[1]	NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. TISSUE=Colon tumor; DOI=10.1016/S0006-291X(02)02488-9; PubMed=12408986 [NCBI, ExPASy, EBI, Israel, Japan] Hood K.L., Tobin J.F., Yoon C.; "Identification and characterization of two novel low-molecular-weight dual specificity phosphatases."; Biochem. Biophys. Res. Commun. 298:545-551(2002).
[2]	NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-73; LEU-102; CYS-104; ARG-110 AND SER-111. TISSUE=Fetal brain; DOI=10.1016/S0167-4781(02)00629-2; PubMed=12591617 [NCBI, ExPASy, EBI, Israel, Japan] Wu Q., Gu S., Dai J., Dai J., Wang L., Li Y., Zeng L., Xu J., Ye X., Zhao W., Ji C., Xie Y., Mao Y.; "Molecular cloning and characterization of a novel dual-specificity phosphatase18 gene from human fetal brain."; Biochim. Biophys. Acta 1625:296-304(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan] Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.; "A genome annotation-driven approach to cloning the human ORFeome."; Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
CATALYTIC ACTIVITY: A phosphoprotein + H₂O = a protein + phosphate.
ENZYME REGULATION: Activated by manganese ions, inhibited by iodoaretic acid.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6.0;
Temperature dependence: Optimum temperature is 55 degrees Celsius;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
TISSUE SPECIFICITY: Widely expressed with highest levels in liver, brain, ovary and testis.
SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF533017; AAN59787.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF461689; AAN77931.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456406; CAG30292.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030987; AAH30987.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_689724.3; -.

UniGene

Hs.517544

3D structure databases

PDB

2ESB; X-ray; 2.00 A; A=1-188.

[ExPASy / RCSB / EBI]

2ESB; -.

PTM databases

Q8NEJ0; -.

Organism-specific databases

HIX0017667; -.

HGNC:18484; DUSP18.

611446; gene. [NCBI / EBI]

PharmGKB

PA134928498; -.

GeneCards

Q8NEJ0.

Gene expression databases

ArrayExpress

Q8NEJ0; -.

CleanEx

HS_DUSP18; -.

GermOnline

ENSG00000167065; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0004725;	Molecular function: protein tyrosine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0008138;	Molecular function: protein tyrosine/serine/threonine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0006470;	Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR000340; Tyr_Pase_dual_specific.
Graphical view of domain structure.

Pfam

PF00782; DSPc; 1.
Pfam graphical view of domain structure.

SMART

SM00195; DSPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PS50054; TYR_PHOSPHATASE_DUAL; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8NEJ0.

Genome annotation databases

Ensembl

ENSG00000167065; Homo sapiens. [Contig view]

GeneID

150290; -.

KEGG

hsa:150290; -.

Phylogenomic databases

HOGENOM

Q8NEJ0; -.

HOVERGEN

Q8NEJ0; -.

Other

NextBio

86394; -.

SOURCE

DUSP18; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Hydrolase; Nucleus; Protein phosphatase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 188`	`188`	`Dual specificity protein phosphatase 18.`	`PRO_0000094828`
`DOMAIN`	`80 149`	`70`	`Tyrosine-protein phosphatase.`
`ACT_SITE`	`104 104`		`Phosphocysteine intermediate (By similarity).`
`MUTAGEN`	`73 73`		`D->A: Abolishes most of in vitro phosphatase activity.`
`MUTAGEN`	`102 102`		`L->V: No effect on in vitro phosphatase activity.`
`MUTAGEN`	`104 104`		`C->S: Abolishes most of in vitro phosphatase activity.`
`MUTAGEN`	`110 110`		`R->K: Abolishes most of in vitro phosphatase activity.`
`MUTAGEN`	`111 111`		`S->A: Abolishes most of in vitro phosphatase activity.`
`CONFLICT`	`2 2`		`T -> A (in Ref. 2; AAN77931).`
`STRAND`	`21 24`	`4`
`STRAND`	`27 30`	`4`
`HELIX`	`34 36`	`3`
`HELIX`	`38 43`	`6`
`STRAND`	`48 51`	`4`
`STRAND`	`65 68`	`4`
`HELIX`	`79 82`	`4`
`HELIX`	`83 95`	`13`
`STRAND`	`100 103`	`4`
`STRAND`	`105 109`	`5`
`HELIX`	`110 122`	`13`
`HELIX`	`127 137`	`11`
`HELIX`	`145 159`	`15`
`HELIX`	`176 178`	`3`

Sequence information

Length: 188 AA [This is the length of the unprocessed precursor]

Molecular weight: 21066 Da [This is the MW of the unprocessed precursor]

CRC64: A6EDECC3624F570F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAPSCAFPV QFRQPSVSGL SQITKSLYIS NGVAANNKLM LSSNQITMVI NVSVEVVNTL 

        70         80         90        100        110        120 
YEDIQYMQVP VADSPNSRLC DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM 

       130        140        150        160        170        180 
KYHAMSLLDA HTWTKSCRPI IRPNSGFWEQ LIHYEFQLFG KNTVHMVSSP VGMIPDIYEK 


EVRLMIPL

Q8NEJ0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools