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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: PTPRG_HUMAN Q49A02_HUMAN
LinkDB: PTPRG_HUMAN Q49A02_HUMAN
Original site: PTPRG_HUMAN Q49A02_HUMAN 
ID   PTPRG_HUMAN             Reviewed;        1445 AA.
AC   P23470; B2RU12; B7ZLX5; Q15623; Q59EE0; Q68DU5;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 4.
DT   29-OCT-2014, entry version 161.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase gamma;
DE            Short=Protein-tyrosine phosphatase gamma;
DE            Short=R-PTP-gamma;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=PTPRG; Synonyms=PTPG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8382771;
RA   Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D.,
RA   D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K.,
RA   Musacchio J.M., Sap J., Schlessinger J.;
RT   "Identification of a carbonic anhydrase-like domain in the
RT   extracellular region of RPTP gamma defines a new subfamily of receptor
RT   tyrosine phosphatases.";
RL   Mol. Cell. Biol. 13:1497-1506(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-92.
RX   PubMed=8833149; DOI=10.1006/geno.1996.0109;
RA   Kastury K., Ohta M., Lasota J., Moir D., Dorman T., Laforgia S.,
RA   Druck T., Huebner K.;
RT   "Structure of the human receptor tyrosine phosphatase gamma gene
RT   (PTPRG) and relation to the familial RCC t(3;8) chromosome
RT   translocation.";
RL   Genomics 32:225-235(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Aortic endothelium;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   HIS-92.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-1445 (ISOFORM 2).
RC   TISSUE=Prostate;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 836-1445.
RC   TISSUE=Placenta;
RX   PubMed=2170109;
RA   Krueger N.X., Streuli M., Saito H.;
RT   "Structural diversity and evolution of human receptor-like protein
RT   tyrosine phosphatases.";
RL   EMBO J. 9:3241-3252(1990).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 874-1118 AND 1175-1409.
RC   TISSUE=Brain;
RX   PubMed=2169617; DOI=10.1073/pnas.87.18.7000;
RA   Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M.,
RA   Ricca G., Jaye M., Schlessinger J.;
RT   "Cloning of three human tyrosine phosphatases reveals a multigene
RT   family of receptor-linked protein-tyrosine-phosphatases expressed in
RT   brain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113 AND ASN-444.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 827-1445, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ARG-958; LYS-960; ASP-1305 AND
RP   ASP-1306.
RX   PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA   Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA   Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT   "Large-scale structural analysis of the classical human protein
RT   tyrosine phosphatome.";
RL   Cell 136:352-363(2009).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 830-1127.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the human receptor phosphatase PTPRG.";
RL   Submitted (JUL-2006) to the PDB data bank.
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 819-1130.
RG   New York structural genomix research consortium (NYSGXRC);
RT   "Structural genomics of protein phosphatases.";
RL   Submitted (MAR-2008) to the PDB data bank.
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 56-320, INTERACTION WITH
RP   CNTN3; CNTN4; CNTN5 AND CNTN6, AND DISULFIDE BOND.
RX   PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA   Bouyain S., Watkins D.J.;
RT   "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct
RT   members of the contactin family of neural recognition molecules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC   -!- FUNCTION: Possesses tyrosine phosphatase activity.
CC       {ECO:0000269|PubMed:19167335}.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
CC       ECO:0000269|PubMed:19167335}.
CC   -!- SUBUNIT: Monomer; active form. Homodimer; inactive form
CC       (Probable). Interacts with CNTN3, CNTN4, CNTN5 and CNTN6.
CC       {ECO:0000269|PubMed:19167335, ECO:0000269|PubMed:20133774,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       P35222:CTNNB1; NbExp=2; IntAct=EBI-2258115, EBI-491549;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P23470-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P23470-2; Sequence=VSP_024353;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Found in a variety of tissues.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 5 subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 alpha-carbonic anhydrase domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD93108.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PTPRGID41930ch3p21.html";
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DR   EMBL; L09247; AAA60224.1; -; mRNA.
DR   EMBL; U46116; AAC50439.1; -; Genomic_DNA.
DR   EMBL; U46089; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46090; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46091; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46092; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46093; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46094; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46095; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46096; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46097; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46098; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46099; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46100; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46101; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46102; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46103; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46104; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46105; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46106; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46107; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46108; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46109; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46110; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46111; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46112; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46113; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46114; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; U46115; AAC50439.1; JOINED; Genomic_DNA.
DR   EMBL; AB209871; BAD93108.1; ALT_INIT; mRNA.
DR   EMBL; AC004695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC098482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW65397.1; -; Genomic_DNA.
DR   EMBL; BC140904; AAI40905.1; -; mRNA.
DR   EMBL; BC144110; AAI44111.1; -; mRNA.
DR   EMBL; CR749269; CAH18125.1; -; mRNA.
DR   EMBL; X54132; CAA38067.1; -; mRNA.
DR   CCDS; CCDS2895.1; -. [P23470-1]
DR   PIR; A48148; A48148.
DR   RefSeq; NP_002832.3; NM_002841.3. [P23470-1]
DR   RefSeq; XP_005265410.1; XM_005265353.2. [P23470-2]
DR   UniGene; Hs.595541; -.
DR   PDB; 2H4V; X-ray; 1.55 A; A/B=831-1127.
DR   PDB; 2HY3; X-ray; 2.60 A; A/B=820-1130.
DR   PDB; 2NLK; X-ray; 2.40 A; A=827-1445.
DR   PDB; 2PBN; X-ray; 1.70 A; A=820-1130.
DR   PDB; 3JXH; X-ray; 1.70 A; C=56-320.
DR   PDB; 3QCB; X-ray; 2.10 A; A/B=825-1128.
DR   PDB; 3QCC; X-ray; 2.10 A; A/B=825-1128.
DR   PDB; 3QCD; X-ray; 1.80 A; A=825-1128.
DR   PDB; 3QCE; X-ray; 2.10 A; A/B=825-1128.
DR   PDB; 3QCF; X-ray; 2.50 A; A/B=825-1128.
DR   PDB; 3QCG; X-ray; 2.05 A; A=825-1128.
DR   PDB; 3QCH; X-ray; 2.40 A; A=825-1128.
DR   PDB; 3QCI; X-ray; 2.27 A; A=825-1128.
DR   PDB; 3QCJ; X-ray; 2.26 A; A=825-1128.
DR   PDB; 3QCK; X-ray; 2.05 A; A=825-1128.
DR   PDB; 3QCL; X-ray; 2.40 A; A=825-1128.
DR   PDB; 3QCM; X-ray; 2.40 A; A/B=825-1128.
DR   PDB; 3QCN; X-ray; 2.41 A; A=825-1128.
DR   PDBsum; 2H4V; -.
DR   PDBsum; 2HY3; -.
DR   PDBsum; 2NLK; -.
DR   PDBsum; 2PBN; -.
DR   PDBsum; 3JXH; -.
DR   PDBsum; 3QCB; -.
DR   PDBsum; 3QCC; -.
DR   PDBsum; 3QCD; -.
DR   PDBsum; 3QCE; -.
DR   PDBsum; 3QCF; -.
DR   PDBsum; 3QCG; -.
DR   PDBsum; 3QCH; -.
DR   PDBsum; 3QCI; -.
DR   PDBsum; 3QCJ; -.
DR   PDBsum; 3QCK; -.
DR   PDBsum; 3QCL; -.
DR   PDBsum; 3QCM; -.
DR   PDBsum; 3QCN; -.
DR   ProteinModelPortal; P23470; -.
DR   SMR; P23470; 58-320, 347-435, 826-1412.
DR   BioGrid; 111757; 11.
DR   IntAct; P23470; 22.
DR   MINT; MINT-1349880; -.
DR   STRING; 9606.ENSP00000418112; -.
DR   BindingDB; P23470; -.
DR   ChEMBL; CHEMBL4905; -.
DR   PhosphoSite; P23470; -.
DR   DMDM; 229463033; -.
DR   MaxQB; P23470; -.
DR   PaxDb; P23470; -.
DR   PRIDE; P23470; -.
DR   DNASU; 5793; -.
DR   Ensembl; ENST00000295874; ENSP00000295874; ENSG00000144724. [P23470-2]
DR   Ensembl; ENST00000474889; ENSP00000418112; ENSG00000144724. [P23470-1]
DR   GeneID; 5793; -.
DR   KEGG; hsa:5793; -.
DR   UCSC; uc003dlb.3; human. [P23470-1]
DR   UCSC; uc003dlc.3; human. [P23470-2]
DR   CTD; 5793; -.
DR   GeneCards; GC03P061522; -.
DR   H-InvDB; HIX0024329; -.
DR   HGNC; HGNC:9671; PTPRG.
DR   MIM; 176886; gene.
DR   neXtProt; NX_P23470; -.
DR   PharmGKB; PA34016; -.
DR   eggNOG; COG5599; -.
DR   GeneTree; ENSGT00760000118900; -.
DR   HOGENOM; HOG000060222; -.
DR   HOVERGEN; HBG053760; -.
DR   InParanoid; P23470; -.
DR   KO; K16667; -.
DR   OMA; WRGCNKI; -.
DR   OrthoDB; EOG7K6PT4; -.
DR   PhylomeDB; P23470; -.
DR   TreeFam; TF351978; -.
DR   SignaLink; P23470; -.
DR   ChiTaRS; PTPRG; human.
DR   EvolutionaryTrace; P23470; -.
DR   GeneWiki; PTPRG; -.
DR   GenomeRNAi; 5793; -.
DR   NextBio; 22556; -.
DR   PRO; PR:P23470; -.
DR   Bgee; P23470; -.
DR   CleanEx; HS_PTPRG; -.
DR   ExpressionAtlas; P23470; baseline and differential.
DR   Genevestigator; P23470; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:GOC.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.200.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 2.
DR   InterPro; IPR001148; Carbonic_anhydrase_a.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   SUPFAM; SSF52799; SSF52799; 2.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
KW   Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Polymorphism;
KW   Protein phosphatase; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19
FT   CHAIN        20   1445       Receptor-type tyrosine-protein
FT                                phosphatase gamma.
FT                                /FTId=PRO_0000025441.
FT   TOPO_DOM     20    736       Extracellular. {ECO:0000255}.
FT   TRANSMEM    737    762       Helical. {ECO:0000255}.
FT   TOPO_DOM    763   1445       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       58    321       Alpha-carbonic anhydrase.
FT   DOMAIN      349    448       Fibronectin type-III.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      848   1119       Tyrosine-protein phosphatase 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   DOMAIN     1150   1410       Tyrosine-protein phosphatase 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   REGION     1060   1066       Substrate binding. {ECO:0000250}.
FT   ACT_SITE   1060   1060       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160,
FT                                ECO:0000255|PROSITE-ProRule:PRU10044}.
FT   BINDING    1028   1028       Substrate. {ECO:0000250}.
FT   BINDING    1104   1104       Substrate. {ECO:0000250}.
FT   SITE       1351   1351       Ancestral active site.
FT   MOD_RES    1182   1182       Phosphoserine.
FT                                {ECO:0000269|PubMed:21406692}.
FT   CARBOHYD    109    109       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    113    113       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    156    156       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    444    444       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    619    619       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    631    631       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    722    722       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     78    261       {ECO:0000269|PubMed:20133774}.
FT   VAR_SEQ     764    792       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_024353.
FT   VARIANT      92     92       Y -> H (in dbSNP:rs62620047).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8833149}.
FT                                /FTId=VAR_070892.
FT   VARIANT     574    574       G -> S (in dbSNP:rs2292245).
FT                                /FTId=VAR_020301.
FT   VARIANT     639    639       Q -> R (in dbSNP:rs9870460).
FT                                /FTId=VAR_031562.
FT   MUTAGEN     958    958       R->E: Loss of dimerization; when
FT                                associated with E-960.
FT                                {ECO:0000269|PubMed:19167335}.
FT   MUTAGEN     960    960       K->E: Loss of dimerization; when
FT                                associated with E-958.
FT                                {ECO:0000269|PubMed:19167335}.
FT   MUTAGEN    1305   1305       D->K: Loss of dimerization; when
FT                                associated with K-1306.
FT                                {ECO:0000269|PubMed:19167335}.
FT   MUTAGEN    1306   1306       D->K: Loss of dimerization; when
FT                                associated with K-1305.
FT                                {ECO:0000269|PubMed:19167335}.
FT   CONFLICT     80     80       G -> S (in Ref. 1; AAA60224).
FT                                {ECO:0000305}.
FT   CONFLICT    549    549       A -> V (in Ref. 2; AAC50439).
FT                                {ECO:0000305}.
FT   CONFLICT    756    756       I -> T (in Ref. 2; AAC50439).
FT                                {ECO:0000305}.
FT   CONFLICT    805    805       S -> R (in Ref. 7; CAH18125).
FT                                {ECO:0000305}.
FT   CONFLICT   1316   1316       C -> Y (in Ref. 7; CAH18125).
FT                                {ECO:0000305}.
FT   CONFLICT   1407   1407       M -> R (in Ref. 1; AAA60224 and 2;
FT                                AAC50439). {ECO:0000305}.
FT   HELIX        64     66
FT   HELIX        68     70
FT   HELIX        71     74
FT   HELIX        76     79
FT   HELIX        90     92
FT   STRAND      103    106
FT   STRAND      116    119
FT   STRAND      124    127
FT   STRAND      133    135
FT   STRAND      143    152
FT   STRAND      162    165
FT   STRAND      171    179
FT   TURN        181    183
FT   HELIX       187    192
FT   STRAND      197    209
FT   HELIX       212    214
FT   HELIX       215    223
FT   STRAND      230    232
FT   HELIX       238    241
FT   STRAND      249    254
FT   STRAND      265    272
FT   STRAND      274    277
FT   HELIX       278    285
FT   STRAND      288    290
FT   STRAND      299    301
FT   HELIX       831    861
FT   TURN        867    870
FT   HELIX       872    877
FT   HELIX       887    889
FT   STRAND      890    892
FT   TURN        899    901
FT   HELIX       902    905
FT   STRAND      906    912
FT   STRAND      915    917
FT   STRAND      921    924
FT   HELIX       929    931
FT   HELIX       932    942
FT   STRAND      946    949
FT   STRAND      953    955
FT   STRAND      967    973
FT   STRAND      976    985
FT   STRAND      987    998
FT   STRAND     1016   1023
FT   STRAND     1028   1031
FT   HELIX      1036   1047
FT   STRAND     1056   1064
FT   HELIX      1065   1082
FT   STRAND     1084   1086
FT   HELIX      1088   1095
FT   TURN       1096   1098
FT   HELIX      1106   1121
FT   HELIX      1129   1131
FT   HELIX      1132   1139
FT   HELIX      1149   1157
FT   STRAND     1172   1174
FT   STRAND     1207   1211
FT   STRAND     1219   1224
FT   HELIX      1228   1230
FT   HELIX      1231   1241
FT   STRAND     1245   1248
FT   STRAND     1270   1272
FT   STRAND     1275   1286
FT   STRAND     1292   1305
FT   STRAND     1308   1315
FT   STRAND     1318   1320
FT   HELIX      1326   1328
FT   HELIX      1329   1340
FT   STRAND     1347   1354
FT   HELIX      1356   1374
FT   STRAND     1375   1377
FT   HELIX      1379   1389
FT   HELIX      1397   1408
SQ   SEQUENCE   1445 AA;  162003 MW;  A48A007BA14082BC CRC64;
     MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR RRKASGDPYW
     AYSGAYGPEH WVTSSVSCGG RHQSPIDILD QYARVGEEYQ ELQLDGFDNE SSNKTWMKNT
     GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSINGRRF PVEMQIFFYN
     PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD
     LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
     YLRNNFRPQQ RLHDRVVSKS AVRDSWNHDM TDFLENPLGT EASKVCSSPP IHMKVQPLNQ
     TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL
     FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
     TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT
     AASASKQAAR PVLATTEALA SPGPDGDSSP TKDGEGTEEG EKDEKSESED GEREHEEDGE
     KDSEKKEKSG VTHAAEERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA VPTDQTGGRR
     DAGPGLDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP MSRGDRFSED SRFITVNPAE
     KNTSGMISRP APGRMEWIIP LIVVSALTFV CLILLIAVLV YWRGCNKIKS KGFPRRFREV
     PSSGERGEKG SRKCFQTAHF YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHIGEL
     YSNNQHGFSE DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD
     SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI TNLVEKGRRK
     CDQYWPTENS EEYGNIIVTL KSTKIHACYT VRRFSIRNTK VKKGQKGNPK GRQNERVVIQ
     YHYTQWPDMG VPEYALPVLT FVRRSSAARM PETGPVLVHC SAGVGRTGTY IVIDSMLQQI
     KDKSTVNVLG FLKHIRTQRN YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL
     IPGVGGKTRL EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM
     KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP DNQSLAEDEF
     VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL EATQDDYVLE VRHFQCPKWP
     NPDAPISSTF ELINVIKEEA LTRDGPTIVH DEYGAVSAGM LCALTTLSQQ LENENAVDVF
     QVAKMINLMR PGVFTDIEQY QFIYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES
     MESLV
//
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Ontology (11)   
   GO (11)   
Disease (1)   
   OMIM (1)   
Drug (1)   
   CHEMBL-UP (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (10)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (5)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (43)   
   EMBL (43)   
3D Structure (18)   
   PDB (18)   
Protein domain (18)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (5)   
   SMART (3)   
Literature (11)   
   PubMed (11)   
All databases (116)   

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ID   Q49A02_HUMAN            Unreviewed;        80 AA.
AC   Q49A02;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   09-JUL-2014, entry version 44.
DE   SubName: Full=PTPRG protein;
GN   Name=PTPRG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC036018; AAH36018.1; -; mRNA.
DR   EMBL; BC048961; AAH48961.1; -; mRNA.
DR   RefSeq; NP_002832.3; NM_002841.3.
DR   UniGene; Hs.595541; -.
DR   DNASU; 5793; -.
DR   GeneID; 5793; -.
DR   KEGG; hsa:5793; -.
DR   CTD; 5793; -.
DR   KO; K16667; -.
DR   ChiTaRS; PTPRG; human.
DR   GenomeRNAi; 5793; -.
DR   NextBio; 22556; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   80 AA;  9062 MW;  CFCC975E9161F735 CRC64;
     MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR RRKASGDPYW
     AYSGFCSVAQ AGVQYTLAQS
//
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Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Literature (1)   
   PubMed (1)   
All databases (8)   

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