CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012420
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cullin-7 
Protein Synonyms/Alias
 CUL-7 
Gene Name
 CUL7 
Gene Synonyms/Alias
 KIAA0076 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
115EEMETDVKSLIQRALubiquitination[1]
255RVLFSLVKRYLHVTSubiquitination[2, 3]
566LINCHVYKKYGPEALubiquitination[4]
567INCHVYKKYGPEALAubiquitination[1, 5]
610DAAKVEAKEPPSQSPubiquitination[1]
651SEGTQENKVKPLLLQubiquitination[5]
653GTQENKVKPLLLQLQubiquitination[5]
765ALEKHLGKLELAQELubiquitination[4]
970GLEILGPKPTFWPVFubiquitination[5]
1153CWRAVVEKQVNNFLTubiquitination[1]
1312LQSLSTSKELQRQFHubiquitination[1]
1431RYSNFYNKSQSHPALubiquitination[1, 2, 3, 5]
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] 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] 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]
 [5] 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] 
Functional Description
 Component of a probable SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably plays a role in the degradation of proteins involved in endothelial proliferation and/or differentiation (By similarity). Seems not to promote polyubiquitination and proteasomal degradation of TP53. In vitro, complexes of CUL7 with either CUL9 or FBXW8 or TP53 contain E3 ubiquitin-protein ligase activity. In complex with FBXW8, mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. 
Sequence Annotation
 DOMAIN 814 993 DOC.
 REGION 360 460 Interaction with TP53.
 MOD_RES 339 339 Phosphoserine.
 CROSSLNK 1576 1576 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Disease mutation; Dwarfism; Golgi apparatus; Host-virus interaction; Isopeptide bond; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1698 AA 
Protein Sequence
MVGELRYREF RVPLGPGLHA YPDELIRQRV GHDGHPEYQI RWLILRRGDE GDGGSGQVDC 60
KAEHILLWMS KDEIYANCHK MLGEDGQVIG PSQESAGEVG ALDKSVLEEM ETDVKSLIQR 120
ALRQLEECVG TIPPAPLLHT VHVLSAYASI EPLTGVFKDP RVLDLLMHML SSPDYQIRWS 180
AGRMIQALSS HDAGTRTQIL LSLSQQEAIE KHLDFDSRCA LLALFAQATL SEHPMSFEGI 240
QLPQVPGRVL FSLVKRYLHV TSLLDQLNDS AAEPGAQNTS APEELSGERG QLELEFSMAM 300
GTLISELVQA MRWDQASDRP RSSARSPGSI FQPQLADVSP GLPAAQAQPS FRRSRRFRPR 360
SEFASGNTYA LYVRDTLQPG MRVRMLDDYE EISAGDEGEF RQSNNGVPPV QVFWESTGRT 420
YWVHWHMLEI LGFEEDIEDM VEADEYQGAV ASRVLGRALP AWRWRPMTEL YAVPYVLPED 480
EDTEECEHLT LAEWWELLFF IKKLDGPDHQ EVLQILQENL DGEILDDEIL AELAVPIELA 540
QDLLLTLPQR LNDSALRDLI NCHVYKKYGP EALAGNQAYP SLLEAQEDVL LLDAQAQAKD 600
SEDAAKVEAK EPPSQSPNTP LQRLVEGYGP AGKILLDLEQ ALSSEGTQEN KVKPLLLQLQ 660
RQPQPFLALM QSLDTPETNR TLHLTVLRIL KQLVDFPEAL LLPWHEAVDA CMACLRSPNT 720
DREVLQELIF FLHRLTSVSR DYAVVLNQLG ARDAISKALE KHLGKLELAQ ELRDMVFKCE 780
KHAHLYRKLI TNILGGCIQM VLGQIEDHRR THQPINIPFF DVFLRYLCQG SSVEVKEDKC 840
WEKVEVSSNP HRASKLTDHN PKTYWESNGS AGSHYITLHM RRGILIRQLT LLVASEDSSY 900
MPARVVVCGG DSTSSLHTEL NSVNVMPSAS RVILLENLTR FWPIIQIRIK RCQQGGIDTR 960
IRGLEILGPK PTFWPVFREQ LCRHTRLFYM VRAQAWSQDM AEDRRSLLHL SSRLNGALRQ 1020
EQNFADRFLP DDEAAQALGK TCWEALVSPV VQNITSPDED GISPLGWLLD QYLECQEAVF 1080
NPQSRGPAFF SRVRRLTHLL VHVEPCEAPP PVVATPRPKG RNRSHDWSSL ATRGLPSSIM 1140
RNLTRCWRAV VEKQVNNFLT SSWRDDDFVP RYCEHFNILQ NSSSELFGPR AAFLLALQNG 1200
CAGALLKLPF LKAAHVSEQF ARHIDQQIQG SRIGGAQEME RLAQLQQCLQ AVLIFSGLEI 1260
ATTFEHYYQH YMADRLLGVV SSWLEGAVLE QIGPCFPNRL PQQMLQSLST SKELQRQFHV 1320
YQLQQLDQEL LKLEDTEKKI QVGLGASGKE HKSEKEEEAG AAAVVDVAEG EEEEEENEDL 1380
YYEGAMPEVS VLVLSRHSWP VASICHTLNP RTCLPSYLRG TLNRYSNFYN KSQSHPALER 1440
GSQRRLQWTW LGWAELQFGN QTLHVSTVQM WLLLYLNDLK AVSVESLLAF SGLSADMLNQ 1500
AIGPLTSSRG PLDLHEQKDI PGGVLKIRDG SKEPRSRWDI VRLIPPQTYL QAEGEDGQNL 1560
EKRRNLLNCL IVRILKAHGD EGLHIDQLVC LVLEAWQKGP CPPRGLVSSL GKGSACSSTD 1620
VLSCILHLLG KGTLRRHDDR PQVLSYAVPV TVMEPHTESL NPGSSGPNPP LTFHTLQIRS 1680
RGVPYASCTA TQSFSTFR 1698 
Gene Ontology
 GO:0005680; C:anaphase-promoting complex; NAS:UniProtKB.
 GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0007030; P:Golgi organization; ISS:UniProtKB.
 GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProtKB.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0006508; P:proteolysis; NAS:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
 GO:0001570; P:vasculogenesis; ISS:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR004939; APC_su10/DOC_dom.
 IPR021097; CPH_domain.
 IPR016158; Cullin_homology.
 IPR001373; Cullin_N.
 IPR008979; Galactose-bd-like.
 IPR014722; Rib_L2_dom2. 
Pfam
 PF03256; APC10
 PF11515; Cul7
 PF00888; Cullin 
SMART
  
PROSITE
 PS01256; CULLIN_1
 PS50069; CULLIN_2
 PS51284; DOC 
PRINTS