Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23470

- PTPRG_HUMAN

UniProt

P23470 - PTPRG_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase gamma

Gene

PTPRG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (05 May 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Possesses tyrosine phosphatase activity.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1028 – 10281SubstrateBy similarity
    Active sitei1060 – 10601Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1104 – 11041SubstrateBy similarity
    Sitei1351 – 13511Ancestral active site

    GO - Molecular functioni

    1. identical protein binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein tyrosine phosphatase activity Source: UniProtKB
    4. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. brain development Source: Ensembl
    2. negative regulation of neuron projection development Source: Ensembl
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiP23470.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase gamma (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase gamma
    Short name:
    R-PTP-gamma
    Gene namesi
    Name:PTPRG
    Synonyms:PTPG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9671. PTPRG.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi958 – 9581R → E: Loss of dimerization; when associated with E-960. 1 Publication
    Mutagenesisi960 – 9601K → E: Loss of dimerization; when associated with E-958. 1 Publication
    Mutagenesisi1305 – 13051D → K: Loss of dimerization; when associated with K-1306. 1 Publication
    Mutagenesisi1306 – 13061D → K: Loss of dimerization; when associated with K-1305. 1 Publication

    Organism-specific databases

    PharmGKBiPA34016.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Chaini20 – 14451426Receptor-type tyrosine-protein phosphatase gammaPRO_0000025441Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi78 ↔ 2611 Publication
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi444 – 4441N-linked (GlcNAc...)1 Publication
    Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1182 – 11821Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP23470.
    PaxDbiP23470.
    PRIDEiP23470.

    PTM databases

    PhosphoSiteiP23470.

    Expressioni

    Tissue specificityi

    Found in a variety of tissues.

    Gene expression databases

    ArrayExpressiP23470.
    BgeeiP23470.
    CleanExiHS_PTPRG.
    GenevestigatoriP23470.

    Interactioni

    Subunit structurei

    Monomer; active form. Homodimer; inactive form Probable. Interacts with CNTN3, CNTN4, CNTN5 and CNTN6.2 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352222EBI-2258115,EBI-491549

    Protein-protein interaction databases

    BioGridi111757. 6 interactions.
    IntActiP23470. 22 interactions.
    MINTiMINT-1349880.
    STRINGi9606.ENSP00000418112.

    Structurei

    Secondary structure

    1
    1445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 663
    Helixi68 – 703
    Helixi71 – 744
    Helixi76 – 794
    Helixi90 – 923
    Beta strandi103 – 1064
    Beta strandi116 – 1194
    Beta strandi124 – 1274
    Beta strandi133 – 1353
    Beta strandi143 – 15210
    Beta strandi162 – 1654
    Beta strandi171 – 1799
    Turni181 – 1833
    Helixi187 – 1926
    Beta strandi197 – 20913
    Helixi212 – 2143
    Helixi215 – 2239
    Beta strandi230 – 2323
    Helixi238 – 2414
    Beta strandi249 – 2546
    Beta strandi265 – 2728
    Beta strandi274 – 2774
    Helixi278 – 2858
    Beta strandi288 – 2903
    Beta strandi299 – 3013
    Helixi831 – 86131
    Turni867 – 8704
    Helixi872 – 8776
    Helixi887 – 8893
    Beta strandi890 – 8923
    Turni899 – 9013
    Helixi902 – 9054
    Beta strandi906 – 9127
    Beta strandi915 – 9173
    Beta strandi921 – 9244
    Helixi929 – 9313
    Helixi932 – 94211
    Beta strandi946 – 9494
    Beta strandi953 – 9553
    Beta strandi967 – 9737
    Beta strandi976 – 98510
    Beta strandi987 – 99812
    Beta strandi1016 – 10238
    Beta strandi1028 – 10314
    Helixi1036 – 104712
    Beta strandi1056 – 10649
    Helixi1065 – 108218
    Beta strandi1084 – 10863
    Helixi1088 – 10958
    Turni1096 – 10983
    Helixi1106 – 112116
    Helixi1129 – 11313
    Helixi1132 – 11398
    Helixi1149 – 11579
    Beta strandi1172 – 11743
    Beta strandi1207 – 12115
    Beta strandi1219 – 12246
    Helixi1228 – 12303
    Helixi1231 – 124111
    Beta strandi1245 – 12484
    Beta strandi1270 – 12723
    Beta strandi1275 – 128612
    Beta strandi1292 – 130514
    Beta strandi1308 – 13158
    Beta strandi1318 – 13203
    Helixi1326 – 13283
    Helixi1329 – 134012
    Beta strandi1347 – 13548
    Helixi1356 – 137419
    Beta strandi1375 – 13773
    Helixi1379 – 138911
    Helixi1397 – 140812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H4VX-ray1.55A/B831-1127[»]
    2HY3X-ray2.60A/B820-1130[»]
    2NLKX-ray2.40A827-1445[»]
    2PBNX-ray1.70A820-1130[»]
    3JXHX-ray1.70C56-320[»]
    3QCBX-ray2.10A/B825-1128[»]
    3QCCX-ray2.10A/B825-1128[»]
    3QCDX-ray1.80A825-1128[»]
    3QCEX-ray2.10A/B825-1128[»]
    3QCFX-ray2.50A/B825-1128[»]
    3QCGX-ray2.05A825-1128[»]
    3QCHX-ray2.40A825-1128[»]
    3QCIX-ray2.27A825-1128[»]
    3QCJX-ray2.26A825-1128[»]
    3QCKX-ray2.05A825-1128[»]
    3QCLX-ray2.40A825-1128[»]
    3QCMX-ray2.40A/B825-1128[»]
    3QCNX-ray2.41A825-1128[»]
    ProteinModelPortaliP23470.
    SMRiP23470. Positions 58-320, 347-445, 826-1412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23470.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 736717ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini763 – 1445683CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei737 – 76226HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 321264Alpha-carbonic anhydraseAdd
    BLAST
    Domaini349 – 448100Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini848 – 1119272Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1150 – 1410261Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1060 – 10667Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000060222.
    HOVERGENiHBG053760.
    KOiK16667.
    OMAiWRGCNKI.
    OrthoDBiEOG7K6PT4.
    PhylomeDBiP23470.
    TreeFamiTF351978.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProiIPR001148. Carbonic_anhydrase_a.
    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]
    PfamiPF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23470-1) [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

    MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR     50
    RRKASGDPYW AYSGAYGPEH WVTSSVSCGG RHQSPIDILD QYARVGEEYQ 100
    ELQLDGFDNE SSNKTWMKNT GKTVAILLKD DYFVSGAGLP GRFKAEKVEF 150
    HWGHSNGSAG SEHSINGRRF PVEMQIFFYN PDDFDSFQTA ISENRIIGAM 200
    AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD LLPASLGSYY 250
    RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE 300
    YLRNNFRPQQ RLHDRVVSKS AVRDSWNHDM TDFLENPLGT EASKVCSSPP 350
    IHMKVQPLNQ TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK 400
    DSDKDLKATI SHVSPDSLYL FRVQAVCRND MRSDFSQTML FQANTTRIFQ 450
    GTRIVKTGVP TASPASSADM APISSGSSTW TSSGIPFSFV SMATGMGPSS 500
    SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT AASASKQAAR 550
    PVLATTEALA SPGPDGDSSP TKDGEGTEEG EKDEKSESED GEREHEEDGE 600
    KDSEKKEKSG VTHAAEERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA 650
    VPTDQTGGRR DAGPGLDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP 700
    MSRGDRFSED SRFITVNPAE KNTSGMISRP APGRMEWIIP LIVVSALTFV 750
    CLILLIAVLV YWRGCNKIKS KGFPRRFREV PSSGERGEKG SRKCFQTAHF 800
    YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHIGEL YSNNQHGFSE 850
    DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD 900
    SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI 950
    TNLVEKGRRK CDQYWPTENS EEYGNIIVTL KSTKIHACYT VRRFSIRNTK 1000
    VKKGQKGNPK GRQNERVVIQ YHYTQWPDMG VPEYALPVLT FVRRSSAARM 1050
    PETGPVLVHC SAGVGRTGTY IVIDSMLQQI KDKSTVNVLG FLKHIRTQRN 1100
    YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL IPGVGGKTRL 1150
    EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM 1200
    KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP 1250
    DNQSLAEDEF VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL 1300
    EATQDDYVLE VRHFQCPKWP NPDAPISSTF ELINVIKEEA LTRDGPTIVH 1350
    DEYGAVSAGM LCALTTLSQQ LENENAVDVF QVAKMINLMR PGVFTDIEQY 1400
    QFIYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES MESLV 1445
    Length:1,445
    Mass (Da):162,003
    Last modified:May 5, 2009 - v4
    Checksum:iA48A007BA14082BC
    GO
    Isoform 2 (identifier: P23470-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         764-792: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,416
    Mass (Da):158,771
    Checksum:i8DFA46915A799CFD
    GO

    Sequence cautioni

    The sequence BAD93108.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801G → S in AAA60224. (PubMed:8382771)Curated
    Sequence conflicti549 – 5491A → V in AAC50439. (PubMed:8833149)Curated
    Sequence conflicti756 – 7561I → T in AAC50439. (PubMed:8833149)Curated
    Sequence conflicti805 – 8051S → R in CAH18125. (PubMed:17974005)Curated
    Sequence conflicti1316 – 13161C → Y in CAH18125. (PubMed:17974005)Curated
    Sequence conflicti1407 – 14071M → R in AAA60224. (PubMed:8382771)Curated
    Sequence conflicti1407 – 14071M → R in AAC50439. (PubMed:8833149)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921Y → H.2 Publications
    Corresponds to variant rs62620047 [ dbSNP | Ensembl ].
    VAR_070892
    Natural varianti574 – 5741G → S.
    Corresponds to variant rs2292245 [ dbSNP | Ensembl ].
    VAR_020301
    Natural varianti639 – 6391Q → R.
    Corresponds to variant rs9870460 [ dbSNP | Ensembl ].
    VAR_031562

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei764 – 79229Missing in isoform 2. 2 PublicationsVSP_024353Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09247 mRNA. Translation: AAA60224.1.
    U46116
    , U46089, U46090, U46091, U46092, U46093, U46094, U46095, U46096, U46097, U46098, U46099, U46100, U46101, U46102, U46103, U46104, U46105, U46106, U46107, U46108, U46109, U46110, U46111, U46112, U46113, U46114, U46115 Genomic DNA. Translation: AAC50439.1.
    AB209871 mRNA. Translation: BAD93108.1. Different initiation.
    AC004695 Genomic DNA. No translation available.
    AC092502 Genomic DNA. No translation available.
    AC096919 Genomic DNA. No translation available.
    AC098482 Genomic DNA. No translation available.
    AC103587 Genomic DNA. No translation available.
    AC103921 Genomic DNA. No translation available.
    AC104849 Genomic DNA. No translation available.
    AC105939 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65397.1.
    BC140904 mRNA. Translation: AAI40905.1.
    BC144110 mRNA. Translation: AAI44111.1.
    CR749269 mRNA. Translation: CAH18125.1.
    X54132 mRNA. Translation: CAA38067.1.
    CCDSiCCDS2895.1. [P23470-1]
    PIRiA48148.
    RefSeqiNP_002832.3. NM_002841.3. [P23470-1]
    XP_005265410.1. XM_005265353.2. [P23470-2]
    UniGeneiHs.595541.

    Genome annotation databases

    EnsembliENST00000295874; ENSP00000295874; ENSG00000144724. [P23470-2]
    ENST00000474889; ENSP00000418112; ENSG00000144724. [P23470-1]
    GeneIDi5793.
    KEGGihsa:5793.
    UCSCiuc003dlb.3. human. [P23470-1]
    uc003dlc.3. human. [P23470-2]

    Polymorphism databases

    DMDMi229463033.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    L09247 mRNA. Translation: AAA60224.1 .
    U46116
    , U46089 , U46090 , U46091 , U46092 , U46093 , U46094 , U46095 , U46096 , U46097 , U46098 , U46099 , U46100 , U46101 , U46102 , U46103 , U46104 , U46105 , U46106 , U46107 , U46108 , U46109 , U46110 , U46111 , U46112 , U46113 , U46114 , U46115 Genomic DNA. Translation: AAC50439.1 .
    AB209871 mRNA. Translation: BAD93108.1 . Different initiation.
    AC004695 Genomic DNA. No translation available.
    AC092502 Genomic DNA. No translation available.
    AC096919 Genomic DNA. No translation available.
    AC098482 Genomic DNA. No translation available.
    AC103587 Genomic DNA. No translation available.
    AC103921 Genomic DNA. No translation available.
    AC104849 Genomic DNA. No translation available.
    AC105939 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65397.1 .
    BC140904 mRNA. Translation: AAI40905.1 .
    BC144110 mRNA. Translation: AAI44111.1 .
    CR749269 mRNA. Translation: CAH18125.1 .
    X54132 mRNA. Translation: CAA38067.1 .
    CCDSi CCDS2895.1. [P23470-1 ]
    PIRi A48148.
    RefSeqi NP_002832.3. NM_002841.3. [P23470-1 ]
    XP_005265410.1. XM_005265353.2. [P23470-2 ]
    UniGenei Hs.595541.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H4V X-ray 1.55 A/B 831-1127 [» ]
    2HY3 X-ray 2.60 A/B 820-1130 [» ]
    2NLK X-ray 2.40 A 827-1445 [» ]
    2PBN X-ray 1.70 A 820-1130 [» ]
    3JXH X-ray 1.70 C 56-320 [» ]
    3QCB X-ray 2.10 A/B 825-1128 [» ]
    3QCC X-ray 2.10 A/B 825-1128 [» ]
    3QCD X-ray 1.80 A 825-1128 [» ]
    3QCE X-ray 2.10 A/B 825-1128 [» ]
    3QCF X-ray 2.50 A/B 825-1128 [» ]
    3QCG X-ray 2.05 A 825-1128 [» ]
    3QCH X-ray 2.40 A 825-1128 [» ]
    3QCI X-ray 2.27 A 825-1128 [» ]
    3QCJ X-ray 2.26 A 825-1128 [» ]
    3QCK X-ray 2.05 A 825-1128 [» ]
    3QCL X-ray 2.40 A 825-1128 [» ]
    3QCM X-ray 2.40 A/B 825-1128 [» ]
    3QCN X-ray 2.41 A 825-1128 [» ]
    ProteinModelPortali P23470.
    SMRi P23470. Positions 58-320, 347-445, 826-1412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111757. 6 interactions.
    IntActi P23470. 22 interactions.
    MINTi MINT-1349880.
    STRINGi 9606.ENSP00000418112.

    Chemistry

    BindingDBi P23470.
    ChEMBLi CHEMBL4905.

    PTM databases

    PhosphoSitei P23470.

    Polymorphism databases

    DMDMi 229463033.

    Proteomic databases

    MaxQBi P23470.
    PaxDbi P23470.
    PRIDEi P23470.

    Protocols and materials databases

    DNASUi 5793.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295874 ; ENSP00000295874 ; ENSG00000144724 . [P23470-2 ]
    ENST00000474889 ; ENSP00000418112 ; ENSG00000144724 . [P23470-1 ]
    GeneIDi 5793.
    KEGGi hsa:5793.
    UCSCi uc003dlb.3. human. [P23470-1 ]
    uc003dlc.3. human. [P23470-2 ]

    Organism-specific databases

    CTDi 5793.
    GeneCardsi GC03P061522.
    H-InvDB HIX0024329.
    HGNCi HGNC:9671. PTPRG.
    MIMi 176886. gene.
    neXtProti NX_P23470.
    PharmGKBi PA34016.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000060222.
    HOVERGENi HBG053760.
    KOi K16667.
    OMAi WRGCNKI.
    OrthoDBi EOG7K6PT4.
    PhylomeDBi P23470.
    TreeFami TF351978.

    Enzyme and pathway databases

    SignaLinki P23470.

    Miscellaneous databases

    ChiTaRSi PTPRG. human.
    EvolutionaryTracei P23470.
    GeneWikii PTPRG.
    GenomeRNAii 5793.
    NextBioi 22556.
    PROi P23470.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23470.
    Bgeei P23470.
    CleanExi HS_PTPRG.
    Genevestigatori P23470.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProi IPR001148. Carbonic_anhydrase_a.
    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 PF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases."
      Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D., D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K., Musacchio J.M., Sap J., Schlessinger J.
      Mol. Cell. Biol. 13:1497-1506(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure of the human receptor tyrosine phosphatase gamma gene (PTPRG) and relation to the familial RCC t(3;8) chromosome translocation."
      Kastury K., Ohta M., Lasota J., Moir D., Dorman T., Laforgia S., Druck T., Huebner K.
      Genomics 32:225-235(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-92.
    3. 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).
      Tissue: Aortic endothelium.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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] (ISOFORMS 1 AND 2), VARIANT HIS-92.
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-1445 (ISOFORM 2).
      Tissue: Prostate.
    8. "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] OF 836-1445.
      Tissue: Placenta.
    9. "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain."
      Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G., Jaye M., Schlessinger J.
      Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-1118 AND 1175-1409.
      Tissue: Brain.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113 AND ASN-444.
      Tissue: Plasma.
    11. "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-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 (2.4 ANGSTROMS) OF 827-1445, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-958; LYS-960; ASP-1305 AND ASP-1306.
    13. "Crystal structure of the human receptor phosphatase PTPRG."
      Structural genomics consortium (SGC)
      Submitted (JUL-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 830-1127.
    14. "Structural genomics of protein phosphatases."
      New York structural genomix research consortium (NYSGXRC)
      Submitted (MAR-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 819-1130.
    15. "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
      Bouyain S., Watkins D.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 56-320, INTERACTION WITH CNTN3; CNTN4; CNTN5 AND CNTN6, DISULFIDE BOND.

    Entry informationi

    Entry nameiPTPRG_HUMAN
    AccessioniPrimary (citable) accession number: P23470
    Secondary accession number(s): B2RU12
    , B7ZLX5, Q15623, Q59EE0, Q68DU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 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 3
      Human chromosome 3: 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

    Dasty 3