling.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25216. Regulation of IFNA signaling.
    SABIO-RKP18031.
    SignaLinkiP18031.

    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
    Synonyms:PTP1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9642. PTPN1.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications
    Note: Interacts with EPHA3 at the cell membrane.

    GO - Cellular componenti

    1. cytoplasmic vesicle Source: Ensembl
    2. cytosol Source: Reactome
    3. early endosome Source: UniProtKB
    4. endoplasmic reticulum Source: HPA
    5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    6. sorting endosome Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501S → A or D: No phosphorylation. 2 Publications
    Mutagenesisi181 – 1811D → A: Substrate-trapping mutant. 1 Publication
    Mutagenesisi215 – 2151C → S: Catalytically inactive mutant; abolishes sulfhydration. 1 Publication

    Organism-specific databases

    PharmGKBiPA33985.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Tyrosine-protein phosphatase non-receptor type 1PRO_0000094748Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei20 – 201Phosphotyrosine1 Publication
    Modified residuei50 – 501Phosphoserine; by PKB/AKT1, CLK1 and CLK22 Publications
    Modified residuei66 – 661Phosphotyrosine; by EGFR1 Publication
    Cross-linki215 ↔ 216N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form
    Modified residuei215 – 2151Cysteine persulfide1 Publication
    Modified residuei215 – 2151S-nitrosocysteine; in reversibly inhibited form1 Publication
    Modified residuei242 – 2421Phosphoserine; by CLK1 and CLK21 Publication
    Modified residuei243 – 2431Phosphoserine; by CLK1 and CLK21 Publication
    Modified residuei352 – 3521Phosphoserine3 Publications
    Modified residuei378 – 3781Phosphoserine; by PKC2 Publications
    Modified residuei386 – 3861Phosphoserine; by CDK11 Publication

    Post-translational modificationi

    Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction.2 Publications
    Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.8 Publications
    S-nitrosylation of Cys-215 inactivates the enzyme activity.1 Publication
    Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.

    Keywords - PTMi

    Acetylation, Oxidation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP18031.
    PaxDbiP18031.
    PeptideAtlasiP18031.
    PRIDEiP18031.

    2D gel databases

    OGPiP18031.

    PTM databases

    PhosphoSiteiP18031.

    Miscellaneous databases

    PMAP-CutDBP18031.

    Expressioni

    Gene expression databases

    ArrayExpressiP18031.
    BgeeiP18031.
    CleanExiHS_PTPN1.
    GenevestigatoriP18031.

    Organism-specific databases

    HPAiCAB009329.
    CAB015217.
    HPA012542.

    Interactioni

    Subunit structurei

    Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts with MET.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAR1P569455EBI-968788,EBI-702093
    Bcar1Q611405EBI-968788,EBI-77088From a different organism.
    Bcar1Q637675EBI-968788,EBI-1176801From a different organism.
    BCRP11274-13EBI-968788,EBI-8658094
    CAPN1P073844EBI-968788,EBI-1542113
    CAV1Q031355EBI-968788,EBI-603614
    Cdh2P151163EBI-968788,EBI-397974From a different organism.
    CrkQ637682EBI-968788,EBI-8423843From a different organism.
    CTTNQ142472EBI-968788,EBI-351886
    EGFRP005334EBI-968788,EBI-297353
    EPORP192353EBI-968788,EBI-617321
    GHRP109125EBI-968788,EBI-286316
    GRB2P629932EBI-968788,EBI-401755
    Grb2P629943EBI-968788,EBI-401775From a different organism.
    IGF1RP080693EBI-968788,EBI-475981
    INSRP0621333EBI-968788,EBI-475899
    Irs1P355703EBI-968788,EBI-520230From a different organism.
    ITGB1P055562EBI-968788,EBI-703066
    ITGB3P051064EBI-968788,EBI-702847
    JAK2O606745EBI-968788,EBI-518647
    LATO435613EBI-968788,EBI-1222766
    METP085813EBI-968788,EBI-1039152
    NTRK1P046292EBI-968788,EBI-1028226
    PDGFRBP096193EBI-968788,EBI-641237
    PdgfrbP056223EBI-968788,EBI-1554855From a different organism.
    Plcg1P106864EBI-968788,EBI-520788From a different organism.
    Ptk2P341522EBI-968788,EBI-77070From a different organism.
    PxnQ8VI362EBI-968788,EBI-983394From a different organism.
    ROS1P089223EBI-968788,EBI-7371065
    SRCP1293114EBI-968788,EBI-621482
    STAT3P407632EBI-968788,EBI-518675
    STAT5AP422292EBI-968788,EBI-749537
    Sumo1P631662EBI-968788,EBI-80152From a different organism.
    TRPV6Q9H1D06EBI-968788,EBI-7198335
    TXNP105992EBI-968788,EBI-594644

    Protein-protein interaction databases

    BioGridi111736. 37 interactions.
    DIPiDIP-38014N.
    IntActiP18031. 79 interactions.
    MINTiMINT-441655.
    STRINGi9606.ENSP00000360683.

    Structurei

    Secondary structure

    1
    435
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Helixi16 – 2611
    Turni33 – 364
    Helixi38 – 436
    Beta strandi45 – 484
    Turni53 – 553
    Beta strandi56 – 583
    Beta strandi61 – 633
    Beta strandi66 – 749
    Turni75 – 784
    Beta strandi79 – 846
    Turni89 – 913
    Helixi92 – 10211
    Beta strandi106 – 1094
    Beta strandi113 – 1153
    Beta strandi118 – 1214
    Beta strandi128 – 1303
    Beta strandi133 – 1353
    Turni136 – 1394
    Beta strandi140 – 14910
    Beta strandi151 – 16212
    Turni163 – 1653
    Beta strandi168 – 1769
    Beta strandi181 – 1833
    Beta strandi186 – 1883
    Helixi189 – 20012
    Turni201 – 2044
    Beta strandi211 – 22010
    Helixi221 – 23717
    Beta strandi238 – 2403
    Helixi241 – 2433
    Helixi246 – 2538
    Turni254 – 2563
    Helixi264 – 28118
    Turni282 – 2843
    Helixi287 – 2959
    Turni296 – 2983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A5YX-ray2.50A1-330[»]
    1AAXX-ray1.90A1-321[»]
    1BZCX-ray2.35A1-321[»]
    1BZHX-ray2.10A1-298[»]
    1BZJX-ray2.25A2-298[»]
    1C83X-ray1.80A1-298[»]
    1C84X-ray2.35A1-298[»]
    1C85X-ray2.72A1-298[»]
    1C86X-ray2.30A1-298[»]
    1C87X-ray2.10A1-298[»]
    1C88X-ray1.80A1-298[»]
    1ECVX-ray1.95A1-298[»]
    1EENX-ray1.90A1-321[»]
    1EEOX-ray1.80A1-321[»]
    1G1FX-ray2.00A1-298[»]
    1G1GX-ray2.20A1-298[»]
    1G1HX-ray2.40A1-298[»]
    1G7FX-ray1.80A1-298[»]
    1G7GX-ray2.20A1-298[»]
    1GFYX-ray2.13A1-298[»]
    1I57X-ray2.10A1-298[»]
    1JF7X-ray2.20A/B1-298[»]
    1KAKX-ray2.50A1-298[»]
    1KAVX-ray2.35A1-298[»]
    1L8GX-ray2.50A1-321[»]
    1LQFX-ray2.50A/B/C/D1-283[»]
    1NL9X-ray2.40A1-321[»]
    1NNYX-ray2.40A1-321[»]
    1NO6X-ray2.40A1-321[»]
    1NWEX-ray3.10A1-298[»]
    1NWLX-ray2.40A1-298[»]
    1NZ7X-ray2.40A1-321[»]
    1OEMX-ray1.80X1-321[»]
    1OEOX-ray2.15X1-321[»]
    1OESX-ray2.20A1-321[»]
    1OETX-ray2.30A1-321[»]
    1OEUX-ray2.50A1-321[»]
    1OEVX-ray2.20A1-321[»]
    1ONYX-ray2.15A1-321[»]
    1ONZX-ray2.40A1-321[»]
    1PA1X-ray1.60A1-298[»]
    1PH0X-ray2.20A1-321[»]
    1PTTX-ray2.90A1-321[»]
    1PTUX-ray2.60A1-321[»]
    1PTVX-ray2.30A1-321[»]
    1PTYX-ray1.85A1-321[»]
    1PXHX-ray2.15A1-321[»]
    1PYNX-ray2.20A1-321[»]
    1Q1MX-ray2.60A1-321[»]
    1Q6JX-ray2.20A1-298[»]
    1Q6MX-ray2.20A1-298[»]
    1Q6NX-ray2.10A/B1-298[»]
    1Q6PX-ray2.30A/B1-298[»]
    1Q6SX-ray2.20A/B1-298[»]
    1Q6TX-ray2.30A/B1-298[»]
    1QXKX-ray2.30A1-321[»]
    1SUGX-ray1.95A1-321[»]
    1T48X-ray2.20A1-298[»]
    1T49X-ray1.90A1-298[»]
    1T4JX-ray2.70A1-298[»]
    1WAXX-ray2.20A1-321[»]
    1XBOX-ray2.50A1-321[»]
    2AZRX-ray2.00A1-299[»]
    2B07X-ray2.10A1-299[»]
    2B4SX-ray2.30A/C1-298[»]
    2BGDX-ray2.40A1-321[»]
    2BGEX-ray1.80A1-321[»]
    2CM2X-ray1.50A2-298[»]
    2CM3X-ray2.10A/B1-298[»]
    2CM7X-ray2.10A1-321[»]
    2CM8X-ray2.10A1-321[»]
    2CMAX-ray2.30A1-321[»]
    2CMBX-ray1.70A1-298[»]
    2CMCX-ray2.20A1-298[»]
    2CNEX-ray1.80A1-298[»]
    2CNFX-ray2.20A1-321[»]
    2CNGX-ray1.90A1-321[»]
    2CNHX-ray1.80A1-321[»]
    2CNIX-ray2.00A1-321[»]
    2F6FX-ray2.00A1-298[»]
    2F6TX-ray1.70A1-298[»]
    2F6VX-ray1.70A1-298[»]
    2F6WX-ray2.20A1-298[»]
    2F6YX-ray2.15A1-298[»]
    2F6ZX-ray1.70A1-298[»]
    2F70X-ray2.12A1-298[»]
    2F71X-ray1.55A1-298[»]
    2FJMX-ray2.10A/B1-298[»]
    2FJNX-ray2.20A/B1-298[»]
    2H4GX-ray2.50A1-299[»]
    2H4KX-ray2.30A1-299[»]
    2HB1X-ray2.00A1-299[»]
    2HNPX-ray2.85A1-321[»]
    2HNQX-ray2.85A1-321[»]
    2NT7X-ray2.10A1-299[»]
    2NTAX-ray2.10A1-299[»]
    2QBPX-ray2.50A1-299[»]
    2QBQX-ray2.10A1-299[»]
    2QBRX-ray2.30A1-299[»]
    2QBSX-ray2.10A1-299[»]
    2VEUX-ray2.40A1-321[»]
    2VEVX-ray1.80A1-321[»]
    2VEWX-ray2.00A1-321[»]
    2VEXX-ray2.20A1-321[»]
    2VEYX-ray2.20A1-321[»]
    2ZMMX-ray2.10A1-299[»]
    2ZN7X-ray2.10A1-299[»]
    3A5JX-ray1.70A2-321[»]
    3A5KX-ray1.85A2-298[»]
    3CWEX-ray1.60A1-283[»]
    3D9CX-ray2.30A1-321[»]
    3EAXX-ray1.90A1-321[»]
    3EB1X-ray2.40A1-321[»]
    3EU0X-ray2.70A1-282[»]
    3I7ZX-ray2.30A1-321[»]
    3I80X-ray2.25A1-321[»]
    3QKPX-ray2.05A1-321[»]
    3QKQX-ray2.20A1-321[»]
    3SMEX-ray1.70A1-298[»]
    3ZMPX-ray2.62A/B1-321[»]
    3ZMQX-ray3.30A1-321[»]
    3ZV2X-ray2.80A1-320[»]
    4BJOX-ray2.06A/B2-321[»]
    4I8NX-ray2.50A1-320[»]
    ProteinModelPortaliP18031.
    SMRiP18031. Positions 2-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18031.

    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.
    HOGENOMiHOG000273908.
    HOVERGENiHBG008321.
    InParanoidiP18031.
    KOiK05696.
    OMAiMCMATVL.
    OrthoDBiEOG7RV9G4.
    PhylomeDBiP18031.
    TreeFamiTF315897.

    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.

    P18031-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS    50
    PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW 100
    EQKSRGVVML NRVMEKGSLK CAQYWPQKEE KEMIFEDTNL KLTLISEDIK 150
    SYYTVRQLEL ENLTTQETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE 200
    SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL 250
    LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE 300
    PPPEHIPPPP RPPKRILEPH NGKCREFFPN HQWVKEETQE DKDCPIKEEK 350
    GSPLNAAPYG IESMSQDTEV RSRVVGGSLR GAQAASPAKG EPSLPEKDED 400
    HALSYWKPFL VNMCVATVLT AGAYLCYRFL FNSNT 435
    Length:435
    Mass (Da):49,967
    Last modified:November 1, 1990 - v1
    Checksum:i802377DCD33F41FD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti381 – 3811G → S.
    Corresponds to variant rs16995304 [ dbSNP | Ensembl ].
    VAR_022013
    Natural varianti387 – 3871P → L Associated with low glucose tolerance.
    Corresponds to variant rs16995309 [ dbSNP | Ensembl ].
    VAR_022014

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31724 mRNA. Translation: AAA60223.1.
    M33689 mRNA. Translation: AAA60157.1.
    M33684
    , M33688, M33687, M33686, M33685 Genomic DNA. Translation: AAA60158.1.
    BT006752 mRNA. Translation: AAP35398.1.
    AL133230, AL034429 Genomic DNA. Translation: CAC00618.2.
    AL034429, AL133230 Genomic DNA. Translation: CAI23215.1.
    BC015660 mRNA. Translation: AAH15660.1.
    BC018164 mRNA. Translation: AAH18164.1.
    CCDSiCCDS13430.1.
    PIRiA35992. TPHUN1.
    RefSeqiNP_001265547.1. NM_001278618.1.
    NP_002818.1. NM_002827.3.
    UniGeneiHs.417549.

    Genome annotation databases

    EnsembliENST00000371621; ENSP00000360683; ENSG00000196396.
    GeneIDi5770.
    KEGGihsa:5770.
    UCSCiuc002xvl.3. human.

    Polymorphism databases

    DMDMi131467.

    Keywords - Coding sequence diversityi

    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
    M31724 mRNA. Translation: AAA60223.1 .
    M33689 mRNA. Translation: AAA60157.1 .
    M33684
    , M33688 , M33687 , M33686 , M33685 Genomic DNA. Translation: AAA60158.1 .
    BT006752 mRNA. Translation: AAP35398.1 .
    AL133230 , AL034429 Genomic DNA. Translation: CAC00618.2 .
    AL034429 , AL133230 Genomic DNA. Translation: CAI23215.1 .
    BC015660 mRNA. Translation: AAH15660.1 .
    BC018164 mRNA. Translation: AAH18164.1 .
    CCDSi CCDS13430.1.
    PIRi A35992. TPHUN1.
    RefSeqi NP_001265547.1. NM_001278618.1.
    NP_002818.1. NM_002827.3.
    UniGenei Hs.417549.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A5Y X-ray 2.50 A 1-330 [» ]
    1AAX X-ray 1.90 A 1-321 [» ]
    1BZC X-ray 2.35 A 1-321 [» ]
    1BZH X-ray 2.10 A 1-298 [» ]
    1BZJ X-ray 2.25 A 2-298 [» ]
    1C83 X-ray 1.80 A 1-298 [» ]
    1C84 X-ray 2.35 A 1-298 [» ]
    1C85 X-ray 2.72 A 1-298 [» ]
    1C86 X-ray 2.30 A 1-298 [» ]
    1C87 X-ray 2.10 A 1-298 [» ]
    1C88 X-ray 1.80 A 1-298 [» ]
    1ECV X-ray 1.95 A 1-298 [» ]
    1EEN X-ray 1.90 A 1-321 [» ]
    1EEO X-ray 1.80 A 1-321 [» ]
    1G1F X-ray 2.00 A 1-298 [» ]
    1G1G X-ray 2.20 A 1-298 [» ]
    1G1H X-ray 2.40 A 1-298 [» ]
    1G7F X-ray 1.80 A 1-298 [» ]
    1G7G X-ray 2.20 A 1-298 [» ]
    1GFY X-ray 2.13 A 1-298 [» ]
    1I57 X-ray 2.10 A 1-298 [» ]
    1JF7 X-ray 2.20 A/B 1-298 [» ]
    1KAK X-ray 2.50 A 1-298 [» ]
    1KAV X-ray 2.35 A 1-298 [» ]
    1L8G X-ray 2.50 A 1-321 [» ]
    1LQF X-ray 2.50 A/B/C/D 1-283 [» ]
    1NL9 X-ray 2.40 A 1-321 [» ]
    1NNY X-ray 2.40 A 1-321 [» ]
    1NO6 X-ray 2.40 A 1-321 [» ]
    1NWE X-ray 3.10 A 1-298 [» ]
    1NWL X-ray 2.40 A 1-298 [» ]
    1NZ7 X-ray 2.40 A 1-321 [» ]
    1OEM X-ray 1.80 X 1-321 [» ]
    1OEO X-ray 2.15 X 1-321 [» ]
    1OES X-ray 2.20 A 1-321 [» ]
    1OET X-ray 2.30 A 1-321 [» ]
    1OEU X-ray 2.50 A 1-321 [» ]
    1OEV X-ray 2.20 A 1-321 [» ]
    1ONY X-ray 2.15 A 1-321 [» ]
    1ONZ X-ray 2.40 A 1-321 [» ]
    1PA1 X-ray 1.60 A 1-298 [» ]
    1PH0 X-ray 2.20 A 1-321 [» ]
    1PTT X-ray 2.90 A 1-321 [» ]
    1PTU X-ray 2.60 A 1-321 [» ]
    1PTV X-ray 2.30 A 1-321 [» ]
    1PTY X-ray 1.85 A 1-321 [» ]
    1PXH X-ray 2.15 A 1-321 [» ]
    1PYN X-ray 2.20 A 1-321 [» ]
    1Q1M X-ray 2.60 A 1-321 [» ]
    1Q6J X-ray 2.20 A 1-298 [» ]
    1Q6M X-ray 2.20 A 1-298 [» ]
    1Q6N X-ray 2.10 A/B 1-298 [» ]
    1Q6P X-ray 2.30 A/B 1-298 [» ]
    1Q6S X-ray 2.20 A/B 1-298 [» ]
    1Q6T X-ray 2.30 A/B 1-298 [» ]
    1QXK X-ray 2.30 A 1-321 [» ]
    1SUG X-ray 1.95 A 1-321 [» ]
    1T48 X-ray 2.20 A 1-298 [» ]
    1T49 X-ray 1.90 A 1-298 [» ]
    1T4J X-ray 2.70 A 1-298 [» ]
    1WAX X-ray 2.20 A 1-321 [» ]
    1XBO X-ray 2.50 A 1-321 [» ]
    2AZR X-ray 2.00 A 1-299 [» ]
    2B07 X-ray 2.10 A 1-299 [» ]
    2B4S X-ray 2.30 A/C 1-298 [» ]
    2BGD X-ray 2.40 A 1-321 [» ]
    2BGE X-ray 1.80 A 1-321 [» ]
    2CM2 X-ray 1.50 A 2-298 [» ]
    2CM3 X-ray 2.10 A/B 1-298 [» ]
    2CM7 X-ray 2.10 A 1-321 [» ]
    2CM8 X-ray 2.10 A 1-321 [» ]
    2CMA X-ray 2.30 A 1-321 [» ]
    2CMB X-ray 1.70 A 1-298 [» ]
    2CMC X-ray 2.20 A 1-298 [» ]
    2CNE X-ray 1.80 A 1-298 [» ]
    2CNF X-ray 2.20 A 1-321 [» ]
    2CNG X-ray 1.90 A 1-321 [» ]
    2CNH X-ray 1.80 A 1-321 [» ]
    2CNI X-ray 2.00 A 1-321 [» ]
    2F6F X-ray 2.00 A 1-298 [» ]
    2F6T X-ray 1.70 A 1-298 [» ]
    2F6V X-ray 1.70 A 1-298 [» ]
    2F6W X-ray 2.20 A 1-298 [» ]
    2F6Y X-ray 2.15 A 1-298 [» ]
    2F6Z X-ray 1.70 A 1-298 [» ]
    2F70 X-ray 2.12 A 1-298 [» ]
    2F71 X-ray 1.55 A 1-298 [» ]
    2FJM X-ray 2.10 A/B 1-298 [» ]
    2FJN X-ray 2.20 A/B 1-298 [» ]
    2H4G X-ray 2.50 A 1-299 [» ]
    2H4K X-ray 2.30 A 1-299 [» ]
    2HB1 X-ray 2.00 A 1-299 [» ]
    2HNP X-ray 2.85 A 1-321 [» ]
    2HNQ X-ray 2.85 A 1-321 [» ]
    2NT7 X-ray 2.10 A 1-299 [» ]
    2NTA X-ray 2.10 A 1-299 [» ]
    2QBP X-ray 2.50 A 1-299 [» ]
    2QBQ X-ray 2.10 A 1-299 [» ]
    2QBR X-ray 2.30 A 1-299 [» ]
    2QBS X-ray 2.10 A 1-299 [» ]
    2VEU X-ray 2.40 A 1-321 [» ]
    2VEV X-ray 1.80 A 1-321 [» ]
    2VEW X-ray 2.00 A 1-321 [» ]
    2VEX X-ray 2.20 A 1-321 [» ]
    2VEY X-ray 2.20 A 1-321 [» ]
    2ZMM X-ray 2.10 A 1-299 [» ]
    2ZN7 X-ray 2.10 A 1-299 [» ]
    3A5J X-ray 1.70 A 2-321 [» ]
    3A5K X-ray 1.85 A 2-298 [» ]
    3CWE X-ray 1.60 A 1-283 [» ]
    3D9C X-ray 2.30 A 1-321 [» ]
    3EAX X-ray 1.90 A 1-321 [» ]
    3EB1 X-ray 2.40 A 1-321 [» ]
    3EU0 X-ray 2.70 A 1-282 [» ]
    3I7Z X-ray 2.30 A 1-321 [» ]
    3I80 X-ray 2.25 A 1-321 [» ]
    3QKP X-ray 2.05 A 1-321 [» ]
    3QKQ X-ray 2.20 A 1-321 [» ]
    3SME X-ray 1.70 A 1-298 [» ]
    3ZMP X-ray 2.62 A/B 1-321 [» ]
    3ZMQ X-ray 3.30 A 1-321 [» ]
    3ZV2 X-ray 2.80 A 1-320 [» ]
    4BJO X-ray 2.06 A/B 2-321 [» ]
    4I8N X-ray 2.50 A 1-320 [» ]
    ProteinModelPortali P18031.
    SMRi P18031. Positions 2-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111736. 37 interactions.
    DIPi DIP-38014N.
    IntActi P18031. 79 interactions.
    MINTi MINT-441655.
    STRINGi 9606.ENSP00000360683.

    Chemistry

    BindingDBi P18031.
    ChEMBLi CHEMBL335.
    DrugBanki DB00720. Clodronate.
    DB01133. Tiludronate.

    PTM databases

    PhosphoSitei P18031.

    Polymorphism databases

    DMDMi 131467.

    2D gel databases

    OGPi P18031.

    Proteomic databases

    MaxQBi P18031.
    PaxDbi P18031.
    PeptideAtlasi P18031.
    PRIDEi P18031.

    Protocols and materials databases

    DNASUi 5770.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371621 ; ENSP00000360683 ; ENSG00000196396 .
    GeneIDi 5770.
    KEGGi hsa:5770.
    UCSCi uc002xvl.3. human.

    Organism-specific databases

    CTDi 5770.
    GeneCardsi GC20P049126.
    H-InvDB HIX0027718.
    HGNCi HGNC:9642. PTPN1.
    HPAi CAB009329.
    CAB015217.
    HPA012542.
    MIMi 176885. gene.
    neXtProti NX_P18031.
    PharmGKBi PA33985.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000273908.
    HOVERGENi HBG008321.
    InParanoidi P18031.
    KOi K05696.
    OMAi MCMATVL.
    OrthoDBi EOG7RV9G4.
    PhylomeDBi P18031.
    TreeFami TF315897.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.
    Reactomei REACT_111133. Growth hormone receptor signaling.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25216. Regulation of IFNA signaling.
    SABIO-RK P18031.
    SignaLinki P18031.

    Miscellaneous databases

    ChiTaRSi PTPN1. human.
    EvolutionaryTracei P18031.
    GeneWikii PTPN1.
    GenomeRNAii 5770.
    NextBioi 22442.
    PMAP-CutDB P18031.
    PROi P18031.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18031.
    Bgeei P18031.
    CleanExi HS_PTPN1.
    Genevestigatori P18031.

    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: Placenta.
    2. "Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B."
      Brown-Shimer S., Johnson K.A., Lawrence J.B., Johnson C., Bruskin A., Green N.R., Hill D.E.
      Proc. Natl. Acad. Sci. U.S.A. 87:5148-5152(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Placenta.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Eye and Lymph.
    6. "Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins."
      Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M., Cool D.E., Krebs E.G., Fischer E.H., Walsh K.A.
      Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-321, ACETYLATION AT MET-1.
      Tissue: Placenta.
    7. "Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation."
      Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.K.
      EMBO J. 12:1937-1946(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-352; SER-378 AND SER-386.
    8. "The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence."
      Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G.
      Cell 68:545-560(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor."
      Liu F., Chernoff J.
      Biochem. J. 327:139-145(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-66.
    10. "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B."
      Moeslein F.M., Myers M.P., Landreth G.E.
      J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-50; SER-242 AND SER-243, MUTAGENESIS OF SER-50.
    11. "Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor."
      Ravichandran L.V., Chen H., Li Y., Quon M.J.
      Mol. Endocrinol. 15:1768-1780(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-50, MUTAGENESIS OF SER-50.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase."
      Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M.
      J. Biol. Chem. 283:34374-34383(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF MET, INTERACTION WITH MET.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: INTERACTION WITH EPHA3, FUNCTION IN EPHA3 DEPHOSPHORYLATION, SUBCELLULAR LOCATION.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "H2s-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response."
      Krishnan N., Fu C., Pappin D.J., Tonks N.K.
      Sci. Signal. 4:RA86-RA86(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SULFHYDRATION AT CYS-215, S-NITROSYLATION AT CYS-215, MUTAGENESIS OF CYS-215, MUTAGENESIS OF ASP-181 AND CYS-215.
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of human protein tyrosine phosphatase 1B."
      Barford D., Flint A.J., Tonks N.K.
      Science 263:1397-1404(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-321.
    21. "Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design."
      Puius Y.A., Zhao Y., Sullivan M., Lawrence D.S., Almo S.C., Zhang Z.Y.
      Proc. Natl. Acad. Sci. U.S.A. 94:13420-13425(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-298 OF MUTANT SER-215.
    22. "Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography."
      Pannifer A.D., Flint A.J., Tonks N.K., Barford D.
      J. Biol. Chem. 273:10454-10462(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-285.
    23. "Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics."
      Groves M.R., Yao Z.-J., Roller P.P., Burke T.R. Jr., Barford D.
      Biochemistry 37:17773-17783(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-298.
    24. "Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate."
      Salmeen A., Andersen J.N., Myers M.P., Meng T.-C., Hinks J.A., Tonks N.K., Barford D.
      Nature 423:769-773(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, CROSS-LINK 215-CYS-SER-216.
    25. "Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B."
      Van Montfort R.L.M., Congreve M., Tisi D., Carr R., Jhoti H.
      Nature 423:773-777(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, CROSS-LINK 215-CYS-SER-216.
    26. "Protein tyrosine phosphatase 1B variant associated with fat distribution and insulin metabolism."
      Ukkola O., Rankinen T., Lakka T., Leon A.S., Skinner J.S., Wilmore J.H., Rao D.C., Kesaeniemi Y.A., Bouchard C.
      Obes. Res. 13:829-834(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF VARIANT LEU-387 WITH LOW GLUCOSE TOLERANCE.

    Entry informationi

    Entry nameiPTN1_HUMAN
    AccessioniPrimary (citable) accession number: P18031
    Secondary accession number(s): Q5TGD8, Q9BQV9, Q9NQQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 185 of the entry and version 1 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 chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3