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 27-MAR-2024, entry version 184. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9606-ENSP00000357087; -. DR PeptideAtlas; Q9BVJ7; -. DR ProteomicsDB; 79212; -. DR Pumba; Q9BVJ7; -. DR Antibodypedia; 20475; 211 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 AGR; HGNC:21480; -. 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; PAHYQYL; -. DR OrthoDB; 318623at2759; -. 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 1173 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 175 other cell types or tissues. DR ExpressionAtlas; Q9BVJ7; baseline and differential. 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:0060271; P:cilium assembly; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB. DR CDD; cd14504; DUSP23; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. 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:SF98; CYCLIN-DEPENDENT KINASE INHIBITOR 3-RELATED; 1. DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q9BVJ7; HS. 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 //