CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012386
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Conserved oligomeric Golgi complex subunit 2 
Protein Synonyms/Alias
 COG complex subunit 2; Component of oligomeric Golgi complex 2; Low density lipoprotein receptor defect C-complementing protein 
Gene Name
 COG2 
Gene Synonyms/Alias
 LDLC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MEKSRMNLPKacetylation[1]
19PDTLCFDKDEFMKEDubiquitination[2]
24FDKDEFMKEDFDVDHubiquitination[2, 3]
54DDLELYYKLLKTAMVubiquitination[2, 4]
57ELYYKLLKTAMVELIubiquitination[5]
119AVDERMSKQEDIRKKubiquitination[2]
145RSVEKIEKILNSQSSubiquitination[2]
153ILNSQSSKETSALEAubiquitination[2, 5, 6]
188QFHAVQSKGMPLLDKubiquitination[2, 5]
195KGMPLLDKVRPRIAGubiquitination[2]
239RTYATIDKTRDAEALubiquitination[2, 5]
343NPDAFHEKYTISMDFubiquitination[5]
379AYHSFNKKWNLPVYFubiquitination[2]
503GSGPSETKPVVSISRubiquitination[5]
584DSCFGFLKSALEVPRubiquitination[2]
598RLYRRTNKEVPTTASubiquitination[2]
627SGHKDKLKQAIIQQWubiquitination[2]
658SDVLNSVKKMEESLKubiquitination[2]
659DVLNSVKKMEESLKRubiquitination[2]
672KRLKQARKTTPANPVubiquitination[2]
690GGMSDDDKIRLQLALubiquitination[2]
717GLQASDIKSFSALAEubiquitination[2, 5, 6, 7]
730AELVAAAKDQATAEQubiquitination[5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 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]
 [4] 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]
 [5] 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]
 [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] 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
 Required for normal Golgi morphology and function. 
Sequence Annotation
  
Keyword
 Alternative splicing; Complete proteome; Golgi apparatus; Membrane; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 738 AA 
Protein Sequence
MEKSRMNLPK GPDTLCFDKD EFMKEDFDVD HFVSDCRKRV QLEELRDDLE LYYKLLKTAM 60
VELINKDYAD FVNLSTNLVG MDKALNQLSV PLGQLREEVL SLRSSVSEGI RAVDERMSKQ 120
EDIRKKKMCV LRLIQVIRSV EKIEKILNSQ SSKETSALEA SSPLLTGQIL ERIATEFNQL 180
QFHAVQSKGM PLLDKVRPRI AGITAMLQQS LEGLLLEGLQ TSDVDIIRHC LRTYATIDKT 240
RDAEALVGQV LVKPYIDEVI IEQFVESHPN GLQVMYNKLL EFVPHHCRLL REVTGGAISS 300
EKGNTVPGYD FLVNSVWPQI VQGLEEKLPS LFNPGNPDAF HEKYTISMDF VRRLERQCGS 360
QASVKRLRAH PAYHSFNKKW NLPVYFQIRF REIAGSLEAA LTDVLEDAPA ESPYCLLASH 420
RTWSSLRRCW SDEMFLPLLV HRLWRLTLQI LARYSVFVNE LSLRPISNES PKEIKKPLVT 480
GSKEPSITQG NTEDQGSGPS ETKPVVSISR TQLVYVVADL DKLQEQLPEL LEIIKPKLEM 540
IGFKNFSSIS AALEDSQSSF SACVPSLSSK IIQDLSDSCF GFLKSALEVP RLYRRTNKEV 600
PTTASSYVDS ALKPLFQLQS GHKDKLKQAI IQQWLEGTLS ESTHKYYETV SDVLNSVKKM 660
EESLKRLKQA RKTTPANPVG PSGGMSDDDK IRLQLALDVE YLGEQIQKLG LQASDIKSFS 720
ALAELVAAAK DQATAEQP 738 
Gene Ontology
 GO:0000139; C:Golgi membrane; TAS:ProtInc.
 GO:0005795; C:Golgi stack; IDA:UniProtKB.
 GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
 GO:0008565; F:protein transporter activity; IMP:UniProtKB.
 GO:0007030; P:Golgi organization; IMP:UniProtKB.
 GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:UniProtKB.
 GO:0006886; P:intracellular protein transport; TAS:ProtInc.
 GO:0009312; P:oligosaccharide biosynthetic process; TAS:ProtInc.
 GO:0006486; P:protein glycosylation; TAS:ProtInc. 
Interpro
 IPR009316; COG2.
 IPR024603; COG_complex_COG2_C.
 IPR024602; COG_su2_N. 
Pfam
 PF06148; COG2
 PF12022; DUF3510 
SMART
  
PROSITE
  
PRINTS