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Q9BV47 (DUS26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 26

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase SKRP3
Low-molecular-mass dual-specificity phosphatase 4
Short name=DSP-4
Short name=LDP-4
Mitogen-activated protein kinase phosphatase 8
Short name=MAP kinase phosphatase 8
Short name=MKP-8
Novel amplified gene in thyroid anaplastic cancer
Gene names
Name:DUSP26
Synonyms:DUSP24, LDP4, MKP8, NATA1, SKRP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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). Ref.1 Ref.2 Ref.3 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with HSF4. Ref.8

Subcellular location

Cytoplasm. Nucleus. Golgi apparatus Ref.1 Ref.3.

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. Ref.1 Ref.2 Ref.3 Ref.8

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Golgi apparatus
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.8. Source: UniProt

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from mutant phenotype Ref.1. Source: UniProt

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: UniProt

peptidyl-tyrosine dephosphorylation

Inferred from mutant phenotype Ref.1. Source: GOC

positive regulation of cell adhesion

Inferred from mutant phenotype PubMed 19043453. Source: UniProt

positive regulation of peptidyl-serine dephosphorylation

Inferred from direct assay PubMed 20562916. Source: UniProt

protein dephosphorylation

Inferred from direct assay Ref.1PubMed 19043453. Source: UniProt

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 19043453. Source: UniProt

cytoplasm

Inferred from direct assay Ref.1PubMed 19043453. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.1. Source: UniProt

   Molecular_functionRNA polymerase II activating transcription factor binding

Inferred from physical interaction Ref.8. Source: UniProt

p53 binding

Inferred from physical interaction PubMed 20562916. Source: UniProt

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 19043453. Source: UniProt

phosphoserine phosphatase activity

Inferred from direct assay PubMed 20562916. Source: UniProt

protein tyrosine phosphatase activity

Inferred from mutant phenotype Ref.1. Source: UniProt

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046379EBI-2924519,EBI-366083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BV47-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BV47-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Dual specificity protein phosphatase 26
PRO_0000292219

Regions

Domain61 – 206146Tyrosine-protein phosphatase

Sites

Active site1521Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence1 – 125125Missing in isoform 2.
VSP_026406

Experimental info

Mutagenesis1521C → A or S: Loss of activity. Ref.1 Ref.2 Ref.8

Secondary structure

............................ 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 60E944304905086D

FASTA21123,946
        10         20         30         40         50         60 
MCPGNWLWAS MTFMARFSRS SSRSPVRTRG TLEEMPTVQH PFLNVFELER LLYTGKTACN 

        70         80         90        100        110        120 
HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHSRWR GTPEAYEGLG IRYLGVEAHD 

       130        140        150        160        170        180 
SPAFDMSIHF QTAADFIHRA LSQPGGKILV HCAVGVSRSA TLVLAYLMLY HHLTLVEAIK 

       190        200        210 
KVKDHRGIIP NRGFLRQLLA LDRRLRQGLE A 

« Hide

Isoform 2 [UniParc].

Checksum: 4DD29AFD5989528B
Show »

FASTA869,652

References

« Hide 'large scale' references
[1]"MKP-8, a novel MAPK phosphatase that inhibits p38 kinase."
Vasudevan S.A., Skoko J., Wang K., Burlingame S.M., Patel P.N., Lazo J.S., Nuchtern J.G., Yang J.
Biochem. Biophys. Res. Commun. 330:511-518(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"A novel amplification target, DUSP26, promotes anaplastic thyroid cancer cell growth by inhibiting p38 MAPK activity."
Yu W., Imoto I., Inoue J., Onda M., Emi M., Inazawa J.
Oncogene 26:1178-1187(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-152, FUNCTION, TISSUE SPECIFICITY.
[3]"Characterization of a novel low-molecular-mass dual specificity phosphatase-4 (LDP-4) expressed in brain."
Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M., Kikuchi K.
Mol. Cell. Biochem. 296:177-184(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Identification of a novel dual specificity phosphatase, SKRP3."
Zama T., Aoki R., Murata M., Ikeda Y.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Lung.
[8]"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."
Hu Y., Mivechi N.F.
Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-152, INTERACTION WITH HSF4, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY902194 mRNA. Translation: AAX07132.1.
AB158288 mRNA. Translation: BAD82942.1.
AB237597 mRNA. Translation: BAE46506.1.
AB103376 mRNA. Translation: BAD91015.1.
AK055704 mRNA. Translation: BAB70991.1.
CH471080 Genomic DNA. Translation: EAW63392.1.
CH471080 Genomic DNA. Translation: EAW63393.1.
CH471080 Genomic DNA. Translation: EAW63394.1.
BC001613 mRNA. Translation: AAH01613.1.
BC003115 mRNA. Translation: AAH03115.1.
BC067804 mRNA. Translation: AAH67804.1.
RefSeqNP_076930.1. NM_024025.1.
XP_005273690.1. XM_005273633.1.
UniGeneHs.8719.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E0TX-ray1.67A61-211[»]
4B04X-ray2.20A/B/C/D61-211[»]
4HRFX-ray1.68A/B/C/D61-211[»]
ProteinModelPortalQ9BV47.
SMRQ9BV47. Positions 31-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122457. 1 interaction.
IntActQ9BV47. 1 interaction.
STRING9606.ENSP00000256261.

Polymorphism databases

DMDM74752374.

Proteomic databases

PaxDbQ9BV47.
PRIDEQ9BV47.

Protocols and materials databases

DNASU78986.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256261; ENSP00000256261; ENSG00000133878. [Q9BV47-1]
ENST00000523956; ENSP00000429176; ENSG00000133878. [Q9BV47-1]
GeneID78986.
KEGGhsa:78986.
UCSCuc003xjp.3. human. [Q9BV47-1]

Organism-specific databases

CTD78986.
GeneCardsGC08M033448.
HGNCHGNC:28161. DUSP26.
HPAHPA018221.
neXtProtNX_Q9BV47.
PharmGKBPA142671921.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000233767.
HOVERGENHBG001524.
InParanoidQ9BV47.
KOK14165.
OMAMAFMSRF.
OrthoDBEOG7CZK7N.
PhylomeDBQ9BV47.
TreeFamTF105128.

Gene expression databases

ArrayExpressQ9BV47.
BgeeQ9BV47.
CleanExHS_DUSP26.
GenevestigatorQ9BV47.

Family and domain databases

InterProIPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BV47.
GenomeRNAi78986.
NextBio67552.
PROQ9BV47.

Entry information

Entry nameDUS26_HUMAN
AccessionPrimary (citable) accession number: Q9BV47
Secondary accession number(s): D3DSV8, Q9BTW0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM