CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001530
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dual specificity protein phosphatase 14 
Protein Synonyms/Alias
 MKP-1-like protein tyrosine phosphatase; MKP-L; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6 
Gene Name
 DUSP14 
Gene Synonyms/Alias
 MKP6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
96YFDTVADKIHSVSRKubiquitination[1]
103KIHSVSRKHGATLVHubiquitination[2, 3]
168YERQLFGKSTVKMVQubiquitination[2, 3]
172LFGKSTVKMVQTPYGubiquitination[4, 5]
187IVPDVYEKESRHLMPubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
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] 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]
 [3] 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]
 [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] 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]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases. 
Sequence Annotation
 DOMAIN 91 156 Tyrosine-protein phosphatase.
 ACT_SITE 111 111 Phosphocysteine intermediate.  
Keyword
 3D-structure; Complete proteome; Hydrolase; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 198 AA 
Protein Sequence
MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRGS VASNRHLLQA RGITCIVNAT 60
IEIPNFNWPQ FEYVKVPLAD MPHAPIGLYF DTVADKIHSV SRKHGATLVH CAAGVSRSAT 120
LCIAYLMKFH NVCLLEAYNW VKARRPVIRP NVGFWRQLID YERQLFGKST VKMVQTPYGI 180
VPDVYEKESR HLMPYWGI 198 
Gene Ontology
 GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:RefGenome. 
Interpro
 IPR020417; Atypical_DUSP.
 IPR020420; Atypical_DUSP_famB.
 IPR000340; Dual-sp_phosphatase_cat-dom.
 IPR020422; Dual-sp_phosphatase_subgr_cat.
 IPR024950; DUSP.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS. 
Pfam
 PF00782; DSPc 
SMART
 SM00195; DSPc 
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50054; TYR_PHOSPHATASE_DUAL 
PRINTS
 PR01908; ADSPHPHTASE.
 PR01910; ADSPHPHTASEB.