Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dual specificity protein phosphatase 22

Gene

Dusp22

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK).1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Phosphocysteine intermediate

GO - Molecular functioni

  1. protein tyrosine/serine/threonine phosphatase activity Source: MGI
  2. protein tyrosine phosphatase activity Source: MGI

GO - Biological processi

  1. negative regulation of T cell activation Source: MGI
  2. negative regulation of T cell mediated immunity Source: MGI
  3. negative regulation of T cell receptor signaling pathway Source: MGI
  4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  5. peptidyl-tyrosine dephosphorylation Source: GOC
  6. positive regulation of JNK cascade Source: MGI
  7. protein dephosphorylation Source: GO_Central
  8. regulation of cell proliferation Source: MGI
  9. transforming growth factor beta receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 22 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Low molecular weight dual specificity phosphatase 2
Short name:
LMW-DSP2
Gene namesi
Name:Dusp22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1915926. Dusp22.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571D → A: Great decrease in activity. 1 Publication
Mutagenesisi88 – 881C → S: Complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 184183Dual specificity protein phosphatase 22PRO_0000244752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity

Post-translational modificationi

Myristoylation regulates subcellular location, and is necessary for activation of JNK.By similarity

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

MaxQBiQ99N11.
PaxDbiQ99N11.
PRIDEiQ99N11.

Expressioni

Tissue specificityi

Specifically expressed in the testis.1 Publication

Gene expression databases

BgeeiQ99N11.
CleanExiMM_DUSP22.
ExpressionAtlasiQ99N11. baseline and differential.
GenevestigatoriQ99N11.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi222825. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ99N11.
SMRiQ99N11. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 13369Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ99N11.
KOiK14165.
OMAiLFIGNFK.
OrthoDBiEOG7966HM.
PhylomeDBiQ99N11.
TreeFamiTF105126.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99N11-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGSGMSQILP GLYIGNFKDA RDAEQLSRNK VTHILSVHDT ARPMLEGVKY
60 70 80 90 100
LCIPAADTPS QNLTRHFKES IKFIHECRLQ GESCLVHCLA GVSRSVTLVI
110 120 130 140 150
AYIMTVTDFG WEDALHTVRA GRSCANPNLG FQRQLQEFEK HEVHQYRQWL
160 170 180
REEYGENPLR DAEEAKNILA APGILKYWAF LRRL
Length:184
Mass (Da):20,997
Last modified:June 1, 2001 - v1
Checksum:i64953325E88AB577
GO
Isoform 2 (identifier: Q99N11-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-184: AAPGILKYWAFLRRL → GKYKEQGRMEPRPSSRRWSSFSTLPPLTYNNYTTET

Show »
Length:205
Mass (Da):23,489
Checksum:i643BD84636335A75
GO

Sequence cautioni

The sequence CAI24592.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 18415AAPGI…FLRRL → GKYKEQGRMEPRPSSRRWSS FSTLPPLTYNNYTTET in isoform 2. 2 PublicationsVSP_019615Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237619 mRNA. Translation: AAK15038.1.
AK149363 mRNA. Translation: BAE28836.1.
AL731659 Genomic DNA. Translation: CAI24592.1. Sequence problems.
AL731659 Genomic DNA. Translation: CAI24593.1.
AL731659 Genomic DNA. Translation: CAI24594.1.
BC108362 mRNA. Translation: AAI08363.1.
CCDSiCCDS26417.1. [Q99N11-1]
CCDS26418.1. [Q99N11-2]
RefSeqiNP_001033044.1. NM_001037955.4. [Q99N11-2]
NP_598829.1. NM_134068.3. [Q99N11-1]
UniGeneiMm.289646.

Genome annotation databases

EnsembliENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. [Q99N11-1]
ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255. [Q99N11-2]
GeneIDi105352.
KEGGimmu:105352.
UCSCiuc007pyx.1. mouse. [Q99N11-2]
uc007pyy.1. mouse. [Q99N11-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237619 mRNA. Translation: AAK15038.1.
AK149363 mRNA. Translation: BAE28836.1.
AL731659 Genomic DNA. Translation: CAI24592.1. Sequence problems.
AL731659 Genomic DNA. Translation: CAI24593.1.
AL731659 Genomic DNA. Translation: CAI24594.1.
BC108362 mRNA. Translation: AAI08363.1.
CCDSiCCDS26417.1. [Q99N11-1]
CCDS26418.1. [Q99N11-2]
RefSeqiNP_001033044.1. NM_001037955.4. [Q99N11-2]
NP_598829.1. NM_134068.3. [Q99N11-1]
UniGeneiMm.289646.

3D structure databases

ProteinModelPortaliQ99N11.
SMRiQ99N11. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222825. 2 interactions.

Proteomic databases

MaxQBiQ99N11.
PaxDbiQ99N11.
PRIDEiQ99N11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. [Q99N11-1]
ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255. [Q99N11-2]
GeneIDi105352.
KEGGimmu:105352.
UCSCiuc007pyx.1. mouse. [Q99N11-2]
uc007pyy.1. mouse. [Q99N11-1]

Organism-specific databases

CTDi56940.
MGIiMGI:1915926. Dusp22.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ99N11.
KOiK14165.
OMAiLFIGNFK.
OrthoDBiEOG7966HM.
PhylomeDBiQ99N11.
TreeFamiTF105126.

Miscellaneous databases

NextBioi357626.
PROiQ99N11.
SOURCEiSearch...

Gene expression databases

BgeeiQ99N11.
CleanExiMM_DUSP22.
ExpressionAtlasiQ99N11. baseline and differential.
GenevestigatoriQ99N11.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain."
    Aoyama K., Nagata M., Oshima K., Matsuda T., Aoki N.
    J. Biol. Chem. 276:27575-27583(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-57 AND CYS-88.
    Tissue: Testis.
  2. "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.
    , 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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Retina.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORM 2).
    Strain: NMRI.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiDUS22_MOUSE
AccessioniPrimary (citable) accession number: Q99N11
Secondary accession number(s): Q5SQN9, Q5SQP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.