Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BVJ7 (DUS23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.5 Ref.6

Subcellular location

Cytoplasmcytosol. 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 componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 150150Dual specificity protein phosphatase 23
PRO_0000094835

Regions

Domain75 – 14066Tyrosine-protein phosphatase

Sites

Active site951Phosphocysteine intermediate By similarity

Natural variations

Natural variant1241E → V.
Corresponds to variant rs11544443 [ dbSNP | Ensembl ].
VAR_051756
Natural variant1311G → S.
Corresponds to variant rs1129923 [ dbSNP | Ensembl ].
VAR_023199

Experimental info

Sequence conflict1321S → P in BAA91172. Ref.2

Secondary structure

.......................... 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BVJ7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 4B72EFA0434B1B5F

FASTA15016,588
        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 

« Hide

References

« Hide '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. 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].
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. expand/collapse author list , 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.
CCDSCCDS1187.1.
RefSeqNP_060293.2. NM_017823.3.
XP_005245346.1. XM_005245289.1.
UniGeneHs.425801.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IMGX-ray1.93A2-150[»]
4ERCX-ray1.15A/B1-150[»]
ProteinModelPortalQ9BVJ7.
SMRQ9BVJ7. Positions 1-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120275. 22 interactions.
IntActQ9BVJ7. 21 interactions.
MINTMINT-1412836.
STRING9606.ENSP00000357087.

Chemistry

ChEMBLCHEMBL2396506.

Polymorphism databases

DMDM73620828.

Proteomic databases

MaxQBQ9BVJ7.
PaxDbQ9BVJ7.
PeptideAtlasQ9BVJ7.
PRIDEQ9BVJ7.

Protocols and materials databases

DNASU54935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368107; ENSP00000357087; ENSG00000158716.
ENST00000368108; ENSP00000357088; ENSG00000158716.
ENST00000368109; ENSP00000357089; ENSG00000158716.
GeneID54935.
KEGGhsa:54935.
UCSCuc001ftz.1. human.

Organism-specific databases

CTD54935.
GeneCardsGC01P159750.
HGNCHGNC:21480. DUSP23.
HPAHPA045792.
neXtProtNX_Q9BVJ7.
PharmGKBPA134983082.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000108423.
HOVERGENHBG056524.
InParanoidQ9BVJ7.
KOK14165.
OMAAVVQFYQ.
OrthoDBEOG7PK90Q.
PhylomeDBQ9BVJ7.
TreeFamTF105125.

Enzyme and pathway databases

SABIO-RKQ9BVJ7.

Gene expression databases

BgeeQ9BVJ7.
CleanExHS_DUSP23.
GenevestigatorQ9BVJ7.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF00782. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BVJ7.
GeneWikiDUSP23.
GenomeRNAi54935.
NextBio58050.
PROQ9BVJ7.

Entry information

Entry nameDUS23_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 119 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM