ID DUS5_HUMAN Reviewed; 384 AA.
AC Q16690; Q12997; Q5T603;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 01-MAY-2013, entry version 123.
DE RecName: Full=Dual specificity protein phosphatase 5;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity protein phosphatase hVH3;
GN Name=DUSP5; Synonyms=VH3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=7961985;
RA Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.;
RT "A novel dual specificity phosphatase induced by serum stimulation and
RT heat shock.";
RL J. Biol. Chem. 269:29897-29902(1994).
RN [2]
RP SEQUENCE REVISION.
RA Bottaro D.P.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7836374; DOI=10.1074/jbc.270.3.1156;
RA Kwak S.P., Dixon J.E.;
RT "Multiple dual specificity protein tyrosine phosphatases are expressed
RT and regulated differentially in liver cell lines.";
RL J. Biol. Chem. 270:1156-1160(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 178-384, AND ACTIVE SITE.
RX PubMed=17078075; DOI=10.1002/prot.21224;
RA Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J.;
RT "Crystal structure of the catalytic domain of human DUSP5, a dual
RT specificity MAP kinase protein phosphatase.";
RL Proteins 66:253-258(2007).
CC -!- FUNCTION: Displays phosphatase activity toward several substrates.
CC The highest relative activity is toward ERK1.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Non-receptor class dual specificity subfamily.
CC -!- SIMILARITY: Contains 1 rhodanese domain.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U15932; AAA64693.2; -; mRNA.
DR EMBL; U16996; AAB06261.1; -; mRNA.
DR EMBL; AL355512; CAI15120.1; -; Genomic_DNA.
DR EMBL; BC062545; AAH62545.1; -; mRNA.
DR IPI; IPI00003478; -.
DR PIR; I38890; I38890.
DR RefSeq; NP_004410.3; NM_004419.3.
DR UniGene; Hs.2128; -.
DR PDB; 2G6Z; X-ray; 2.70 A; A/B/C=178-384.
DR PDBsum; 2G6Z; -.
DR ProteinModelPortal; Q16690; -.
DR STRING; 9606.ENSP00000358596; -.
DR PhosphoSite; Q16690; -.
DR DMDM; 215273975; -.
DR PaxDb; Q16690; -.
DR PRIDE; Q16690; -.
DR DNASU; 1847; -.
DR Ensembl; ENST00000369583; ENSP00000358596; ENSG00000138166.
DR GeneID; 1847; -.
DR KEGG; hsa:1847; -.
DR UCSC; uc001kzd.3; human.
DR CTD; 1847; -.
DR GeneCards; GC10P112247; -.
DR H-InvDB; HIX0001673; -.
DR HGNC; HGNC:3071; DUSP5.
DR HPA; HPA055143; -.
DR MIM; 603069; gene.
DR neXtProt; NX_Q16690; -.
DR PharmGKB; PA27528; -.
DR eggNOG; COG2453; -.
DR HOVERGEN; HBG007347; -.
DR InParanoid; Q16690; -.
DR KO; K04459; -.
DR OMA; WQKLKKD; -.
DR OrthoDB; EOG4SN1NV; -.
DR PhylomeDB; Q16690; -.
DR ChEMBL; CHEMBL1250380; -.
DR ChiTaRS; DUSP5; human.
DR EvolutionaryTrace; Q16690; -.
DR GenomeRNAi; 1847; -.
DR NextBio; 7565; -.
DR Bgee; Q16690; -.
DR CleanEx; HS_DUSP5; -.
DR Genevestigator; Q16690; -.
DR GermOnline; ENSG00000138166; Homo sapiens.
DR GO; GO:0005654; C:nucleoplasm; IBA:RefGenome.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0001706; P:endoderm formation; IBA:RefGenome.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR InterPro; IPR024950; DUSP.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR10159; PTHR10159; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Hydrolase; Nucleus; Polymorphism;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1 384 Dual specificity protein phosphatase 5.
FT /FTId=PRO_0000094802.
FT DOMAIN 19 141 Rhodanese.
FT DOMAIN 180 384 Tyrosine-protein phosphatase.
FT MOTIF 53 74 Nuclear localization signal (Potential).
FT COMPBIAS 79 82 Poly-Gly.
FT ACT_SITE 263 263 Phosphocysteine intermediate.
FT VARIANT 154 154 E -> D (in dbSNP:rs2282238).
FT /FTId=VAR_020298.
FT VARIANT 220 220 A -> T (in dbSNP:rs1889566).
FT /FTId=VAR_059777.
FT VARIANT 220 220 A -> V (in dbSNP:rs1889565).
FT /FTId=VAR_059778.
FT VARIANT 322 322 P -> L (in dbSNP:rs35101549).
FT /FTId=VAR_047368.
FT CONFLICT 9 11 RQL -> GHV (in Ref. 1; AAA64693).
FT CONFLICT 71 71 A -> R (in Ref. 1; AAA64693).
FT CONFLICT 105 106 AR -> F (in Ref. 1; AAA64693).
FT CONFLICT 220 220 A -> M (in Ref. 1; AAA64693, 3; AAB06261
FT and 5; AAH62545).
FT CONFLICT 382 382 T -> Q (in Ref. 1; AAA64693).
FT STRAND 180 183
FT STRAND 186 190
FT HELIX 191 194
FT HELIX 197 203
FT STRAND 207 210
FT STRAND 223 227
FT HELIX 239 241
FT HELIX 242 254
FT STRAND 259 268
FT HELIX 269 282
FT HELIX 286 296
FT HELIX 304 317
SQ SEQUENCE 384 AA; 42047 MW; 2E4B2938F886CB4E CRC64;
MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV VLRRARGGAV
SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR EESAARVVLT SLLACLPAGP
RVYFLKGGYE TFYSEYPECC VDVKPISQEK IESERALISQ CGKPVVNVSY RPAYDQGGPV
EILPFLYLGS AYHASKCEFL ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS
HFQEAIDFID CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV
SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ GAYCTFPASV
LAPVPTHSTV SELSRSPVAT ATSC
//
