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Protein Page:
CUL3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CUL3 a core component of multiple cullin-RING-based BCR (BTB- CUL3-RBX1) 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 E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with CAND1. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the susbstrate recognition component. SPOP is involved in ubiquitination of BMI1, H2AFY and DAXX, and probably GLI2 or GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31A or -B. BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; possibly by mediating ubiquitination of SLC12A3/NCC. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Forms neddylation-dependent homodimers. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein acting as both, adapter to cullin and substrate recognition subunit. The BCR complex may be active as a heterodimeric complex, in which NEDD8, covalently attached to one CUL3 molecule, binds to the C-terminus of a second CUL3 molecule. Interacts with RBX1, RNF7, CYCE and CAND1. Part of the BCR(SPOP) containing SPOP. Part of the probable BCR(KLHL9-KLHL13) complex with BTB domain proteins KLHL9 and KLHL13. Part of the BCR(KBTBD10) complex containing KBTBD10. Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL12 and RBX1. Component of the BCR(KLHL3) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL3 and RBX1 (Probable). Part of the BCR(ENC1) complex containing ENC1. Part of a complex consisting of BMI1, CUL3 and SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with KCTD5, KLHL9, KLHL13, GAN, ZBTB16, KLHL21, KLHL3, KLHL15, KLHL20, C16orf44, GMCL1P1, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with KLHL17; the interaction regulates surface GRIK2 expression. Widely expressed. Belongs to the cullin family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; Ubiquitin ligase; Cell cycle regulation
Chromosomal Location of Human Ortholog: 2q36.2
Cellular Component: cytosol; Golgi membrane; membrane; nucleoplasm; polar microtubule
Molecular Function: cyclin binding; POZ domain binding; protein binding; protein heterodimerization activity; protein homodimerization activity; ubiquitin protein ligase binding; ubiquitin-protein ligase activity
Biological Process: cell cycle arrest; cell migration; cell projection organization and biogenesis; COPII coating of Golgi vesicle; cyclin catabolic process; embryonic cleavage; ER to Golgi vesicle-mediated transport; G1/S transition of mitotic cell cycle; gastrulation; integrin-mediated signaling pathway; MAPKKK cascade; mitotic metaphase plate congression; negative regulation of Rho protein signal transduction; negative regulation of transcription from RNA polymerase II promoter; positive regulation of cell proliferation; positive regulation of cytokinesis; positive regulation of mitotic metaphase/anaphase transition; proteasomal ubiquitin-dependent protein catabolic process; protein monoubiquitination; protein polyubiquitination; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; stem cell division; stress fiber formation; trophectodermal cellular morphogenesis; Wnt receptor signaling pathway
Disease: Pseudohypoaldosteronism, Type Iie
Reference #:  Q13618 (UniProtKB)
Alt. Names/Synonyms: CUL-3; CUL3; cullin 3; Cullin-3; KIAA0617
Gene Symbols: CUL3
Molecular weight: 88,930 Da
Basal Isoelectric point: 8.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CUL3

Protein Structure Not Found.
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Sites Implicated In
intracellular localization: Y764‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K6‑ub __MSNLSkGTGSRKD
0 1 K28 FPMTMDEKYVNSIWD
0 1 S50‑p EIQRKNNsGLSFEEL
0 1 Y58‑p GLSFEELyRNAYtMV
0 1 T63‑p ELyRNAYtMVLHKHG
0 1 T164‑p IRDHLRQtLLDMIAR
0 1 K235 NSASVYIKKVEARIN
0 1 K254‑ub RVMHCLDkSTEEPIV
0 6 K262‑ub STEEPIVkVVERELI
0 22 K292‑ub VHMLKNGkTEDLGCM
0 1 K301‑ub EDLGCMYkLFSRVPN
0 1 T312‑p RVPNGLKtMCECMss
0 1 S318‑p KtMCECMssyLREQG
0 1 S319‑p tMCECMssyLREQGk
0 1 Y320‑p MCECMssyLREQGkA
0 1 K326‑ub syLREQGkALVSEEG
0 2 K336‑ub VSEEGEGkNPVDYIQ
0 6 K349‑ub IQGLLDLkSRFDRFL
0 24 Y376 TIAGDFEYFLNLNSR
0 2 K401‑ub DKLKKGVkGLTEQEV
0 1 K414‑ub EVETILDkAMVLFRF
0 1 T442‑p HLARRLLtNkSVSDD
0 2 K444‑ub ARRLLtNkSVSDDSE
0 1 S450 NkSVSDDSEKNMIsK
0 1 S456‑p DSEKNMIsKLkTECG
0 2 K459‑ac KNMIsKLkTECGCQF
0 1 K459‑ub KNMIsKLkTECGCQF
0 3 S478‑p EGMFRDMsISNTtMD
0 3 T483‑p DMsISNTtMDEFRQH
0 8 Y512‑p VRVLTTGyWPTQSAT
0 1 S556‑p TLQHHMGsADLNATF
0 1 K569‑ub TFYGPVKkEDGSEVG
0 1 S585‑p GGAQVTGsNTRKHIL
0 1 K638‑ub LQSLACGkPTQRVLT
0 3 K651‑ac LTKEPKSkEIENGHI
0 2 K668‑ub VNDQFTSkLHRVKIQ
0 1 K680‑ub KIQTVAAkQGEsDPE
0 1 S684‑p VAAkQGEsDPERKET
0 1 K700‑ub QKVDDDRkHEIEAAI
0 2 K712‑ub AAIVRIMkSRKKMQH
1 1 K712‑ne AAIVRIMkSRKKMQH
0 15 S737‑p LKARFLPsPVVIKKR
0 1 K742 LPsPVVIKKRIEGLI
1 0 Y764‑p TPEDRKVyTYVA___
  mouse

 
K6 __MSNLSKGTGSRKD
K28‑ub FPMTMDEkYVNSIWD
S50 EIQRKNNSGLSFEEL
Y58 GLSFEELYRNAYTMV
T63 ELYRNAYTMVLHKHG
T164 IRDHLRQTLLDMIAR
K235‑ub NSASVYIkKVEARIN
K254 RVMHCLDKSTEEPIV
K262‑ub STEEPIVkVVERELI
K292‑ub VHMLKNGkTEDLACM
K301 EDLACMYKLFSRVPN
T312 RVPNGLKTMCECMSC
S318 KTMCECMSCYLREQG
C319 TMCECMSCYLREQGK
Y320 MCECMSCYLREQGKA
K326 CYLREQGKALVSEEG
K336 VSEEGEGKNPVDYIQ
K349‑ub IQGLLDLkSRFDRFL
Y376‑p TIAGDFEyFLNLNSR
K401 DKLKKGVKGLTEQEV
K414 EVETILDKAMVLFRF
T442 HLARRLLTNKSVSDD
K444 ARRLLTNKSVSDDsE
S450‑p NKSVSDDsEKNMISK
S456 DsEKNMISKLKTECG
K459 KNMISKLKTECGCQF
K459 KNMISKLKTECGCQF
S478 EGMFRDMSISNTTMD
T483 DMSISNTTMDEFRQH
Y512‑p VRVLTTGyWPTQSAT
S556 TLQHHMGSADLNATF
K569 TFYGPVKKEDGSEVG
S585 GGAQVTGSNTRKHIL
K638 LQSLACGKPTQRVLT
K651 LTKEPKSKEIESGHI
K668‑ub VNDQFTSkLHRVKIQ
K680 KIQTVAAKQGEsDPE
S684‑p VAAKQGEsDPERKET
K700 QKVDDDRKHEIEAAI
K712 AAIVRIMKSRKKMQH
K712 AAIVRIMKSRKKMQH
S737‑p LKARFLPsPVVIkKR
K742‑ub LPsPVVIkKRIEGLI
Y764 TPEDRKVYTYVA___
  rat

 
K6 __MSNLSKGTGSRKD
K28 FPMTMDEKYVNSIWD
S50 EIQRKNNSGLSFEEL
Y58 GLSFEELYRNAYTMV
T63 ELYRNAYTMVLHKHG
T164 IRDHLRQTLLDMIAR
K235 NSASVYIKKVEARIN
K254 RVMHCLDKSTEEPIV
K262 STEEPIVKVVERELI
K292 VHMLKNGKTEDLACM
K301 EDLACMYKLFSRVPN
T312 RVPNGLKTMCECMSS
S318 KTMCECMSSYLREQG
S319 TMCECMSSYLREQGK
Y320 MCECMSSYLREQGKA
K326 SYLREQGKALVSEEG
K336 VSEEGEGKNPVDYIQ
K349 IQGLLDLKSRFDRFL
Y376‑p TIAGDFEyFLNLNSR
K401 DKLKKGVKGLTEQEV
K414 EVETILDKAMVLFRF
T442 HLARRLLTNKSVSDD
K444 ARRLLTNKSVSDDSE
S450 NKSVSDDSEKNMISK
S456 DSEKNMISKLKTECG
K459 KNMISKLKTECGCQF
K459 KNMISKLKTECGCQF
S478 EGMFRDMSISNTTMD
T483 DMSISNTTMDEFRQH
Y512 VRVLTTGYWPTQSAT
S556 TLQHHMGSADLNATF
K569 TFYGPVKKEDGSEVG
S585 GGAQVTGSNTRKHIL
K638 LQSLACGKPTQRVLT
K651‑ac LTKEPKSkEIESGHI
K668 VNDQFTSKLHRVKIQ
K680 KIQTVAAKQGESDPE
S684 VAAKQGESDPERKET
K700 QKVDDDRKHEIEAAI
K712 AAIVRIMKSRKKMQH
K712 AAIVRIMKSRKKMQH
S737‑p LKARFLPsPVVIKKR
K742 LPsPVVIKKRIEGLI
Y764 TPEDRKVYTYVA___
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