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Database: UniProt
Entry: Q99952
LinkDB: Q99952
Original site: Q99952 
ID   PTN18_HUMAN             Reviewed;         460 AA.
AC   Q99952; B4E1E6; Q53P42;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   19-MAR-2014, entry version 122.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 18;
DE            EC=3.1.3.48;
DE   AltName: Full=Brain-derived phosphatase;
GN   Name=PTPN18; Synonyms=BDP1;
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), TISSUE SPECIFICITY, AND
RP   CHARACTERIZATION.
RC   TISSUE=Brain;
RX   PubMed=8950995;
RA   Kim Y.W., Wang H.-Y., Sures I., Lammers R., Martell K.J., Ullrich A.;
RT   "Characterization of the PEST family protein tyrosine phosphatase
RT   BDP1.";
RL   Oncogene 13:2275-2279(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 6-299.
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: Differentially dephosphorylate autophosphorylated
CC       tyrosine kinases which are known to be overexpressed in tumor
CC       tissues.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with PSTPIP1 (By similarity).
CC   -!- INTERACTION:
CC       O43586:PSTPIP1; NbExp=4; IntAct=EBI-1384210, EBI-1050964;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99952-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99952-2; Sequence=VSP_043073;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, colon and several tumor-
CC       derived cell lines.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class 4 subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; X79568; CAA56105.1; -; mRNA.
DR   EMBL; AK303804; BAG64758.1; -; mRNA.
DR   EMBL; AC132479; AAY24077.1; -; Genomic_DNA.
DR   EMBL; CH471263; EAW55618.1; -; Genomic_DNA.
DR   EMBL; CH471263; EAW55619.1; -; Genomic_DNA.
DR   RefSeq; NP_001135842.1; NM_001142370.1.
DR   RefSeq; NP_055184.2; NM_014369.3.
DR   UniGene; Hs.516390; -.
DR   UniGene; Hs.744861; -.
DR   PDB; 2OC3; X-ray; 1.50 A; A=6-299.
DR   PDB; 4GFU; X-ray; 2.00 A; A=6-300.
DR   PDB; 4GFV; X-ray; 2.10 A; A/B=6-300.
DR   PDBsum; 2OC3; -.
DR   PDBsum; 4GFU; -.
DR   PDBsum; 4GFV; -.
DR   ProteinModelPortal; Q99952; -.
DR   SMR; Q99952; 6-293.
DR   BioGrid; 117693; 2.
DR   IntAct; Q99952; 4.
DR   MINT; MINT-2815851; -.
DR   STRING; 9606.ENSP00000175756; -.
DR   PhosphoSite; Q99952; -.
DR   DMDM; 215273871; -.
DR   PaxDb; Q99952; -.
DR   PRIDE; Q99952; -.
DR   DNASU; 26469; -.
DR   Ensembl; ENST00000175756; ENSP00000175756; ENSG00000072135. [Q99952-1]
DR   Ensembl; ENST00000347849; ENSP00000310092; ENSG00000072135. [Q99952-2]
DR   GeneID; 26469; -.
DR   KEGG; hsa:26469; -.
DR   UCSC; uc002trb.3; human. [Q99952-2]
DR   UCSC; uc002trc.3; human. [Q99952-1]
DR   CTD; 26469; -.
DR   GeneCards; GC02P131113; -.
DR   HGNC; HGNC:9649; PTPN18.
DR   HPA; CAB012174; -.
DR   HPA; HPA053367; -.
DR   MIM; 606587; gene.
DR   neXtProt; NX_Q99952; -.
DR   PharmGKB; PA33991; -.
DR   eggNOG; COG5599; -.
DR   HOGENOM; HOG000115776; -.
DR   HOVERGEN; HBG053419; -.
DR   InParanoid; Q99952; -.
DR   KO; K01104; -.
DR   OMA; NCAPLYD; -.
DR   OrthoDB; EOG744T8Z; -.
DR   PhylomeDB; Q99952; -.
DR   TreeFam; TF351977; -.
DR   ChiTaRS; PTPN18; human.
DR   EvolutionaryTrace; Q99952; -.
DR   GeneWiki; PTPN18; -.
DR   GenomeRNAi; 26469; -.
DR   NextBio; 48711; -.
DR   PRO; PR:Q99952; -.
DR   ArrayExpress; Q99952; -.
DR   Bgee; Q99952; -.
DR   CleanEx; HS_BDP1; -.
DR   CleanEx; HS_PTPN18; -.
DR   Genevestigator; Q99952; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 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; Alternative splicing; Complete proteome; Cytoplasm;
KW   Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN         1    460       Tyrosine-protein phosphatase non-receptor
FT                                type 18.
FT                                /FTId=PRO_0000094773.
FT   DOMAIN       26    291       Tyrosine-protein phosphatase.
FT   REGION      229    235       Substrate binding (By similarity).
FT   ACT_SITE    229    229       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     197    197       Substrate (By similarity).
FT   BINDING     276    276       Substrate (By similarity).
FT   MOD_RES     389    389       Phosphotyrosine (By similarity).
FT   MOD_RES     426    426       Phosphotyrosine (By similarity).
FT   VAR_SEQ      32    138       Missing (in isoform 2).
FT                                /FTId=VSP_043073.
FT   VARIANT     193    193       M -> V (in dbSNP:rs3739124).
FT                                /FTId=VAR_047651.
FT   CONFLICT    356    357       VV -> EE (in Ref. 1; CAA56105).
FT   CONFLICT    378    379       Missing (in Ref. 1; CAA56105).
FT   HELIX        11     14
FT   HELIX        20     22
FT   HELIX        25     43
FT   HELIX        49     52
FT   TURN         54     56
FT   HELIX        57     59
FT   HELIX        69     71
FT   STRAND       72     74
FT   HELIX        79     81
FT   STRAND       85     93
FT   STRAND       97    104
FT   HELIX       109    111
FT   HELIX       112    121
FT   STRAND      126    129
FT   STRAND      133    135
FT   STRAND      152    154
FT   STRAND      157    168
FT   STRAND      171    180
FT   STRAND      183    192
FT   STRAND      197    199
FT   HELIX       205    218
FT   STRAND      225    228
FT   STRAND      230    233
FT   HELIX       234    250
FT   HELIX       260    268
FT   HELIX       278    292
SQ   SEQUENCE   460 AA;  50482 MW;  67ED24A0504D1883 CRC64;
     MSRSLDSARS FLERLEARGG REGAVLAGEF SDIQACSAAW KADGVCSTVA GSRPENVRKN
     RYKDVLPYDQ TRVILSLLQE EGHSDYINGN FIRGVDGSLA YIATQGPLPH TLLDFWRLVW
     EFGVKVILMA CREIENGRKR CERYWAQEQE PLQTGLFCIT LIKEKWLNED IMLRTLKVTF
     QKESRSVYQL QYMSWPDRGV PSSPDHMLAM VEEARRLQGS GPEPLCVHCS AGCGRTGVLC
     TVDYVRQLLL TQMIPPDFSL FDVVLKMRKQ RPAAVQTEEQ YRFLYHTVAQ MFCSTLQNAS
     PHYQNIKENC APLYDDALFL RTPQALLAIP RPPGGVLRSI SVPGSPGHAM ADTYAVVQKR
     GAPAGAGSGT QTGTGTGTGA RSAEEAPLYS KVTPRAQRPG AHAEDARGTL PGRVPADQSP
     AGSGAYEDVA GGAQTGGLGF NLRIGRPKGP RDPPAEWTRV
//
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