Q9BV47 (DUS26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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 component	Cytoplasm Golgi apparatus Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TP53	P04637	9	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Dual specificity protein phosphatase 26

PRO_0000292219

Regions

Domain

61 – 206

146

Tyrosine-protein phosphatase

Sites

Active site

152

1

Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence

1 – 125

125

Missing in isoform 2.

VSP_026406

Experimental info

Mutagenesis

152

1

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

Secondary structure

1

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211

Helix Strand Turn

Details...

Beta strand

62 – 66

5

Beta strand

69 – 72

4

Helix

74 – 77

4

Helix

80 – 86

7

Beta strand

90 – 93

4

Turn

98 – 100

3

Helix

106 – 109

4

Beta strand

112 – 115

4

Helix

127 – 142

16

Beta strand

148 – 151

4

Beta strand

153 – 156

4

Helix

157 – 170

14

Helix

175 – 184

10

Helix

192 – 207

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 60E944304905086D	FASTA	211	23,946
	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
	Isoform 2 [UniParc]. Checksum: 4DD29AFD5989528B	FASTA	86	9,652
	10 20 30 40 50 60 MSIHFQTAAD FIHRALSQPG GKILVHCAVG VSRSATLVLA YLMLYHHLTL VEAIKKVKDH 70 80 RGIIPNRGFL RQLLALDRRL RQGLEA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

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.

IPI

IPI00031482.
IPI00847898.

RefSeq

NP_076930.1. NM_024025.1.

UniGene

Hs.8719.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E0T	X-ray	1.67	A	61-211	[»]
4HRF	X-ray	1.68	A/B/C/D	61-211	[»]

ProteinModelPortal

Q9BV47.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BV47. 1 interaction.

STRING

9606.ENSP00000256261.

Polymorphism databases

DMDM

74752374.

Proteomic databases

PaxDb

Q9BV47.

PRIDE

Q9BV47.

Protocols and materials databases

DNASU

78986.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256261; ENSP00000256261; ENSG00000133878.
ENST00000523956; ENSP00000429176; ENSG00000133878.

GeneID

78986.

KEGG

hsa:78986.

UCSC

uc003xjp.3. human.

Organism-specific databases

CTD

78986.

GeneCards

GC08M033448.

HGNC

HGNC:28161. DUSP26.

neXtProt

NX_Q9BV47.

PharmGKB

PA142671921.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000233767.

HOVERGEN

HBG001524.

InParanoid

Q9BV47.

KO

K14165.

OMA

PAVQHPF.

OrthoDB

EOG4BCDP2.

PhylomeDB

Q9BV47.

Gene expression databases

ArrayExpress

Q9BV47.

Bgee

Q9BV47.

CleanEx

HS_DUSP26.

Genevestigator

Q9BV47.

Family and domain databases

InterPro

IPR020417. 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]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

PRINTS

PR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.

SMART

SM00195. DSPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BV47.

GenomeRNAi

78986.

NextBio

67552.

Entry information

Entry name

DUS26_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.