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Q9NRW4 (DUS22_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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 22

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
JNK-stimulatory phosphatase-1
Short name=JSP-1
Low molecular weight dual specificity phosphatase 2
Short name=LMW-DSP2
Mitogen-activated protein kinase phosphatase x
Short name=MAP kinase phosphatase x
Short name=MKP-x
Gene names
Name:DUSP22
Synonyms:JSP1, LMWDSP2, MKPX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Monomer. Ref.9

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Ubiquitous. Highest expression seen in heart, placenta, lung, liver, kidney and pancreas. Ref.1

Post-translational modification

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

Sequence similarities

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

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence AAH16844.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protein phosphatase
   PTMLipoprotein
Myristate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement PubMed 9205128. Source: ProtInc

cell proliferation

Traceable author statement PubMed 9205128. Source: ProtInc

inactivation of MAPK activity

Traceable author statement PubMed 9205128. Source: ProtInc

multicellular organismal development

Traceable author statement PubMed 9205128. Source: ProtInc

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 16636663. Source: MGI

positive regulation of JNK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

transforming growth factor beta receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

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 Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRW4-1)

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.
Isoform 2 (identifier: Q9NRW4-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 184183Dual specificity protein phosphatase 22
PRO_0000244751

Regions

Domain65 – 13369Tyrosine-protein phosphatase

Sites

Active site881Phosphocysteine intermediate By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Ref.8

Natural variations

Alternative sequence170 – 18415AAPGI…FLRRL → GKYKEQGRTEPQPGARRWSS FPALAPLTYDNYTTET in isoform 2.
VSP_019614
Natural variant1191R → H.
Corresponds to variant rs7768224 [ dbSNP | Ensembl ].
VAR_026912

Secondary structure

........................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B3F962A087C2BA20

FASTA18420,910
        10         20         30         40         50         60 
MGNGMNKILP GLYIGNFKDA RDAEQLSKNK VTHILSVHDS ARPMLEGVKY LCIPAADSPS 

        70         80         90        100        110        120 
QNLTRHFKES IKFIHECRLR GESCLVHCLA GVSRSVTLVI AYIMTVTDFG WEDALHTVRA 

       130        140        150        160        170        180 
GRSCANPNVG FQRQLQEFEK HEVHQYRQWL KEEYGESPLQ DAEEAKNILA APGILKFWAF 


LRRL 

« Hide

Isoform 2 [UniParc].

Checksum: 48334A97991FCFF8
Show »

FASTA20523,268

References

« Hide 'large scale' references
[1]"Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1."
Shen Y., Luche R., Wei B., Gordon M.L., Diltz C.D., Tonks N.K.
Proc. Natl. Acad. Sci. U.S.A. 98:13613-13618(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
[2]"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndromes patient."
Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y., Gu W., Fu G., Huang C.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hematopoietic stem cell.
[3]"Cloning and characterization of human LMW-DSP2 gene."
Mao Y., Xie Y., Cheng H.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"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] (ISOFORM 2).
Tissue: Thalamus.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 1).
Tissue: Lung and Pancreas.
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-184 (ISOFORM 2).
Tissue: Myeloid.
[8]"Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis."
Schwertassek U., Buckley D.A., Xu C.F., Lindsay A.J., McCaffrey M.W., Neubert T.A., Tonks N.K.
FEBS J. 277:2463-2473(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[9]"Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution."
Yokota T., Nara Y., Kashima A., Matsubara K., Misawa S., Kato R., Sugio S.
Proteins 66:272-278(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-163, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF424702 mRNA. Translation: AAL18850.1.
AF165519 mRNA. Translation: AAF86649.1.
AY249859 mRNA. Translation: AAP76376.1.
AK296402 mRNA. Translation: BAG59068.1.
AL365272 Genomic DNA. Translation: CAH72534.1.
AL365272 Genomic DNA. Translation: CAH72535.1.
BC016844 mRNA. Translation: AAH16844.1. Different initiation.
BC022847 mRNA. Translation: AAH22847.1.
AB208997 mRNA. Translation: BAD92234.1.
CCDSCCDS4468.1. [Q9NRW4-1]
CCDS69035.1. [Q9NRW4-2]
RefSeqNP_001273484.1. NM_001286555.1. [Q9NRW4-2]
NP_064570.1. NM_020185.4. [Q9NRW4-1]
UniGeneHs.29106.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WRMX-ray1.50A1-163[»]
ProteinModelPortalQ9NRW4.
SMRQ9NRW4. Positions 1-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121264. 5 interactions.
IntActQ9NRW4. 1 interaction.
STRING9606.ENSP00000345281.

Chemistry

BindingDBQ9NRW4.
ChEMBLCHEMBL3924.

Polymorphism databases

DMDM74752929.

Proteomic databases

MaxQBQ9NRW4.
PaxDbQ9NRW4.
PRIDEQ9NRW4.

Protocols and materials databases

DNASU56940.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344450; ENSP00000345281; ENSG00000112679. [Q9NRW4-1]
ENST00000419235; ENSP00000397459; ENSG00000112679. [Q9NRW4-2]
GeneID56940.
KEGGhsa:56940.
UCSCuc003msx.3. human. [Q9NRW4-1]
uc011dhn.1. human. [Q9NRW4-2]

Organism-specific databases

CTD56940.
GeneCardsGC06P000292.
HGNCHGNC:16077. DUSP22.
HPAHPA031394.
neXtProtNX_Q9NRW4.
PharmGKBPA134991025.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000007880.
HOVERGENHBG054344.
InParanoidQ9NRW4.
KOK14165.
OMALFIGNFK.
OrthoDBEOG7966HM.
PhylomeDBQ9NRW4.
TreeFamTF105126.

Enzyme and pathway databases

SABIO-RKQ9NRW4.
SignaLinkQ9NRW4.

Gene expression databases

ArrayExpressQ9NRW4.
BgeeQ9NRW4.
CleanExHS_DUSP22.
GenevestigatorQ9NRW4.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. 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]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUSP22. human.
EvolutionaryTraceQ9NRW4.
GeneWikiDUSP22.
GenomeRNAi56940.
NextBio62505.
PROQ9NRW4.

Entry information

Entry nameDUS22_HUMAN
AccessionPrimary (citable) accession number: Q9NRW4
Secondary accession number(s): B4DK56 expand/collapse secondary AC list , Q59GW2, Q5VWR2, Q96AR1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2000
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 6

Human chromosome 6: entries, gene names and cross-references to MIM