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Dual specificity protein phosphatase 26 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP3) (Low-molecular-mass dual-specificity phosphatase 4) (DSP-4) (LDP-4) (Mitogen-activated protein kinase phosphatase 8) (MAP kinase phosphatase 8) (MKP-8) (Novel amplified gene in thyroid anaplastic cancer)

 DUS26_HUMAN             Reviewed;         211 AA.
Q9BV47; D3DSV8; Q9BTW0;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 135.
RecName: Full=Dual specificity protein phosphatase 26;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=Dual specificity phosphatase SKRP3;
AltName: Full=Low-molecular-mass dual-specificity phosphatase 4;
Short=DSP-4;
Short=LDP-4;
AltName: Full=Mitogen-activated protein kinase phosphatase 8;
Short=MAP kinase phosphatase 8;
Short=MKP-8;
AltName: Full=Novel amplified gene in thyroid anaplastic cancer;
Name=DUSP26; Synonyms=DUSP24, LDP4, MKP8, NATA1, SKRP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152,
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15796912; DOI=10.1016/j.bbrc.2005.03.028;
Vasudevan S.A., Skoko J., Wang K., Burlingame S.M., Patel P.N.,
Lazo J.S., Nuchtern J.G., Yang J.;
"MKP-8, a novel MAPK phosphatase that inhibits p38 kinase.";
Biochem. Biophys. Res. Commun. 330:511-518(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152,
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16924234; DOI=10.1038/sj.onc.1209899;
Yu W., Imoto I., Inoue J., Onda M., Emi M., Inazawa J.;
"A novel amplification target, DUSP26, promotes anaplastic thyroid
cancer cell growth by inhibiting p38 MAPK activity.";
Oncogene 26:1178-1187(2007).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=17001450; DOI=10.1007/s11010-006-9313-5;
Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M.,
Kikuchi K.;
"Characterization of a novel low-molecular-mass dual specificity
phosphatase-4 (LDP-4) expressed in brain.";
Mol. Cell. Biochem. 296:177-184(2007).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zama T., Aoki R., Murata M., Ikeda Y.;
"Identification of a novel dual specificity phosphatase, SKRP3.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and 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).
[8]
FUNCTION, MUTAGENESIS OF CYS-152, INTERACTION WITH HSF4, AND TISSUE
SPECIFICITY.
PubMed=16581800; DOI=10.1128/MCB.26.8.3282-3294.2006;
Hu Y., Mivechi N.F.;
"Association and regulation of heat shock transcription factor 4b with
both extracellular signal-regulated kinase mitogen-activated protein
kinase and dual-specificity tyrosine phosphatase DUSP26.";
Mol. Cell. Biol. 26:3282-3294(2006).
-!- FUNCTION: Inactivates MAPK1 and MAPK3 which leads to
dephosphorylation of heat shock factor protein 4 and a reduction
in its DNA-binding activity. Inhibits MAP kinase p38 by
dephosphorylating it and inhibits p38-mediated apoptosis in
anaplastic thyroid cancer cells. Can also induce activation of MAP
kinase p38 and c-Jun N-terminal kinase (JNK).
{ECO:0000269|PubMed:15796912, ECO:0000269|PubMed:16581800,
ECO:0000269|PubMed:16924234, ECO:0000269|PubMed:17001450}.
-!- 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.
-!- SUBUNIT: Interacts with HSF4. {ECO:0000269|PubMed:16581800}.
-!- INTERACTION:
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-2924519, EBI-739580;
A6NEM1:GOLGA6L9; NbExp=4; IntAct=EBI-2924519, EBI-5916454;
P04637:TP53; NbExp=9; IntAct=EBI-2924519, EBI-366083;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Golgi apparatus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BV47-1; Sequence=Displayed;
Name=2;
IsoId=Q9BV47-2; Sequence=VSP_026406;
-!- TISSUE SPECIFICITY: Brain. In the brain it is expressed
ubiquitously except in the hippocampus. Expressed in embryonal
cancers (retinoblastoma, neuroepithilioma and neuroblastoma) and
in anaplatic thyroid cancer. {ECO:0000269|PubMed:15796912,
ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:16924234,
ECO:0000269|PubMed:17001450}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY902194; AAX07132.1; -; mRNA.
EMBL; AB158288; BAD82942.1; -; mRNA.
EMBL; AB237597; BAE46506.1; -; mRNA.
EMBL; AB103376; BAD91015.1; -; mRNA.
EMBL; AK055704; BAB70991.1; -; mRNA.
EMBL; CH471080; EAW63392.1; -; Genomic_DNA.
EMBL; CH471080; EAW63393.1; -; Genomic_DNA.
EMBL; CH471080; EAW63394.1; -; Genomic_DNA.
EMBL; BC001613; AAH01613.1; -; mRNA.
EMBL; BC003115; AAH03115.1; -; mRNA.
EMBL; BC067804; AAH67804.1; -; mRNA.
CCDS; CCDS6092.1; -. [Q9BV47-1]
RefSeq; NP_001292044.1; NM_001305115.1. [Q9BV47-1]
RefSeq; NP_001292045.1; NM_001305116.1. [Q9BV47-1]
RefSeq; NP_076930.1; NM_024025.2. [Q9BV47-1]
UniGene; Hs.8719; -.
PDB; 2E0T; X-ray; 1.67 A; A=61-211.
PDB; 4B04; X-ray; 2.20 A; A/B/C/D=61-211.
PDB; 4HRF; X-ray; 1.68 A; A/B/C/D=61-211.
PDB; 5GTJ; X-ray; 2.00 A; A/B/C/D=39-211.
PDBsum; 2E0T; -.
PDBsum; 4B04; -.
PDBsum; 4HRF; -.
PDBsum; 5GTJ; -.
ProteinModelPortal; Q9BV47; -.
SMR; Q9BV47; -.
BioGrid; 122457; 25.
IntAct; Q9BV47; 7.
STRING; 9606.ENSP00000256261; -.
ChEMBL; CHEMBL2295562; -.
DEPOD; Q9BV47; -.
iPTMnet; Q9BV47; -.
PhosphoSitePlus; Q9BV47; -.
BioMuta; DUSP26; -.
DMDM; 74752374; -.
PaxDb; Q9BV47; -.
PeptideAtlas; Q9BV47; -.
PRIDE; Q9BV47; -.
DNASU; 78986; -.
Ensembl; ENST00000256261; ENSP00000256261; ENSG00000133878. [Q9BV47-1]
Ensembl; ENST00000523956; ENSP00000429176; ENSG00000133878. [Q9BV47-1]
GeneID; 78986; -.
KEGG; hsa:78986; -.
UCSC; uc003xjp.4; human. [Q9BV47-1]
CTD; 78986; -.
DisGeNET; 78986; -.
EuPathDB; HostDB:ENSG00000133878.8; -.
GeneCards; DUSP26; -.
HGNC; HGNC:28161; DUSP26.
HPA; HPA018221; -.
neXtProt; NX_Q9BV47; -.
OpenTargets; ENSG00000133878; -.
PharmGKB; PA142671921; -.
eggNOG; KOG1716; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000118853; -.
HOGENOM; HOG000233767; -.
HOVERGEN; HBG001524; -.
InParanoid; Q9BV47; -.
KO; K14165; -.
OMA; YLMIRQN; -.
OrthoDB; EOG091G0249; -.
PhylomeDB; Q9BV47; -.
TreeFam; TF105128; -.
BRENDA; 3.1.3.16; 2681.
SIGNOR; Q9BV47; -.
EvolutionaryTrace; Q9BV47; -.
GenomeRNAi; 78986; -.
PRO; PR:Q9BV47; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000133878; -.
CleanEx; HS_DUSP26; -.
ExpressionAtlas; Q9BV47; baseline and differential.
Genevisible; Q9BV47; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0004647; F:phosphoserine phosphatase activity; IDA:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:1902310; P:positive regulation of peptidyl-serine dephosphorylation; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
CDD; cd00127; DSPc; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR020405; Atypical_DUSP_famA.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PRINTS; PR01908; ADSPHPHTASE.
PRINTS; PR01909; ADSPHPHTASEA.
SMART; SM00195; DSPc; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Golgi apparatus; Hydrolase; Nucleus; Protein phosphatase;
Reference proteome.
CHAIN 1 211 Dual specificity protein phosphatase 26.
/FTId=PRO_0000292219.
DOMAIN 61 206 Tyrosine-protein phosphatase.
ACT_SITE 152 152 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
VAR_SEQ 1 125 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026406.
MUTAGEN 152 152 C->A,S: Loss of activity.
{ECO:0000269|PubMed:15796912,
ECO:0000269|PubMed:16581800,
ECO:0000269|PubMed:16924234}.
HELIX 45 54 {ECO:0000244|PDB:5GTJ}.
STRAND 62 66 {ECO:0000244|PDB:2E0T}.
STRAND 69 72 {ECO:0000244|PDB:2E0T}.
HELIX 74 77 {ECO:0000244|PDB:2E0T}.
HELIX 80 86 {ECO:0000244|PDB:2E0T}.
STRAND 90 93 {ECO:0000244|PDB:2E0T}.
TURN 98 100 {ECO:0000244|PDB:4HRF}.
HELIX 106 109 {ECO:0000244|PDB:2E0T}.
STRAND 112 115 {ECO:0000244|PDB:2E0T}.
HELIX 127 142 {ECO:0000244|PDB:2E0T}.
STRAND 148 151 {ECO:0000244|PDB:2E0T}.
STRAND 153 156 {ECO:0000244|PDB:2E0T}.
HELIX 157 170 {ECO:0000244|PDB:2E0T}.
HELIX 175 184 {ECO:0000244|PDB:2E0T}.
HELIX 192 207 {ECO:0000244|PDB:2E0T}.
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


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