CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019275
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DCN1-like protein 1 
Protein Synonyms/Alias
 DCUN1 domain-containing protein 1; Defective in cullin neddylation protein 1-like protein 1; Squamous cell carcinoma-related oncogene 
Gene Name
 DCUN1D1 
Gene Synonyms/Alias
 DCUN1L1; RP42; SCCRO 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57LYIRESVKGSLDRKKubiquitination[1, 2, 3]
63VKGSLDRKKLEQLYNubiquitination[2, 3, 4, 5, 6, 7, 8]
64KGSLDRKKLEQLYNRubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
80KDPQDENKIGIDGIQubiquitination[3]
138CDSIEKLKAQIPKMEubiquitination[2]
143KLKAQIPKMEQELKEubiquitination[1, 2, 3, 4, 5, 7, 8]
149PKMEQELKEPGRFKDubiquitination[1, 2, 3, 5, 6, 7, 8, 9]
155LKEPGRFKDFYQFTFubiquitination[7]
191LVLNGRFKFLDLWNKubiquitination[5, 8]
Reference
 [1] 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]
 [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] 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]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] 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]
 [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] 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]
 [9] 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
Functional Description
 Part of an E3 ubiquitin ligase complex for neddylation. Required for neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes by enhancing the rate of cullins neddylation. Functions to recruit the NEDD8-charged E2 enzyme to the cullin component. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity). 
Sequence Annotation
 DOMAIN 8 45 UBA-like.
 DOMAIN 60 248 DCUN1.  
Keyword
 3D-structure; Complete proteome; Proto-oncogene; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 259 AA 
Protein Sequence
MNKLKSSQKD KVRQFMIFTQ SSEKTAVSCL SQNDWKLDVA TDNFFQNPEL YIRESVKGSL 60
DRKKLEQLYN RYKDPQDENK IGIDGIQQFC DDLALDPASI SVLIIAWKFR AATQCEFSKQ 120
EFMDGMTELG CDSIEKLKAQ IPKMEQELKE PGRFKDFYQF TFNFAKNPGQ KGLDLEMAIA 180
YWNLVLNGRF KFLDLWNKFL LEHHKRSIPK DTWNLLLDFS TMIADDMSNY DEEGAWPVLI 240
DDFVEFARPQ IAGTKSTTV 259 
Gene Ontology
 GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB. 
Interpro
 IPR014764; DCN-prot.
 IPR005176; PONY_dom.
 IPR009060; UBA-like. 
Pfam
 PF03556; Cullin_binding 
SMART
  
PROSITE
 PS51229; DCUN1 
PRINTS