CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005690
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dual specificity protein phosphatase 1 
Protein Synonyms/Alias
 Dual specificity protein phosphatase hVH1; Mitogen-activated protein kinase phosphatase 1; MAP kinase phosphatase 1; MKP-1; Protein-tyrosine phosphatase CL100 
Gene Name
 DUSP1 
Gene Synonyms/Alias
 CL100; MKP1; PTPN10; VH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57TIVRRRAKGAMGLEHacetylation[1]
57TIVRRRAKGAMGLEHubiquitination[2, 3]
97SAALDGAKRDGTLALubiquitination[4]
122AAQVFFLKGGYEAFSubiquitination[2, 3]
280LMRTNRVKLDEAFEFubiquitination[2, 3, 4, 5, 6, 7]
289DEAFEFVKQRRSIISubiquitination[2, 3, 4, 5, 7]
Reference
 [1] Acetylation of mitogen-activated protein kinase phosphatase-1 inhibits Toll-like receptor signaling.
 Cao W, Bao C, Padalko E, Lowenstein CJ.
 J Exp Med. 2008 Jun 9;205(6):1491-503. [PMID: 18504304]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle (By similarity). 
Sequence Annotation
 DOMAIN 20 137 Rhodanese.
 DOMAIN 175 367 Tyrosine-protein phosphatase.
 ACT_SITE 258 258 Phosphocysteine intermediate (By
 MOD_RES 359 359 Phosphoserine; by MAPK1 and MAPK3 (By
 MOD_RES 364 364 Phosphoserine; by MAPK1 and MAPK3 (By  
Keyword
 Cell cycle; Complete proteome; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 367 AA 
Protein Sequence
MVMEVGTLDA GGLRALLGER AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM 60
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARAAQVFF 120
LKGGYEAFSA SCPELCSKQS TPMGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILPF 180
LYLGSAYHAS RKDMLDALGI TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA 240
IDFIDSIKNA GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS 300
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHST NSALSYLQSP 360
ITTSPSC 367 
Gene Ontology
 GO:0005654; C:nucleoplasm; IBA:RefGenome.
 GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
 GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
 GO:0008330; F:protein tyrosine/threonine phosphatase activity; IEA:Compara.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0032870; P:cellular response to hormone stimulus; IEA:Compara.
 GO:0001706; P:endoderm formation; IBA:RefGenome.
 GO:0035556; P:intracellular signal transduction; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0042981; P:regulation of apoptotic process; IBA:RefGenome.
 GO:0051592; P:response to calcium ion; IEA:Compara.
 GO:0051591; P:response to cAMP; IEA:Compara.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0042542; P:response to hydrogen peroxide; IEA:Compara.
 GO:0009416; P:response to light stimulus; IEA:Compara.
 GO:0006979; P:response to oxidative stress; TAS:ProtInc.
 GO:0032526; P:response to retinoic acid; IEA:Compara.
 GO:0033574; P:response to testosterone stimulus; IEA:Compara. 
Interpro
 IPR020417; Atypical_DUSP.
 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. 
Pfam
 PF00782; DSPc
 PF00581; Rhodanese 
SMART
 SM00195; DSPc
 SM00450; RHOD 
PROSITE
 PS50206; RHODANESE_3
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50054; TYR_PHOSPHATASE_DUAL 
PRINTS
 PR01908; ADSPHPHTASE.
 PR01764; MAPKPHPHTASE.