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Q16827

- PTPRO_HUMAN

UniProt

Q16827 - PTPRO_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase O

Gene

PTPRO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1102 – 11021SubstrateBy similarity
    Active sitei1136 – 11361Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1180 – 11801SubstrateBy similarity

    GO - Molecular functioni

    1. phosphatase activity Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: UniProtKB
    4. protein tyrosine phosphatase activity Source: UniProtKB
    5. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB
    6. Wnt-protein binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: UniProtKB
    2. cell morphogenesis Source: UniProtKB
    3. glomerular visceral epithelial cell differentiation Source: UniProtKB
    4. glomerulus development Source: UniProtKB
    5. lamellipodium assembly Source: UniProtKB
    6. monocyte chemotaxis Source: UniProtKB
    7. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    8. negative regulation of cell-substrate adhesion Source: UniProtKB
    9. negative regulation of glomerular filtration Source: UniProtKB
    10. negative regulation of neuron projection development Source: UniProtKB
    11. negative regulation of retinal ganglion cell axon guidance Source: UniProtKB
    12. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    13. protein dephosphorylation Source: UniProtKB
    14. regulation of glomerular filtration Source: UniProtKB
    15. slit diaphragm assembly Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase, Receptor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase O (EC:3.1.3.48)
    Short name:
    R-PTP-O
    Alternative name(s):
    Glomerular epithelial protein 1
    Protein tyrosine phosphatase U2
    Short name:
    PTP-U2
    Short name:
    PTPase U2
    Gene namesi
    Name:PTPRO
    Synonyms:GLEPP1, PTPU2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9678. PTPRO.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. axon Source: UniProtKB
    3. dendritic spine Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. growth cone Source: UniProtKB
    6. integral component of membrane Source: UniProtKB
    7. integral component of plasma membrane Source: UniProtKB
    8. lamellipodium Source: UniProtKB
    9. lateral plasma membrane Source: UniProtKB
    10. neuron projection Source: UniProtKB
    11. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Nephrotic syndrome 6 (NPHS6) [MIM:614196]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614196. phenotype.
    Orphaneti93214. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial proliferation.
    93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
    93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
    93216. Familial idiopathic steroid-resistant nephrotic syndrome with minimal changes.
    PharmGKBiPA34023.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 12161187Receptor-type tyrosine-protein phosphatase OPRO_0000025458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi26 – 261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence Analysis
    Modified residuei865 – 8651PhosphoserineBy similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ16827.
    PaxDbiQ16827.
    PRIDEiQ16827.

    PTM databases

    PhosphoSiteiQ16827.

    Expressioni

    Tissue specificityi

    Glomerulus of kidney. Also detected in brain, lung and placenta.1 Publication

    Inductioni

    By various differentiation-inducing agents.

    Gene expression databases

    ArrayExpressiQ16827.
    BgeeiQ16827.
    CleanExiHS_PTPRO.
    GenevestigatoriQ16827.

    Organism-specific databases

    HPAiHPA034525.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046262EBI-723739,EBI-641062
    TEKQ027632EBI-723739,EBI-2257090

    Protein-protein interaction databases

    BioGridi111764. 7 interactions.
    IntActiQ16827. 25 interactions.
    MINTiMINT-1415956.
    STRINGi9606.ENSP00000281171.

    Structurei

    Secondary structure

    1
    1216
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi920 – 9223
    Helixi923 – 94624
    Turni947 – 9515
    Helixi956 – 9583
    Helixi960 – 9656
    Turni975 – 9773
    Beta strandi978 – 9803
    Turni988 – 9914
    Beta strandi992 – 9987
    Beta strandi1007 – 10104
    Helixi1015 – 10173
    Helixi1018 – 102710
    Beta strandi1032 – 10354
    Beta strandi1039 – 10413
    Beta strandi1053 – 10564
    Beta strandi1058 – 10603
    Beta strandi1063 – 107210
    Beta strandi1074 – 108512
    Beta strandi1088 – 109710
    Beta strandi1103 – 11053
    Helixi1108 – 112720
    Beta strandi1132 – 11409
    Helixi1141 – 115818
    Beta strandi1160 – 11623
    Helixi1164 – 11729
    Helixi1182 – 120221

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G59X-ray2.19A/B914-1200[»]
    2GJTX-ray2.15A/B916-1208[»]
    ProteinModelPortaliQ16827.
    SMRiQ16827. Positions 916-1208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16827.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 822793ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini844 – 1216373CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei823 – 84321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 12475Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini142 – 21170Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini246 – 30661Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini329 – 42597Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini435 – 53197Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini532 – 62897Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini631 – 72494Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini725 – 81793Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini938 – 1195258Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1136 – 11427Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000243992.
    HOVERGENiHBG053763.
    InParanoidiQ16827.
    KOiK18035.
    OMAiSTMVTEM.
    OrthoDBiEOG7PCJFZ.
    PhylomeDBiQ16827.
    TreeFamiTF351926.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.190.10. 1 hit.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 4 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS50853. FN3. 5 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16827-1) [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

    MGHLPTGIHG ARRLLPLLWL FVLFKNATAF HVTVQDDNNI VVSLEASDVI     50
    SPASVYVVKI TGESKNYFFE FEEFNSTLPP PVIFKASYHG LYYIITLVVV 100
    NGNVVTKPSR SITVLTKPLP VTSVSIYDYK PSPETGVLFE IHYPEKYNVF 150
    TRVNISYWEG KDFRTMLYKD FFKGKTVFNH WLPGMCYSNI TFQLVSEATF 200
    NKSTLVEYSG VSHEPKQHRT APYPPQNISV RIVNLNKNNW EEQSGNFPEE 250
    SFMRSQDTIG KEKLFHFTEE TPEIPSGNIS SGWPDFNSSD YETTSQPYWW 300
    DSASAAPESE DEFVSVLPME YENNSTLSET EKSTSGSFSF FPVQMILTWL 350
    PPKPPTAFDG FHIHIEREEN FTEYLMVDEE AHEFVAELKE PGKYKLSVTT 400
    FSSSGSCETR KSQSAKSLSF YISPSGEWIE ELTEKPQHVS VHVLSSTTAL 450
    MSWTSSQENY NSTIVSVVSL TCQKQKESQR LEKQYCTQVN SSKPIIENLV 500
    PGAQYQVVIY LRKGPLIGPP SDPVTFAIVP TGIKDLMLYP LGPTAVVLSW 550
    TRPYLGVFRK YVVEMFYFNP ATMTSEWTTY YEIAATVSLT ASVRIANLLP 600
    AWYYNFRVTM VTWGDPELSC CDSSTISFIT APVAPEITSV EYFNSLLYIS 650
    WTYGDDTTDL SHSRMLHWMV VAEGKKKIKK SVTRNVMTAI LSLPPGDIYN 700
    LSVTACTERG SNTSMLRLVK LEPAPPKSLF AVNKTQTSVT LLWVEEGVAD 750
    FFEVFCQQVG SSQKTKLQEP VAVSSHVVTI SSLLPATAYN CSVTSFSHDS 800
    PSVPTFIAVS TMVTEMNPNV VVISVLAILS TLLIGLLLVT LIILRKKHLQ 850
    MARECGAGTF VNFASLERDG KLPYNWRRSI FAFLTLLPSC LWTDYLLAFY 900
    INPWSKNGLK KRKLTNPVQL DDFDAYIKDM AKDSDYKFSL QFEELKLIGL 950
    DIPHFAADLP LNRCKNRYTN ILPYDFSRVR LVSMNEEEGA DYINANYIPG 1000
    YNSPQEYIAT QGPLPETRND FWKMVLQQKS QIIVMLTQCN EKRRVKCDHY 1050
    WPFTEEPIAY GDITVEMISE EEQDDWACRH FRINYADEMQ DVMHFNYTAW 1100
    PDHGVPTANA AESILQFVHM VRQQATKSKG PMIIHCSAGV GRTGTFIALD 1150
    RLLQHIRDHE FVDILGLVSE MRSYRMSMVQ TEEQYIFIHQ CVQLMWMKKK 1200
    QQFCISDVIY ENVSKS 1216
    Length:1,216
    Mass (Da):138,344
    Last modified:October 14, 2008 - v2
    Checksum:iC902B48D1A73BFE1
    GO
    Isoform 2 (identifier: Q16827-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         876-903: Missing.

    Show »
    Length:1,188
    Mass (Da):134,941
    Checksum:iC27FCA3BDFA0D1EF
    GO
    Isoform 3 (identifier: Q16827-3) [UniParc]FASTAAdd to Basket

    Also known as: PTPROt

    The sequence of this isoform differs from the canonical sequence as follows:
         1-811: Missing.

    Note: Predominantly expressed in B-lymphoid tissues.

    Show »
    Length:405
    Mass (Da):47,163
    Checksum:iD7BED5FFF7312782
    GO
    Isoform 4 (identifier: Q16827-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-811: Missing.
         876-903: Missing.

    Show »
    Length:377
    Mass (Da):43,760
    Checksum:i42E10120DBF2D1EF
    GO
    Isoform 5 (identifier: Q16827-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         594-597: RIAN → VIFP
         598-1216: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:597
    Mass (Da):67,672
    Checksum:iC0B2674199E893AA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591E → G in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti159 – 1591E → G in AAA82892. (PubMed:7665166)Curated
    Sequence conflicti196 – 1961S → C in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti205 – 2051L → V in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti314 – 3141V → F in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti441 – 4411V → F in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti672 – 6721A → T in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti698 – 6981I → T in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti705 – 7051A → T in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti753 – 7531E → K in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti756 – 7583CQQ → FQH in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti775 – 7751S → P in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti790 – 7901N → S in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti861 – 8633VNF → ANC in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti876 – 8761W → C in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti876 – 8761W → C in AAA82892. (PubMed:7665166)Curated
    Sequence conflicti896 – 8961L → P in CAA88425. (PubMed:7753550)Curated
    Sequence conflicti896 – 8961L → P in AAA82892. (PubMed:7665166)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 811811Missing in isoform 3 and isoform 4. 2 PublicationsVSP_043136Add
    BLAST
    Alternative sequencei594 – 5974RIAN → VIFP in isoform 5. 1 PublicationVSP_054481
    Alternative sequencei598 – 1216619Missing in isoform 5. 1 PublicationVSP_054482Add
    BLAST
    Alternative sequencei876 – 90328Missing in isoform 2 and isoform 4. 3 PublicationsVSP_035586Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48541 mRNA. Translation: CAA88425.1.
    U20489 mRNA. Translation: AAA82892.1.
    AF187043 mRNA. Translation: AAF04086.1.
    AF187044 mRNA. Translation: AAF04087.1.
    AK290982 mRNA. Translation: BAF83671.1.
    AC007542 Genomic DNA. No translation available.
    AC022334 Genomic DNA. No translation available.
    AC092183 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96349.1.
    CH471094 Genomic DNA. Translation: EAW96350.1.
    CH471094 Genomic DNA. Translation: EAW96351.1.
    BC035960 mRNA. Translation: AAH35960.1.
    BC126201 mRNA. Translation: AAI26202.1.
    BC126203 mRNA. Translation: AAI26204.1.
    CCDSiCCDS44837.1. [Q16827-3]
    CCDS53754.1. [Q16827-4]
    CCDS8674.1. [Q16827-2]
    CCDS8675.1. [Q16827-1]
    PIRiA57064.
    S60613.
    RefSeqiNP_002839.1. NM_002848.3. [Q16827-2]
    NP_109592.1. NM_030667.2. [Q16827-1]
    NP_109593.1. NM_030668.2. [Q16827-4]
    NP_109594.1. NM_030669.2. [Q16827-3]
    NP_109595.1. NM_030670.2. [Q16827-4]
    NP_109596.1. NM_030671.2. [Q16827-3]
    UniGeneiHs.160871.

    Genome annotation databases

    EnsembliENST00000281171; ENSP00000281171; ENSG00000151490. [Q16827-1]
    ENST00000348962; ENSP00000343434; ENSG00000151490. [Q16827-2]
    ENST00000442921; ENSP00000404188; ENSG00000151490. [Q16827-3]
    ENST00000445537; ENSP00000393449; ENSG00000151490. [Q16827-3]
    ENST00000542557; ENSP00000437571; ENSG00000151490. [Q16827-4]
    ENST00000543886; ENSP00000444173; ENSG00000151490. [Q16827-5]
    ENST00000544244; ENSP00000439234; ENSG00000151490. [Q16827-4]
    GeneIDi5800.
    KEGGihsa:5800.
    UCSCiuc001rcv.2. human. [Q16827-1]
    uc001rcw.2. human. [Q16827-2]
    uc001rcx.2. human. [Q16827-3]
    uc001rcz.2. human. [Q16827-4]

    Polymorphism databases

    DMDMi209572663.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48541 mRNA. Translation: CAA88425.1 .
    U20489 mRNA. Translation: AAA82892.1 .
    AF187043 mRNA. Translation: AAF04086.1 .
    AF187044 mRNA. Translation: AAF04087.1 .
    AK290982 mRNA. Translation: BAF83671.1 .
    AC007542 Genomic DNA. No translation available.
    AC022334 Genomic DNA. No translation available.
    AC092183 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96349.1 .
    CH471094 Genomic DNA. Translation: EAW96350.1 .
    CH471094 Genomic DNA. Translation: EAW96351.1 .
    BC035960 mRNA. Translation: AAH35960.1 .
    BC126201 mRNA. Translation: AAI26202.1 .
    BC126203 mRNA. Translation: AAI26204.1 .
    CCDSi CCDS44837.1. [Q16827-3 ]
    CCDS53754.1. [Q16827-4 ]
    CCDS8674.1. [Q16827-2 ]
    CCDS8675.1. [Q16827-1 ]
    PIRi A57064.
    S60613.
    RefSeqi NP_002839.1. NM_002848.3. [Q16827-2 ]
    NP_109592.1. NM_030667.2. [Q16827-1 ]
    NP_109593.1. NM_030668.2. [Q16827-4 ]
    NP_109594.1. NM_030669.2. [Q16827-3 ]
    NP_109595.1. NM_030670.2. [Q16827-4 ]
    NP_109596.1. NM_030671.2. [Q16827-3 ]
    UniGenei Hs.160871.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G59 X-ray 2.19 A/B 914-1200 [» ]
    2GJT X-ray 2.15 A/B 916-1208 [» ]
    ProteinModelPortali Q16827.
    SMRi Q16827. Positions 916-1208.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111764. 7 interactions.
    IntActi Q16827. 25 interactions.
    MINTi MINT-1415956.
    STRINGi 9606.ENSP00000281171.

    PTM databases

    PhosphoSitei Q16827.

    Polymorphism databases

    DMDMi 209572663.

    Proteomic databases

    MaxQBi Q16827.
    PaxDbi Q16827.
    PRIDEi Q16827.

    Protocols and materials databases

    DNASUi 5800.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000281171 ; ENSP00000281171 ; ENSG00000151490 . [Q16827-1 ]
    ENST00000348962 ; ENSP00000343434 ; ENSG00000151490 . [Q16827-2 ]
    ENST00000442921 ; ENSP00000404188 ; ENSG00000151490 . [Q16827-3 ]
    ENST00000445537 ; ENSP00000393449 ; ENSG00000151490 . [Q16827-3 ]
    ENST00000542557 ; ENSP00000437571 ; ENSG00000151490 . [Q16827-4 ]
    ENST00000543886 ; ENSP00000444173 ; ENSG00000151490 . [Q16827-5 ]
    ENST00000544244 ; ENSP00000439234 ; ENSG00000151490 . [Q16827-4 ]
    GeneIDi 5800.
    KEGGi hsa:5800.
    UCSCi uc001rcv.2. human. [Q16827-1 ]
    uc001rcw.2. human. [Q16827-2 ]
    uc001rcx.2. human. [Q16827-3 ]
    uc001rcz.2. human. [Q16827-4 ]

    Organism-specific databases

    CTDi 5800.
    GeneCardsi GC12P015375.
    HGNCi HGNC:9678. PTPRO.
    HPAi HPA034525.
    MIMi 600579. gene.
    614196. phenotype.
    neXtProti NX_Q16827.
    Orphaneti 93214. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial proliferation.
    93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
    93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
    93216. Familial idiopathic steroid-resistant nephrotic syndrome with minimal changes.
    PharmGKBi PA34023.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000243992.
    HOVERGENi HBG053763.
    InParanoidi Q16827.
    KOi K18035.
    OMAi STMVTEM.
    OrthoDBi EOG7PCJFZ.
    PhylomeDBi Q16827.
    TreeFami TF351926.

    Miscellaneous databases

    EvolutionaryTracei Q16827.
    GeneWikii PTPRO.
    GenomeRNAii 5800.
    NextBioi 22592.
    PROi Q16827.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16827.
    Bgeei Q16827.
    CleanExi HS_PTPRO.
    Genevestigatori Q16827.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.190.10. 1 hit.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00041. fn3. 2 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 4 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50853. FN3. 5 hits.
    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, expression and chromosomal localization of a novel gene for protein tyrosine phosphatase (PTP-U2) induced by various differentiation-inducing agents."
      Seimiya H., Sawabe T., Inazawa J., Tsuruo T.
      Oncogene 10:1731-1738(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. "Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein tyrosine phosphatase: characterization of the GLEPP1 protein distribution in human kidney and assignment of the GLEPP1 gene to human chromosome 12p12-p13."
      Wiggins R.C., Wiggins J.E., Goyal M., Wharram B.L., Thomas P.E.
      Genomics 27:174-181(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Kidney.
    3. "PTPROt: an alternatively spliced and developmentally regulated B-lymphoid phosphatase that promotes G0/G1 arrest."
      Aguiar R.C., Yakushijin Y., Kharbanda S., Tiwari S., Freeman G.J., Shipp M.A.
      Blood 94:2403-2413(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY.
    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] (ISOFORM 4).
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 5).
      Tissue: Brain and Kidney.
    8. Cited for: INVOLVEMENT IN NPHS6.
    9. "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 (2.15 ANGSTROMS) OF 916-1208, FUNCTION.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 914-1200.

    Entry informationi

    Entry nameiPTPRO_HUMAN
    AccessioniPrimary (citable) accession number: Q16827
    Secondary accession number(s): A0AV39
    , Q13101, Q8IYG3, Q9UBF0, Q9UBT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 138 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 12
      Human chromosome 12: 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