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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   26-NOV-2014, entry version 129.
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. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- SUBUNIT: Interacts with PSTPIP1. {ECO:0000250}.
CC   -!- INTERACTION:
CC       O43586:PSTPIP1; NbExp=4; IntAct=EBI-1384210, EBI-1050964;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}.
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. {ECO:0000269|PubMed:8950995}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class 4 subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
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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   CCDS; CCDS2161.1; -. [Q99952-1]
DR   CCDS; CCDS46410.1; -. [Q99952-2]
DR   RefSeq; NP_001135842.1; NM_001142370.1. [Q99952-2]
DR   RefSeq; NP_055184.2; NM_014369.3. [Q99952-1]
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; 7-295.
DR   BioGrid; 117693; 2.
DR   IntAct; Q99952; 5.
DR   MINT; MINT-2815851; -.
DR   STRING; 9606.ENSP00000175756; -.
DR   PhosphoSite; Q99952; -.
DR   DMDM; 215273871; -.
DR   MaxQB; Q99952; -.
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   GeneTree; ENSGT00770000120452; -.
DR   HOGENOM; HOG000115776; -.
DR   HOVERGEN; HBG053419; -.
DR   InParanoid; Q99952; -.
DR   KO; K18024; -.
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   Bgee; Q99952; -.
DR   CleanEx; HS_BDP1; -.
DR   CleanEx; HS_PTPN18; -.
DR   ExpressionAtlas; Q99952; baseline and differential.
DR   Genevestigator; Q99952; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; TAS:GOC.
DR   GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR   Gene3D; 3.90.190.10; -; 1.
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; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 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                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   REGION      229    235       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    229    229       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160,
FT                                ECO:0000255|PROSITE-ProRule:PRU10044}.
FT   BINDING     197    197       Substrate. {ECO:0000250}.
FT   BINDING     276    276       Substrate. {ECO:0000250}.
FT   MOD_RES     389    389       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     426    426       Phosphotyrosine. {ECO:0000250}.
FT   VAR_SEQ      32    138       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
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                                {ECO:0000305}.
FT   CONFLICT    378    379       Missing (in Ref. 1; CAA56105).
FT                                {ECO:0000305}.
FT   HELIX        11     14       {ECO:0000244|PDB:2OC3}.
FT   HELIX        20     22       {ECO:0000244|PDB:4GFV}.
FT   HELIX        25     43       {ECO:0000244|PDB:2OC3}.
FT   HELIX        49     52       {ECO:0000244|PDB:2OC3}.
FT   TURN         54     56       {ECO:0000244|PDB:2OC3}.
FT   HELIX        57     59       {ECO:0000244|PDB:2OC3}.
FT   HELIX        69     71       {ECO:0000244|PDB:2OC3}.
FT   STRAND       72     74       {ECO:0000244|PDB:2OC3}.
FT   HELIX        79     81       {ECO:0000244|PDB:2OC3}.
FT   STRAND       85     93       {ECO:0000244|PDB:2OC3}.
FT   STRAND       97    104       {ECO:0000244|PDB:2OC3}.
FT   HELIX       109    111       {ECO:0000244|PDB:2OC3}.
FT   HELIX       112    121       {ECO:0000244|PDB:2OC3}.
FT   STRAND      126    129       {ECO:0000244|PDB:2OC3}.
FT   STRAND      133    135       {ECO:0000244|PDB:2OC3}.
FT   STRAND      152    154       {ECO:0000244|PDB:2OC3}.
FT   STRAND      157    168       {ECO:0000244|PDB:2OC3}.
FT   STRAND      171    180       {ECO:0000244|PDB:2OC3}.
FT   STRAND      183    192       {ECO:0000244|PDB:2OC3}.
FT   STRAND      197    199       {ECO:0000244|PDB:2OC3}.
FT   HELIX       205    218       {ECO:0000244|PDB:2OC3}.
FT   STRAND      225    228       {ECO:0000244|PDB:2OC3}.
FT   STRAND      230    233       {ECO:0000244|PDB:2OC3}.
FT   HELIX       234    250       {ECO:0000244|PDB:2OC3}.
FT   HELIX       260    268       {ECO:0000244|PDB:2OC3}.
FT   HELIX       278    292       {ECO:0000244|PDB:2OC3}.
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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