Q9NRW4 (DUS22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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 component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Lipoprotein Myristate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic 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 peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC positive regulation of JNK cascade 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_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 184

183

Dual specificity protein phosphatase 22

PRO_0000244751

Regions

Domain

65 – 133

69

Tyrosine-protein phosphatase

Sites

Active site

88

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine Ref.8

Natural variations

Alternative sequence

170 – 184

15

AAPGI…FLRRL → GKYKEQGRTEPQPGARRWSS FPALAPLTYDNYTTET in isoform 2.

VSP_019614

Natural variant

119

1

R → H.
Corresponds to variant rs7768224 [ dbSNP | Ensembl ].

VAR_026912

Secondary structure

1

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184

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Beta strand

12 – 15

4

Helix

19 – 21

3

Helix

23 – 28

6

Beta strand

31 – 36

6

Beta strand

49 – 52

4

Helix

64 – 66

3

Helix

67 – 79

13

Beta strand

83 – 87

5

Beta strand

89 – 93

5

Helix

94 – 105

12

Helix

111 – 121

11

Helix

129 – 141

13

Helix

143 – 153

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B3F962A087C2BA20	FASTA	184	20,910
	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
	Isoform 2 [UniParc]. Checksum: 48334A97991FCFF8	FASTA	205	23,268
	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 DAEEAKNILG KYKEQGRTEP 190 200 QPGARRWSSF PALAPLTYDN YTTET

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.

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.

IPI

IPI00024617.
IPI00646309.

RefSeq

NP_064570.1. NM_020185.3.

UniGene

Hs.29106.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WRM	X-ray	1.50	A	1-163	[»]

ProteinModelPortal

Q9NRW4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NRW4. 1 interaction.

STRING

9606.ENSP00000345281.

Polymorphism databases

DMDM

74752929.

Proteomic databases

PaxDb

Q9NRW4.

PRIDE

Q9NRW4.

Protocols and materials databases

DNASU

56940.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344450; ENSP00000345281; ENSG00000112679.

GeneID

56940.

KEGG

hsa:56940.

UCSC

uc003msx.3. human.
uc011dhn.1. human.

Organism-specific databases

CTD

56940.

GeneCards

GC06P000292.

HGNC

HGNC:16077. DUSP22.

HPA

HPA031394.

neXtProt

NX_Q9NRW4.

PharmGKB

PA134991025.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000007880.

HOVERGEN

HBG054344.

InParanoid

Q9NRW4.

KO

K04459.

OMA

WLREEYG.

OrthoDB

EOG4RFKT3.

PhylomeDB

Q9NRW4.

Gene expression databases

Bgee

Q9NRW4.

CleanEx

HS_DUSP22.

Genevestigator

Q9NRW4.

GermOnline

ENSG00000112679. Homo sapiens.

Family and domain databases

InterPro

IPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

PRINTS

PR01908. ADSPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9NRW4.

ChEMBL

CHEMBL3924.

ChiTaRS

DUSP22. human.

EvolutionaryTrace

Q9NRW4.

GenomeRNAi

56940.

NextBio

62505.

Entry information

Entry name

DUS22_HUMAN

Accession

Primary (citable) accession number: Q9NRW4
Secondary accession number(s): B4DK56 , Q59GW2, Q5VWR2, Q96AR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.