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P43378

- PTN9_HUMAN

UniProt

P43378 - PTN9_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 9

Gene

PTPN9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei470 – 4701SubstrateBy similarity
    Active sitei515 – 5151Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei559 – 5591SubstrateBy similarity

    GO - Molecular functioni

    1. non-membrane spanning protein tyrosine phosphatase activity Source: ProtInc
    2. protein binding Source: IntAct
    3. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 9 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase MEG2
    Short name:
    PTPase MEG2
    Gene namesi
    Name:PTPN9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9661. PTPN9.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34005.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Tyrosine-protein phosphatase non-receptor type 9PRO_0000094764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP43378.
    PaxDbiP43378.
    PRIDEiP43378.

    PTM databases

    PhosphoSiteiP43378.

    Expressioni

    Gene expression databases

    ArrayExpressiP43378.
    BgeeiP43378.
    CleanExiHS_PTPN9.
    GenevestigatoriP43378.

    Organism-specific databases

    HPAiHPA041922.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GHRP109122EBI-742898,EBI-286316
    NSFP464592EBI-742898,EBI-712251

    Protein-protein interaction databases

    BioGridi111744. 6 interactions.
    IntActiP43378. 7 interactions.
    MINTiMINT-1455219.
    STRINGi9606.ENSP00000303554.

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi288 – 31225
    Helixi320 – 3234
    Turni325 – 3273
    Helixi328 – 3303
    Turni340 – 3423
    Beta strandi343 – 3453
    Beta strandi350 – 3523
    Beta strandi359 – 3657
    Beta strandi368 – 3758
    Helixi380 – 3823
    Helixi383 – 39210
    Beta strandi397 – 4004
    Beta strandi404 – 4063
    Beta strandi423 – 4264
    Beta strandi429 – 43810
    Beta strandi440 – 45112
    Turni452 – 4554
    Beta strandi456 – 46510
    Beta strandi470 – 4723
    Helixi478 – 49720
    Beta strandi511 – 5144
    Beta strandi516 – 5194
    Helixi520 – 53819
    Beta strandi539 – 5413
    Helixi543 – 5508
    Turni551 – 5533
    Helixi561 – 57717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PA5X-ray1.60A/B277-582[»]
    4GE2X-ray1.80A/B277-582[»]
    4GE5X-ray2.00A/B277-582[»]
    4GE6X-ray1.40A/B277-582[»]
    4ICZX-ray1.90A277-582[»]
    ProteinModelPortaliP43378.
    SMRiP43378. Positions 48-237, 277-583.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43378.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 243160CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST
    Domaini303 – 574272Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni515 – 5217Substrate bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000006971.
    HOVERGENiHBG006880.
    InParanoidiP43378.
    KOiK18038.
    OMAiMTTRFEE.
    OrthoDBiEOG79GT5R.
    PhylomeDBiP43378.
    TreeFamiTF351975.

    Family and domain databases

    Gene3Di3.40.525.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM01100. CRAL_TRIO_N. 1 hit.
    SM00194. PTPc. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view]
    SUPFAMiSSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P43378-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF    50
    LMARKFDVLR AIELFHSYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN 100
    VRDPTGASIA LFTARLHHPH KSVQHVVLQA LFYLLDRAVD SFETQRNGLV 150
    FIYDMCGSNY ANFELDLGKK VLNLLKGAFP ARLKKVLIVG APIWFRVPYS 200
    IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK IDLATWNFQF 250
    LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNARQK 300
    QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS 350
    GHTQTDYINA SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM 400
    TTRFEEGGRR KCGQYWPLEK DSRIRFGFLT VTNLGVENMN HYKKTTLEIH 450
    NTEERQKRQV THFQFLSWPD YGVPSSAASL IDFLRVVRNQ QSLAVSNMGA 500
    RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT LNVFQTVSRM 550
    RTQRAFSIQT PEQYYFCYKA ILEFAEKEGM VSSGQNLLAV ESQ 593
    Length:593
    Mass (Da):68,020
    Last modified:November 1, 1995 - v1
    Checksum:i9BD75A5A986DDA0B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83738 mRNA. Translation: AAA60226.1.
    BT007405 mRNA. Translation: AAP36073.1.
    BC010863 mRNA. Translation: AAH10863.1.
    CCDSiCCDS10280.1.
    PIRiA42690.
    RefSeqiNP_002824.1. NM_002833.3.
    UniGeneiHs.445775.

    Genome annotation databases

    EnsembliENST00000306726; ENSP00000303554; ENSG00000169410.
    GeneIDi5780.
    KEGGihsa:5780.
    UCSCiuc002bal.3. human.

    Polymorphism databases

    DMDMi1172724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83738 mRNA. Translation: AAA60226.1 .
    BT007405 mRNA. Translation: AAP36073.1 .
    BC010863 mRNA. Translation: AAH10863.1 .
    CCDSi CCDS10280.1.
    PIRi A42690.
    RefSeqi NP_002824.1. NM_002833.3.
    UniGenei Hs.445775.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PA5 X-ray 1.60 A/B 277-582 [» ]
    4GE2 X-ray 1.80 A/B 277-582 [» ]
    4GE5 X-ray 2.00 A/B 277-582 [» ]
    4GE6 X-ray 1.40 A/B 277-582 [» ]
    4ICZ X-ray 1.90 A 277-582 [» ]
    ProteinModelPortali P43378.
    SMRi P43378. Positions 48-237, 277-583.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111744. 6 interactions.
    IntActi P43378. 7 interactions.
    MINTi MINT-1455219.
    STRINGi 9606.ENSP00000303554.

    Chemistry

    BindingDBi P43378.
    ChEMBLi CHEMBL6117.

    PTM databases

    PhosphoSitei P43378.

    Polymorphism databases

    DMDMi 1172724.

    Proteomic databases

    MaxQBi P43378.
    PaxDbi P43378.
    PRIDEi P43378.

    Protocols and materials databases

    DNASUi 5780.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306726 ; ENSP00000303554 ; ENSG00000169410 .
    GeneIDi 5780.
    KEGGi hsa:5780.
    UCSCi uc002bal.3. human.

    Organism-specific databases

    CTDi 5780.
    GeneCardsi GC15M075759.
    HGNCi HGNC:9661. PTPN9.
    HPAi HPA041922.
    MIMi 600768. gene.
    neXtProti NX_P43378.
    PharmGKBi PA34005.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000006971.
    HOVERGENi HBG006880.
    InParanoidi P43378.
    KOi K18038.
    OMAi MTTRFEE.
    OrthoDBi EOG79GT5R.
    PhylomeDBi P43378.
    TreeFami TF351975.

    Miscellaneous databases

    ChiTaRSi PTPN9. human.
    EvolutionaryTracei P43378.
    GeneWikii PTPN9.
    GenomeRNAii 5780.
    NextBioi 22478.
    PROi P43378.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43378.
    Bgeei P43378.
    CleanExi HS_PTPN9.
    Genevestigatori P43378.

    Family and domain databases

    Gene3Di 3.40.525.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM01100. CRAL_TRIO_N. 1 hit.
    SM00194. PTPc. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    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 expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p."
      Gu M., Warshawsky I., Majerus P.W.
      Proc. Natl. Acad. Sci. U.S.A. 89:2980-2984(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "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].
    3. "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: Pancreas.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "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 (1.6 ANGSTROMS) OF 277-582, FUNCTION.

    Entry informationi

    Entry nameiPTN9_HUMAN
    AccessioniPrimary (citable) accession number: P43378
    Secondary accession number(s): Q53XR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 144 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, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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