Q8VE01 (DUS18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 18
EC=3.1.3.16
EC=3.1.3.48

Gene names

Name:

Dusp18

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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 component	Cytoplasm Membrane Mitochondrion Mitochondrion inner membrane Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from Biological aspect of Ancestor. Source: RefGenome 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_component	extrinsic to mitochondrial inner membrane Inferred from sequence or structural similarity Ref.4. Source: MGI intrinsic to 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 nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

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_0000094829
Regions
	Domain	80 – 149	70	Tyrosine-protein phosphatase
	Region	95 – 141	47	Sufficient for mitochondrial localization
Sites
	Active site	104	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8VE01 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 86CB43E390DC7DE3	FASTA	188	21,119
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00123649.
RefSeq	NP_776106.1. NM_173745.5.
UniGene	Mm.32588.
3D structure databases
ProteinModelPortal	Q8VE01.
SMR	Q8VE01. Positions 19-179.
ModBase	Search...
PTM databases
PhosphoSite	Q8VE01.
Proteomic databases
PRIDE	Q8VE01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000055931; ENSMUSP00000057346; ENSMUSG00000047205. ENSMUST00000109996; ENSMUSP00000105624; ENSMUSG00000047205.
GeneID	75219.
KEGG	mmu:75219.
UCSC	uc007htu.2. mouse.
Organism-specific databases
CTD	150290.
MGI	MGI:1922469. Dusp18.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00700000104026.
HOGENOM	HOG000233766.
HOVERGEN	HBG051422.
InParanoid	Q8VE01.
KO	K14165.
OMA	AMEDFYQ.
OrthoDB	EOG4VQ9QB.
Gene expression databases
ArrayExpress	Q8VE01.
Bgee	Q8VE01.
CleanEx	MM_DUSP18.
Genevestigator	Q8VE01.
GermOnline	ENSMUSG00000047205. Mus musculus.
Family and domain databases
InterPro	IPR020417. 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]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PRINTS	PR01908. ADSPHPHTASE. PR01910. ADSPHPHTASEB.
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
NextBio	342484.
SOURCE	Search...

Entry information

Entry name

DUS18_MOUSE

Accession

Primary (citable) accession number: Q8VE01

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	March 1, 2002
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program