Q8NEJ0 (DUS18_HUMAN) 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

Alternative name(s):
Low molecular weight dual specificity phosphatase 20
Short name=LMW-DSP20

Gene names

Name:	DUSP18
Synonyms:	LMWDSP20

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + 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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from direct assay Ref.1. Source: UniProtKB 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_0000094828

Regions

Domain

80 – 149

70

Tyrosine-protein phosphatase

Sites

Active site

104

1

Phosphocysteine intermediate By similarity

Experimental info

Mutagenesis

73

1

D → A: Abolishes most of in vitro phosphatase activity. Ref.2

Mutagenesis

102

1

L → V: No effect on in vitro phosphatase activity. Ref.2

Mutagenesis

104

1

C → S: Abolishes most of in vitro phosphatase activity. Ref.2

Mutagenesis

110

1

R → K: Abolishes most of in vitro phosphatase activity. Ref.2

Mutagenesis

111

1

S → A: Abolishes most of in vitro phosphatase activity. Ref.2

Sequence conflict

2

1

T → A in AAN77931. Ref.2

Secondary structure

1

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188

Helix Strand Turn

Details...

Beta strand

21 – 24

4

Beta strand

27 – 30

4

Helix

34 – 36

3

Helix

38 – 43

6

Beta strand

48 – 51

4

Beta strand

65 – 68

4

Helix

79 – 82

4

Helix

83 – 95

13

Beta strand

100 – 103

4

Beta strand

105 – 109

5

Helix

110 – 122

13

Helix

127 – 137

11

Helix

145 – 159

15

Helix

176 – 178

3

Sequences

	Sequence		Length	Mass (Da)
	Q8NEJ0 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: A6EDECC3624F570F	FASTA	188	21,066
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00168678.

RefSeq

NP_689724.3. NM_152511.3.

UniGene

Hs.517544.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ESB	X-ray	2.00	A	1-188	[»]

ProteinModelPortal

Q8NEJ0.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000333917.

PTM databases

PhosphoSite

Q8NEJ0.

Polymorphism databases

DMDM

29840768.

Proteomic databases

PaxDb

Q8NEJ0.

PRIDE

Q8NEJ0.

Protocols and materials databases

DNASU

150290.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334679; ENSP00000333917; ENSG00000167065.
ENST00000377087; ENSP00000366291; ENSG00000167065.
ENST00000404885; ENSP00000385463; ENSG00000167065.
ENST00000407308; ENSP00000386063; ENSG00000167065.

GeneID

150290.

KEGG

hsa:150290.

UCSC

uc003aiu.3. human.

Organism-specific databases

CTD

150290.

GeneCards

GC22M031048.

HGNC

HGNC:18484. DUSP18.

HPA

CAB034070.

MIM

611446. gene.

neXtProt

NX_Q8NEJ0.

PharmGKB

PA134928498.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000233766.

HOVERGEN

HBG051422.

InParanoid

Q8NEJ0.

KO

K14165.

OMA

AMEDFYQ.

OrthoDB

EOG4VQ9QB.

PhylomeDB

Q8NEJ0.

Gene expression databases

ArrayExpress

Q8NEJ0.

Bgee

Q8NEJ0.

CleanEx

HS_DUSP18.

Genevestigator

Q8NEJ0.

GermOnline

ENSG00000167065. Homo sapiens.

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.
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

EvolutionaryTrace

Q8NEJ0.

GenomeRNAi

150290.

NextBio

86394.

SOURCE

Search...

Entry information

Entry name

DUS18_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.