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Q8VE01 (DUS18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Dusp18
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.4

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.4

Subcellular location

Cytoplasm. Nucleus By similarity. Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note: Translocates to cytoplasm in response to apoptotic stimuli such as staurosporine treatment. Ref.4

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-tyrosine dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein localization to organelle

Inferred from sequence or structural similarity Ref.4. Source: MGI

protein targeting to membrane

Inferred from sequence or structural similarity Ref.4. Source: MGI

protein targeting to mitochondrion

Inferred from sequence or structural similarity Ref.4. Source: MGI

response to antibiotic

Inferred from sequence or structural similarity Ref.4. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity Ref.4. Source: MGI

extrinsic component of mitochondrial inner membrane

Inferred from sequence or structural similarity Ref.4. Source: MGI

intrinsic component of mitochondrial inner membrane

Inferred from sequence or structural similarity Ref.4. Source: MGI

mitochondrial inner membrane

Inferred from sequence or structural similarity Ref.4. Source: MGI

mitochondrial intermembrane space

Inferred from sequence or structural similarity Ref.4. Source: MGI

mitochondrion

Inferred from sequence or structural similarity Ref.4. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionMAP kinase tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

phosphatase activity

Inferred from sequence or structural similarity Ref.4. Source: MGI

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Dual specificity protein phosphatase 18
PRO_0000094829

Regions

Domain80 – 14970Tyrosine-protein phosphatase
Region95 – 14147Sufficient for mitochondrial localization

Sites

Active site1041Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VE01 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 86CB43E390DC7DE3

FASTA18821,119
        10         20         30         40         50         60 
MTSPWSAFPV QIPQPSIRGL SQITKSLFIS NGVAANNKLL LSSNQITTVI NVSVEVANTF 

        70         80         90        100        110        120 
YEDIQYVQVP VVDAPVARLS NFFDSVADRI HSVEMQKGRT LLHCAAGVSR SAALCLAYLM 

       130        140        150        160        170        180 
KYHAMSLVDA HTWTKSCRPI IRPNSGFWEQ LIHYELQLFG KNTMQMMDSP MGRIPDIYEK 


ETRLMIPL 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head and Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Strain: Czech II.
Tissue: Mammary tumor.
[4]"Dual specificity phosphatases 18 and 21 target to opposing sides of the mitochondrial inner membrane."
Rardin M.J., Wiley S.E., Murphy A.N., Pagliarini D.J., Dixon J.E.
J. Biol. Chem. 283:15440-15450(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK015917 mRNA. Translation: BAC25470.1.
AK081916 mRNA. Translation: BAC38371.1.
AL731853 Genomic DNA. Translation: CAI51861.1.
BC020036 mRNA. Translation: AAH20036.1.
CCDSCCDS24369.1.
RefSeqNP_776106.1. NM_173745.5.
XP_006514936.1. XM_006514873.1.
UniGeneMm.32588.

3D structure databases

ProteinModelPortalQ8VE01.
SMRQ8VE01. Positions 19-179.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8VE01.

Proteomic databases

PRIDEQ8VE01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055931; ENSMUSP00000057346; ENSMUSG00000047205.
ENSMUST00000109996; ENSMUSP00000105624; ENSMUSG00000047205.
GeneID75219.
KEGGmmu:75219.
UCSCuc007htu.2. mouse.

Organism-specific databases

CTD150290.
MGIMGI:1922469. Dusp18.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00750000117525.
HOGENOMHOG000233766.
HOVERGENHBG051422.
InParanoidQ8VE01.
KOK14165.
OMAASPCAFP.
OrthoDBEOG7PK90H.
PhylomeDBQ8VE01.
TreeFamTF316009.

Gene expression databases

BgeeQ8VE01.
CleanExMM_DUSP18.
GenevestigatorQ8VE01.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. 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]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio342484.
PROQ8VE01.
SOURCESearch...

Entry information

Entry nameDUS18_MOUSE
AccessionPrimary (citable) accession number: Q8VE01
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot