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Dual specificity protein phosphatase 23 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular mass dual specificity phosphatase 3) (LDP-3) (VH1-like phosphatase Z)

 DUS23_HUMAN             Reviewed;         150 AA.
Q9BVJ7; Q9NX48;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 149.
RecName: Full=Dual specificity protein phosphatase 23;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=Low molecular mass dual specificity phosphatase 3;
Short=LDP-3;
AltName: Full=VH1-like phosphatase Z;
Name=DUSP23; Synonyms=LDP3, VHZ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15281913; DOI=10.1042/BJ20040498;
Takagaki K., Satoh T., Tanuma N., Masuda K., Takekawa M., Shima H.,
Kikuchi K.;
"Characterization of a novel low-molecular-mass dual-specificity
phosphatase-3 (LDP-3) that enhances activation of JNK and p38.";
Biochem. J. 383:447-455(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Carcinoma;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[5]
ENZYME ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=15201283; DOI=10.1074/jbc.M403412200;
Alonso A., Burkhalter S., Sasin J., Tautz L., Bogetz J., Huynh H.,
Bremer M.C.D., Holsinger L.J., Godzik A., Mustelin T.;
"The minimal essential core of a cysteine-based protein-tyrosine
phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ.";
J. Biol. Chem. 279:35768-35774(2004).
[6]
ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=15147733; DOI=10.1016/j.biocel.2003.12.014;
Wu Q., Li Y., Gu S., Li N., Zheng D., Li D., Zheng Z., Ji C., Xie Y.,
Mao Y.;
"Molecular cloning and characterization of a novel dual-specificity
phosphatase 23 gene from human fetal brain.";
Int. J. Biochem. Cell Biol. 36:1542-1553(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[9]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-150.
PubMed=18245086; DOI=10.1074/jbc.M708945200;
Agarwal R., Burley S.K., Swaminathan S.;
"Structure of human dual specificity protein phosphatase 23, VHZ,
enzyme-substrate/product complex.";
J. Biol. Chem. 283:8946-8953(2008).
-!- FUNCTION: Protein phosphatase that mediates dephosphorylation of
proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it
can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta
(MAPK10) in vitro. Able to enhance activation of JNK and p38
(MAPK14). {ECO:0000269|PubMed:15147733,
ECO:0000269|PubMed:15201283}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.498 mM for p-nitrophenylphosphate
{ECO:0000269|PubMed:15201283};
-!- INTERACTION:
Q96B26:EXOSC8; NbExp=10; IntAct=EBI-724940, EBI-371922;
Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-724940, EBI-740897;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Mainly
cytosolic. Also nuclear.
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen,
prostate, colon, adrenal gland, mammary gland, thyroid and
trachea. Expressed at lower level in uterus, small intestine,
bladder, bone marrow, brain, spinal cord and stomach.
{ECO:0000269|PubMed:15147733, ECO:0000269|PubMed:15201283}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-!- CAUTION: Was originally erroneously termed DUSP25. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB164404; BAD12141.1; -; mRNA.
EMBL; AK000449; BAA91172.1; -; mRNA.
EMBL; AL590560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001140; AAH01140.1; -; mRNA.
CCDS; CCDS1187.1; -.
RefSeq; NP_001306587.1; NM_001319658.1.
RefSeq; NP_001306588.1; NM_001319659.1.
RefSeq; NP_060293.2; NM_017823.4.
UniGene; Hs.425801; -.
PDB; 2IMG; X-ray; 1.93 A; A=2-150.
PDB; 4ERC; X-ray; 1.15 A; A/B=1-150.
PDBsum; 2IMG; -.
PDBsum; 4ERC; -.
ProteinModelPortal; Q9BVJ7; -.
SMR; Q9BVJ7; -.
BioGrid; 120275; 68.
IntAct; Q9BVJ7; 30.
MINT; Q9BVJ7; -.
STRING; 9606.ENSP00000357087; -.
BindingDB; Q9BVJ7; -.
ChEMBL; CHEMBL2396506; -.
DrugBank; DB04214; 4-Nitrophenyl Phosphate.
DEPOD; Q9BVJ7; -.
iPTMnet; Q9BVJ7; -.
PhosphoSitePlus; Q9BVJ7; -.
SwissPalm; Q9BVJ7; -.
BioMuta; DUSP23; -.
DMDM; 73620828; -.
EPD; Q9BVJ7; -.
MaxQB; Q9BVJ7; -.
PaxDb; Q9BVJ7; -.
PeptideAtlas; Q9BVJ7; -.
PRIDE; Q9BVJ7; -.
DNASU; 54935; -.
Ensembl; ENST00000368107; ENSP00000357087; ENSG00000158716.
Ensembl; ENST00000368108; ENSP00000357088; ENSG00000158716.
Ensembl; ENST00000368109; ENSP00000357089; ENSG00000158716.
GeneID; 54935; -.
KEGG; hsa:54935; -.
UCSC; uc001ftz.2; human.
CTD; 54935; -.
DisGeNET; 54935; -.
EuPathDB; HostDB:ENSG00000158716.8; -.
GeneCards; DUSP23; -.
HGNC; HGNC:21480; DUSP23.
HPA; HPA028211; -.
HPA; HPA045792; -.
neXtProt; NX_Q9BVJ7; -.
OpenTargets; ENSG00000158716; -.
PharmGKB; PA134983082; -.
eggNOG; KOG1720; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00390000010254; -.
HOGENOM; HOG000108423; -.
HOVERGEN; HBG056524; -.
InParanoid; Q9BVJ7; -.
KO; K14165; -.
OMA; AVHCMHG; -.
OrthoDB; EOG091G0XEO; -.
PhylomeDB; Q9BVJ7; -.
TreeFam; TF105125; -.
SABIO-RK; Q9BVJ7; -.
EvolutionaryTrace; Q9BVJ7; -.
GeneWiki; DUSP23; -.
GenomeRNAi; 54935; -.
PRO; PR:Q9BVJ7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158716; -.
CleanEx; HS_DUSP23; -.
ExpressionAtlas; Q9BVJ7; baseline and differential.
Genevisible; Q9BVJ7; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
Pfam; PF00782; DSPc; 1.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
Polymorphism; Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712}.
CHAIN 2 150 Dual specificity protein phosphatase 23.
/FTId=PRO_0000094835.
DOMAIN 75 140 Tyrosine-protein phosphatase.
ACT_SITE 95 95 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
VARIANT 124 124 E -> V (in dbSNP:rs11544443).
/FTId=VAR_051756.
VARIANT 131 131 G -> S (in dbSNP:rs1129923).
/FTId=VAR_023199.
CONFLICT 132 132 S -> P (in Ref. 2; BAA91172).
{ECO:0000305}.
STRAND 9 12 {ECO:0000244|PDB:4ERC}.
TURN 13 15 {ECO:0000244|PDB:4ERC}.
STRAND 16 20 {ECO:0000244|PDB:4ERC}.
HELIX 25 33 {ECO:0000244|PDB:4ERC}.
STRAND 36 41 {ECO:0000244|PDB:4ERC}.
STRAND 43 45 {ECO:0000244|PDB:4ERC}.
HELIX 50 52 {ECO:0000244|PDB:4ERC}.
STRAND 56 60 {ECO:0000244|PDB:4ERC}.
HELIX 71 86 {ECO:0000244|PDB:4ERC}.
STRAND 90 94 {ECO:0000244|PDB:4ERC}.
STRAND 96 99 {ECO:0000244|PDB:4ERC}.
HELIX 100 114 {ECO:0000244|PDB:4ERC}.
HELIX 118 128 {ECO:0000244|PDB:4ERC}.
HELIX 136 149 {ECO:0000244|PDB:4ERC}.
SEQUENCE 150 AA; 16588 MW; 4B72EFA0434B1B5F CRC64;
MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR
LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD
AIAEIRRLRP GSIETYEQEK AVFQFYQRTK


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