Full text data of PTPN9
PTPN9
[Confidence: low (only semi-automatic identification from reviews)]
Tyrosine-protein phosphatase non-receptor type 9; 3.1.3.48 (Protein-tyrosine phosphatase MEG2; PTPase MEG2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tyrosine-protein phosphatase non-receptor type 9; 3.1.3.48 (Protein-tyrosine phosphatase MEG2; PTPase MEG2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P43378
ID PTN9_HUMAN Reviewed; 593 AA.
AC P43378; Q53XR9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 9;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase MEG2;
DE Short=PTPase MEG2;
GN Name=PTPN9;
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].
RC TISSUE=Placenta;
RX PubMed=1557404; DOI=10.1073/pnas.89.7.2980;
RA Gu M., Warshawsky I., Majerus P.W.;
RT "Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-
RT phosphatase with sequence homology to retinaldehyde-binding protein
RT and yeast SEC14p.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2980-2984(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-582, AND FUNCTION.
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).
CC -!- FUNCTION: Protein-tyrosine phosphatase that could participate in
CC the transfer of hydrophobic ligands or in functions of the Golgi
CC apparatus.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- INTERACTION:
CC P10912:GHR; NbExp=2; IntAct=EBI-742898, EBI-286316;
CC P46459:NSF; NbExp=2; IntAct=EBI-742898, EBI-712251;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class 3 subfamily.
CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M83738; AAA60226.1; -; mRNA.
DR EMBL; BT007405; AAP36073.1; -; mRNA.
DR EMBL; BC010863; AAH10863.1; -; mRNA.
DR PIR; A42690; A42690.
DR RefSeq; NP_002824.1; NM_002833.3.
DR UniGene; Hs.445775; -.
DR PDB; 2PA5; X-ray; 1.60 A; A/B=277-582.
DR PDB; 4GE2; X-ray; 1.80 A; A/B=277-582.
DR PDB; 4GE5; X-ray; 2.00 A; A/B=277-582.
DR PDB; 4GE6; X-ray; 1.40 A; A/B=277-582.
DR PDBsum; 2PA5; -.
DR PDBsum; 4GE2; -.
DR PDBsum; 4GE5; -.
DR PDBsum; 4GE6; -.
DR ProteinModelPortal; P43378; -.
DR SMR; P43378; 48-237, 277-583.
DR IntAct; P43378; 7.
DR MINT; MINT-1455219; -.
DR STRING; 9606.ENSP00000303554; -.
DR BindingDB; P43378; -.
DR ChEMBL; CHEMBL6117; -.
DR PhosphoSite; P43378; -.
DR DMDM; 1172724; -.
DR PaxDb; P43378; -.
DR PRIDE; P43378; -.
DR DNASU; 5780; -.
DR Ensembl; ENST00000306726; ENSP00000303554; ENSG00000169410.
DR GeneID; 5780; -.
DR KEGG; hsa:5780; -.
DR UCSC; uc002bal.3; human.
DR CTD; 5780; -.
DR GeneCards; GC15M075759; -.
DR HGNC; HGNC:9661; PTPN9.
DR HPA; HPA041922; -.
DR MIM; 600768; gene.
DR neXtProt; NX_P43378; -.
DR PharmGKB; PA34005; -.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000006971; -.
DR HOVERGEN; HBG006880; -.
DR InParanoid; P43378; -.
DR KO; K01104; -.
DR OMA; MTTRFEE; -.
DR OrthoDB; EOG79GT5R; -.
DR PhylomeDB; P43378; -.
DR ChiTaRS; PTPN9; human.
DR EvolutionaryTrace; P43378; -.
DR GeneWiki; PTPN9; -.
DR GenomeRNAi; 5780; -.
DR NextBio; 22478; -.
DR PRO; PR:P43378; -.
DR ArrayExpress; P43378; -.
DR Bgee; P43378; -.
DR CleanEx; HS_PTPN9; -.
DR Genevestigator; P43378; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1 593 Tyrosine-protein phosphatase non-receptor
FT type 9.
FT /FTId=PRO_0000094764.
FT DOMAIN 84 243 CRAL-TRIO.
FT DOMAIN 303 574 Tyrosine-protein phosphatase.
FT REGION 515 521 Substrate binding (By similarity).
FT ACT_SITE 515 515 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 470 470 Substrate (By similarity).
FT BINDING 559 559 Substrate (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT HELIX 288 312
FT HELIX 320 323
FT TURN 325 327
FT HELIX 328 330
FT TURN 340 342
FT STRAND 343 345
FT STRAND 350 352
FT STRAND 359 365
FT STRAND 368 375
FT HELIX 380 382
FT HELIX 383 392
FT STRAND 397 400
FT STRAND 404 406
FT STRAND 423 426
FT STRAND 429 438
FT STRAND 440 451
FT TURN 452 455
FT STRAND 456 465
FT STRAND 470 472
FT HELIX 478 497
FT STRAND 511 514
FT STRAND 516 519
FT HELIX 520 538
FT STRAND 539 541
FT HELIX 543 550
FT TURN 551 553
FT HELIX 561 577
SQ SEQUENCE 593 AA; 68020 MW; 9BD75A5A986DDA0B CRC64;
MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR
AIELFHSYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH
KSVQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP
ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK
IDLATWNFQF LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNARQK
QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA
SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK
DSRIRFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL
IDFLRVVRNQ QSLAVSNMGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT
LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEKEGM VSSGQNLLAV ESQ
//
ID PTN9_HUMAN Reviewed; 593 AA.
AC P43378; Q53XR9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 9;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase MEG2;
DE Short=PTPase MEG2;
GN Name=PTPN9;
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].
RC TISSUE=Placenta;
RX PubMed=1557404; DOI=10.1073/pnas.89.7.2980;
RA Gu M., Warshawsky I., Majerus P.W.;
RT "Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-
RT phosphatase with sequence homology to retinaldehyde-binding protein
RT and yeast SEC14p.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2980-2984(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-582, AND FUNCTION.
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).
CC -!- FUNCTION: Protein-tyrosine phosphatase that could participate in
CC the transfer of hydrophobic ligands or in functions of the Golgi
CC apparatus.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- INTERACTION:
CC P10912:GHR; NbExp=2; IntAct=EBI-742898, EBI-286316;
CC P46459:NSF; NbExp=2; IntAct=EBI-742898, EBI-712251;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class 3 subfamily.
CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M83738; AAA60226.1; -; mRNA.
DR EMBL; BT007405; AAP36073.1; -; mRNA.
DR EMBL; BC010863; AAH10863.1; -; mRNA.
DR PIR; A42690; A42690.
DR RefSeq; NP_002824.1; NM_002833.3.
DR UniGene; Hs.445775; -.
DR PDB; 2PA5; X-ray; 1.60 A; A/B=277-582.
DR PDB; 4GE2; X-ray; 1.80 A; A/B=277-582.
DR PDB; 4GE5; X-ray; 2.00 A; A/B=277-582.
DR PDB; 4GE6; X-ray; 1.40 A; A/B=277-582.
DR PDBsum; 2PA5; -.
DR PDBsum; 4GE2; -.
DR PDBsum; 4GE5; -.
DR PDBsum; 4GE6; -.
DR ProteinModelPortal; P43378; -.
DR SMR; P43378; 48-237, 277-583.
DR IntAct; P43378; 7.
DR MINT; MINT-1455219; -.
DR STRING; 9606.ENSP00000303554; -.
DR BindingDB; P43378; -.
DR ChEMBL; CHEMBL6117; -.
DR PhosphoSite; P43378; -.
DR DMDM; 1172724; -.
DR PaxDb; P43378; -.
DR PRIDE; P43378; -.
DR DNASU; 5780; -.
DR Ensembl; ENST00000306726; ENSP00000303554; ENSG00000169410.
DR GeneID; 5780; -.
DR KEGG; hsa:5780; -.
DR UCSC; uc002bal.3; human.
DR CTD; 5780; -.
DR GeneCards; GC15M075759; -.
DR HGNC; HGNC:9661; PTPN9.
DR HPA; HPA041922; -.
DR MIM; 600768; gene.
DR neXtProt; NX_P43378; -.
DR PharmGKB; PA34005; -.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000006971; -.
DR HOVERGEN; HBG006880; -.
DR InParanoid; P43378; -.
DR KO; K01104; -.
DR OMA; MTTRFEE; -.
DR OrthoDB; EOG79GT5R; -.
DR PhylomeDB; P43378; -.
DR ChiTaRS; PTPN9; human.
DR EvolutionaryTrace; P43378; -.
DR GeneWiki; PTPN9; -.
DR GenomeRNAi; 5780; -.
DR NextBio; 22478; -.
DR PRO; PR:P43378; -.
DR ArrayExpress; P43378; -.
DR Bgee; P43378; -.
DR CleanEx; HS_PTPN9; -.
DR Genevestigator; P43378; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1 593 Tyrosine-protein phosphatase non-receptor
FT type 9.
FT /FTId=PRO_0000094764.
FT DOMAIN 84 243 CRAL-TRIO.
FT DOMAIN 303 574 Tyrosine-protein phosphatase.
FT REGION 515 521 Substrate binding (By similarity).
FT ACT_SITE 515 515 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 470 470 Substrate (By similarity).
FT BINDING 559 559 Substrate (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT HELIX 288 312
FT HELIX 320 323
FT TURN 325 327
FT HELIX 328 330
FT TURN 340 342
FT STRAND 343 345
FT STRAND 350 352
FT STRAND 359 365
FT STRAND 368 375
FT HELIX 380 382
FT HELIX 383 392
FT STRAND 397 400
FT STRAND 404 406
FT STRAND 423 426
FT STRAND 429 438
FT STRAND 440 451
FT TURN 452 455
FT STRAND 456 465
FT STRAND 470 472
FT HELIX 478 497
FT STRAND 511 514
FT STRAND 516 519
FT HELIX 520 538
FT STRAND 539 541
FT HELIX 543 550
FT TURN 551 553
FT HELIX 561 577
SQ SEQUENCE 593 AA; 68020 MW; 9BD75A5A986DDA0B CRC64;
MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR
AIELFHSYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH
KSVQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP
ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK
IDLATWNFQF LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNARQK
QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA
SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK
DSRIRFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL
IDFLRVVRNQ QSLAVSNMGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT
LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEKEGM VSSGQNLLAV ESQ
//
MIM
600768
*RECORD*
*FIELD* NO
600768
*FIELD* TI
*600768 PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 9; PTPN9
*FIELD* TX
Gu et al. (1992) cloned a cDNA for a protein tyrosine phosphatase
read more(PTPase), which they designated MEG2, by screening libraries of the
MEG-01 megakaryocyte leukemia cell line and of human umbilical vein
endothelial cells. The MEG2 cDNA encodes a 593-amino acid protein which
has no apparent signal or transmembrane domains but does include a
C-terminal region with a catalytic domain that shows 30-40% identity
with other PTPases. The N-terminal 254 amino acids are about 28%
identical to cellular retinaldehyde binding protein-1 (RLBP1; 180090)
and 24% identical to the yeast protein SEC14p; the former is a carrier
protein for 11-cis-retinaldehyde or 11-cis-retinol found in the retina
and pineal gland, and the latter is a phosphatidylinositol transfer
protein required for protein secretion from the Golgi apparatus. Gu et
al. (1992) speculated that MEG2 may, like RLBP1 and SEC14p (601504),
participate in the transfer of hydrophobic ligands or may be involved in
Golgi-related functions. Recombinantly expressed MEG2 was shown to have
PTPase activity and an approximately 4-kb RNA was detected on Northern
blots in a variety of cell lines, indicating widespread expression of
the gene.
*FIELD* RF
1. Gu, M.; Warshawsky, I.; Majerus, P. W.: Cloning and expression
of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence
homology to retinaldehyde-binding protein and yeast SEC14p. Proc.
Nat. Acad. Sci. 89: 2980-2984, 1992.
*FIELD* CD
Alan F. Scott: 9/11/1995
*FIELD* ED
dkim: 07/23/1998
mark: 11/14/1996
mark: 9/11/1995
*RECORD*
*FIELD* NO
600768
*FIELD* TI
*600768 PROTEIN-TYROSINE PHOSPHATASE, NONRECEPTOR-TYPE, 9; PTPN9
*FIELD* TX
Gu et al. (1992) cloned a cDNA for a protein tyrosine phosphatase
read more(PTPase), which they designated MEG2, by screening libraries of the
MEG-01 megakaryocyte leukemia cell line and of human umbilical vein
endothelial cells. The MEG2 cDNA encodes a 593-amino acid protein which
has no apparent signal or transmembrane domains but does include a
C-terminal region with a catalytic domain that shows 30-40% identity
with other PTPases. The N-terminal 254 amino acids are about 28%
identical to cellular retinaldehyde binding protein-1 (RLBP1; 180090)
and 24% identical to the yeast protein SEC14p; the former is a carrier
protein for 11-cis-retinaldehyde or 11-cis-retinol found in the retina
and pineal gland, and the latter is a phosphatidylinositol transfer
protein required for protein secretion from the Golgi apparatus. Gu et
al. (1992) speculated that MEG2 may, like RLBP1 and SEC14p (601504),
participate in the transfer of hydrophobic ligands or may be involved in
Golgi-related functions. Recombinantly expressed MEG2 was shown to have
PTPase activity and an approximately 4-kb RNA was detected on Northern
blots in a variety of cell lines, indicating widespread expression of
the gene.
*FIELD* RF
1. Gu, M.; Warshawsky, I.; Majerus, P. W.: Cloning and expression
of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence
homology to retinaldehyde-binding protein and yeast SEC14p. Proc.
Nat. Acad. Sci. 89: 2980-2984, 1992.
*FIELD* CD
Alan F. Scott: 9/11/1995
*FIELD* ED
dkim: 07/23/1998
mark: 11/14/1996
mark: 9/11/1995