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Q15678

- PTN14_HUMAN

UniProt

Q15678 - PTN14_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 14

Gene

PTPN14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor.7 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1079 – 10791SubstrateBy similarity
    Active sitei1121 – 11211Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1165 – 11651SubstrateBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: UniProtKB
    3. receptor tyrosine kinase binding Source: UniProtKB
    4. transcription cofactor activity Source: UniProtKB

    GO - Biological processi

    1. lymphangiogenesis Source: UniProtKB
    2. negative regulation of cell proliferation Source: UniProtKB
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. protein dephosphorylation Source: ProtInc
    5. regulation of protein export from nucleus Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase non-receptor type 14 (EC:3.1.3.48)
    Alternative name(s):
    Protein-tyrosine phosphatase pez
    Gene namesi
    Name:PTPN14
    Synonyms:PEZ, PTPD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9647. PTPN14.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton By similarity. Nucleus
    Note: Translocation into the nucleus is associated with induction of cell proliferation. Partially colocalized with actin filaments at the plasma membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Choanal atresia and lymphedema (CHATLY) [MIM:613611]: A disease characterized by posterior choanal atresia and lymphedema. Additional features are a high-arched palate, hypoplastic nipples, and mild pectus excavatum.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in PTPN14 predicted to result in frameshift and premature truncation, has been shown to be the cause of choanal atresia and lymphedema in one family.
    Influence clinical severity of hereditary haemorragic telagiectasia (HHT).
    Frequently mutated in a variety of human cancers.

    Organism-specific databases

    MIMi613611. phenotype.
    PharmGKBiPA33989.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11871187Tyrosine-protein phosphatase non-receptor type 14PRO_0000219437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei486 – 4861Phosphoserine1 Publication
    Modified residuei591 – 5911Phosphoserine1 Publication
    Modified residuei594 – 5941Phosphoserine1 Publication
    Modified residuei642 – 6421Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated by the ECS (Elongin BC-CUL2/5-SOCS-box protein)/LRR1 E3 ligase complex and subsequently targeted to proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15678.
    PaxDbiQ15678.
    PRIDEiQ15678.

    PTM databases

    PhosphoSiteiQ15678.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Inductioni

    Up-regulated at protein level by cell density. However, at the mRNA level remains the same regardless of the status of cell density.1 Publication

    Gene expression databases

    ArrayExpressiQ15678.
    BgeeiQ15678.
    CleanExiHS_PTPN14.
    GenevestigatoriQ15678.

    Organism-specific databases

    HPAiCAB011469.
    HPA053864.

    Interactioni

    Subunit structurei

    Interacts with FLT4; the interaction is enhanced by stimulation with VEGFC. Interacts (via PPxY motifs) with YAP1 (via WW domains); this interaction leads to the cytoplasmic sequestration of YAP1 and inhibits its transcriptional co-activator activity.3 Publications

    Protein-protein interaction databases

    BioGridi111748. 33 interactions.
    IntActiQ15678. 10 interactions.
    STRINGi9606.ENSP00000355923.

    Structurei

    Secondary structure

    1
    1187
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi896 – 9038
    Helixi909 – 9146
    Turni926 – 9294
    Helixi931 – 9333
    Helixi946 – 9483
    Beta strandi964 – 9729
    Beta strandi975 – 9828
    Turni987 – 9893
    Helixi990 – 99910
    Beta strandi1004 – 10074
    Beta strandi1011 – 10133
    Beta strandi1032 – 10354
    Beta strandi1038 – 104710
    Beta strandi1049 – 106012
    Turni1061 – 10633
    Beta strandi1066 – 10749
    Beta strandi1079 – 10813
    Helixi1086 – 110318
    Helixi1105 – 11073
    Beta strandi1117 – 11259
    Helixi1126 – 114217
    Helixi1149 – 11579
    Helixi1167 – 118317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BZLX-ray1.65A886-1187[»]
    ProteinModelPortaliQ15678.
    SMRiQ15678. Positions 24-303, 895-1184.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15678.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 306286FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini909 – 1180272Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1121 – 11277Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi566 – 5738Poly-Pro
    Compositional biasi709 – 7168Poly-Glu

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000115775.
    HOVERGENiHBG053757.
    InParanoidiQ15678.
    KOiK18025.
    OMAiVTTKFRT.
    OrthoDBiEOG7PK8XS.
    PhylomeDBiQ15678.
    TreeFamiTF315900.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR011993. PH_like_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR014392. Tyr_Pase_non-rcpt_typ-14/21.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000934. Tyr-Ptase_nr14. 1 hit.
    PRINTSiPR00935. BAND41.
    PR00700. PRTYPHPHTASE.
    SMARTiSM00295. B41. 1 hit.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF52799. SSF52799. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 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.

    Q15678-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFGLKLRRT RRYNVLSKNC FVTRIRLLDS NVIECTLSVE STGQECLEAV     50
    AQRLELRETH YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM 100
    FYVPNVSWLQ QEATRYQYYL QVKKDVLEGR LRCTLDQVIR LAGLAVQADF 150
    GDYNQFDSQD FLREYVLFPM DLALEEAVLE ELTQKVAQEH KAHSGILPAE 200
    AELMYINEVE RLDGFGQEIF PVKDNHGNCV HLGIFFMGIF VRNRIGRQAV 250
    IYRWNDMGNI THNKSTILVE LINKEETALF HTDDIENAKY ISRLFATRHK 300
    FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPV HVQCGEHYSE 350
    THTSQDSIFH GNEEALYCNS HNSLDLNYLN GTVTNGSVCS VHSVNSLNCS 400
    QSFIQASPVS SNLSIPGSDI MRADYIPSHR HSAIIVPSYR PTPDYETVMR 450
    QMKRGILHTD SQSQSLRNLN IINTHAYNQP EDLVYSQPEM RERHPYTVPY 500
    GPQGVYSNKL VSPSDQRNPK NNVVPSKPGA SAISHTVSTP ELANMQLQGS 550
    HNYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR 600
    KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGTVNKR HSLEVMNSMV 650
    RGMEAMTLKS LHLPMARRNT LREQGPPEEG SGSHEVPQLP QYHHKKTFSD 700
    ATMLIHSSES EEEEEEAPES VPQIPMLREK MEYSAQLQAA LARIPNKPPP 750
    EYPGPRKSVS NGALRQDQAS LPPAMARARV LRHGPAKAIS MSRTDPPAVN 800
    GASLGPSISE PDLTSVKERV KKEPVKERPV SEMFSLEDSI IEREMMIRNL 850
    EKQKMAGLEA QKRPLMLAAL NGLSVARVSG REENRVDATR VPMDERFRTL 900
    KKKLEEGMVF TEYEQIPKKK ANGIFSTAAL PENAERSRIR EVVPYEENRV 950
    ELIPTKENNT GYINASHIKV VVGGAEWHYI ATQGPLPHTC HDFWQMVWEQ 1000
    GVNVIAMVTA EEEGGRTKSH RYWPKLGSKH SSATYGKFKV TTKFRTDSVC 1050
    YATTGLKVKH LLSGQERTVW HLQYTDWPDH GCPEDVQGFL SYLEEIQSVR 1100
    RHTNSMLEGT KNRHPPIVVH CSAGVGRTGV LILSELMIYC LEHNEKVEVP 1150
    MMLRLLREQR MFMIQTIAQY KFVYQVLIQF LQNSRLI 1187
    Length:1,187
    Mass (Da):135,261
    Last modified:October 14, 2008 - v2
    Checksum:i1D22F1C8ED06C096
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti392 – 3921H → D in CAA57993. (PubMed:7733990)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti159 – 1591Q → E in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035849
    Natural varianti360 – 3601H → P in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035850
    Natural varianti505 – 5051V → F.
    Corresponds to variant rs12239356 [ dbSNP | Ensembl ].
    VAR_046995

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82676 mRNA. Translation: CAA57993.1.
    AL929236
    , AL445305, AL592216, AL603838 Genomic DNA. Translation: CAH70919.1.
    AL603838
    , AL445305, AL592216, AL929236 Genomic DNA. Translation: CAH72982.1.
    AL445305
    , AL592216, AL603838, AL929236 Genomic DNA. Translation: CAH73027.1.
    AL592216
    , AL445305, AL603838, AL929236 Genomic DNA. Translation: CAH73479.1.
    CH471100 Genomic DNA. Translation: EAW93351.1.
    BC101754 mRNA. Translation: AAI01755.1.
    BC104803 mRNA. Translation: AAI04804.1.
    CCDSiCCDS1514.1.
    PIRiJC4155.
    RefSeqiNP_005392.2. NM_005401.4.
    UniGeneiHs.193557.

    Genome annotation databases

    EnsembliENST00000366956; ENSP00000355923; ENSG00000152104.
    GeneIDi5784.
    KEGGihsa:5784.
    UCSCiuc001hkk.2. human.

    Polymorphism databases

    DMDMi209572662.

    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
    X82676 mRNA. Translation: CAA57993.1 .
    AL929236
    , AL445305 , AL592216 , AL603838 Genomic DNA. Translation: CAH70919.1 .
    AL603838
    , AL445305 , AL592216 , AL929236 Genomic DNA. Translation: CAH72982.1 .
    AL445305
    , AL592216 , AL603838 , AL929236 Genomic DNA. Translation: CAH73027.1 .
    AL592216
    , AL445305 , AL603838 , AL929236 Genomic DNA. Translation: CAH73479.1 .
    CH471100 Genomic DNA. Translation: EAW93351.1 .
    BC101754 mRNA. Translation: AAI01755.1 .
    BC104803 mRNA. Translation: AAI04804.1 .
    CCDSi CCDS1514.1.
    PIRi JC4155.
    RefSeqi NP_005392.2. NM_005401.4.
    UniGenei Hs.193557.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BZL X-ray 1.65 A 886-1187 [» ]
    ProteinModelPortali Q15678.
    SMRi Q15678. Positions 24-303, 895-1184.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111748. 33 interactions.
    IntActi Q15678. 10 interactions.
    STRINGi 9606.ENSP00000355923.

    PTM databases

    PhosphoSitei Q15678.

    Polymorphism databases

    DMDMi 209572662.

    Proteomic databases

    MaxQBi Q15678.
    PaxDbi Q15678.
    PRIDEi Q15678.

    Protocols and materials databases

    DNASUi 5784.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366956 ; ENSP00000355923 ; ENSG00000152104 .
    GeneIDi 5784.
    KEGGi hsa:5784.
    UCSCi uc001hkk.2. human.

    Organism-specific databases

    CTDi 5784.
    GeneCardsi GC01M214523.
    HGNCi HGNC:9647. PTPN14.
    HPAi CAB011469.
    HPA053864.
    MIMi 603155. gene.
    613611. phenotype.
    neXtProti NX_Q15678.
    PharmGKBi PA33989.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000115775.
    HOVERGENi HBG053757.
    InParanoidi Q15678.
    KOi K18025.
    OMAi VTTKFRT.
    OrthoDBi EOG7PK8XS.
    PhylomeDBi Q15678.
    TreeFami TF315900.

    Miscellaneous databases

    ChiTaRSi PTPN14. human.
    EvolutionaryTracei Q15678.
    GeneWikii PTPN14.
    GenomeRNAii 5784.
    NextBioi 22502.
    PROi Q15678.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15678.
    Bgeei Q15678.
    CleanExi HS_PTPN14.
    Genevestigatori Q15678.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR011993. PH_like_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR014392. Tyr_Pase_non-rcpt_typ-14/21.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000934. Tyr-Ptase_nr14. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00700. PRTYPHPHTASE.
    SMARTi SM00295. B41. 1 hit.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF52799. SSF52799. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 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. "Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains."
      Smith A.L., Mitchell P.J., Shipley J., Gusterson B.A., Rogers M.V., Crompton M.R.
      Biochem. Biophys. Res. Commun. 209:959-965(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    2. "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].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Heart and Lung.
    5. "Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation."
      Wadham C., Gamble J.R., Vadas M.A., Khew-Goodall Y.
      J. Cell Sci. 113:3117-3123(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    6. "The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin."
      Wadham C., Gamble J.R., Vadas M.A., Khew-Goodall Y.
      Mol. Biol. Cell 14:2520-2529(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The protein tyrosine phosphatase Pez regulates TGFbeta, epithelial-mesenchymal transition, and organ development."
      Wyatt L., Wadham C., Crocker L.A., Lardelli M., Khew-Goodall Y.
      J. Cell Biol. 178:1223-1235(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function and choanal development in humans."
      Au A.C., Hernandez P.A., Lieber E., Nadroo A.M., Shen Y.M., Kelley K.A., Gelb B.D., Diaz G.A.
      Am. J. Hum. Genet. 87:436-444(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FLT4, INVOLVEMENT IN CHATLY.
    12. "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-591; SER-594 AND SER-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "PTPN14 is required for the density-dependent control of YAP1."
      Wang W., Huang J., Wang X., Yuan J., Li X., Feng L., Park J.I., Chen J.
      Genes Dev. 26:1959-1971(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION, FUNCTION, INTERACTION WITH YAP1; CUL2 AND LRR1, UBIQUITINATION.
    14. Cited for: INVOLVEMENT IN HEREDITARY HAEMORRAGIC TELAGIECTASIA, FUNCTION.
    15. "PTPN14 interacts with and negatively regulates the oncogenic function of YAP."
      Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H., Zhang J.
      Oncogene 32:1266-1273(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YAP1, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution."
      Barr A.J., Debreczeni J.E., Eswaran J., Knapp S.
      Proteins 63:1132-1136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 886-1187.
    17. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-159 AND PRO-360.

    Entry informationi

    Entry nameiPTN14_HUMAN
    AccessioniPrimary (citable) accession number: Q15678
    Secondary accession number(s): Q5VSI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 139 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

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