Full text data of DUSP23
DUSP23
(LDP3, VHZ)
[Confidence: low (only semi-automatic identification from reviews)]
Dual specificity protein phosphatase 23; 3.1.3.16; 3.1.3.48 (Low molecular mass dual specificity phosphatase 3; LDP-3; VH1-like phosphatase Z)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dual specificity protein phosphatase 23; 3.1.3.16; 3.1.3.48 (Low molecular mass dual specificity phosphatase 3; LDP-3; VH1-like phosphatase Z)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BVJ7
ID DUS23_HUMAN Reviewed; 150 AA.
AC Q9BVJ7; Q9NX48;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 114.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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
RP 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.,
RA Buerckstuemmer T., 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 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,
RT enzyme-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
CC can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta
CC (MAPK10) in vitro. Able to enhance activation of JNK and p38
CC (MAPK14).
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.498 mM for p-nitrophenylphosphate;
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
CC trachea. Expressed at lower level in uterus, small intestine,
CC bladder, bone marrow, brain, spinal cord and stomach.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class dual specificity subfamily.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -!- CAUTION: Was originally erroneously termed DUSP25.
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DR EMBL; AB164404; BAD12141.1; -; mRNA.
DR EMBL; AK000449; BAA91172.1; -; mRNA.
DR EMBL; AL590560; CAH71101.1; -; Genomic_DNA.
DR EMBL; BC001140; AAH01140.1; -; mRNA.
DR RefSeq; NP_060293.2; NM_017823.3.
DR RefSeq; XP_005245346.1; XM_005245289.1.
DR UniGene; Hs.425801; -.
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 ProteinModelPortal; Q9BVJ7; -.
DR SMR; Q9BVJ7; 1-150.
DR IntAct; Q9BVJ7; 21.
DR MINT; MINT-1412836; -.
DR STRING; 9606.ENSP00000357087; -.
DR DMDM; 73620828; -.
DR PaxDb; Q9BVJ7; -.
DR PeptideAtlas; Q9BVJ7; -.
DR PRIDE; Q9BVJ7; -.
DR DNASU; 54935; -.
DR Ensembl; ENST00000368107; ENSP00000357087; ENSG00000158716.
DR Ensembl; ENST00000368108; ENSP00000357088; ENSG00000158716.
DR Ensembl; ENST00000368109; ENSP00000357089; ENSG00000158716.
DR GeneID; 54935; -.
DR KEGG; hsa:54935; -.
DR UCSC; uc001ftz.1; human.
DR CTD; 54935; -.
DR GeneCards; GC01P159750; -.
DR HGNC; HGNC:21480; DUSP23.
DR HPA; HPA045792; -.
DR neXtProt; NX_Q9BVJ7; -.
DR PharmGKB; PA134983082; -.
DR eggNOG; COG2453; -.
DR HOGENOM; HOG000108423; -.
DR HOVERGEN; HBG056524; -.
DR InParanoid; Q9BVJ7; -.
DR KO; K14165; -.
DR OMA; CERKPPN; -.
DR OrthoDB; EOG7PK90Q; -.
DR PhylomeDB; Q9BVJ7; -.
DR SABIO-RK; Q9BVJ7; -.
DR EvolutionaryTrace; Q9BVJ7; -.
DR GeneWiki; DUSP23; -.
DR GenomeRNAi; 54935; -.
DR NextBio; 58050; -.
DR PRO; PR:Q9BVJ7; -.
DR Bgee; Q9BVJ7; -.
DR CleanEx; HS_DUSP23; -.
DR Genevestigator; Q9BVJ7; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR Pfam; PF00782; DSPc; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
KW Polymorphism; Protein phosphatase; Reference proteome.
FT CHAIN 1 150 Dual specificity protein phosphatase 23.
FT /FTId=PRO_0000094835.
FT DOMAIN 75 140 Tyrosine-protein phosphatase.
FT ACT_SITE 95 95 Phosphocysteine intermediate (By
FT similarity).
FT VARIANT 124 124 E -> V (in dbSNP:rs11544443).
FT /FTId=VAR_051756.
FT VARIANT 131 131 G -> S (in dbSNP:rs1129923).
FT /FTId=VAR_023199.
FT CONFLICT 132 132 S -> P (in Ref. 2; BAA91172).
FT STRAND 9 12
FT TURN 13 15
FT STRAND 16 20
FT HELIX 25 33
FT STRAND 36 41
FT STRAND 43 45
FT HELIX 50 52
FT STRAND 56 60
FT HELIX 71 86
FT STRAND 90 94
FT STRAND 96 99
FT HELIX 100 114
FT HELIX 118 128
FT HELIX 136 149
SQ SEQUENCE 150 AA; 16588 MW; 4B72EFA0434B1B5F CRC64;
MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR
LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD
AIAEIRRLRP GSIETYEQEK AVFQFYQRTK
//
ID DUS23_HUMAN Reviewed; 150 AA.
AC Q9BVJ7; Q9NX48;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 114.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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
RP 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.,
RA Buerckstuemmer T., 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 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,
RT enzyme-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
CC can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta
CC (MAPK10) in vitro. Able to enhance activation of JNK and p38
CC (MAPK14).
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.498 mM for p-nitrophenylphosphate;
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
CC trachea. Expressed at lower level in uterus, small intestine,
CC bladder, bone marrow, brain, spinal cord and stomach.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class dual specificity subfamily.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -!- CAUTION: Was originally erroneously termed DUSP25.
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DR EMBL; AB164404; BAD12141.1; -; mRNA.
DR EMBL; AK000449; BAA91172.1; -; mRNA.
DR EMBL; AL590560; CAH71101.1; -; Genomic_DNA.
DR EMBL; BC001140; AAH01140.1; -; mRNA.
DR RefSeq; NP_060293.2; NM_017823.3.
DR RefSeq; XP_005245346.1; XM_005245289.1.
DR UniGene; Hs.425801; -.
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 ProteinModelPortal; Q9BVJ7; -.
DR SMR; Q9BVJ7; 1-150.
DR IntAct; Q9BVJ7; 21.
DR MINT; MINT-1412836; -.
DR STRING; 9606.ENSP00000357087; -.
DR DMDM; 73620828; -.
DR PaxDb; Q9BVJ7; -.
DR PeptideAtlas; Q9BVJ7; -.
DR PRIDE; Q9BVJ7; -.
DR DNASU; 54935; -.
DR Ensembl; ENST00000368107; ENSP00000357087; ENSG00000158716.
DR Ensembl; ENST00000368108; ENSP00000357088; ENSG00000158716.
DR Ensembl; ENST00000368109; ENSP00000357089; ENSG00000158716.
DR GeneID; 54935; -.
DR KEGG; hsa:54935; -.
DR UCSC; uc001ftz.1; human.
DR CTD; 54935; -.
DR GeneCards; GC01P159750; -.
DR HGNC; HGNC:21480; DUSP23.
DR HPA; HPA045792; -.
DR neXtProt; NX_Q9BVJ7; -.
DR PharmGKB; PA134983082; -.
DR eggNOG; COG2453; -.
DR HOGENOM; HOG000108423; -.
DR HOVERGEN; HBG056524; -.
DR InParanoid; Q9BVJ7; -.
DR KO; K14165; -.
DR OMA; CERKPPN; -.
DR OrthoDB; EOG7PK90Q; -.
DR PhylomeDB; Q9BVJ7; -.
DR SABIO-RK; Q9BVJ7; -.
DR EvolutionaryTrace; Q9BVJ7; -.
DR GeneWiki; DUSP23; -.
DR GenomeRNAi; 54935; -.
DR NextBio; 58050; -.
DR PRO; PR:Q9BVJ7; -.
DR Bgee; Q9BVJ7; -.
DR CleanEx; HS_DUSP23; -.
DR Genevestigator; Q9BVJ7; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR Pfam; PF00782; DSPc; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Nucleus;
KW Polymorphism; Protein phosphatase; Reference proteome.
FT CHAIN 1 150 Dual specificity protein phosphatase 23.
FT /FTId=PRO_0000094835.
FT DOMAIN 75 140 Tyrosine-protein phosphatase.
FT ACT_SITE 95 95 Phosphocysteine intermediate (By
FT similarity).
FT VARIANT 124 124 E -> V (in dbSNP:rs11544443).
FT /FTId=VAR_051756.
FT VARIANT 131 131 G -> S (in dbSNP:rs1129923).
FT /FTId=VAR_023199.
FT CONFLICT 132 132 S -> P (in Ref. 2; BAA91172).
FT STRAND 9 12
FT TURN 13 15
FT STRAND 16 20
FT HELIX 25 33
FT STRAND 36 41
FT STRAND 43 45
FT HELIX 50 52
FT STRAND 56 60
FT HELIX 71 86
FT STRAND 90 94
FT STRAND 96 99
FT HELIX 100 114
FT HELIX 118 128
FT HELIX 136 149
SQ SEQUENCE 150 AA; 16588 MW; 4B72EFA0434B1B5F CRC64;
MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR
LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD
AIAEIRRLRP GSIETYEQEK AVFQFYQRTK
//