DUS26_HUMAN
ID DUS26_HUMAN Reviewed; 211 AA.
AC Q9BV47; D3DSV8; Q9BTW0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Dual specificity protein phosphatase 26;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase SKRP3;
DE AltName: Full=Low-molecular-mass dual-specificity phosphatase 4;
DE Short=DSP-4;
DE Short=LDP-4;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 8;
DE Short=MAP kinase phosphatase 8;
DE Short=MKP-8;
DE AltName: Full=Novel amplified gene in thyroid anaplastic cancer;
GN Name=DUSP26; Synonyms=DUSP24, LDP4, MKP8, NATA1, SKRP3;
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] (ISOFORM 1), MUTAGENESIS OF CYS-152, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15796912; DOI=10.1016/j.bbrc.2005.03.028;
RA Vasudevan S.A., Skoko J., Wang K., Burlingame S.M., Patel P.N., Lazo J.S.,
RA Nuchtern J.G., Yang J.;
RT "MKP-8, a novel MAPK phosphatase that inhibits p38 kinase.";
RL Biochem. Biophys. Res. Commun. 330:511-518(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152, FUNCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=16924234; DOI=10.1038/sj.onc.1209899;
RA Yu W., Imoto I., Inoue J., Onda M., Emi M., Inazawa J.;
RT "A novel amplification target, DUSP26, promotes anaplastic thyroid cancer
RT cell growth by inhibiting p38 MAPK activity.";
RL Oncogene 26:1178-1187(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=17001450; DOI=10.1007/s11010-006-9313-5;
RA Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M.,
RA Kikuchi K.;
RT "Characterization of a novel low-molecular-mass dual specificity
RT phosphatase-4 (LDP-4) expressed in brain.";
RL Mol. Cell. Biochem. 296:177-184(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zama T., Aoki R., Murata M., Ikeda Y.;
RT "Identification of a novel dual specificity phosphatase, SKRP3.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and 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 [8]
RP FUNCTION, MUTAGENESIS OF CYS-152, INTERACTION WITH HSF4, AND TISSUE
RP SPECIFICITY.
RX PubMed=16581800; DOI=10.1128/mcb.26.8.3282-3294.2006;
RA Hu Y., Mivechi N.F.;
RT "Association and regulation of heat shock transcription factor 4b with both
RT extracellular signal-regulated kinase mitogen-activated protein kinase and
RT dual-specificity tyrosine phosphatase DUSP26.";
RL Mol. Cell. Biol. 26:3282-3294(2006).
CC -!- FUNCTION: Inactivates MAPK1 and MAPK3 which leads to dephosphorylation
CC of heat shock factor protein 4 and a reduction in its DNA-binding
CC activity. Inhibits MAP kinase p38 by dephosphorylating it and inhibits
CC p38-mediated apoptosis in anaplastic thyroid cancer cells. Can also
CC induce activation of MAP kinase p38 and c-Jun N-terminal kinase (JNK).
CC {ECO:0000269|PubMed:15796912, ECO:0000269|PubMed:16581800,
CC ECO:0000269|PubMed:16924234, ECO:0000269|PubMed:17001450}.
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 -!- SUBUNIT: Interacts with HSF4. {ECO:0000269|PubMed:16581800}.
CC -!- INTERACTION:
CC Q9BV47; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2924519, EBI-739580;
CC Q9BV47; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2924519, EBI-3866279;
CC Q9BV47; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2924519, EBI-5916454;
CC Q9BV47; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-2924519, EBI-717919;
CC Q9BV47; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2924519, EBI-3044087;
CC Q9BV47; P04637: TP53; NbExp=9; IntAct=EBI-2924519, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BV47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BV47-2; Sequence=VSP_026406;
CC -!- TISSUE SPECIFICITY: Brain. In the brain it is expressed ubiquitously
CC except in the hippocampus. Expressed in embryonal cancers
CC (retinoblastoma, neuroepithilioma and neuroblastoma) and in anaplatic
CC thyroid cancer. {ECO:0000269|PubMed:15796912,
CC ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:16924234,
CC ECO:0000269|PubMed:17001450}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AY902194; AAX07132.1; -; mRNA.
DR EMBL; AB158288; BAD82942.1; -; mRNA.
DR EMBL; AB237597; BAE46506.1; -; mRNA.
DR EMBL; AB103376; BAD91015.1; -; mRNA.
DR EMBL; AK055704; BAB70991.1; -; mRNA.
DR EMBL; CH471080; EAW63392.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63393.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63394.1; -; Genomic_DNA.
DR EMBL; BC001613; AAH01613.1; -; mRNA.
DR EMBL; BC003115; AAH03115.1; -; mRNA.
DR EMBL; BC067804; AAH67804.1; -; mRNA.
DR CCDS; CCDS6092.1; -. [Q9BV47-1]
DR RefSeq; NP_001292044.1; NM_001305115.1. [Q9BV47-1]
DR RefSeq; NP_001292045.1; NM_001305116.1. [Q9BV47-1]
DR RefSeq; NP_076930.1; NM_024025.2. [Q9BV47-1]
DR PDB; 2E0T; X-ray; 1.67 A; A=61-211.
DR PDB; 4B04; X-ray; 2.20 A; A/B/C/D=61-211.
DR PDB; 4HRF; X-ray; 1.68 A; A/B/C/D=61-211.
DR PDB; 5GTJ; X-ray; 2.00 A; A/B/C/D=39-211.
DR PDBsum; 2E0T; -.
DR PDBsum; 4B04; -.
DR PDBsum; 4HRF; -.
DR PDBsum; 5GTJ; -.
DR AlphaFoldDB; Q9BV47; -.
DR SMR; Q9BV47; -.
DR BioGRID; 122457; 57.
DR IntAct; Q9BV47; 16.
DR MINT; Q9BV47; -.
DR STRING; 9606.ENSP00000256261; -.
DR BindingDB; Q9BV47; -.
DR ChEMBL; CHEMBL2295562; -.
DR DEPOD; DUSP26; -.
DR iPTMnet; Q9BV47; -.
DR PhosphoSitePlus; Q9BV47; -.
DR BioMuta; DUSP26; -.
DR DMDM; 74752374; -.
DR MassIVE; Q9BV47; -.
DR PaxDb; Q9BV47; -.
DR PeptideAtlas; Q9BV47; -.
DR PRIDE; Q9BV47; -.
DR ProteomicsDB; 79169; -. [Q9BV47-1]
DR Antibodypedia; 10741; 232 antibodies from 31 providers.
DR DNASU; 78986; -.
DR Ensembl; ENST00000256261.9; ENSP00000256261.4; ENSG00000133878.9. [Q9BV47-1]
DR Ensembl; ENST00000523956.1; ENSP00000429176.1; ENSG00000133878.9. [Q9BV47-1]
DR GeneID; 78986; -.
DR KEGG; hsa:78986; -.
DR MANE-Select; ENST00000256261.9; ENSP00000256261.4; NM_024025.3; NP_076930.1.
DR UCSC; uc003xjp.4; human. [Q9BV47-1]
DR CTD; 78986; -.
DR DisGeNET; 78986; -.
DR GeneCards; DUSP26; -.
DR HGNC; HGNC:28161; DUSP26.
DR HPA; ENSG00000133878; Group enriched (skeletal muscle, tongue).
DR MIM; 618368; gene.
DR neXtProt; NX_Q9BV47; -.
DR OpenTargets; ENSG00000133878; -.
DR PharmGKB; PA142671921; -.
DR VEuPathDB; HostDB:ENSG00000133878; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000158107; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR InParanoid; Q9BV47; -.
DR OMA; TVYFDEC; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9BV47; -.
DR TreeFam; TF105128; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; Q9BV47; -.
DR SignaLink; Q9BV47; -.
DR SIGNOR; Q9BV47; -.
DR BioGRID-ORCS; 78986; 17 hits in 1027 CRISPR screens.
DR EvolutionaryTrace; Q9BV47; -.
DR GenomeRNAi; 78986; -.
DR Pharos; Q9BV47; Tbio.
DR PRO; PR:Q9BV47; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BV47; protein.
DR Bgee; ENSG00000133878; Expressed in hindlimb stylopod muscle and 155 other tissues.
DR ExpressionAtlas; Q9BV47; baseline and differential.
DR Genevisible; Q9BV47; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 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; Alternative splicing; Cytoplasm; Golgi apparatus; Hydrolase;
KW Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..211
FT /note="Dual specificity protein phosphatase 26"
FT /id="PRO_0000292219"
FT DOMAIN 60..207
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 152
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026406"
FT MUTAGEN 152
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15796912,
FT ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:16924234"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:5GTJ"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2E0T"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2E0T"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2E0T"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:2E0T"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2E0T"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4HRF"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2E0T"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2E0T"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:2E0T"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2E0T"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2E0T"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:2E0T"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2E0T"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:2E0T"
SQ SEQUENCE 211 AA; 23946 MW; 60E944304905086D CRC64;
MCPGNWLWAS MTFMARFSRS SSRSPVRTRG TLEEMPTVQH PFLNVFELER LLYTGKTACN
HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHSRWR GTPEAYEGLG IRYLGVEAHD
SPAFDMSIHF QTAADFIHRA LSQPGGKILV HCAVGVSRSA TLVLAYLMLY HHLTLVEAIK
KVKDHRGIIP NRGFLRQLLA LDRRLRQGLE A
