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Database: UniProt
Entry: Q16690
LinkDB: Q16690
Original site: Q16690 
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   09-JUL-2014, entry version 135.
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 protein]-serine/threonine phosphate + H(2)O
CC       = [a protein]-serine/threonine + phosphate.
CC   -!- INTERACTION:
CC       P28482:MAPK1; NbExp=4; IntAct=EBI-7487376, EBI-959949;
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.
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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   CCDS; CCDS7566.1; -.
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   SMR; Q16690; 22-140, 178-320.
DR   BioGrid; 108180; 3.
DR   IntAct; Q16690; 1.
DR   MINT; MINT-8277166; -.
DR   STRING; 9606.ENSP00000358596; -.
DR   ChEMBL; CHEMBL1250380; -.
DR   PhosphoSite; Q16690; -.
DR   DMDM; 215273975; -.
DR   MaxQB; Q16690; -.
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; SPVHQLK; -.
DR   OrthoDB; EOG75MVWD; -.
DR   PhylomeDB; Q16690; -.
DR   TreeFam; TF105122; -.
DR   SignaLink; Q16690; -.
DR   ChiTaRS; DUSP5; human.
DR   EvolutionaryTrace; Q16690; -.
DR   GeneWiki; DUSP5; -.
DR   GenomeRNAi; 1847; -.
DR   NextBio; 7565; -.
DR   PRO; PR:Q16690; -.
DR   Bgee; Q16690; -.
DR   CleanEx; HS_DUSP5; -.
DR   Genevestigator; Q16690; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
DR   GO; GO:0001706; P:endoderm formation; IBA:RefGenome.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; TAS:GOC.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:RefGenome.
DR   Gene3D; 3.40.250.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 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; IPR029021; Prot-tyrosine_phosphatase-like.
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; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF52821; SSF52821; 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
//
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