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Q05209

- PTN12_HUMAN

UniProt

Q05209 - PTN12_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 12

Gene

PTPN12

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 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.1 Publication

    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. non-membrane spanning protein tyrosine phosphatase activity Source: ProtInc
    2. protein binding Source: UniProtKB
    3. SH3 domain binding 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 12 (EC:3.1.3.48)
    Alternative name(s):
    PTP-PEST
    Protein-tyrosine phosphatase G1
    Short name:
    PTPG1
    Gene namesi
    Name:PTPN12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9645. PTPN12.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: UniProtKB-KW
    3. cytoplasm Source: HPA
    4. cytosol Source: Ensembl
    5. plasma membrane Source: HPA
    6. podosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm

    Pathology & Biotechi

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    PharmGKBiPA33987.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 780780Tyrosine-protein phosphatase non-receptor type 12PRO_0000094771Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei19 – 191Phosphoserine2 Publications
    Modified residuei332 – 3321Phosphoserine3 Publications
    Modified residuei435 – 4351Phosphoserine3 Publications
    Modified residuei449 – 4491Phosphoserine3 Publications
    Modified residuei468 – 4681Phosphoserine2 Publications
    Modified residuei519 – 5191Phosphothreonine2 Publications
    Modified residuei567 – 5671Phosphoserine2 Publications
    Modified residuei569 – 5691Phosphothreonine2 Publications
    Modified residuei571 – 5711Phosphoserine2 Publications
    Modified residuei596 – 5961PhosphoserineBy similarity
    Modified residuei598 – 5981PhosphothreonineBy similarity
    Modified residuei603 – 6031Phosphoserine4 Publications
    Modified residuei606 – 6061Phosphoserine3 Publications
    Modified residuei608 – 6081Phosphoserine2 Publications
    Modified residuei613 – 6131Phosphoserine2 Publications
    Modified residuei673 – 6731Phosphoserine5 Publications
    Modified residuei689 – 6891Phosphoserine3 Publications
    Modified residuei693 – 6931Phosphothreonine3 Publications

    Post-translational modificationi

    Phosphorylated by STK24/MST3 and this results in inhibition of its activity.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ05209.
    PaxDbiQ05209.
    PRIDEiQ05209.

    PTM databases

    PhosphoSiteiQ05209.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05209.
    BgeeiQ05209.
    CleanExiHS_PTPN12.
    GenevestigatoriQ05209.

    Organism-specific databases

    HPAiHPA007097.

    Interactioni

    Subunit structurei

    Interacts with TGFB1I1 By similarity. Interacts with PSTPIP1. Interacts with PTK2B/PYK2. Interacts with LPXN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAR1P569454EBI-2266035,EBI-702093
    ERBB2P046264EBI-2266035,EBI-641062
    PDGFRBP096193EBI-2266035,EBI-641237
    TEKQ027632EBI-2266035,EBI-2257090

    Protein-protein interaction databases

    BioGridi111746. 41 interactions.
    IntActiQ05209. 37 interactions.
    MINTiMINT-243699.
    STRINGi9606.ENSP00000248594.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05209.
    SMRiQ05209. 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
    Regioni345 – 43894Interaction with TGFB1I1By similarityAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000252955.
    HOVERGENiHBG007666.
    InParanoidiQ05209.
    KOiK18024.
    OMAiTWSFHGP.
    OrthoDBiEOG744T8Z.
    PhylomeDBiQ05209.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q05209-1) [UniParc]FASTAAdd to Basket

    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

    MEQVEILRKF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT    50
    ATGEKEENVK KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP 100
    KAYVATQGPL ANTVIDFWRM IWEYNVVIIV MACREFEMGR KKCERYWPLY 150
    GEDPITFAPF KISCEDEQAR TDYFIRTLLL EFQNESRRLY QFHYVNWPDH 200
    DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA ICAIDYTWNL 250
    LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL 300
    YEIHGAQKIA DGVNEINTEN MVSSIEPEKQ DSPPPKPPRT RSCLVEGDAK 350
    EEILQPPEPH PVPPILTPSP PSAFPTVTTV WQDNDRYHPK PVLHMVSSEQ 400
    HSADLNRNYS KSTELPGKNE STIEQIDKKL ERNLSFEIKK VPLQEGPKSF 450
    DGNTLLNRGH AIKIKSASPC IADKISKPQE LSSDLNVGDT SQNSCVDCSV 500
    TQSNKVSVTP PEESQNSDTP PRPDRLPLDE KGHVTWSFHG PENAIPIPDL 550
    SEGNSSDINY QTRKTVSLTP SPTTQVETPD LVDHDNTSPL FRTPLSFTNP 600
    LHSDDSDSDE RNSDGAVTQN KTNISTASAT VSAATSTESI STRKVLPMSI 650
    ARHNIAGTTH SGAEKDVDVS EDSPPPLPER TPESFVLASE HNTPVRSEWS 700
    ELQSQERSEQ KKSEGLITSE NEKCDHPAGG IHYEMCIECP PTFSDKREQI 750
    SENPTEATDI GFGNRCGKPK GPRDPPSEWT 780
    Length:780
    Mass (Da):88,106
    Last modified:January 11, 2011 - v3
    Checksum:i663DB3E5176FD7FD
    GO
    Isoform 2 (identifier: Q05209-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-130: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:650
    Mass (Da):72,778
    Checksum:i217EF3041B7E5EDB
    GO
    Isoform 3 (identifier: Q05209-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-119: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:661
    Mass (Da):74,138
    Checksum:i74E2947477636633
    GO

    Sequence cautioni

    The sequence BAD92761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211I → V in BAA02648. (PubMed:1472029)Curated
    Sequence conflicti121 – 1211I → V in AAB30047. (PubMed:7509295)Curated
    Sequence conflicti612 – 6121N → D in BAG59344. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611K → R in colon cancer. 1 Publication
    VAR_006385
    Natural varianti322 – 3221V → I.4 Publications
    Corresponds to variant rs9640663 [ dbSNP | Ensembl ].
    VAR_019512
    Natural varianti573 – 5731T → A.1 Publication
    Corresponds to variant rs3750050 [ dbSNP | Ensembl ].
    VAR_020297
    Natural varianti706 – 7061E → K.
    Corresponds to variant rs2230602 [ dbSNP | Ensembl ].
    VAR_057129

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 130130Missing in isoform 2. 1 PublicationVSP_046274Add
    BLAST
    Alternative sequencei1 – 119119Missing in isoform 3. CuratedVSP_054168Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13380 mRNA. Translation: BAA02648.1.
    M93425 mRNA. Translation: AAA36529.1.
    AK289573 mRNA. Translation: BAF82262.1.
    AK296764 mRNA. Translation: BAG59344.1.
    AB209524 mRNA. Translation: BAD92761.1. Different initiation.
    AC006451 Genomic DNA. Translation: AAQ96881.1.
    CH236949 Genomic DNA. Translation: EAL24198.1.
    CH471091 Genomic DNA. Translation: EAW77036.1.
    CH471091 Genomic DNA. Translation: EAW77037.1.
    BC050008 mRNA. Translation: AAH50008.2.
    S69184 mRNA. Translation: AAB30047.2.
    CCDSiCCDS47619.1. [Q05209-3]
    CCDS47620.1. [Q05209-2]
    CCDS5592.1. [Q05209-1]
    PIRiJC1368.
    RefSeqiNP_001124480.1. NM_001131008.1. [Q05209-3]
    NP_001124481.1. NM_001131009.1. [Q05209-2]
    NP_002826.3. NM_002835.3. [Q05209-1]
    UniGeneiHs.61812.

    Genome annotation databases

    EnsembliENST00000248594; ENSP00000248594; ENSG00000127947. [Q05209-1]
    ENST00000415482; ENSP00000392429; ENSG00000127947. [Q05209-3]
    ENST00000435495; ENSP00000397991; ENSG00000127947. [Q05209-2]
    GeneIDi5782.
    KEGGihsa:5782.
    UCSCiuc003ugh.2. human. [Q05209-1]

    Polymorphism databases

    DMDMi317373522.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13380 mRNA. Translation: BAA02648.1 .
    M93425 mRNA. Translation: AAA36529.1 .
    AK289573 mRNA. Translation: BAF82262.1 .
    AK296764 mRNA. Translation: BAG59344.1 .
    AB209524 mRNA. Translation: BAD92761.1 . Different initiation.
    AC006451 Genomic DNA. Translation: AAQ96881.1 .
    CH236949 Genomic DNA. Translation: EAL24198.1 .
    CH471091 Genomic DNA. Translation: EAW77036.1 .
    CH471091 Genomic DNA. Translation: EAW77037.1 .
    BC050008 mRNA. Translation: AAH50008.2 .
    S69184 mRNA. Translation: AAB30047.2 .
    CCDSi CCDS47619.1. [Q05209-3 ]
    CCDS47620.1. [Q05209-2 ]
    CCDS5592.1. [Q05209-1 ]
    PIRi JC1368.
    RefSeqi NP_001124480.1. NM_001131008.1. [Q05209-3 ]
    NP_001124481.1. NM_001131009.1. [Q05209-2 ]
    NP_002826.3. NM_002835.3. [Q05209-1 ]
    UniGenei Hs.61812.

    3D structure databases

    ProteinModelPortali Q05209.
    SMRi Q05209. Positions 3-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111746. 41 interactions.
    IntActi Q05209. 37 interactions.
    MINTi MINT-243699.
    STRINGi 9606.ENSP00000248594.

    Chemistry

    BindingDBi Q05209.
    ChEMBLi CHEMBL3236.

    PTM databases

    PhosphoSitei Q05209.

    Polymorphism databases

    DMDMi 317373522.

    Proteomic databases

    MaxQBi Q05209.
    PaxDbi Q05209.
    PRIDEi Q05209.

    Protocols and materials databases

    DNASUi 5782.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248594 ; ENSP00000248594 ; ENSG00000127947 . [Q05209-1 ]
    ENST00000415482 ; ENSP00000392429 ; ENSG00000127947 . [Q05209-3 ]
    ENST00000435495 ; ENSP00000397991 ; ENSG00000127947 . [Q05209-2 ]
    GeneIDi 5782.
    KEGGi hsa:5782.
    UCSCi uc003ugh.2. human. [Q05209-1 ]

    Organism-specific databases

    CTDi 5782.
    GeneCardsi GC07P077166.
    H-InvDB HIX0033626.
    HGNCi HGNC:9645. PTPN12.
    HPAi HPA007097.
    MIMi 600079. gene.
    neXtProti NX_Q05209.
    PharmGKBi PA33987.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000252955.
    HOVERGENi HBG007666.
    InParanoidi Q05209.
    KOi K18024.
    OMAi TWSFHGP.
    OrthoDBi EOG744T8Z.
    PhylomeDBi Q05209.
    TreeFami TF351977.

    Miscellaneous databases

    ChiTaRSi PTPN12. human.
    GeneWikii PTPN12.
    GenomeRNAii 5782.
    NextBioi 22488.
    PROi Q05209.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05209.
    Bgeei Q05209.
    CleanExi HS_PTPN12.
    Genevestigatori Q05209.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-322.
      Tissue: Colon.
    2. "Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase."
      Yang Q., Co D., Sommercorn J., Tonks N.K.
      J. Biol. Chem. 268:6622-6628(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Erratum
      Yang Q., Co D., Sommercorn J., Tonks N.K.
      J. Biol. Chem. 268:17650-17650(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 495-517 AND 526-780.
    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] (ISOFORMS 1 AND 2), VARIANTS ILE-322 AND ALA-573.
      Tissue: Cerebellum and Tongue.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-322.
      Tissue: Brain.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Testis.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-8, ACETYLATION AT MET-1.
      Tissue: Platelet.
    10. "Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells."
      Takekawa M., Itoh F., Hinoda Y., Adachi M., Ariyama T., Inazawa J., Imai K., Yachi A.
      FEBS Lett. 339:222-228(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-136 (ISOFORM 1), VARIANT COLON CANCER ARG-61.
    11. "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion."
      Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L.
      EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSTPIP1.
    12. "Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST."
      Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D.
      J. Biol. Chem. 281:38405-38417(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY STK24.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells."
      Sahu S.N., Nunez S., Bai G., Gupta A.
      Am. J. Physiol. 292:C2288-C2296(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2B/PYK2, FUNCTION.
    15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND THR-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-468; THR-519; SER-567; THR-569; SER-571; SER-603; SER-606; SER-608; SER-613; SER-689 AND THR-693, VARIANT [LARGE SCALE ANALYSIS] ILE-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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-19; SER-435; SER-449 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-332; SER-435; SER-449; SER-603; SER-606 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPTN12_HUMAN
    AccessioniPrimary (citable) accession number: Q05209
    Secondary accession number(s): A4D1C5
    , B4DKY2, E9PBR5, E9PEH9, Q16130, Q59FD6, Q75MN8, Q86XU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3