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Reviewed, UniProtKB/Swiss-Prot Q99952 (PTN18_HUMAN)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tyrosine-protein phosphatase non-receptor type 18
    EC=3.1.3.48
Alternative name(s):
    Brain-derived phosphatase
Gene names
Name: PTPN18
Synonyms: BDP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with PSTPIP1 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Tissue specificity

Expressed in brain, colon and several tumor-derived cell lines. Ref.1

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processprotein amino acid dephosphorylation Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnon-membrane spanning protein tyrosine phosphatase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Tyrosine-protein phosphatase non-receptor type 18
PRO_0000094773

Regions

Domain26 – 291266Tyrosine-protein phosphatase

Sites

Active site2291Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue101Phosphoserine Ref.5
Modified residue3891Phosphotyrosine Ref.4 Ref.6
Modified residue4261Phosphotyrosine By similarity

Natural variations

Natural variant1931M → V: dbSNP rs3739124.
VAR_047651

Experimental info

Sequence conflict356 – 3572VV → EE in CAA56105. Ref.1
Sequence conflict378 – 3792Missing in CAA56105. Ref.1

Secondary structure

............................................... 460
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99952-1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 67ED24A0504D1883

FASTA46050,482
        10         20         30         40         50         60 
MSRSLDSARS FLERLEARGG REGAVLAGEF SDIQACSAAW KADGVCSTVA GSRPENVRKN 

        70         80         90        100        110        120 
RYKDVLPYDQ TRVILSLLQE EGHSDYINGN FIRGVDGSLA YIATQGPLPH TLLDFWRLVW 

       130        140        150        160        170        180 
EFGVKVILMA CREIENGRKR CERYWAQEQE PLQTGLFCIT LIKEKWLNED IMLRTLKVTF 

       190        200        210        220        230        240 
QKESRSVYQL QYMSWPDRGV PSSPDHMLAM VEEARRLQGS GPEPLCVHCS AGCGRTGVLC 

       250        260        270        280        290        300 
TVDYVRQLLL TQMIPPDFSL FDVVLKMRKQ RPAAVQTEEQ YRFLYHTVAQ MFCSTLQNAS 

       310        320        330        340        350        360 
PHYQNIKENC APLYDDALFL RTPQALLAIP RPPGGVLRSI SVPGSPGHAM ADTYAVVQKR 

       370        380        390        400        410        420 
GAPAGAGSGT QTGTGTGTGA RSAEEAPLYS KVTPRAQRPG AHAEDARGTL PGRVPADQSP 

       430        440        450        460 
AGSGAYEDVA GGAQTGGLGF NLRIGRPKGP RDPPAEWTRV 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the PEST family protein tyrosine phosphatase BDP1."
Kim Y.W., Wang H.-Y., Sures I., Lammers R., Martell K.J., Ullrich A.
Oncogene 13:2275-2279(1996) [PubMed: 8950995] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION.
Tissue: Brain.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-389, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.
Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, MASS SPECTROMETRY.
Tissue: T-cell.
[6]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-389, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

X79568 mRNA. Translation: CAA56105.1.
AC132479 Genomic DNA. Translation: AAY24077.1.
CH471263 Genomic DNA. Translation: EAW55619.1.
IPIIPI00219132.
RefSeqNP_055184.2.
UniGeneHs.591549

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2OC3X-ray1.50A6-299[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ99952.

Proteomic databases

PRIDEQ99952.

Genome annotation databases

EnsemblENSG00000072135. Homo sapiens. [Contig view]
GeneID26469.
KEGGhsa:26469.

Organism-specific databases

GeneCardsGC02P130829.
H-InvDBHIX0023989.
HGNCHGNC:9649. PTPN18.
HPACAB012174.
MIM606587. gene.
PharmGKBPA33991.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ99952.
OMAQ99952. MADTYAV.

Enzyme and pathway databases

BRENDA3.1.3.48. 247.

Gene expression databases

ArrayExpressQ99952.
BgeeQ99952.
CleanExHS_BDP1.
HS_PTPN18.
GermOnlineENSG00000072135. Homo sapiens.

Family and domain databases

InterProIPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio48711.
SOURCESearch...

Entry information

Entry namePTN18_HUMAN
AccessionPrimary (citable) accession number: Q99952
Secondary accession number(s): Q53P42
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: November 25, 2008
Last modified: June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents