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Q9Y2R2

- PTN22_HUMAN

UniProt

Q9Y2R2 - PTN22_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 22

Gene

PTPN22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
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    Functioni

    Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-493' residue. Dephosphorylates the immune system activator SKAP2.4 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Down-regulated by phosphorylation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei195 – 1951SubstrateBy similarity
    Active sitei227 – 2271Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei274 – 2741Substrate1 Publication

    GO - Molecular functioni

    1. kinase binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. protein tyrosine phosphatase activity Source: UniProtKB
    4. SH3 domain binding Source: BHF-UCL

    GO - Biological processi

    1. negative regulation of T cell activation Source: BHF-UCL
    2. negative regulation of T cell receptor signaling pathway Source: UniProtKB
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. phosphoanandamide dephosphorylation Source: BHF-UCL
    5. protein dephosphorylation Source: BHF-UCL
    6. regulation of B cell receptor signaling pathway Source: BHF-UCL
    7. regulation of innate immune response Source: BHF-UCL
    8. regulation of natural killer cell proliferation Source: BHF-UCL
    9. T cell differentiation Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    SignaLinkiQ9Y2R2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 22 (EC:3.1.3.48)
    Alternative name(s):
    Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP
    Lymphoid phosphatase
    Short name:
    LyP
    PEST-domain phosphatase
    Short name:
    PEP
    Gene namesi
    Name:PTPN22
    Synonyms:PTPN8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9652. PTPN22.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic side of plasma membrane Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi35 – 351S → E: Loss of phosphorylation by PKC/PRKCD. 1 Publication
    Mutagenesisi36 – 361T → E: No effect on phosphorylation by PKC/PRKCD. 1 Publication
    Mutagenesisi129 – 1291C → S: Decreases activity 2 fold. 1 Publication
    Mutagenesisi231 – 2311C → S: Decreases activity 7 fold. 1 Publication

    Keywords - Diseasei

    Systemic lupus erythematosus

    Organism-specific databases

    MIMi152700. phenotype.
    Orphaneti397. Giant cell arteritis.
    900. Granulomatosis with polyangiitis.
    85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    93552. Pediatric systemic lupus erythematosus.
    536. Systemic lupus erythematosus.
    PharmGKBiPA33995.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 807807Tyrosine-protein phosphatase non-receptor type 22PRO_0000094775Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351Phosphoserine; by PKC/PRKCD1 Publication
    Disulfide bondi129 ↔ 2271 Publication
    Modified residuei635 – 6351PhosphoserineBy similarity
    Modified residuei684 – 6841PhosphoserineBy similarity
    Modified residuei692 – 6921PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability to dephosphorylate and inactivate the SRC family kinases.1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2R2.
    PaxDbiQ9Y2R2.
    PRIDEiQ9Y2R2.

    PTM databases

    PhosphoSiteiQ9Y2R2.

    Expressioni

    Tissue specificityi

    Both isoform 1 and 4 are predominantly expressed in lymphoid tissues and cells. Isoform 1 is expressed in thymocytes and both mature B and T-cells.

    Gene expression databases

    ArrayExpressiQ9Y2R2.
    BgeeiQ9Y2R2.
    CleanExiHS_PTPN22.
    GenevestigatoriQ9Y2R2.

    Organism-specific databases

    HPAiCAB012209.
    HPA004912.
    HPA013350.

    Interactioni

    Subunit structurei

    Interacts with CSK. Interacts with LPXN By similarity. Interacts with CBL.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CD247P209634EBI-1211241,EBI-1165705
    GRB2P629932EBI-1211241,EBI-401755
    LCKP062395EBI-1211241,EBI-1348
    ZAP70P434034EBI-1211241,EBI-1211276

    Protein-protein interaction databases

    BioGridi117604. 12 interactions.
    DIPiDIP-29953N.
    IntActiQ9Y2R2. 16 interactions.
    STRINGi9606.ENSP00000352833.

    Structurei

    Secondary structure

    1
    807
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi21 – 4020
    Helixi47 – 504
    Helixi52 – 554
    Beta strandi59 – 624
    Helixi67 – 693
    Beta strandi70 – 723
    Turni80 – 834
    Beta strandi86 – 927
    Beta strandi95 – 1028
    Helixi107 – 1093
    Helixi110 – 11910
    Beta strandi124 – 1274
    Beta strandi131 – 1333
    Beta strandi135 – 1373
    Beta strandi146 – 1483
    Beta strandi151 – 1533
    Beta strandi156 – 16510
    Beta strandi167 – 17812
    Beta strandi181 – 19010
    Beta strandi195 – 1973
    Helixi199 – 2024
    Helixi203 – 21513
    Beta strandi218 – 2214
    Beta strandi223 – 2264
    Beta strandi228 – 2325
    Helixi233 – 24816
    Helixi258 – 2669
    Helixi276 – 30126

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P6XX-ray1.90A/B1-302[»]
    2QCJX-ray3.00A/B1-294[»]
    2QCTX-ray2.80A/B1-294[»]
    3BRHX-ray2.20A/B1-310[»]
    3H2XX-ray2.20A1-302[»]
    3OLRX-ray2.50A/B/C/D1-294[»]
    3OMHX-ray2.90A/B/C/D1-294[»]
    4J51X-ray2.30A/B1-303[»]
    ProteinModelPortaliQ9Y2R2.
    SMRiQ9Y2R2. Positions 1-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2R2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 289266Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni227 – 2337Substrate binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    HOVERGENiHBG103877.
    InParanoidiQ9Y2R2.
    KOiK18024.
    OrthoDBiEOG744T8Z.
    PhylomeDBiQ9Y2R2.
    TreeFamiTF351977.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR016276. Non-rcpt_Tyr_Pase_8/22.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000930. PTPN8_PTPN22. 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]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2R2-1) [UniParc]FASTAAdd to Basket

    Also known as: LyP1

    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

    MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE    50
    KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI 100
    ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ 150
    LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS 200
    SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG 250
    IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK 300
    HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE 350
    SSSFDFRTSE ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK 400
    AFPIVGEPLQ KHQSLDLGSL LFEGCSNSKP VNAAGRYFNS KVPITRTKST 450
    PFELIQQRET KEVDSKENFS YLESQPHDSC FVEMQAQKVM HVSSAELNYS 500
    LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW PPSGTSSKMS 550
    LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES 600
    AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKVKI 650
    GTSLEWGGTS EPKKFDDSVI LRPSKSVKLR SPKSELHQDR SSPPPPLPER 700
    TLESFFLADE DCMQAQSIET YSTSYPDTME NSTSSKQTLK TPGKSFTRSK 750
    SLKILRNMKK SICNSCPPNK PAESVQSNNS SSFLNFGFAN RFSKPKGPRN 800
    PPPTWNI 807
    Length:807
    Mass (Da):91,705
    Last modified:March 27, 2002 - v2
    Checksum:i1ABE8AE89C9D9FBF
    GO
    Isoform 2 (identifier: Q9Y2R2-2) [UniParc]FASTAAdd to Basket

    Also known as: LyP2

    The sequence of this isoform differs from the canonical sequence as follows:
         685-807: ELHQDRSSPP...PRNPPPTWNI → GKNFSWL

    Note: Due to intron retention.

    Show »
    Length:691
    Mass (Da):78,769
    Checksum:iA85EF69FDFDE9D58
    GO
    Isoform 3 (identifier: Q9Y2R2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         251-305: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:752
    Mass (Da):85,138
    Checksum:i826CAD31B7C20983
    GO
    Isoform 4 (identifier: Q9Y2R2-4) [UniParc]FASTAAdd to Basket

    Also known as: LYP3

    The sequence of this isoform differs from the canonical sequence as follows:
         647-674: Missing.

    Show »
    Length:779
    Mass (Da):88,647
    Checksum:iAEA60DFC0BB05C11
    GO
    Isoform 5 (identifier: Q9Y2R2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         137-160: Missing.
         181-203: ETRTIYQFHYKNWPDHDVPSSID → VSVILAHQTSLQNLFSQITPAHF
         204-807: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:179
    Mass (Da):20,932
    Checksum:iE5F9FFCC426C6E2C
    GO
    Isoform 6 (identifier: Q9Y2R2-6) [UniParc]FASTAAdd to Basket

    Also known as: PTPN22.6

    The sequence of this isoform differs from the canonical sequence as follows:
         124-250: Missing.
         788-807: FANRFSKPKGPRNPPPTWNI → MCVILLKS

    Note: Lacks most of the phosphatase domain and functions as a dominant negative isoform of the full length PTPN22.

    Show »
    Length:668
    Mass (Da):75,488
    Checksum:i93025ACF91033DAA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 522KP → NA in AAD00904. (PubMed:10068674)Curated
    Sequence conflicti51 – 522KP → NA in AAD00905. (PubMed:10068674)Curated
    Sequence conflicti126 – 1261V → G in AAD27764. (PubMed:21044313)Curated
    Sequence conflicti147 – 1471G → V in AAD27764. (PubMed:21044313)Curated
    Sequence conflicti240 – 2401I → IV in AAD00905. (PubMed:10068674)Curated
    Sequence conflicti372 – 3721A → V in AK310570. (PubMed:14702039)Curated
    Sequence conflicti420 – 4201L → P in AAD27764. (PubMed:21044313)Curated
    Sequence conflicti742 – 7421P → S in AAD27764. (PubMed:21044313)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti620 – 6201R → W Confers susceptibility to systemic lupus erythematosus and type 1 diabetes mellitus; affects CSK kinase binding. 6 Publications
    Corresponds to variant rs2476601 [ dbSNP | Ensembl ].
    VAR_022605

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei124 – 250127Missing in isoform 6. 1 PublicationVSP_044428Add
    BLAST
    Alternative sequencei137 – 16024Missing in isoform 5. 1 PublicationVSP_039725Add
    BLAST
    Alternative sequencei181 – 20323ETRTI…PSSID → VSVILAHQTSLQNLFSQITP AHF in isoform 5. 1 PublicationVSP_039726Add
    BLAST
    Alternative sequencei204 – 807604Missing in isoform 5. 1 PublicationVSP_039727Add
    BLAST
    Alternative sequencei251 – 30555Missing in isoform 3. 1 PublicationVSP_039728Add
    BLAST
    Alternative sequencei647 – 67428Missing in isoform 4. 1 PublicationVSP_039729Add
    BLAST
    Alternative sequencei685 – 807123ELHQD…PTWNI → GKNFSWL in isoform 2. 1 PublicationVSP_005134Add
    BLAST
    Alternative sequencei788 – 80720FANRF…PTWNI → MCVILLKS in isoform 6. 1 PublicationVSP_044429Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001846 mRNA. Translation: AAD00904.1.
    AF001847 mRNA. Translation: AAD00905.1.
    GU479452 mRNA. Translation: ADD59979.1.
    AF077031 mRNA. Translation: AAD27764.1.
    AK310570 mRNA. No translation available.
    EF064714 Genomic DNA. Translation: ABK41897.1.
    AL137856 Genomic DNA. Translation: CAI19068.1.
    CH471122 Genomic DNA. Translation: EAW56575.1.
    CH471122 Genomic DNA. Translation: EAW56576.1.
    BC017785 mRNA. Translation: AAH17785.1.
    BC071670 mRNA. Translation: AAH71670.1.
    CCDSiCCDS863.1. [Q9Y2R2-1]
    CCDS864.2. [Q9Y2R2-3]
    RefSeqiNP_001180360.1. NM_001193431.1. [Q9Y2R2-4]
    NP_036543.4. NM_012411.4. [Q9Y2R2-3]
    NP_057051.3. NM_015967.5. [Q9Y2R2-1]
    UniGeneiHs.535276.

    Genome annotation databases

    EnsembliENST00000460620; ENSP00000433141; ENSG00000134242. [Q9Y2R2-5]
    GeneIDi26191.
    KEGGihsa:26191.
    UCSCiuc001eds.3. human. [Q9Y2R2-1]
    uc001edt.3. human. [Q9Y2R2-5]
    uc009wgq.3. human. [Q9Y2R2-3]
    uc009wgs.2. human. [Q9Y2R2-6]
    uc021orx.1. human. [Q9Y2R2-4]

    Polymorphism databases

    DMDMi20139861.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001846 mRNA. Translation: AAD00904.1 .
    AF001847 mRNA. Translation: AAD00905.1 .
    GU479452 mRNA. Translation: ADD59979.1 .
    AF077031 mRNA. Translation: AAD27764.1 .
    AK310570 mRNA. No translation available.
    EF064714 Genomic DNA. Translation: ABK41897.1 .
    AL137856 Genomic DNA. Translation: CAI19068.1 .
    CH471122 Genomic DNA. Translation: EAW56575.1 .
    CH471122 Genomic DNA. Translation: EAW56576.1 .
    BC017785 mRNA. Translation: AAH17785.1 .
    BC071670 mRNA. Translation: AAH71670.1 .
    CCDSi CCDS863.1. [Q9Y2R2-1 ]
    CCDS864.2. [Q9Y2R2-3 ]
    RefSeqi NP_001180360.1. NM_001193431.1. [Q9Y2R2-4 ]
    NP_036543.4. NM_012411.4. [Q9Y2R2-3 ]
    NP_057051.3. NM_015967.5. [Q9Y2R2-1 ]
    UniGenei Hs.535276.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P6X X-ray 1.90 A/B 1-302 [» ]
    2QCJ X-ray 3.00 A/B 1-294 [» ]
    2QCT X-ray 2.80 A/B 1-294 [» ]
    3BRH X-ray 2.20 A/B 1-310 [» ]
    3H2X X-ray 2.20 A 1-302 [» ]
    3OLR X-ray 2.50 A/B/C/D 1-294 [» ]
    3OMH X-ray 2.90 A/B/C/D 1-294 [» ]
    4J51 X-ray 2.30 A/B 1-303 [» ]
    ProteinModelPortali Q9Y2R2.
    SMRi Q9Y2R2. Positions 1-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117604. 12 interactions.
    DIPi DIP-29953N.
    IntActi Q9Y2R2. 16 interactions.
    STRINGi 9606.ENSP00000352833.

    Chemistry

    BindingDBi Q9Y2R2.
    ChEMBLi CHEMBL2889.

    PTM databases

    PhosphoSitei Q9Y2R2.

    Polymorphism databases

    DMDMi 20139861.

    Proteomic databases

    MaxQBi Q9Y2R2.
    PaxDbi Q9Y2R2.
    PRIDEi Q9Y2R2.

    Protocols and materials databases

    DNASUi 26191.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000460620 ; ENSP00000433141 ; ENSG00000134242 . [Q9Y2R2-5 ]
    GeneIDi 26191.
    KEGGi hsa:26191.
    UCSCi uc001eds.3. human. [Q9Y2R2-1 ]
    uc001edt.3. human. [Q9Y2R2-5 ]
    uc009wgq.3. human. [Q9Y2R2-3 ]
    uc009wgs.2. human. [Q9Y2R2-6 ]
    uc021orx.1. human. [Q9Y2R2-4 ]

    Organism-specific databases

    CTDi 26191.
    GeneCardsi GC01M114356.
    HGNCi HGNC:9652. PTPN22.
    HPAi CAB012209.
    HPA004912.
    HPA013350.
    MIMi 152700. phenotype.
    600716. gene.
    neXtProti NX_Q9Y2R2.
    Orphaneti 397. Giant cell arteritis.
    900. Granulomatosis with polyangiitis.
    85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    93552. Pediatric systemic lupus erythematosus.
    536. Systemic lupus erythematosus.
    PharmGKBi PA33995.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOVERGENi HBG103877.
    InParanoidi Q9Y2R2.
    KOi K18024.
    OrthoDBi EOG744T8Z.
    PhylomeDBi Q9Y2R2.
    TreeFami TF351977.

    Enzyme and pathway databases

    SignaLinki Q9Y2R2.

    Miscellaneous databases

    EvolutionaryTracei Q9Y2R2.
    GeneWikii PTPN22.
    GenomeRNAii 26191.
    NextBioi 35503189.
    PROi Q9Y2R2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2R2.
    Bgeei Q9Y2R2.
    CleanExi HS_PTPN22.
    Genevestigatori Q9Y2R2.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR016276. Non-rcpt_Tyr_Pase_8/22.
    IPR029021. Prot-tyrosine_phosphatase-like.
    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 PIRSF000930. PTPN8_PTPN22. 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. "Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp."
      Cohen S., Dadi H., Shaoul E., Sharfe N., Roifman C.M.
      Blood 93:2013-2024(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CBL.
    2. "Identification of a variant form of tyrosine phosphatase LYP."
      Wang S., Dong H., Han J., Ho W.T., Fu X., Zhao Z.J.
      BMC Mol. Biol. 11:78-78(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT TRP-620.
    3. "Human protein tyrosine phosphatase (70zpep) homolog."
      Liu T., Zhang J., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TRP-620.
    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 6).
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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], VARIANT TRP-620.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-620.
    8. "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] (ISOFORMS 3 AND 5).
      Tissue: Lymph.
    9. Cited for: FUNCTION.
    10. "Protein tyrosine phosphatase PTPN22 in human autoimmunity."
      Vang T., Miletic A.V., Bottini N., Mustelin T.
      Autoimmunity 40:453-461(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    11. "PTPN22.6, a dominant negative isoform of PTPN22 and potential biomarker of rheumatoid arthritis."
      Chang H.H., Tai T.S., Lu B., Iannaccone C., Cernadas M., Weinblatt M., Shadick N., Miaw S.C., Ho I.C.
      PLoS ONE 7:E33067-E33067(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 6).
    12. "Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases."
      Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A., Zhang Z.Y.
      Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-35 AND THR-36.
    13. "Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: insights into redox regulation."
      Tsai S.J., Sen U., Zhao L., Greenleaf W.B., Dasgupta J., Fiorillo E., Orru V., Bottini N., Chen X.S.
      Biochemistry 48:4838-4845(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-302, DISULFIDE BOND, MUTAGENESIS OF CYS-129 AND CYS-231.
    14. "Large-scale structural analysis of the classical human protein tyrosine phosphatome."
      Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
      Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-302, FUNCTION.
    15. "Lyp/PTPN22 phosphatase domain: substrate recognition and specificity for Src family kinases."
      Seidel R.D., Love J., Piserchio A., Cowburn D.
      Submitted (DEC-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-310 IN COMPLEX WITH SUBSTRATE.
    16. "Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
      Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
      J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-294 OF MUTANT SER-227 ALONE AND IN COMPLEX WITH SKAP2 PEPTIDE, SUBSTRATE SPECIFICITY, FUNCTION.
    17. Cited for: VARIANT TRP-620, INVOLVEMENT IN SLE.
    18. Cited for: VARIANT TRP-620, CHARACTERIZATION OF VARIANT TRP-620.

    Entry informationi

    Entry nameiPTN22_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2R2
    Secondary accession number(s): A0N0K6
    , B1ALC8, D4NZ71, E9PLD8, E9PPI1, O95063, O95064, Q6IPX8, Q8WVM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: March 27, 2002
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 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. 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