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P35831

- PTN12_MOUSE

UniProt

P35831 - PTN12_MOUSE

Protein

Tyrosine-protein phosphatase non-receptor type 12

Gene

Ptpn12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei199 – 1991SubstrateBy similarity
    Active sitei231 – 2311Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei278 – 2781SubstrateBy similarity

    GO - Molecular functioni

    1. phosphoprotein phosphatase activity Source: MGI
    2. protein binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein dephosphorylation Source: MGI
    2. tissue regeneration Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 12 (EC:3.1.3.48)
    Alternative name(s):
    MPTP-PEST
    Protein-tyrosine phosphatase P19
    Short name:
    P19-PTP
    Gene namesi
    Name:Ptpn12
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:104673. Ptpn12.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell projectionpodosome 1 Publication

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: UniProtKB-KW
    3. cytosol Source: MGI
    4. plasma membrane Source: Ensembl
    5. podosome Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 775775Tyrosine-protein phosphatase non-receptor type 12PRO_0000094772Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei19 – 191PhosphoserineBy similarity
    Modified residuei331 – 3311Phosphoserine2 Publications
    Modified residuei434 – 4341Phosphoserine1 Publication
    Modified residuei448 – 4481PhosphoserineBy similarity
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei519 – 5191PhosphothreonineBy similarity
    Modified residuei550 – 5501Phosphoserine1 Publication
    Modified residuei567 – 5671PhosphoserineBy similarity
    Modified residuei569 – 5691PhosphothreonineBy similarity
    Modified residuei596 – 5961Phosphoserine1 Publication
    Modified residuei598 – 5981Phosphothreonine1 Publication
    Modified residuei603 – 6031Phosphoserine1 Publication
    Modified residuei606 – 6061Phosphoserine1 Publication
    Modified residuei608 – 6081Phosphoserine1 Publication
    Modified residuei613 – 6131PhosphoserineBy similarity
    Modified residuei673 – 6731PhosphoserineBy similarity
    Modified residuei748 – 7481Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by STK24/MST3 and this results in inhibition of its activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP35831.
    PaxDbiP35831.
    PRIDEiP35831.

    PTM databases

    PhosphoSiteiP35831.

    Expressioni

    Gene expression databases

    ArrayExpressiP35831.
    BgeeiP35831.
    GenevestigatoriP35831.

    Interactioni

    Subunit structurei

    Interacts with PTK2B/PYK2. Interacts with PSTPIP1 and TGFB1I1. Interacts with LPXN.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Pstpip1P978145EBI-2642957,EBI-7484574
    Shc1P980832EBI-2642957,EBI-300201

    Protein-protein interaction databases

    BioGridi202478. 2 interactions.
    IntActiP35831. 5 interactions.
    MINTiMINT-1618529.
    STRINGi10090.ENSMUSP00000030556.

    Structurei

    3D structure databases

    ProteinModelPortaliP35831.
    SMRiP35831. Positions 3-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 293266Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni231 – 2377Substrate bindingBy similarity
    Regioni344 – 43794Interaction with TGFB1I1Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00750000117233.
    HOGENOMiHOG000252955.
    HOVERGENiHBG007666.
    InParanoidiQ80UM4.
    KOiK18024.
    OMAiTWSFHGP.
    OrthoDBiEOG744T8Z.
    TreeFamiTF351977.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR012266. Ptpn_12.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000932. Tyr-Ptase_nr12. 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.

    P35831-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEQVEILRRF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT    50
    ATGEKEENVK KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP 100
    KAYVATQGPL ANTVIDFWRM IWEYNVVIIV MACREFEMGR KKCERYWPLY 150
    GEDPITFAPF KISCENEQAR TDYFIRTLLL EFQNESRRLY QFHYVNWPDH 200
    DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA ICAIDYTWNL 250
    LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL 300
    YEIHGAQKIA DGNEITTGTM VSSIDSEKQD SPPPKPPRTR SCLVEGDAKE 350
    EILQPPEPHP VPPILTPSPP SAFPTVTTVW QDSDRYHPKP VLHMASPEQH 400
    PADLNRSYDK SADPMGKSES AIEHIDKKLE RNLSFEIKKV PLQEGPKSFD 450
    GNTLLNRGHA IKIKSASSSV VDRTSKPQEL SAGALKVDDV SQNSCADCSA 500
    AHSHRAAESS EESQSNSHTP PRPDCLPLDK KGHVTWSLHG PENATPVPDS 550
    PDGKSPDNHS QTLKTVSSTP NSTAEEEAHD LTEHHNSSPL LKAPLSFTNP 600
    LHSDDSDSDG GSSDGAVTRN KTSISTASAT VSPASSAESA CTRRVLPMSI 650
    ARQEVAGTPH SGAEKDADVS EESPPPLPER TPESFVLADM PVRPEWHELP 700
    NQEWSEQRES EGLTTSGNEK HDAGGIHTEA SADSPPAFSD KKDQITKSPA 750
    EVTDIGFGNR CGKPKGPREP PSEWT 775
    Length:775
    Mass (Da):86,526
    Last modified:July 27, 2011 - v3
    Checksum:iED1A7A577CE4352C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1112LA → FR in CAA60477. (PubMed:7772023)Curated
    Sequence conflicti128 – 1281I → M in CAA60477. (PubMed:7772023)Curated
    Sequence conflicti296 – 2961K → N in CAA45037. (PubMed:1590786)Curated
    Sequence conflicti310 – 3101A → R in CAA60477. (PubMed:7772023)Curated
    Sequence conflicti328 – 3325KQDSP → DETS in CAA45037. (PubMed:1590786)Curated
    Sequence conflicti380 – 3801W → V in CAA45037. (PubMed:1590786)Curated
    Sequence conflicti414 – 4152PM → QW in CAA60477. (PubMed:7772023)Curated
    Sequence conflicti606 – 6072SD → WH in CAA60477. (PubMed:7772023)Curated
    Sequence conflicti642 – 6421T → H in CAA60477. (PubMed:7772023)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63440 mRNA. Translation: CAA45037.1. Sequence problems.
    X86781 Genomic DNA. Translation: CAA60477.1.
    AK154107 mRNA. Translation: BAE32381.1.
    CH466586 Genomic DNA. Translation: EDL03216.1.
    BC051980 mRNA. Translation: AAH51980.1.
    CCDSiCCDS19102.1.
    PIRiJH0609.
    S55345.
    RefSeqiNP_035333.2. NM_011203.2.
    UniGeneiMm.319117.

    Genome annotation databases

    EnsembliENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
    GeneIDi19248.
    KEGGimmu:19248.
    UCSCiuc008woh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63440 mRNA. Translation: CAA45037.1 . Sequence problems.
    X86781 Genomic DNA. Translation: CAA60477.1 .
    AK154107 mRNA. Translation: BAE32381.1 .
    CH466586 Genomic DNA. Translation: EDL03216.1 .
    BC051980 mRNA. Translation: AAH51980.1 .
    CCDSi CCDS19102.1.
    PIRi JH0609.
    S55345.
    RefSeqi NP_035333.2. NM_011203.2.
    UniGenei Mm.319117.

    3D structure databases

    ProteinModelPortali P35831.
    SMRi P35831. Positions 3-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202478. 2 interactions.
    IntActi P35831. 5 interactions.
    MINTi MINT-1618529.
    STRINGi 10090.ENSMUSP00000030556.

    PTM databases

    PhosphoSitei P35831.

    Proteomic databases

    MaxQBi P35831.
    PaxDbi P35831.
    PRIDEi P35831.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030556 ; ENSMUSP00000030556 ; ENSMUSG00000028771 .
    GeneIDi 19248.
    KEGGi mmu:19248.
    UCSCi uc008woh.1. mouse.

    Organism-specific databases

    CTDi 5782.
    MGIi MGI:104673. Ptpn12.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00750000117233.
    HOGENOMi HOG000252955.
    HOVERGENi HBG007666.
    InParanoidi Q80UM4.
    KOi K18024.
    OMAi TWSFHGP.
    OrthoDBi EOG744T8Z.
    TreeFami TF351977.

    Miscellaneous databases

    ChiTaRSi PTPN12. mouse.
    NextBioi 296078.
    PROi P35831.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35831.
    Bgeei P35831.
    Genevestigatori P35831.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR012266. Ptpn_12.
    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 PIRSF000932. Tyr-Ptase_nr12. 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. "Differential expression of a novel murine non-receptor protein tyrosine phosphatase during differentiation of P19 embryonal carcinoma cells."
      den Hertog J., Pals C.E., Jonk L.J., Kruijer W.
      Biochem. Biophys. Res. Commun. 184:1241-1249(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase."
      Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M., Adachi M., Imai K., Yachi A.
      Biochem. Biophys. Res. Commun. 189:1223-1230(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 297-416.
    3. "Murine protein tyrosine phosphatase-PEST, a stable cytosolic protein tyrosine phosphatase."
      Charest A., Wagner J., Shen S.H., Tremblay M.L.
      Biochem. J. 308:425-432(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
    7. "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain."
      Nishiya N., Iwabuchi Y., Shibanuma M., Cote J.-F., Tremblay M.L., Nose K.
      J. Biol. Chem. 274:9847-9853(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    8. "PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding PTP-PEST toward a specific dephosphorylation of WASP."
      Cote J.-F., Chung P.L., Theberge J.-F., Halle M., Spencer S., Lasky L.A., Tremblay M.L.
      J. Biol. Chem. 277:2973-2986(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSTPIP1.
    9. "Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast."
      Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A.
      J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LPXN AND PTK2B/PYK2.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    11. "Leupaxin binds to PEST domain tyrosine phosphatase PEP."
      Watanabe N., Amano N., Ishizuka H., Mashima K.
      Mol. Cell. Biochem. 269:13-17(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPXN.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-596; THR-598; SER-603; SER-606 AND SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPTN12_MOUSE
    AccessioniPrimary (citable) accession number: P35831
    Secondary accession number(s): Q80UM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3