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Dual specificity protein phosphatase 18 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 20) (LMW-DSP20)

 DUS18_HUMAN             Reviewed;         188 AA.
Q8NEJ0; B3KPA4;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
27-SEP-2017, entry version 129.
RecName: Full=Dual specificity protein phosphatase 18;
EC=3.1.3.16 {ECO:0000269|PubMed:12408986, ECO:0000269|PubMed:12591617};
EC=3.1.3.48 {ECO:0000269|PubMed:12408986, ECO:0000269|PubMed:12591617};
AltName: Full=Low molecular weight dual specificity phosphatase 20 {ECO:0000303|PubMed:12408986};
Short=LMW-DSP20;
Name=DUSP18; Synonyms=LMWDSP20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND FUNCTION.
TISSUE=Colon tumor;
PubMed=12408986; DOI=10.1016/S0006-291X(02)02488-9;
Hood K.L., Tobin J.F., Yoon C.;
"Identification and characterization of two novel low-molecular-weight
dual specificity phosphatases.";
Biochem. Biophys. Res. Commun. 298:545-551(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF ASP-73; LEU-102; CYS-104; ARG-110 AND SER-111.
TISSUE=Fetal brain;
PubMed=12591617; DOI=10.1016/S0167-4781(02)00629-2;
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.;
"Molecular cloning and characterization of a novel dual-specificity
phosphatase18 gene from human fetal brain.";
Biochim. Biophys. Acta 1625:296-304(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=16699184; DOI=10.1107/S0907444906010109;
Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Son J.H., Ryu S.E.,
Kim S.J.;
"Structure of human DSP18, a member of the dual-specificity protein
tyrosine phosphatase family.";
Acta Crystallogr. D 62:582-588(2006).
-!- 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).
{ECO:0000269|PubMed:12408986, ECO:0000269|PubMed:12591617}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:12408986, ECO:0000269|PubMed:12591617}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:12408986, ECO:0000269|PubMed:12591617}.
-!- ENZYME REGULATION: Activated by manganese ions, inhibited by
iodoaretic acid. {ECO:0000269|PubMed:12591617}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.0. {ECO:0000269|PubMed:12591617};
Temperature dependence:
Optimum temperature is 55 degrees Celsius.
{ECO:0000269|PubMed:12591617};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12408986}.
Nucleus {ECO:0000269|PubMed:12408986}. Mitochondrion inner
membrane {ECO:0000250|UniProtKB:Q8VE01}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q8VE01}; Intermembrane side
{ECO:0000250|UniProtKB:Q8VE01}. Note=Translocates to cytoplasm in
response to apoptotic stimuli such as staurosporine treatment.
{ECO:0000250|UniProtKB:Q8VE01}.
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver,
brain, ovary and testis. {ECO:0000269|PubMed:12408986,
ECO:0000269|PubMed:12591617}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF533017; AAN59787.1; -; mRNA.
EMBL; AF461689; AAN77931.1; -; mRNA.
EMBL; CR456406; CAG30292.1; -; mRNA.
EMBL; AK056074; BAG51616.1; -; mRNA.
EMBL; CH471095; EAW59913.1; -; Genomic_DNA.
EMBL; BC030987; AAH30987.1; -; mRNA.
CCDS; CCDS13883.1; -.
RefSeq; NP_001291723.1; NM_001304794.1.
RefSeq; NP_001291724.1; NM_001304795.1.
RefSeq; NP_689724.3; NM_152511.4.
RefSeq; XP_005261425.1; XM_005261368.4.
RefSeq; XP_006724211.1; XM_006724148.3.
RefSeq; XP_011528222.1; XM_011529920.2.
RefSeq; XP_011528223.1; XM_011529921.2.
RefSeq; XP_016884116.1; XM_017028627.1.
RefSeq; XP_016884117.1; XM_017028628.1.
UniGene; Hs.517544; -.
PDB; 2ESB; X-ray; 2.00 A; A=1-188.
PDBsum; 2ESB; -.
ProteinModelPortal; Q8NEJ0; -.
SMR; Q8NEJ0; -.
BioGrid; 127280; 20.
IntAct; Q8NEJ0; 1.
STRING; 9606.ENSP00000333917; -.
DEPOD; Q8NEJ0; -.
PhosphoSitePlus; Q8NEJ0; -.
BioMuta; DUSP18; -.
DMDM; 29840768; -.
MaxQB; Q8NEJ0; -.
PaxDb; Q8NEJ0; -.
PeptideAtlas; Q8NEJ0; -.
PRIDE; Q8NEJ0; -.
DNASU; 150290; -.
Ensembl; ENST00000334679; ENSP00000333917; ENSG00000167065.
Ensembl; ENST00000377087; ENSP00000366291; ENSG00000167065.
Ensembl; ENST00000404885; ENSP00000385463; ENSG00000167065.
Ensembl; ENST00000407308; ENSP00000386063; ENSG00000167065.
GeneID; 150290; -.
KEGG; hsa:150290; -.
UCSC; uc003aiu.4; human.
CTD; 150290; -.
EuPathDB; HostDB:ENSG00000167065.13; -.
GeneCards; DUSP18; -.
HGNC; HGNC:18484; DUSP18.
HPA; CAB034070; -.
HPA; HPA051349; -.
MIM; 611446; gene.
neXtProt; NX_Q8NEJ0; -.
OpenTargets; ENSG00000167065; -.
PharmGKB; PA134928498; -.
eggNOG; KOG1718; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000118853; -.
HOGENOM; HOG000233766; -.
HOVERGEN; HBG051422; -.
InParanoid; Q8NEJ0; -.
KO; K14165; -.
OMA; HVQAIRP; -.
OrthoDB; EOG091G0249; -.
PhylomeDB; Q8NEJ0; -.
TreeFam; TF316009; -.
EvolutionaryTrace; Q8NEJ0; -.
GeneWiki; DUSP18; -.
GenomeRNAi; 150290; -.
PRO; PR:Q8NEJ0; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000167065; -.
CleanEx; HS_DUSP18; -.
ExpressionAtlas; Q8NEJ0; baseline and differential.
Genevisible; Q8NEJ0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
CDD; cd00127; DSPc; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR020420; Atypical_DUSP_famB.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PRINTS; PR01908; ADSPHPHTASE.
PRINTS; PR01910; ADSPHPHTASEB.
SMART; SM00195; DSPc; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Hydrolase; Membrane;
Mitochondrion; Mitochondrion inner membrane; Nucleus;
Protein phosphatase; Reference proteome.
CHAIN 1 188 Dual specificity protein phosphatase 18.
/FTId=PRO_0000094828.
DOMAIN 80 149 Tyrosine-protein phosphatase.
ACT_SITE 104 104 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
MUTAGEN 73 73 D->A: Abolishes most of in vitro
phosphatase activity.
{ECO:0000269|PubMed:12591617}.
MUTAGEN 102 102 L->V: No effect on in vitro phosphatase
activity. {ECO:0000269|PubMed:12591617}.
MUTAGEN 104 104 C->S: Abolishes most of in vitro
phosphatase activity.
{ECO:0000269|PubMed:12591617}.
MUTAGEN 110 110 R->K: Abolishes most of in vitro
phosphatase activity.
{ECO:0000269|PubMed:12591617}.
MUTAGEN 111 111 S->A: Abolishes most of in vitro
phosphatase activity.
{ECO:0000269|PubMed:12591617}.
CONFLICT 2 2 T -> A (in Ref. 2; AAN77931).
{ECO:0000305}.
STRAND 21 24 {ECO:0000244|PDB:2ESB}.
STRAND 27 30 {ECO:0000244|PDB:2ESB}.
HELIX 34 36 {ECO:0000244|PDB:2ESB}.
HELIX 38 43 {ECO:0000244|PDB:2ESB}.
STRAND 48 51 {ECO:0000244|PDB:2ESB}.
STRAND 65 68 {ECO:0000244|PDB:2ESB}.
HELIX 79 82 {ECO:0000244|PDB:2ESB}.
HELIX 83 95 {ECO:0000244|PDB:2ESB}.
STRAND 100 103 {ECO:0000244|PDB:2ESB}.
STRAND 105 109 {ECO:0000244|PDB:2ESB}.
HELIX 110 122 {ECO:0000244|PDB:2ESB}.
HELIX 127 137 {ECO:0000244|PDB:2ESB}.
HELIX 145 159 {ECO:0000244|PDB:2ESB}.
HELIX 176 178 {ECO:0000244|PDB:2ESB}.
SEQUENCE 188 AA; 21066 MW; A6EDECC3624F570F CRC64;
MTAPSCAFPV QFRQPSVSGL SQITKSLYIS NGVAANNKLM LSSNQITMVI NVSVEVVNTL
YEDIQYMQVP VADSPNSRLC DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM
KYHAMSLLDA HTWTKSCRPI IRPNSGFWEQ LIHYEFQLFG KNTVHMVSSP VGMIPDIYEK
EVRLMIPL


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