CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018903
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cullin-5 
Protein Synonyms/Alias
 CUL-5; Vasopressin-activated calcium-mobilizing receptor 1; VACM-1 
Gene Name
 CUL5 
Gene Synonyms/Alias
 VACM1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10TSNLLKNKGSLQFEDubiquitination[1]
384VNDATIFKLELPLKQubiquitination[2, 3]
529PADSVNIKILNAGAWubiquitination[2, 3]
620KISFENLKLATELPDubiquitination[1]
724EAIIQIMKMRKKISNubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
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] 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]
 [3] 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]
 [4] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [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] 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]
 [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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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] 
Functional Description
 Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin- conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAk2. Seems to be involved poteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a cell surface vasopressin receptor. 
Sequence Annotation
 MOD_RES 210 210 Phosphothreonine.
 CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Complete proteome; Host-virus interaction; Isopeptide bond; Phosphoprotein; Receptor; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 780 AA 
Protein Sequence
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK 60
IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEITLMG 120
KQGSNKKSNV EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV 180
RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE 240
EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM 300
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ 360
DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAN YCDMLLRKTP 420
LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL 480
REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS 540
EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL 600
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY EPQVNSPKDF 660
TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII 720
QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQIEWL IEHKYIRRDE SDINTFIYMA 780 
Gene Ontology
 GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005262; F:calcium channel activity; TAS:ProtInc.
 GO:0004872; F:receptor activity; TAS:ProtInc.
 GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0051480; P:cytosolic calcium ion homeostasis; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
 GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0006970; P:response to osmotic stress; IEA:Compara.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
 GO:0016032; P:viral reproduction; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR016157; Cullin_CS.
 IPR016158; Cullin_homology.
 IPR001373; Cullin_N.
 IPR019559; Cullin_neddylation_domain.
 IPR016159; Cullin_repeat-like_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00888; Cullin
 PF10557; Cullin_Nedd8 
SMART
 SM00182; CULLIN
 SM00884; Cullin_Nedd8 
PROSITE
 PS01256; CULLIN_1
 PS50069; CULLIN_2 
PRINTS