DUS23_HUMAN
ID DUS23_HUMAN Reviewed; 150 AA.
AC Q9BVJ7; Q9NX48;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Dual specificity protein phosphatase 23;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Low molecular mass dual specificity phosphatase 3;
DE Short=LDP-3;
DE AltName: Full=VH1-like phosphatase Z;
GN Name=DUSP23; Synonyms=LDP3, VHZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15281913; DOI=10.1042/bj20040498;
RA Takagaki K., Satoh T., Tanuma N., Masuda K., Takekawa M., Shima H.,
RA Kikuchi K.;
RT "Characterization of a novel low-molecular-mass dual-specificity
RT phosphatase-3 (LDP-3) that enhances activation of JNK and p38.";
RL Biochem. J. 383:447-455(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ENZYME ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15201283; DOI=10.1074/jbc.m403412200;
RA Alonso A., Burkhalter S., Sasin J., Tautz L., Bogetz J., Huynh H.,
RA Bremer M.C.D., Holsinger L.J., Godzik A., Mustelin T.;
RT "The minimal essential core of a cysteine-based protein-tyrosine
RT phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ.";
RL J. Biol. Chem. 279:35768-35774(2004).
RN [6]
RP ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15147733; DOI=10.1016/j.biocel.2003.12.014;
RA Wu Q., Li Y., Gu S., Li N., Zheng D., Li D., Zheng Z., Ji C., Xie Y.,
RA Mao Y.;
RT "Molecular cloning and characterization of a novel dual-specificity
RT phosphatase 23 gene from human fetal brain.";
RL Int. J. Biochem. Cell Biol. 36:1542-1553(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-150.
RX PubMed=18245086; DOI=10.1074/jbc.m708945200;
RA Agarwal R., Burley S.K., Swaminathan S.;
RT "Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-
RT substrate/product complex.";
RL J. Biol. Chem. 283:8946-8953(2008).
CC -!- FUNCTION: Protein phosphatase that mediates dephosphorylation of
CC proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can
CC dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in
CC vitro. Able to enhance activation of JNK and p38 (MAPK14).
CC {ECO:0000269|PubMed:15147733, ECO:0000269|PubMed:15201283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.498 mM for p-nitrophenylphosphate {ECO:0000269|PubMed:15201283};
CC -!- INTERACTION:
CC Q9BVJ7; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-724940, EBI-6425205;
CC Q9BVJ7; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-724940, EBI-11977289;
CC Q9BVJ7; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-724940, EBI-742054;
CC Q9BVJ7; Q96B26: EXOSC8; NbExp=12; IntAct=EBI-724940, EBI-371922;
CC Q9BVJ7; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-724940, EBI-2857471;
CC Q9BVJ7; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-724940, EBI-740897;
CC Q9BVJ7; P28062-2: PSMB8; NbExp=5; IntAct=EBI-724940, EBI-372312;
CC Q9BVJ7; Q9UL46: PSME2; NbExp=3; IntAct=EBI-724940, EBI-741630;
CC Q9BVJ7; P15884-3: TCF4; NbExp=3; IntAct=EBI-724940, EBI-13636688;
CC Q9BVJ7; Q8TBC4: UBA3; NbExp=3; IntAct=EBI-724940, EBI-717567;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Mainly
CC cytosolic. Also nuclear.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen,
CC prostate, colon, adrenal gland, mammary gland, thyroid and trachea.
CC Expressed at lower level in uterus, small intestine, bladder, bone
CC marrow, brain, spinal cord and stomach. {ECO:0000269|PubMed:15147733,
CC ECO:0000269|PubMed:15201283}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally erroneously termed DUSP25. {ECO:0000305}.
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DR EMBL; AB164404; BAD12141.1; -; mRNA.
DR EMBL; AK000449; BAA91172.1; -; mRNA.
DR EMBL; AL590560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001140; AAH01140.1; -; mRNA.
DR CCDS; CCDS1187.1; -.
DR RefSeq; NP_001306587.1; NM_001319658.1.
DR RefSeq; NP_001306588.1; NM_001319659.1.
DR RefSeq; NP_060293.2; NM_017823.4.
DR PDB; 2IMG; X-ray; 1.93 A; A=2-150.
DR PDB; 4ERC; X-ray; 1.15 A; A/B=1-150.
DR PDBsum; 2IMG; -.
DR PDBsum; 4ERC; -.
DR AlphaFoldDB; Q9BVJ7; -.
DR SMR; Q9BVJ7; -.
DR BioGRID; 120275; 118.
DR IntAct; Q9BVJ7; 48.
DR MINT; Q9BVJ7; -.
DR STRING; 9606.ENSP00000357087; -.
DR BindingDB; Q9BVJ7; -.
DR ChEMBL; CHEMBL2396506; -.
DR DrugBank; DB04214; 4-Nitrophenyl Phosphate.
DR DEPOD; DUSP23; -.
DR iPTMnet; Q9BVJ7; -.
DR PhosphoSitePlus; Q9BVJ7; -.
DR SwissPalm; Q9BVJ7; -.
DR BioMuta; DUSP23; -.
DR DMDM; 73620828; -.
DR EPD; Q9BVJ7; -.
DR jPOST; Q9BVJ7; -.
DR MassIVE; Q9BVJ7; -.
DR MaxQB; Q9BVJ7; -.
DR PaxDb; Q9BVJ7; -.
DR PeptideAtlas; Q9BVJ7; -.
DR PRIDE; Q9BVJ7; -.
DR ProteomicsDB; 79212; -.
DR Antibodypedia; 20475; 186 antibodies from 26 providers.
DR DNASU; 54935; -.
DR Ensembl; ENST00000368107.2; ENSP00000357087.1; ENSG00000158716.9.
DR Ensembl; ENST00000368108.7; ENSP00000357088.3; ENSG00000158716.9.
DR Ensembl; ENST00000368109.5; ENSP00000357089.1; ENSG00000158716.9.
DR GeneID; 54935; -.
DR KEGG; hsa:54935; -.
DR MANE-Select; ENST00000368107.2; ENSP00000357087.1; NM_001319658.2; NP_001306587.1.
DR UCSC; uc001ftz.2; human.
DR CTD; 54935; -.
DR DisGeNET; 54935; -.
DR GeneCards; DUSP23; -.
DR HGNC; HGNC:21480; DUSP23.
DR HPA; ENSG00000158716; Low tissue specificity.
DR MIM; 618361; gene.
DR neXtProt; NX_Q9BVJ7; -.
DR OpenTargets; ENSG00000158716; -.
DR PharmGKB; PA134983082; -.
DR VEuPathDB; HostDB:ENSG00000158716; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00940000161329; -.
DR HOGENOM; CLU_047330_4_2_1; -.
DR InParanoid; Q9BVJ7; -.
DR OMA; CYLVKEQ; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q9BVJ7; -.
DR TreeFam; TF105125; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q9BVJ7; -.
DR SABIO-RK; Q9BVJ7; -.
DR SignaLink; Q9BVJ7; -.
DR BioGRID-ORCS; 54935; 6 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q9BVJ7; -.
DR GeneWiki; DUSP23; -.
DR GenomeRNAi; 54935; -.
DR Pharos; Q9BVJ7; Tbio.
DR PRO; PR:Q9BVJ7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BVJ7; protein.
DR Bgee; ENSG00000158716; Expressed in left adrenal gland cortex and 173 other tissues.
DR ExpressionAtlas; Q9BVJ7; baseline and differential.
DR Genevisible; Q9BVJ7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR026067; Dual_phosphatase_23.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF26; PTHR23339:SF26; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..150
FT /note="Dual specificity protein phosphatase 23"
FT /id="PRO_0000094835"
FT DOMAIN 7..150
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 95
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VARIANT 124
FT /note="E -> V (in dbSNP:rs11544443)"
FT /id="VAR_051756"
FT VARIANT 131
FT /note="G -> S (in dbSNP:rs1129923)"
FT /id="VAR_023199"
FT CONFLICT 132
FT /note="S -> P (in Ref. 2; BAA91172)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4ERC"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4ERC"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:4ERC"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:4ERC"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4ERC"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4ERC"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:4ERC"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4ERC"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:4ERC"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4ERC"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:4ERC"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:4ERC"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:4ERC"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4ERC"
SQ SEQUENCE 150 AA; 16588 MW; 4B72EFA0434B1B5F CRC64;
MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR
LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD
AIAEIRRLRP GSIETYEQEK AVFQFYQRTK
