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Protein

Dual specificity protein phosphatase 18

Gene

DUSP18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Enzyme regulationi

Activated by manganese ions, inhibited by iodoaretic acid.

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  3. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DUSP18
Synonyms:LMWDSP20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18484. DUSP18.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731D → A: Abolishes most of in vitro phosphatase activity. 1 Publication
Mutagenesisi102 – 1021L → V: No effect on in vitro phosphatase activity. 1 Publication
Mutagenesisi104 – 1041C → S: Abolishes most of in vitro phosphatase activity. 1 Publication
Mutagenesisi110 – 1101R → K: Abolishes most of in vitro phosphatase activity. 1 Publication
Mutagenesisi111 – 1111S → A: Abolishes most of in vitro phosphatase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134928498.

Polymorphism and mutation databases

BioMutaiDUSP18.
DMDMi29840768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Dual specificity protein phosphatase 18PRO_0000094828Add
BLAST

Proteomic databases

MaxQBiQ8NEJ0.
PaxDbiQ8NEJ0.
PRIDEiQ8NEJ0.

PTM databases

DEPODiQ8NEJ0.
PhosphoSiteiQ8NEJ0.

Expressioni

Tissue specificityi

Widely expressed with highest levels in liver, brain, ovary and testis.2 Publications

Gene expression databases

BgeeiQ8NEJ0.
CleanExiHS_DUSP18.
ExpressionAtlasiQ8NEJ0. baseline and differential.
GenevestigatoriQ8NEJ0.

Organism-specific databases

HPAiCAB034070.
HPA051349.

Interactioni

Protein-protein interaction databases

BioGridi127280. 1 interaction.
STRINGi9606.ENSP00000333917.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 244Combined sources
Beta strandi27 – 304Combined sources
Helixi34 – 363Combined sources
Helixi38 – 436Combined sources
Beta strandi48 – 514Combined sources
Beta strandi65 – 684Combined sources
Helixi79 – 824Combined sources
Helixi83 – 9513Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi105 – 1095Combined sources
Helixi110 – 12213Combined sources
Helixi127 – 13711Combined sources
Helixi145 – 15915Combined sources
Helixi176 – 1783Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESBX-ray2.00A1-188[»]
ProteinModelPortaliQ8NEJ0.
SMRiQ8NEJ0. Positions 18-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NEJ0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 14970Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ8NEJ0.
KOiK14165.
OMAiASPCAFP.
PhylomeDBiQ8NEJ0.
TreeFamiTF316009.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NEJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPSCAFPV QFRQPSVSGL SQITKSLYIS NGVAANNKLM LSSNQITMVI
60 70 80 90 100
NVSVEVVNTL YEDIQYMQVP VADSPNSRLC DFFDPIADHI HSVEMKQGRT
110 120 130 140 150
LLHCAAGVSR SAALCLAYLM KYHAMSLLDA HTWTKSCRPI IRPNSGFWEQ
160 170 180
LIHYEFQLFG KNTVHMVSSP VGMIPDIYEK EVRLMIPL
Length:188
Mass (Da):21,066
Last modified:October 1, 2002 - v1
Checksum:iA6EDECC3624F570F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21T → A in AAN77931 (PubMed:12591617).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13883.1.
RefSeqiNP_689724.3. NM_152511.4.
XP_005261425.1. XM_005261368.3.
XP_006724211.1. XM_006724148.2.
UniGeneiHs.517544.

Genome annotation databases

EnsembliENST00000334679; ENSP00000333917; ENSG00000167065.
ENST00000377087; ENSP00000366291; ENSG00000167065.
ENST00000404885; ENSP00000385463; ENSG00000167065.
ENST00000407308; ENSP00000386063; ENSG00000167065.
GeneIDi150290.
KEGGihsa:150290.
UCSCiuc003aiu.3. human.

Polymorphism and mutation databases

BioMutaiDUSP18.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13883.1.
RefSeqiNP_689724.3. NM_152511.4.
XP_005261425.1. XM_005261368.3.
XP_006724211.1. XM_006724148.2.
UniGeneiHs.517544.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESBX-ray2.00A1-188[»]
ProteinModelPortaliQ8NEJ0.
SMRiQ8NEJ0. Positions 18-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127280. 1 interaction.
STRINGi9606.ENSP00000333917.

PTM databases

DEPODiQ8NEJ0.
PhosphoSiteiQ8NEJ0.

Polymorphism and mutation databases

BioMutaiDUSP18.
DMDMi29840768.

Proteomic databases

MaxQBiQ8NEJ0.
PaxDbiQ8NEJ0.
PRIDEiQ8NEJ0.

Protocols and materials databases

DNASUi150290.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334679; ENSP00000333917; ENSG00000167065.
ENST00000377087; ENSP00000366291; ENSG00000167065.
ENST00000404885; ENSP00000385463; ENSG00000167065.
ENST00000407308; ENSP00000386063; ENSG00000167065.
GeneIDi150290.
KEGGihsa:150290.
UCSCiuc003aiu.3. human.

Organism-specific databases

CTDi150290.
GeneCardsiGC22M031048.
HGNCiHGNC:18484. DUSP18.
HPAiCAB034070.
HPA051349.
MIMi611446. gene.
neXtProtiNX_Q8NEJ0.
PharmGKBiPA134928498.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ8NEJ0.
KOiK14165.
OMAiASPCAFP.
PhylomeDBiQ8NEJ0.
TreeFamiTF316009.

Miscellaneous databases

EvolutionaryTraceiQ8NEJ0.
GeneWikiiDUSP18.
GenomeRNAii150290.
NextBioi86394.
PROiQ8NEJ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NEJ0.
CleanExiHS_DUSP18.
ExpressionAtlasiQ8NEJ0. baseline and differential.
GenevestigatoriQ8NEJ0.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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).

Entry informationi

Entry nameiDUS18_HUMAN
AccessioniPrimary (citable) accession number: Q8NEJ0
Secondary accession number(s): B3KPA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: October 1, 2002
Last modified: April 29, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.