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Q99N11

- DUS22_MOUSE

UniProt

Q99N11 - DUS22_MOUSE

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Protein
Dual specificity protein phosphatase 22
Gene
Dusp22
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 binding Source: MGI
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC
  3. protein tyrosine/serine/threonine phosphatase activity Source: MGI

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  2. positive regulation of JNK cascade Source: MGI
  3. protein dephosphorylation Source: RefGenome
  4. regulation of cell proliferation Source: MGI
  5. 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. 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 By similarity
Chaini2 – 184183Dual specificity protein phosphatase 22
PRO_0000244752Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiQ99N11.
PRIDEiQ99N11.

Expressioni

Tissue specificityi

Specifically expressed in the testis.1 Publication

Gene expression databases

BgeeiQ99N11.
CleanExiMM_DUSP22.
GenevestigatoriQ99N11.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

BioGridi222825. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ99N11.
SMRiQ99N11. Positions 1-154.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00730000110377.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
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. Align

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

MGSGMSQILP GLYIGNFKDA RDAEQLSRNK VTHILSVHDT ARPMLEGVKY    50
LCIPAADTPS QNLTRHFKES IKFIHECRLQ GESCLVHCLA GVSRSVTLVI 100
AYIMTVTDFG WEDALHTVRA GRSCANPNLG FQRQLQEFEK HEVHQYRQWL 150
REEYGENPLR DAEEAKNILA APGILKYWAF LRRL 184
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 18415AAPGI…FLRRL → GKYKEQGRMEPRPSSRRWSS FSTLPPLTYNNYTTET in isoform 2.
VSP_019615Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS26417.1. [Q99N11-1 ]
CCDS26418.1. [Q99N11-2 ]
RefSeqi NP_001033044.1. NM_001037955.4. [Q99N11-2 ]
NP_598829.1. NM_134068.3. [Q99N11-1 ]
UniGenei Mm.289646.

3D structure databases

ProteinModelPortali Q99N11.
SMRi Q99N11. Positions 1-154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 222825. 2 interactions.

Proteomic databases

PaxDbi Q99N11.
PRIDEi Q99N11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000091672 ; ENSMUSP00000089260 ; ENSMUSG00000069255 . [Q99N11-1 ]
ENSMUST00000095914 ; ENSMUSP00000093603 ; ENSMUSG00000069255 . [Q99N11-2 ]
GeneIDi 105352.
KEGGi mmu:105352.
UCSCi uc007pyx.1. mouse. [Q99N11-2 ]
uc007pyy.1. mouse. [Q99N11-1 ]

Organism-specific databases

CTDi 56940.
MGIi MGI:1915926. Dusp22.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00730000110377.
HOGENOMi HOG000007880.
HOVERGENi HBG054344.
KOi K14165.
OMAi LFIGNFK.
OrthoDBi EOG7966HM.
PhylomeDBi Q99N11.
TreeFami TF105126.

Miscellaneous databases

NextBioi 357626.
PROi Q99N11.
SOURCEi Search...

Gene expression databases

Bgeei Q99N11.
CleanExi MM_DUSP22.
Genevestigatori Q99N11.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR020417. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 97 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