Q9BVJ7 (DUS23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 23
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Low molecular mass dual specificity phosphatase 3
Short name=LDP-3
VH1-like phosphatase Z

Gene names

Name:	DUSP23
Synonyms:	LDP3, VHZ

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	150 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14). Ref.5 Ref.6
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.5 Ref.6 A phosphoprotein + H2O = a protein + phosphate. Ref.5 Ref.6
Subcellular location	Cytoplasm › cytosol. Nucleus. Note: Mainly cytosolic. Also nuclear. Ref.5 Ref.6
Tissue specificity	Widely expressed. Highly expressed in spleen, prostate, colon, adrenal gland, mammary gland, thyroid and trachea. Expressed at lower level in uterus, small intestine, bladder, bone marrow, brain, spinal cord and stomach. Ref.5 Ref.6
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.
Caution	Was originally erroneously termed DUSP25.
Biophysicochemical properties	Kinetic parameters: KM=1.498 mM for p-nitrophenylphosphate Ref.5

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
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	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 150

150

Dual specificity protein phosphatase 23

PRO_0000094835

Regions

Domain

75 – 140

66

Tyrosine-protein phosphatase

Sites

Active site

95

1

Phosphocysteine intermediate By similarity

Natural variations

Natural variant

124

1

E → V.
Corresponds to variant rs11544443 [ dbSNP | Ensembl ].

VAR_051756

Natural variant

131

1

G → S.
Corresponds to variant rs1129923 [ dbSNP | Ensembl ].

VAR_023199

Experimental info

Sequence conflict

132

1

S → P in BAA91172. Ref.2

Secondary structure

1

.

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150

Helix Strand Turn

Details...

Beta strand

9 – 12

4

Turn

13 – 15

3

Beta strand

16 – 20

5

Helix

25 – 33

9

Beta strand

36 – 41

6

Beta strand

43 – 45

3

Helix

50 – 52

3

Beta strand

56 – 60

5

Helix

71 – 86

16

Beta strand

90 – 94

5

Beta strand

96 – 99

4

Helix

100 – 114

15

Helix

118 – 128

11

Helix

136 – 149

14

Sequences

	Sequence		Length	Mass (Da)
	Q9BVJ7 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 4B72EFA0434B1B5F	FASTA	150	16,588
	10 20 30 40 50 60 MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR 70 80 90 100 110 120 LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD 130 140 150 AIAEIRRLRP GSIETYEQEK AVFQFYQRTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38." Takagaki K., Satoh T., Tanuma N., Masuda K., Takekawa M., Shima H., Kikuchi K. Biochem. J. 383:447-455(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Tissue: Carcinoma.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Lung.
[5]	"The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ." Alonso A., Burkhalter S., Sasin J., Tautz L., Bogetz J., Huynh H., Bremer M.C.D., Holsinger L.J., Godzik A., Mustelin T. J. Biol. Chem. 279:35768-35774(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"Molecular cloning and characterization of a novel dual-specificity phosphatase 23 gene from human fetal brain." Wu Q., Li Y., Gu S., Li N., Zheng D., Li D., Zheng Z., Ji C., Xie Y., Mao Y. Int. J. Biochem. Cell Biol. 36:1542-1553(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-substrate/product complex." Agarwal R., Burley S.K., Swaminathan S. J. Biol. Chem. 283:8946-8953(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-150.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB164404 mRNA. Translation: BAD12141.1.
AK000449 mRNA. Translation: BAA91172.1.
AL590560 Genomic DNA. Translation: CAH71101.1.
BC001140 mRNA. Translation: AAH01140.1.

IPI

IPI00306353.

RefSeq

NP_060293.2. NM_017823.3.

UniGene

Hs.425801.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IMG	X-ray	1.93	A	2-150	[»]
4ERC	X-ray	1.15	A/B	1-150	[»]

ProteinModelPortal

Q9BVJ7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BVJ7. 1 interaction.

MINT

MINT-1412836.

STRING

9606.ENSP00000357087.

Polymorphism databases

DMDM

73620828.

Proteomic databases

PaxDb

Q9BVJ7.

PeptideAtlas

Q9BVJ7.

PRIDE

Q9BVJ7.

Protocols and materials databases

DNASU

54935.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368107; ENSP00000357087; ENSG00000158716.
ENST00000368108; ENSP00000357088; ENSG00000158716.
ENST00000368109; ENSP00000357089; ENSG00000158716.

GeneID

54935.

KEGG

hsa:54935.

UCSC

uc001ftz.1. human.

Organism-specific databases

CTD

54935.

GeneCards

GC01P159750.

HGNC

HGNC:21480. DUSP23.

HPA

HPA045792.

neXtProt

NX_Q9BVJ7.

PharmGKB

PA134983082.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000108423.

HOVERGEN

HBG056524.

InParanoid

Q9BVJ7.

KO

K14165.

OMA

HGRTGTM.

OrthoDB

EOG4Q58QR.

PhylomeDB

Q9BVJ7.

Gene expression databases

Bgee

Q9BVJ7.

CleanEx

HS_DUSP23.

Genevestigator

Q9BVJ7.

GermOnline

ENSG00000158716. Homo sapiens.

Family and domain databases

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR026067. Dual_phosphatase_23.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

PANTHER

PTHR23339:SF26. PTHR23339:SF26. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BVJ7.

GenomeRNAi

54935.

NextBio

58050.

Entry information

Entry name

DUS23_HUMAN

Accession

Primary (citable) accession number: Q9BVJ7
Secondary accession number(s): Q9NX48

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 108 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.