Dual specificity protein phosphatase 18

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Reviewed, UniProtKB/Swiss-Prot Q8NEJ0 (DUS18_HUMAN)

Last modified July 7, 2009. Version 62. History...

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

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Names and origin

Protein names

Recommended name:
    Dual specificity protein phosphatase 18
    EC=3.1.3.48
    EC=3.1.3.16
Alternative name(s):
    Low molecular weight dual specificity phosphatase 20

Gene names

Name:	DUSP18
Synonyms:	LMWDSP20

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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. A phosphoprotein + H₂O = a protein + phosphate.
Enzyme regulation	Activated by manganese ions, inhibited by iodoaretic acid.
Subcellular location	Cytoplasm. Nucleus. Ref.1
Tissue specificity	Widely expressed with highest levels in liver, brain, ovary and testis. Ref.1 Ref.2
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0. Temperature dependence: Optimum temperature is 55 degrees Celsius.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 188

188

Dual specificity protein phosphatase 18

PRO_0000094828

Regions

Domain

80 – 149

Tyrosine-protein phosphatase

Sites

Active site

104

Phosphocysteine intermediate By similarity

Experimental info

Mutagenesis

D → A: Abolishes most of in vitro phosphatase activity. Ref.2

Mutagenesis

102

L → V: No effect on in vitro phosphatase activity. Ref.2

Mutagenesis

104

C → S: Abolishes most of in vitro phosphatase activity. Ref.2

Mutagenesis

110

R → K: Abolishes most of in vitro phosphatase activity. Ref.2

Mutagenesis

111

S → A: Abolishes most of in vitro phosphatase activity. Ref.2

Sequence conflict

T → A in AAN77931. Ref.2

Secondary structure

188

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8NEJ0-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: A6EDECC3624F570F
Show »

FASTA

188

21,066

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of two novel low-molecular-weight dual specificity phosphatases." Hood K.L., Tobin J.F., Yoon C. Biochem. Biophys. Res. Commun. 298:545-551(2002) [PubMed: 12408986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Colon tumor.
[2]	"Molecular cloning and characterization of a novel dual-specificity phosphatase18 gene from human fetal brain." 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. Biochim. Biophys. Acta 1625:296-304(2003) [PubMed: 12591617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-73; LEU-102; CYS-104; ARG-110 AND SER-111. Tissue: Fetal brain.
[3]	"A genome annotation-driven approach to cloning the human ORFeome." 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. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AF533017 mRNA. Translation: AAN59787.1.
AF461689 mRNA. Translation: AAN77931.1.
CR456406 mRNA. Translation: CAG30292.1.
BC030987 mRNA. Translation: AAH30987.1.

IPI

IPI00168678.

RefSeq

NP_689724.3.

UniGene

Hs.517544

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ESB	X-ray	2.00	A	1-188	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q8NEJ0.

Genome annotation databases

Ensembl

ENSG00000167065. Homo sapiens. [Contig view]

GeneID

150290.

KEGG

hsa:150290.

UCSC

uc003aiu.2. human.

Organism-specific databases

GeneCards

GC22M029382.

H-InvDB

HIX0017667.

HGNC

HGNC:18484. DUSP18.

MIM

611446. gene.

PharmGKB

PA134928498.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q8NEJ0.

HOVERGEN

Q8NEJ0.

OMA

Q8NEJ0. MGVIPDI.

Enzyme and pathway databases

BRENDA

3.1.3.16. 247.
3.1.3.48. 247.

Gene expression databases

ArrayExpress

Q8NEJ0.

Bgee

Q8NEJ0.

CleanEx

HS_DUSP18.

GermOnline

ENSG00000167065. Homo sapiens.

Family and domain databases

InterPro

IPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR000340. Tyr_Pase_dual_specific.
[Graphical view]

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

SMART

SM00195. DSPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

86394.

SOURCE

Search...

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Entry information

Entry name

DUS18_HUMAN

Accession

Primary (citable) accession number: Q8NEJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	October 1, 2002
Last modified:	July 7, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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