PTN9_HUMAN
ID PTN9_HUMAN Reviewed; 593 AA.
AC P43378; Q53XR9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 203.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 and
RT 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 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 project:
RT 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
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 tyrosine
RT phosphatome.";
RL Cell 136:352-363(2009).
CC -!- FUNCTION: Protein-tyrosine phosphatase that could participate in the
CC transfer of hydrophobic ligands or in functions of the Golgi apparatus.
CC {ECO:0000269|PubMed:19167335}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- INTERACTION:
CC P43378; Q6RW13: AGTRAP; NbExp=5; IntAct=EBI-742898, EBI-741181;
CC P43378; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-742898, EBI-11522760;
CC P43378; Q13520: AQP6; NbExp=3; IntAct=EBI-742898, EBI-13059134;
CC P43378; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-742898, EBI-11343438;
CC P43378; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-742898, EBI-714543;
CC P43378; P18859: ATP5PF; NbExp=3; IntAct=EBI-742898, EBI-2606700;
CC P43378; Q8WZ55: BSND; NbExp=3; IntAct=EBI-742898, EBI-7996695;
CC P43378; P51861: CDR1; NbExp=3; IntAct=EBI-742898, EBI-2836538;
CC P43378; Q9HA82: CERS4; NbExp=3; IntAct=EBI-742898, EBI-2622997;
CC P43378; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-742898, EBI-17278014;
CC P43378; Q96DZ9: CMTM5; NbExp=4; IntAct=EBI-742898, EBI-2548702;
CC P43378; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-742898, EBI-11522780;
CC P43378; Q9NZJ6: COQ3; NbExp=3; IntAct=EBI-742898, EBI-10897372;
CC P43378; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-742898, EBI-18013275;
CC P43378; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-742898, EBI-6942903;
CC P43378; Q9GZP9: DERL2; NbExp=3; IntAct=EBI-742898, EBI-7962814;
CC P43378; Q15125: EBP; NbExp=3; IntAct=EBI-742898, EBI-3915253;
CC P43378; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-742898, EBI-10973142;
CC P43378; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-742898, EBI-3918971;
CC P43378; O00258: GET1; NbExp=3; IntAct=EBI-742898, EBI-18908258;
CC P43378; P10912: GHR; NbExp=2; IntAct=EBI-742898, EBI-286316;
CC P43378; P08034: GJB1; NbExp=3; IntAct=EBI-742898, EBI-17565645;
CC P43378; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-742898, EBI-3917143;
CC P43378; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-742898, EBI-1052304;
CC P43378; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-742898, EBI-18053395;
CC P43378; Q9H400: LIME1; NbExp=3; IntAct=EBI-742898, EBI-2830566;
CC P43378; Q969L2: MAL2; NbExp=4; IntAct=EBI-742898, EBI-944295;
CC P43378; P46459: NSF; NbExp=2; IntAct=EBI-742898, EBI-712251;
CC P43378; Q96AL5: PBX3; NbExp=3; IntAct=EBI-742898, EBI-741171;
CC P43378; O00623: PEX12; NbExp=3; IntAct=EBI-742898, EBI-594836;
CC P43378; O60664: PLIN3; NbExp=3; IntAct=EBI-742898, EBI-725795;
CC P43378; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-742898, EBI-14065960;
CC P43378; O95197: RTN3; NbExp=5; IntAct=EBI-742898, EBI-740467;
CC P43378; O95197-3: RTN3; NbExp=3; IntAct=EBI-742898, EBI-11525735;
CC P43378; O15126: SCAMP1; NbExp=3; IntAct=EBI-742898, EBI-954338;
CC P43378; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-742898, EBI-12243266;
CC P43378; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-742898, EBI-10262251;
CC P43378; P30825: SLC7A1; NbExp=3; IntAct=EBI-742898, EBI-4289564;
CC P43378; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-742898, EBI-10819434;
CC P43378; P08247: SYP; NbExp=3; IntAct=EBI-742898, EBI-9071725;
CC P43378; Q7Z6W1: TMCO2; NbExp=3; IntAct=EBI-742898, EBI-12807858;
CC P43378; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-742898, EBI-11742770;
CC P43378; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-742898, EBI-2548832;
CC P43378; Q9Y320: TMX2; NbExp=3; IntAct=EBI-742898, EBI-6447886;
CC P43378; O95070: YIF1A; NbExp=3; IntAct=EBI-742898, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; M83738; AAA60226.1; -; mRNA.
DR EMBL; BT007405; AAP36073.1; -; mRNA.
DR EMBL; BC010863; AAH10863.1; -; mRNA.
DR CCDS; CCDS10280.1; -.
DR PIR; A42690; A42690.
DR RefSeq; NP_002824.1; NM_002833.3.
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 PDB; 4ICZ; X-ray; 1.90 A; A=277-582.
DR PDB; 6KZQ; X-ray; 1.70 A; A=277-583.
DR PDB; 6L03; X-ray; 2.08 A; A=277-583.
DR PDBsum; 2PA5; -.
DR PDBsum; 4GE2; -.
DR PDBsum; 4GE5; -.
DR PDBsum; 4GE6; -.
DR PDBsum; 4ICZ; -.
DR PDBsum; 6KZQ; -.
DR PDBsum; 6L03; -.
DR AlphaFoldDB; P43378; -.
DR SMR; P43378; -.
DR BioGRID; 111744; 99.
DR IntAct; P43378; 55.
DR MINT; P43378; -.
DR STRING; 9606.ENSP00000482732; -.
DR BindingDB; P43378; -.
DR ChEMBL; CHEMBL6117; -.
DR DEPOD; PTPN9; -.
DR iPTMnet; P43378; -.
DR MetOSite; P43378; -.
DR PhosphoSitePlus; P43378; -.
DR BioMuta; PTPN9; -.
DR DMDM; 1172724; -.
DR EPD; P43378; -.
DR jPOST; P43378; -.
DR MassIVE; P43378; -.
DR MaxQB; P43378; -.
DR PaxDb; P43378; -.
DR PeptideAtlas; P43378; -.
DR PRIDE; P43378; -.
DR ProteomicsDB; 55630; -.
DR Antibodypedia; 27331; 128 antibodies from 29 providers.
DR DNASU; 5780; -.
DR Ensembl; ENST00000618819.5; ENSP00000482732.1; ENSG00000169410.11.
DR GeneID; 5780; -.
DR KEGG; hsa:5780; -.
DR MANE-Select; ENST00000618819.5; ENSP00000482732.1; NM_002833.4; NP_002824.1.
DR UCSC; uc002bal.5; human.
DR CTD; 5780; -.
DR DisGeNET; 5780; -.
DR GeneCards; PTPN9; -.
DR HGNC; HGNC:9661; PTPN9.
DR HPA; ENSG00000169410; Low tissue specificity.
DR MIM; 600768; gene.
DR neXtProt; NX_P43378; -.
DR OpenTargets; ENSG00000169410; -.
DR PharmGKB; PA34005; -.
DR VEuPathDB; HostDB:ENSG00000169410; -.
DR eggNOG; ENOG502QR81; Eukaryota.
DR GeneTree; ENSGT00940000157447; -.
DR InParanoid; P43378; -.
DR OMA; QWTGHPQ; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P43378; -.
DR TreeFam; TF351975; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P43378; -.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR SignaLink; P43378; -.
DR SIGNOR; P43378; -.
DR BioGRID-ORCS; 5780; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; PTPN9; human.
DR EvolutionaryTrace; P43378; -.
DR GeneWiki; PTPN9; -.
DR GenomeRNAi; 5780; -.
DR Pharos; P43378; Tchem.
DR PRO; PR:P43378; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P43378; protein.
DR Bgee; ENSG00000169410; Expressed in ventricular zone and 163 other tissues.
DR ExpressionAtlas; P43378; baseline and differential.
DR Genevisible; P43378; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00650; CRAL_TRIO; 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; SM00404; PTPc_motif; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF52799; SSF52799; 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; Cytoplasm; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..593
FT /note="Tyrosine-protein phosphatase non-receptor type 9"
FT /id="PRO_0000094764"
FT DOMAIN 84..243
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 303..574
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 515
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 515..521
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT HELIX 288..312
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:4GE6"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:4GE6"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2PA5"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 440..451
FT /evidence="ECO:0007829|PDB:4GE6"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 456..465
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 478..497
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 520..538
FT /evidence="ECO:0007829|PDB:4GE6"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:6KZQ"
FT HELIX 543..550
FT /evidence="ECO:0007829|PDB:4GE6"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:4GE6"
FT HELIX 561..577
FT /evidence="ECO:0007829|PDB:4GE6"
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
