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P23469

- PTPRE_HUMAN

UniProt

P23469 - PTPRE_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase epsilon

Gene

PTPRE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function By similarity.By similarity
    Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake By similarity.By similarity
    Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca2+.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei303 – 3031SubstrateBy similarity
    Active sitei335 – 3351Phosphocysteine intermediateBy similarity
    Binding sitei379 – 3791SubstrateBy similarity
    Active sitei630 – 6301Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    2. protein dephosphorylation Source: ProtInc
    3. regulation of mast cell activation Source: Ensembl
    4. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiP23469.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase epsilon (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase epsilon
    Short name:
    R-PTP-epsilon
    Gene namesi
    Name:PTPRE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9669. PTPRE.

    Subcellular locationi

    Isoform 2 : Cytoplasm
    Note: Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34014.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 700681Receptor-type tyrosine-protein phosphatase epsilonPRO_0000025439Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Modified residuei696 – 6961Phosphotyrosine2 Publications

    Post-translational modificationi

    A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.1 Publication
    Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu.2 Publications
    Isoform 1 is glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP23469.
    PaxDbiP23469.
    PRIDEiP23469.

    PTM databases

    PhosphoSiteiP23469.

    Expressioni

    Tissue specificityi

    Expressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells).1 Publication

    Inductioni

    Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA) in HL-60 cells.1 Publication

    Gene expression databases

    ArrayExpressiP23469.
    BgeeiP23469.
    CleanExiHS_PTPRE.
    GenevestigatoriP23469.

    Organism-specific databases

    HPAiHPA015870.
    HPA021872.

    Interactioni

    Subunit structurei

    Monomer. Isoform 2: Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi111755. 5 interactions.
    IntActiP23469. 3 interactions.
    MINTiMINT-1349810.
    STRINGi9606.ENSP00000254667.

    Structurei

    Secondary structure

    1
    700
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi117 – 1193
    Helixi120 – 1267
    Helixi139 – 1413
    Turni152 – 1554
    Helixi157 – 1626
    Beta strandi172 – 1776
    Turni185 – 1884
    Beta strandi189 – 1979
    Beta strandi200 – 2078
    Helixi212 – 2143
    Helixi215 – 22410
    Beta strandi229 – 2324
    Beta strandi236 – 2383
    Beta strandi250 – 2567
    Beta strandi259 – 26810
    Beta strandi270 – 28011
    Beta strandi291 – 2988
    Beta strandi303 – 3053
    Helixi311 – 32313
    Beta strandi331 – 3344
    Beta strandi336 – 3405
    Helixi341 – 35818
    Beta strandi359 – 3613
    Helixi363 – 3719
    Helixi381 – 39616
    Helixi426 – 4349
    Helixi444 – 4474
    Helixi449 – 4524
    Beta strandi464 – 4696
    Beta strandi481 – 4877
    Beta strandi490 – 4923
    Beta strandi496 – 4994
    Turni504 – 5063
    Helixi507 – 51610
    Beta strandi521 – 5244
    Beta strandi528 – 5303
    Beta strandi542 – 5487
    Beta strandi551 – 56010
    Beta strandi562 – 57312
    Beta strandi584 – 5929
    Beta strandi597 – 5993
    Helixi605 – 62016
    Beta strandi626 – 6294
    Beta strandi631 – 6355
    Helixi636 – 65318
    Beta strandi654 – 6563
    Helixi658 – 6669
    Helixi676 – 69015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JJDX-ray3.20A/B/C/D/E/F107-697[»]
    ProteinModelPortaliP23469.
    SMRiP23469. Positions 111-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23469.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 4627ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini70 – 700631CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei47 – 6923HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 394260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini426 – 689264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni335 – 3417Substrate bindingBy similarity

    Domaini

    The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity By similarity.By similarity

    Sequence similaritiesi

    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000231465.
    HOVERGENiHBG053758.
    InParanoidiP23469.
    KOiK18033.
    OMAiIVIDAMI.
    OrthoDBiEOG7B31M8.
    PhylomeDBiP23469.
    TreeFamiTF351829.

    Family and domain databases

    Gene3Di3.90.190.10. 2 hits.
    InterProiIPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR016336. Tyr_Pase_rcpt_a/e-type.
    [Graphical view]
    PfamiPF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002006. PTPR_alpha_epsilon. 1 hit.
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative promoter usage and alternative initiation. Align

    Isoform 1 (identifier: P23469-1) [UniParc]FASTAAdd to Basket

    Also known as: PTPeM, RPTPe, tm-PTPe

    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

    MEPLCPLLLV GFSLPLARAL RGNETTADSN ETTTTSGPPD PGASQPLLAW    50
    LLLPLLLLLL VLLLAAYFFR FRKQRKAVVS TSDKKMPNGI LEEQEQQRVM 100
    LLSRSPSGPK KYFPIPVEHL EEEIRIRSAD DCKQFREEFN SLPSGHIQGT 150
    FELANKEENR EKNRYPNILP NDHSRVILSQ LDGIPCSDYI NASYIDGYKE 200
    KNKFIAAQGP KQETVNDFWR MVWEQKSATI VMLTNLKERK EEKCHQYWPD 250
    QGCWTYGNIR VCVEDCVVLV DYTIRKFCIQ PQLPDGCKAP RLVSQLHFTS 300
    WPDFGVPFTP IGMLKFLKKV KTLNPVHAGP IVVHCSAGVG RTGTFIVIDA 350
    MMAMMHAEQK VDVFEFVSRI RNQRPQMVQT DMQYTFIYQA LLEYYLYGDT 400
    ELDVSSLEKH LQTMHGTTTH FDKIGLEEEF RKLTNVRIMK ENMRTGNLPA 450
    NMKKARVIQI IPYDFNRVIL SMKRGQEYTD YINASFIDGY RQKDYFIATQ 500
    GPLAHTVEDF WRMIWEWKSH TIVMLTEVQE REQDKCYQYW PTEGSVTHGE 550
    ITIEIKNDTL SEAISIRDFL VTLNQPQARQ EEQVRVVRQF HFHGWPEIGI 600
    PAEGKGMIDL IAAVQKQQQQ TGNHPITVHC SAGAGRTGTF IALSNILERV 650
    KAEGLLDVFQ AVKSLRLQRP HMVQTLEQYE FCYKVVQDFI DIFSDYANFK 700

    Note: Produced by alternative promoter usage.

    Length:700
    Mass (Da):80,642
    Last modified:November 1, 1991 - v1
    Checksum:iD096BCADCEA65708
    GO
    Isoform 2 (identifier: P23469-2) [UniParc]FASTAAdd to Basket

    Also known as: PTPeC, cyt-PTPe

    The sequence of this isoform differs from the canonical sequence as follows:
         1-70: MEPLCPLLLV...VLLLAAYFFR → MSNRSSFSRLTW

    Note: Produced by alternative promoter usage.

    Show »
    Length:642
    Mass (Da):74,595
    Checksum:iD39B2835A8D7D949
    GO
    Isoform 3 (identifier: P23469-3) [UniParc]FASTAAdd to Basket

    Also known as: p67

    The sequence of this isoform differs from the canonical sequence as follows:
         1-85: Missing.

    Note: Produced by alternative initiation at Met-86 of isoform 1.

    Show »
    Length:615
    Mass (Da):71,382
    Checksum:iF4FD48DDAAA0B302
    GO

    Sequence cautioni

    The sequence AAC50324.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti516 – 5161E → D in CAC86583. (PubMed:12121439)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8585Missing in isoform 3. CuratedVSP_038490Add
    BLAST
    Alternative sequencei1 – 7070MEPLC…AYFFR → MSNRSSFSRLTW in isoform 2. 2 PublicationsVSP_007778Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54134 mRNA. Translation: CAA38069.1.
    AJ315969 mRNA. Translation: CAC86583.1.
    AK291828 mRNA. Translation: BAF84517.1.
    AL390236 Genomic DNA. Translation: CAH73173.1.
    AL390236 Genomic DNA. Translation: CAH73174.1.
    CH471066 Genomic DNA. Translation: EAW49180.1.
    CH471066 Genomic DNA. Translation: EAW49181.1.
    CH471066 Genomic DNA. Translation: EAW49182.1.
    CH471066 Genomic DNA. Translation: EAW49184.1.
    BC050062 mRNA. Translation: AAH50062.1.
    U36623 mRNA. Translation: AAC50324.1. Sequence problems.
    CCDSiCCDS7657.1. [P23469-1]
    CCDS7658.1. [P23469-2]
    PIRiS12053.
    RefSeqiNP_006495.1. NM_006504.4. [P23469-1]
    NP_569119.1. NM_130435.3. [P23469-2]
    XP_005252748.1. XM_005252691.1. [P23469-1]
    XP_005252749.1. XM_005252692.1. [P23469-1]
    UniGeneiHs.127022.

    Genome annotation databases

    EnsembliENST00000254667; ENSP00000254667; ENSG00000132334. [P23469-1]
    ENST00000306042; ENSP00000303350; ENSG00000132334. [P23469-2]
    GeneIDi5791.
    KEGGihsa:5791.
    UCSCiuc001lkb.3. human. [P23469-1]
    uc001lkd.3. human. [P23469-2]

    Polymorphism databases

    DMDMi126471.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54134 mRNA. Translation: CAA38069.1 .
    AJ315969 mRNA. Translation: CAC86583.1 .
    AK291828 mRNA. Translation: BAF84517.1 .
    AL390236 Genomic DNA. Translation: CAH73173.1 .
    AL390236 Genomic DNA. Translation: CAH73174.1 .
    CH471066 Genomic DNA. Translation: EAW49180.1 .
    CH471066 Genomic DNA. Translation: EAW49181.1 .
    CH471066 Genomic DNA. Translation: EAW49182.1 .
    CH471066 Genomic DNA. Translation: EAW49184.1 .
    BC050062 mRNA. Translation: AAH50062.1 .
    U36623 mRNA. Translation: AAC50324.1 . Sequence problems.
    CCDSi CCDS7657.1. [P23469-1 ]
    CCDS7658.1. [P23469-2 ]
    PIRi S12053.
    RefSeqi NP_006495.1. NM_006504.4. [P23469-1 ]
    NP_569119.1. NM_130435.3. [P23469-2 ]
    XP_005252748.1. XM_005252691.1. [P23469-1 ]
    XP_005252749.1. XM_005252692.1. [P23469-1 ]
    UniGenei Hs.127022.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JJD X-ray 3.20 A/B/C/D/E/F 107-697 [» ]
    ProteinModelPortali P23469.
    SMRi P23469. Positions 111-691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111755. 5 interactions.
    IntActi P23469. 3 interactions.
    MINTi MINT-1349810.
    STRINGi 9606.ENSP00000254667.

    Chemistry

    BindingDBi P23469.
    ChEMBLi CHEMBL4850.

    PTM databases

    PhosphoSitei P23469.

    Polymorphism databases

    DMDMi 126471.

    Proteomic databases

    MaxQBi P23469.
    PaxDbi P23469.
    PRIDEi P23469.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254667 ; ENSP00000254667 ; ENSG00000132334 . [P23469-1 ]
    ENST00000306042 ; ENSP00000303350 ; ENSG00000132334 . [P23469-2 ]
    GeneIDi 5791.
    KEGGi hsa:5791.
    UCSCi uc001lkb.3. human. [P23469-1 ]
    uc001lkd.3. human. [P23469-2 ]

    Organism-specific databases

    CTDi 5791.
    GeneCardsi GC10P129705.
    HGNCi HGNC:9669. PTPRE.
    HPAi HPA015870.
    HPA021872.
    MIMi 600926. gene.
    neXtProti NX_P23469.
    PharmGKBi PA34014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000231465.
    HOVERGENi HBG053758.
    InParanoidi P23469.
    KOi K18033.
    OMAi IVIDAMI.
    OrthoDBi EOG7B31M8.
    PhylomeDBi P23469.
    TreeFami TF351829.

    Enzyme and pathway databases

    SignaLinki P23469.

    Miscellaneous databases

    EvolutionaryTracei P23469.
    GeneWikii PTPRE.
    GenomeRNAii 5791.
    NextBioi 22544.
    PROi P23469.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23469.
    Bgeei P23469.
    CleanExi HS_PTPRE.
    Genevestigatori P23469.

    Family and domain databases

    Gene3Di 3.90.190.10. 2 hits.
    InterProi IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    IPR016336. Tyr_Pase_rcpt_a/e-type.
    [Graphical view ]
    Pfami PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002006. PTPR_alpha_epsilon. 1 hit.
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural diversity and evolution of human receptor-like protein tyrosine phosphatases."
      Krueger N.X., Streuli M., Saito H.
      EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase."
      Wabakken T.K., Hauge H., Finne E.F., Wiedlocha A., Aasheim H.-C.
      Scand. J. Immunol. 56:195-203(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "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 1).
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] (ISOFORM 1).
      Tissue: Brain.
    7. "Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon."
      Elson A., Leder P.
      Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 2), SUBCELLULAR LOCATION, INDUCTION.
    8. "Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate."
      Schmidt A., Rutledge S.J., Endo N., Opas E., Tanaka H., Wesolowski G., Leu C.T., Huang Z., Ramachandaran C., Rodan S.B., Rodan G.A.
      Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation."
      Tanuma N., Nakamura K., Kikuchi K.
      Eur. J. Biochem. 259:46-54(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE.
    10. "Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control."
      Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., Elson A.
      Oncogene 19:4375-4384(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH GRB2.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-696, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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 (3.2 ANGSTROMS) OF 107-697, SUBUNIT.

    Entry informationi

    Entry nameiPTPRE_HUMAN
    AccessioniPrimary (citable) accession number: P23469
    Secondary accession number(s): Q13345
    , Q5VWH3, Q5VWH4, Q96KQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 146 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 10
      Human chromosome 10: 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