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Q8NEJ0 (DUS18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 18

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Low molecular weight dual specificity phosphatase 20
Short name=LMW-DSP20
Gene names
Name:DUSP18
Synonyms:LMWDSP20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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. Ref.2

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Dual specificity protein phosphatase 18
PRO_0000094828

Regions

Domain80 – 14970Tyrosine-protein phosphatase

Sites

Active site1041Phosphocysteine intermediate By similarity

Experimental info

Mutagenesis731D → A: Abolishes most of in vitro phosphatase activity. Ref.2
Mutagenesis1021L → V: No effect on in vitro phosphatase activity. Ref.2
Mutagenesis1041C → S: Abolishes most of in vitro phosphatase activity. Ref.2
Mutagenesis1101R → K: Abolishes most of in vitro phosphatase activity. Ref.2
Mutagenesis1111S → A: Abolishes most of in vitro phosphatase activity. Ref.2
Sequence conflict21T → A in AAN77931. Ref.2

Secondary structure

........................... 188
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8NEJ0 [UniParc].

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

FASTA18821,066
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]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].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[7]"Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family."
Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Son J.H., Ryu S.E., Kim S.J.
Acta Crystallogr. D 62:582-588(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF533017 mRNA. Translation: AAN59787.1.
AF461689 mRNA. Translation: AAN77931.1.
CR456406 mRNA. Translation: CAG30292.1.
AK056074 mRNA. Translation: BAG51616.1.
CH471095 Genomic DNA. Translation: EAW59913.1.
BC030987 mRNA. Translation: AAH30987.1.
RefSeqNP_689724.3. NM_152511.3.
XP_005261423.1. XM_005261366.1.
XP_005261424.1. XM_005261367.1.
XP_005261425.1. XM_005261368.2.
UniGeneHs.517544.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESBX-ray2.00A1-188[»]
ProteinModelPortalQ8NEJ0.
SMRQ8NEJ0. Positions 18-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127280. 1 interaction.
STRING9606.ENSP00000333917.

PTM databases

PhosphoSiteQ8NEJ0.

Polymorphism databases

DMDM29840768.

Proteomic databases

PaxDbQ8NEJ0.
PRIDEQ8NEJ0.

Protocols and materials databases

DNASU150290.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334679; ENSP00000333917; ENSG00000167065.
ENST00000377087; ENSP00000366291; ENSG00000167065.
ENST00000404885; ENSP00000385463; ENSG00000167065.
ENST00000407308; ENSP00000386063; ENSG00000167065.
GeneID150290.
KEGGhsa:150290.
UCSCuc003aiu.3. human.

Organism-specific databases

CTD150290.
GeneCardsGC22M031048.
HGNCHGNC:18484. DUSP18.
HPACAB034070.
HPA051349.
MIM611446. gene.
neXtProtNX_Q8NEJ0.
PharmGKBPA134928498.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000233766.
HOVERGENHBG051422.
InParanoidQ8NEJ0.
KOK14165.
OMAASPCAFP.
PhylomeDBQ8NEJ0.
TreeFamTF316009.

Gene expression databases

ArrayExpressQ8NEJ0.
BgeeQ8NEJ0.
CleanExHS_DUSP18.
GenevestigatorQ8NEJ0.

Family and domain databases

InterProIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8NEJ0.
GeneWikiDUSP18.
GenomeRNAi150290.
NextBio86394.
PROQ8NEJ0.
SOURCESearch...

Entry information

Entry nameDUS18_HUMAN
AccessionPrimary (citable) accession number: Q8NEJ0
Secondary accession number(s): B3KPA4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM