Q16690 (DUS5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 5
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Dual specificity protein phosphatase hVH3

Gene names

Name:	DUSP5
Synonyms:	VH3

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	384 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Displays phosphatase activity toward several substrates. The highest relative activity is toward ERK1.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 rhodanese domain. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endoderm formation Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	nucleoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 384

384

Dual specificity protein phosphatase 5

PRO_0000094802

Regions

Domain

19 – 141

123

Rhodanese

Domain

180 – 384

205

Tyrosine-protein phosphatase

Motif

53 – 74

22

Nuclear localization signal Potential

Compositional bias

79 – 82

4

Poly-Gly

Sites

Active site

263

1

Phosphocysteine intermediate Ref.6

Natural variations

Natural variant

154

1

E → D.
Corresponds to variant rs2282238 [ dbSNP | Ensembl ].

VAR_020298

Natural variant

220

1

A → T.
Corresponds to variant rs1889566 [ dbSNP | Ensembl ].

VAR_059777

Natural variant

220

1

A → V.
Corresponds to variant rs1889565 [ dbSNP | Ensembl ].

VAR_059778

Natural variant

322

1

P → L.
Corresponds to variant rs35101549 [ dbSNP | Ensembl ].

VAR_047368

Experimental info

Sequence conflict

9 – 11

3

RQL → GHV in AAA64693. Ref.1

Sequence conflict

71

1

A → R in AAA64693. Ref.1

Sequence conflict

105 – 106

2

AR → F in AAA64693. Ref.1

Sequence conflict

220

1

A → M in AAA64693. Ref.1

Sequence conflict

220

1

A → M in AAB06261. Ref.3

Sequence conflict

220

1

A → M in AAH62545. Ref.5

Sequence conflict

382

1

T → Q in AAA64693. Ref.1

Secondary structure

1

.

.

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.

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384

Helix Strand Turn

Details...

Beta strand

180 – 183

4

Beta strand

186 – 190

5

Helix

191 – 194

4

Helix

197 – 203

7

Beta strand

207 – 210

4

Beta strand

223 – 227

5

Helix

239 – 241

3

Helix

242 – 254

13

Beta strand

259 – 268

10

Helix

269 – 282

14

Helix

286 – 296

11

Helix

304 – 317

14

Sequences

	Sequence		Length	Mass (Da)
	Q16690 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 2E4B2938F886CB4E	FASTA	384	42,047
	10 20 30 40 50 60 MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV VLRRARGGAV 70 80 90 100 110 120 SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR EESAARVVLT SLLACLPAGP 130 140 150 160 170 180 RVYFLKGGYE TFYSEYPECC VDVKPISQEK IESERALISQ CGKPVVNVSY RPAYDQGGPV 190 200 210 220 230 240 EILPFLYLGS AYHASKCEFL ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS 250 260 270 280 290 300 HFQEAIDFID CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV 310 320 330 340 350 360 SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ GAYCTFPASV 370 380 LAPVPTHSTV SELSRSPVAT ATSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel dual specificity phosphatase induced by serum stimulation and heat shock." Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A. J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[2]	Bottaro D.P. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines." Kwak S.P., Dixon J.E. J. Biol. Chem. 270:1156-1160(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Lymph.
[6]	"Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase." Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J. Proteins 66:253-258(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 178-384, ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U15932 mRNA. Translation: AAA64693.2.
U16996 mRNA. Translation: AAB06261.1.
AL355512 Genomic DNA. Translation: CAI15120.1.
BC062545 mRNA. Translation: AAH62545.1.

IPI

IPI00003478.

PIR

I38890.

RefSeq

NP_004410.3. NM_004419.3.

UniGene

Hs.2128.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G6Z	X-ray	2.70	A/B/C	178-384	[»]

ProteinModelPortal

Q16690.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000358596.

PTM databases

PhosphoSite

Q16690.

Polymorphism databases

DMDM

215273975.

Proteomic databases

PaxDb

Q16690.

PRIDE

Q16690.

Protocols and materials databases

DNASU

1847.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369583; ENSP00000358596; ENSG00000138166.

GeneID

1847.

KEGG

hsa:1847.

UCSC

uc001kzd.3. human.

Organism-specific databases

CTD

1847.

GeneCards

GC10P112247.

H-InvDB

HIX0001673.

HGNC

HGNC:3071. DUSP5.

HPA

HPA055143.

MIM

603069. gene.

neXtProt

NX_Q16690.

PharmGKB

PA27528.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOVERGEN

HBG007347.

InParanoid

Q16690.

KO

K04459.

OMA

WQKLKKD.

OrthoDB

EOG4SN1NV.

PhylomeDB

Q16690.

Gene expression databases

Bgee

Q16690.

CleanEx

HS_DUSP5.

Genevestigator

Q16690.

GermOnline

ENSG00000138166. Homo sapiens.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PIRSF

PIRSF000939. MAPK_Ptase. 1 hit.

PRINTS

PR01764. MAPKPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1250380.

ChiTaRS

DUSP5. human.

EvolutionaryTrace

Q16690.

GenomeRNAi

1847.

NextBio

7565.

SOURCE

Search...

Entry information

Entry name

DUS5_HUMAN

Accession

Primary (citable) accession number: Q16690
Secondary accession number(s): Q12997, Q5T603

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 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.