CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011327
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dual specificity protein phosphatase 2 
Protein Synonyms/Alias
 Dual specificity protein phosphatase PAC-1 
Gene Name
 DUSP2 
Gene Synonyms/Alias
 PAC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
157ALPPTGDKTSRSDSRubiquitination[1, 2, 3]
288DEAFDFVKQRRGVISubiquitination[1, 2, 3, 4, 5, 6]
Reference
 [1] 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]
 [2] 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]
 [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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2. 
Sequence Annotation
 DOMAIN 23 144 Rhodanese.
 DOMAIN 237 302 Tyrosine-protein phosphatase.
 ACT_SITE 257 257 Phosphocysteine intermediate (By  
Keyword
 3D-structure; Complete proteome; Hydrolase; Nucleus; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 314 AA 
Protein Sequence
MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP WNALLRRRAR 60
GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE LRPDSPAHVL LAALLHETRA 120
GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL 180
FLGSCSHSSD LQGLQACGIT AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI 240
GFIDWVKNSG GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF 300
MGQLLQFETQ VLCH 314 
Gene Ontology
 GO:0005654; C:nucleoplasm; IBA:RefGenome.
 GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
 GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
 GO:0008330; F:protein tyrosine/threonine phosphatase activity; TAS:ProtInc.
 GO:0001706; P:endoderm formation; IBA:RefGenome.
 GO:0042981; P:regulation of apoptotic process; IBA:RefGenome. 
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. 
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
 PR01764; MAPKPHPHTASE.