Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6NT99 (DUS23_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
Gene names
Name:Dusp23
Synonyms:Ldp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1

A phosphoprotein + H2O = a protein + phosphate. Ref.1

Subcellular location

Cytoplasm › cytosol By similarity. Nucleus By similarity. Note: Mainly cytosolic. Weakly nuclear By similarity. Ref.1

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

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

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 150150Dual specificity protein phosphatase 23
PRO_0000094836

Regions

Domain75 – 14066Tyrosine-protein phosphatase

Sites

Active site951Phosphocysteine intermediate By similarity

Experimental info

Sequence conflict131P → L in BAB23663. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6NT99 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 00EFC7D3F275CA66

FASTA15016,637
        10         20         30         40         50         60 
MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDQGVRHLV SLTERGPPHS DSCPGLTLHR 

        70         80         90        100        110        120 
MRIPDFCPPS PEQIDQFVKI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERALAAGD 

       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], ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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].
Strain: C57BL/6J.
Tissue: Mammary gland.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB183013 mRNA. Translation: BAD26711.1.
BC069187 mRNA. Translation: AAH69187.1.
AK004912 mRNA. Translation: BAB23663.1.
IPIIPI00339521.
RefSeqNP_081001.1. NM_026725.2.
UniGeneMm.33024.

3D structure databases

ProteinModelPortalQ6NT99.
SMRQ6NT99. Positions 1-150.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000027826.

Proteomic databases

PaxDbQ6NT99.
PRIDEQ6NT99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027826; ENSMUSP00000027826; ENSMUSG00000026544.
GeneID68440.
KEGGmmu:68440.
UCSCuc007dqw.1. mouse.

Organism-specific databases

CTD54935.
MGIMGI:1915690. Dusp23.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00390000010254.
HOGENOMHOG000108423.
HOVERGENHBG056524.
InParanoidQ6NT99.
KOK14165.
OMAHGRTGTM.
OrthoDBEOG4Q58QR.

Gene expression databases

BgeeQ6NT99.
CleanExMM_DUSP23.
GenevestigatorQ6NT99.
GermOnlineENSMUSG00000026544. Mus musculus.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR026067. Dual_phosphatase_23.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR23339:SF26. PTHR23339:SF26. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio327184.
SOURCESearch...

Entry information

Entry nameDUS23_MOUSE
AccessionPrimary (citable) accession number: Q6NT99
Secondary accession number(s): Q9CW48
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents