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Cullin information


Cullin
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Identifiers
SymbolCullin
PfamPF00888
InterProIPR001373
PROSITEPDOC00967
SCOP21ldj / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cullin protein neddylation domain
structure of the cul1-rbx1-skp1-f boxskp2 scf ubiquitin ligase complex
Identifiers
SymbolCullin_Nedd8
PfamPF10557
InterProIPR019559
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cullins are a family of hydrophobic scaffold proteins which provide support for ubiquitin ligases (E3). All eukaryotes appear to have cullins. They combine with RING proteins to form Cullin-RING ubiquitin ligases (CRLs) that are highly diverse and play a role in myriad cellular processes, most notably protein degradation by ubiquitination.[1][2]

The human genome contains eight cullin genes

  • CUL1, part of SCF complex
  • CUL2, part of ECS complex (Elongin C - CUL2 - SOCS-box)
  • CUL3, part of CUL3-BTB complex
  • CUL4A
  • CUL4B
  • CUL5
  • CUL7
  • CUL9, also known as PARC

There is also a more distant member called ANAPC2 (or APC2), part of the Anaphase-promoting complex.

CUL1, 2, 3, 4A, 4B, 5 and 7 each form part of a multi-subunit ubiquitin complex.

  1. ^ Bosu, Dimple R.; Kipreos, Edward T. (2008). "Cullin-RING ubiquitin ligases: Global regulation and activation cycles". Cell Division. 3: 7. doi:10.1186/1747-1028-3-7. PMC 2266742. PMID 18282298.
  2. ^ Bruce, Alberts (2014-11-18). Molecular biology of the cell (Sixth ed.). New York, NY. ISBN 9780815344322. OCLC 887605755.{{cite book}}: CS1 maint: location missing publisher (link)

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