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Q9BVJ7

- DUS23_HUMAN

UniProt

Q9BVJ7 - DUS23_HUMAN

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Protein

Dual specificity protein phosphatase 23

Gene

DUSP23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Kineticsi

  1. KM=1.498 mM for p-nitrophenylphosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SABIO-RKQ9BVJ7.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DUSP23
Synonyms:LDP3, VHZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:21480. DUSP23.

Subcellular locationi

Cytoplasmcytosol. Nucleus
Note: Mainly cytosolic. Also nuclear.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134983082.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 150150Dual specificity protein phosphatase 23PRO_0000094835Add
BLAST

Proteomic databases

MaxQBiQ9BVJ7.
PaxDbiQ9BVJ7.
PeptideAtlasiQ9BVJ7.
PRIDEiQ9BVJ7.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9BVJ7.
CleanExiHS_DUSP23.
GenevestigatoriQ9BVJ7.

Organism-specific databases

HPAiHPA045792.

Interactioni

Protein-protein interaction databases

BioGridi120275. 22 interactions.
IntActiQ9BVJ7. 21 interactions.
MINTiMINT-1412836.
STRINGi9606.ENSP00000357087.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124
Turni13 – 153
Beta strandi16 – 205
Helixi25 – 339
Beta strandi36 – 416
Beta strandi43 – 453
Helixi50 – 523
Beta strandi56 – 605
Helixi71 – 8616
Beta strandi90 – 945
Beta strandi96 – 994
Helixi100 – 11415
Helixi118 – 12811
Helixi136 – 14914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IMGX-ray1.93A2-150[»]
4ERCX-ray1.15A/B1-150[»]
ProteinModelPortaliQ9BVJ7.
SMRiQ9BVJ7. Positions 1-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BVJ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 14066Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00390000010254.
HOGENOMiHOG000108423.
HOVERGENiHBG056524.
InParanoidiQ9BVJ7.
KOiK14165.
OMAiAVVQFYQ.
OrthoDBiEOG7PK90Q.
PhylomeDBiQ9BVJ7.
TreeFamiTF105125.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BVJ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS
60 70 80 90 100
DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG
110 120 130 140 150
RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK
Length:150
Mass (Da):16,588
Last modified:June 1, 2001 - v1
Checksum:i4B72EFA0434B1B5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321S → P in BAA91172. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241E → V.
Corresponds to variant rs11544443 [ dbSNP | Ensembl ].
VAR_051756
Natural varianti131 – 1311G → S.
Corresponds to variant rs1129923 [ dbSNP | Ensembl ].
VAR_023199

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB164404 mRNA. Translation: BAD12141.1.
AK000449 mRNA. Translation: BAA91172.1.
AL590560 Genomic DNA. Translation: CAH71101.1.
BC001140 mRNA. Translation: AAH01140.1.
CCDSiCCDS1187.1.
RefSeqiNP_060293.2. NM_017823.3.
XP_005245346.1. XM_005245289.1.
UniGeneiHs.425801.

Genome annotation databases

EnsembliENST00000368107; ENSP00000357087; ENSG00000158716.
ENST00000368108; ENSP00000357088; ENSG00000158716.
ENST00000368109; ENSP00000357089; ENSG00000158716.
GeneIDi54935.
KEGGihsa:54935.
UCSCiuc001ftz.1. human.

Polymorphism databases

DMDMi73620828.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB164404 mRNA. Translation: BAD12141.1 .
AK000449 mRNA. Translation: BAA91172.1 .
AL590560 Genomic DNA. Translation: CAH71101.1 .
BC001140 mRNA. Translation: AAH01140.1 .
CCDSi CCDS1187.1.
RefSeqi NP_060293.2. NM_017823.3.
XP_005245346.1. XM_005245289.1.
UniGenei Hs.425801.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IMG X-ray 1.93 A 2-150 [» ]
4ERC X-ray 1.15 A/B 1-150 [» ]
ProteinModelPortali Q9BVJ7.
SMRi Q9BVJ7. Positions 1-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120275. 22 interactions.
IntActi Q9BVJ7. 21 interactions.
MINTi MINT-1412836.
STRINGi 9606.ENSP00000357087.

Chemistry

ChEMBLi CHEMBL2396506.

Polymorphism databases

DMDMi 73620828.

Proteomic databases

MaxQBi Q9BVJ7.
PaxDbi Q9BVJ7.
PeptideAtlasi Q9BVJ7.
PRIDEi Q9BVJ7.

Protocols and materials databases

DNASUi 54935.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368107 ; ENSP00000357087 ; ENSG00000158716 .
ENST00000368108 ; ENSP00000357088 ; ENSG00000158716 .
ENST00000368109 ; ENSP00000357089 ; ENSG00000158716 .
GeneIDi 54935.
KEGGi hsa:54935.
UCSCi uc001ftz.1. human.

Organism-specific databases

CTDi 54935.
GeneCardsi GC01P159750.
HGNCi HGNC:21480. DUSP23.
HPAi HPA045792.
neXtProti NX_Q9BVJ7.
PharmGKBi PA134983082.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00390000010254.
HOGENOMi HOG000108423.
HOVERGENi HBG056524.
InParanoidi Q9BVJ7.
KOi K14165.
OMAi AVVQFYQ.
OrthoDBi EOG7PK90Q.
PhylomeDBi Q9BVJ7.
TreeFami TF105125.

Enzyme and pathway databases

SABIO-RK Q9BVJ7.

Miscellaneous databases

EvolutionaryTracei Q9BVJ7.
GeneWikii DUSP23.
GenomeRNAii 54935.
NextBioi 58050.
PROi Q9BVJ7.

Gene expression databases

Bgeei Q9BVJ7.
CleanExi HS_DUSP23.
Genevestigatori Q9BVJ7.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDUS23_HUMAN
AccessioniPrimary (citable) accession number: Q9BVJ7
Secondary accession number(s): Q9NX48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Was originally erroneously termed DUSP25.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3