CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001147
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA/RNP complex-1-interacting phosphatase 
Protein Synonyms/Alias
 Dual specificity protein phosphatase 11; Phosphatase that interacts with RNA/RNP complex 1 
Gene Name
 DUSP11 
Gene Synonyms/Alias
 PIR1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36NHIPERWKDYLPVGQubiquitination[1]
54GTRFIAFKVPLQKSFubiquitination[1]
59AFKVPLQKSFEKKLAubiquitination[1]
64LQKSFEKKLAPEECFubiquitination[1, 2]
79SPLDLFNKIREQNEEubiquitination[1]
129PDDETIFKFKHAVNGubiquitination[1]
131DETIFKFKHAVNGFLubiquitination[1]
206LQNGPIRKNWNSSVPubiquitination[1]
231LMQPVHNKPVKQGPRubiquitination[3, 4]
234PVHNKPVKQGPRYNLubiquitination[1, 3, 4]
266SLQQSVRKFSENPHVubiquitination[1]
299RRYSWNVKPNASRAAubiquitination[1]
Reference
 [1] 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]
 [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] 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]
 [4] 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
 Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism. 
Sequence Annotation
 DOMAIN 128 197 Tyrosine-protein phosphatase.
 ACT_SITE 152 152 Phosphocysteine intermediate.  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Nucleus; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 330 AA 
Protein Sequence
MSQWHHPRSG WGRRRDFSGR SSAKKKGGNH IPERWKDYLP VGQRMPGTRF IAFKVPLQKS 60
FEKKLAPEEC FSPLDLFNKI REQNEELGLI IDLTYTQRYY KPEDLPETVP YLKIFTVGHQ 120
VPDDETIFKF KHAVNGFLKE NKDNDKLIGV HCTHGLNRTG YLICRYLIDV EGVRPDDAIE 180
LFNRCRGHCL ERQNYIEDLQ NGPIRKNWNS SVPRSSDFED SAHLMQPVHN KPVKQGPRYN 240
LHQIQGHSAP RHFHTQTQSL QQSVRKFSEN PHVYQRHHLP PPGPPGEDYS HRRYSWNVKP 300
NASRAAQDRR RWYPYNYSRL SYPACWEWTQ 330 
Gene Ontology
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0006396; P:RNA processing; TAS:ProtInc. 
Interpro
 IPR000340; Dual-sp_phosphatase_cat-dom.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS. 
Pfam
 PF00782; DSPc 
SMART
  
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50054; TYR_PHOSPHATASE_DUAL 
PRINTS