CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011529
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Induced myeloid leukemia cell differentiation protein Mcl-1 
Protein Synonyms/Alias
 Bcl-2-like protein 3; Bcl2-L-3; Bcl-2-related protein EAT/mcl1; mcl1/EAT 
Gene Name
 MCL1 
Gene Synonyms/Alias
 BCL2L3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MFGLKRNAVIGLubiquitination[1, 2]
40GRLLATEKEASARREubiquitination[1, 2, 3, 4, 5, 6, 7]
136YEPEPLGKRPAVLPLubiquitination[2, 6]
194REQATGAKDTKPMGRubiquitination[1, 2, 4, 6, 7, 8]
197ATGAKDTKPMGRSGAubiquitination[1, 2, 3, 4, 6, 7, 8]
234AFQGMLRKLDIKNEDubiquitination[1]
244IKNEDDVKSLSRVMIubiquitination[3, 7]
308TKRDWLVKQRGWDGFubiquitination[1, 7]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis. 
Sequence Annotation
 REGION 104 175 PEST-like.
 MOTIF 209 223 BH3.
 MOTIF 252 272 BH1.
 MOTIF 304 319 BH2.
 MOD_RES 121 121 Phosphoserine.
 MOD_RES 162 162 Phosphoserine.
 MOD_RES 163 163 Phosphothreonine; by MAPK.
 CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 40 40 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 194 194 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Isopeptide bond; Membrane; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS 60
AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM 120
SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE 180
IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE 240
DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR 300
TKRDWLVKQR GWDGFVEFFH VEDLEGGIRN VLLAFAGVAG VGAGLAYLIR 350 
Gene Ontology
 GO:0097136; C:Bcl-2 family protein complex; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005759; C:mitochondrial matrix; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; TAS:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0015266; F:protein channel activity; TAS:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0001709; P:cell fate determination; NAS:UniProtKB.
 GO:0019725; P:cellular homeostasis; NAS:UniProtKB.
 GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
 GO:1900118; P:negative regulation of execution phase of apoptosis; TAS:UniProtKB.
 GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
 GO:2001020; P:regulation of response to DNA damage stimulus; IMP:MGI.
 GO:0034097; P:response to cytokine stimulus; IDA:MGI. 
Interpro
 IPR013281; Apop_reg_Mc1.
 IPR002475; Bcl2-like.
 IPR020717; Bcl2_BH1_motif_CS.
 IPR020726; Bcl2_BH2_motif_CS.
 IPR020728; Bcl2_BH3_motif_CS.
 IPR026298; Blc2_fam. 
Pfam
 PF00452; Bcl-2 
SMART
  
PROSITE
 PS50062; BCL2_FAMILY
 PS01080; BH1
 PS01258; BH2
 PS01259; BH3 
PRINTS
 PR01866; APOPREGMCL1.
 PR01862; BCL2FAMILY.