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Q8NEJ0

- DUS18_HUMAN

UniProt

Q8NEJ0 - DUS18_HUMAN

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Protein

Dual specificity protein phosphatase 18

Gene

DUSP18

Organism
Homo sapiens (Human)
Status
Reviewed - 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: RefGenome
  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: Chromosome 22

Organism-specific databases

HGNCiHGNC:18484. DUSP18.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. 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.

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

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 – 244
Beta strandi27 – 304
Helixi34 – 363
Helixi38 – 436
Beta strandi48 – 514
Beta strandi65 – 684
Helixi79 – 824
Helixi83 – 9513
Beta strandi100 – 1034
Beta strandi105 – 1095
Helixi110 – 12213
Helixi127 – 13711
Helixi145 – 15915
Helixi176 – 1783

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 [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:
EMBL
GenBank
DDBJ
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_152511.3.
XP_005261423.1. XM_005261366.1.
XP_005261424.1. XM_005261367.1.
XP_005261425.1. XM_005261368.2.
XP_006724211.1. XM_006724148.1.
UniGeneiHs.517544.

Genome annotation databases

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

Polymorphism databases

DMDMi29840768.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13883.1.
RefSeqi NP_689724.3. NM_152511.3.
XP_005261423.1. XM_005261366.1.
XP_005261424.1. XM_005261367.1.
XP_005261425.1. XM_005261368.2.
XP_006724211.1. XM_006724148.1.
UniGenei Hs.517544.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ESB X-ray 2.00 A 1-188 [» ]
ProteinModelPortali Q8NEJ0.
SMRi Q8NEJ0. Positions 18-179.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127280. 1 interaction.
STRINGi 9606.ENSP00000333917.

PTM databases

PhosphoSitei Q8NEJ0.

Polymorphism databases

DMDMi 29840768.

Proteomic databases

MaxQBi Q8NEJ0.
PaxDbi Q8NEJ0.
PRIDEi Q8NEJ0.

Protocols and materials databases

DNASUi 150290.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334679 ; ENSP00000333917 ; ENSG00000167065 .
ENST00000377087 ; ENSP00000366291 ; ENSG00000167065 .
ENST00000404885 ; ENSP00000385463 ; ENSG00000167065 .
ENST00000407308 ; ENSP00000386063 ; ENSG00000167065 .
GeneIDi 150290.
KEGGi hsa:150290.
UCSCi uc003aiu.3. human.

Organism-specific databases

CTDi 150290.
GeneCardsi GC22M031048.
HGNCi HGNC:18484. DUSP18.
HPAi CAB034070.
HPA051349.
MIMi 611446. gene.
neXtProti NX_Q8NEJ0.
PharmGKBi PA134928498.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118853.
HOGENOMi HOG000233766.
HOVERGENi HBG051422.
InParanoidi Q8NEJ0.
KOi K14165.
OMAi ASPCAFP.
PhylomeDBi Q8NEJ0.
TreeFami TF316009.

Miscellaneous databases

EvolutionaryTracei Q8NEJ0.
GeneWikii DUSP18.
GenomeRNAii 150290.
NextBioi 86394.
PROi Q8NEJ0.
SOURCEi Search...

Gene expression databases

Bgeei Q8NEJ0.
CleanExi HS_DUSP18.
ExpressionAtlasi Q8NEJ0. baseline and differential.
Genevestigatori Q8NEJ0.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR020417. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 107 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