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Information on EC 2.3.2.B13 - ubiquitin transferase RING E3 (cullin-dependent)
for references in articles please use BRENDA:EC2.3.2.B13
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Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.B13 ubiquitin transferase RING E3 (cullin-dependent)
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show+
=
+
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine
+
[acceptor protein]-L-lysine
=
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine
+
N6-ubiquitinyl-[acceptor protein]-L-lysine
Synonyms
cullin-ring e3 ubiquitin ligase, cul2 e3 ligase, cullin 2 e3 ubiquitin ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CRL
CRL4
cullin-RING E3 ubiquitin ligase
cullin-RING E3 ubiquitin ligase 4
E3 CRL4
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine = [cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[cullin-RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming)
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [APOBEC3]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[APOBEC3]-L-lysine
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Cdt1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Cdt1]-L-lysine
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [CK1alpha]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Ck1alpha]-L-lysine
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [CK1alpha]-L-lysine48
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[CK1alpha]-L-lysine48
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [cyclin D1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[cyclin D1]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Eag1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Eag1]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Grasp65]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Grasp65]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [HIV-1 Gag]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[HIV-1 Gag]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [HPK1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[HPK1]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [IRS1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[IRS1]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [MRFAP1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[MRFAP1]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Mst1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Mst1]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Na+/K+/2Cl- cotransporter]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Na+/K+/2Cl- cotransporter]-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Nanog]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Nanog]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [OCT4]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[OCT4]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [p53]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[p53]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [TBC1D3]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[TBC1D3]-L-lysine
Q14999; Q8N3Y1
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Cdt1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Cdt1]-L-lysine
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [APOBEC3]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[APOBEC3]-L-lysine
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Cdt1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Cdt1]-L-lysine
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [CK1alpha]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Ck1alpha]-L-lysine
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [CK1alpha]-L-lysine48
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[CK1alpha]-L-lysine48
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Na+/K+/2Cl- cotransporter]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Na+/K+/2Cl- cotransporter]-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-ubiquitinyl-[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + [Cdt1]-L-lysine
[cullin-RING-E3-ubiquitin-carrier protein]-L-cysteine + N6-ubiquitinyl-[Cdt1]-L-lysine
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[1-(4-chlorophenyl)-1H-pyrazol-4-yl]-7,8-dihydroxy-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
7,8-dihydroxy-3-(1-phenyl-1H-pyrazol-4-yl)-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
7,8-dihydroxy-3-(1H-pyrazol-4-yl)-2-(trifluoromethyl)-4H-1-benzopyran-4-one
KH-3-115, 13% inhibition at 0.03 mM
7-hydroxy-8-methoxy-3-(1-phenyl-1H-pyrazol-4-yl)-2-(trifluoromethyl)-4H-chromen-4-one
KH-4-119, 13% inhibition at 0.03 mM
3-[1-(4-chlorophenyl)-1H-pyrazol-4-yl]-7,8-dihydroxy-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
KH-4-43, inhibits the ubiquitination of CK1alpha
3-[1-(4-chlorophenyl)-1H-pyrazol-4-yl]-7,8-dihydroxy-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
KH-4-43
3-[1-(4-chlorophenyl)-1H-pyrazol-4-yl]-7,8-dihydroxy-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
KH-4-43, complete inhibition at 0.03 mM
7,8-dihydroxy-3-(1-phenyl-1H-pyrazol-4-yl)-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
33-11
7,8-dihydroxy-3-(1-phenyl-1H-pyrazol-4-yl)-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
33-11, 37% inhibition at 0.03 mM
7,8-dihydroxy-3-phenoxy-2-(trifluoromethyl)-4H-1-benzopyran-4-one
inhibits the ubiquitination of beta-catenin
7,8-dihydroxy-3-phenoxy-2-(trifluoromethyl)-4H-1-benzopyran-4-one
-
additional information
enzyme neddylation reduces its sensitivity to KH-4-43 inhibition on CK1alpha ubiquitination
-
additional information
not inhibited by 3-(1-(4-fluorophenyl)-1H-pyrazol-4-yl)-7,8-dimethoxy-2-(trifluoromethyl)-4H-chromen-4-one, 3-(1-butyl-1H-pyrazol-4-yl)-7,8-dihydroxy-2-(trifluoromethyl)-4H-chromen-4-one, 7,8-dihydroxy-3-(1-propyl-1H-pyrazol-4-yl)-2-(trifluoromethyl)-4H-chromen-4-one, and 3-(1-ethyl-1H-pyrazol-4-yl)-7,8-dihydroxy-2-(trifluoromethyl)-4H-chromen-4-one
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Liver Neoplasms
Cullin-5, a ubiquitin ligase scaffold protein, is significantly underexpressed in endometrial adenocarcinomas and is a target of miR-182.
Neoplasm Metastasis
Cullin5 deficiency promotes small-cell lung cancer metastasis by stabilizing integrin ?1.
Neoplasms
Cullin-5, a ubiquitin ligase scaffold protein, is significantly underexpressed in endometrial adenocarcinomas and is a target of miR-182.
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00593
3-[1-(4-chlorophenyl)-1H-pyrazol-4-yl]-7,8-dihydroxy-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
Homo sapiens
at pH 7.4 and 37°C
0.00501
7,8-dihydroxy-3-(1-phenyl-1H-pyrazol-4-yl)-2-(trifluoromethyl)-2,3-dihydro-4H-1-benzopyran-4-one
Homo sapiens
at pH 7.4 and 37°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
Q14999; Q8N3Y1
CRL7Fbxw8 is an E3 ubiquitin ligase complex, containing cullin 7 as a scaffold, the F-box protein Fbxw8 as a substrate receptor, the Skp1 adaptor, and the ROC1/Rbx1 RING finger protein for working with E2 enzyme to facilitate ubiquitin transfer
physiological function
malfunction
Q14999; Q8N3Y1
enzyme mutations are linked to hereditary human growth retardation disease (3-M syndrome)
malfunction
-
genetic depletion and inhibition of cytosolic enzyme enhance neurite extension and branching in developing neurons
physiological function
Q14999; Q8N3Y1
the enzyme plays a role in growth control and cancer cell proliferation
physiological function
the enzyme plays an essential role in cell cycle progression
physiological function
-
the enzyme regulates neurite morphogenesis during neurodevelopment. The enzyme is vital for regulation of neuritogenesis. The cullin-RING E3 ubiquitin ligase 4-Crbn complex regulates doublecortin stability, affecting microtubule dynamics. Cullin 4a and cullin 4b, the core scaffold proteins of the enzyme, exhibit high expression and activation within the cytosol of developing neurons, regulated by neuronal stimulation through N-methyl D-aspartate receptor signaling
physiological function
the multiprotein CRLpVHL complex is necessary for APOBEC3 protein degradation (A3A, -B, -C, D, F, G, and -H). The enzyme more effectively induces degradation of nuclear, procancer APOBEC3 (A3B) than the cytoplasmic, antiretroviral APOBEC3 (A3G) protein
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q95376_HUMAN
23
0
2729
TrEMBL
other Location (Reliability: 1)
RBX2_HUMAN
113
0
12683
Swiss-Prot
Secretory Pathway (Reliability: 2)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal domain in complex with von Hippel-Lindau tumor suppressor protein, elonhin B, and elongin C, hanging drop vapor diffusion method, using 5 M sodium formate as precipitant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, glutatione S-transferase column chromatography, maltose binding protein-Trap column chromatography, anion exchange chromatorgaphy, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, B.; Zhang, K.; Villhauer, E.; Bhuripanyo, K.; Kiyokawa, H.; Schindelin, H.; Yin, J.
Phage display to identify Nedd8-mimicking peptides as inhibitors of the Nedd8 transfer cascade
ChemBioChem
14
1323-1330
2013
Homo sapiens
brenda
Nguyen, H.; Yang, H.; Fribourgh, J.; Wolfe, L.; Xiong, Y.
Insights into cullin-RING E3 ubiquitin ligase recruitment: Structure of the VHL-EloBC-Cul2 complex
Structure
23
441-449
2015
Homo sapiens (P40337)
brenda
Pan, Z.Q.
Cullin-RING E3 ubiquitin ligase 7 in growth control and cancer
Adv. Exp. Med. Biol.
1217
285-296
2020
Homo sapiens (Q14999 AND Q8N3Y1)
brenda
Ares, G.R.
Ubiquitination of NKCC2 by the cullin-RING E3 ubiquitin ligase family in the thick ascending limb of the loop of Henle
Am. J. Physiol. Renal Physiol.
324
F315-F328
2023
Rattus norvegicus
brenda
Shim, T.; Kim, J.Y.; Kim, W.; Lee, Y.I.; Cho, B.; Moon, C.
Cullin-RING E3 ubiquitin ligase 4 regulates neurite morphogenesis during neurodevelopment
iScience
27
108933
2024
Rattus norvegicus
brenda
Wu, K.; DeVita, R.; Pan, Z.
Modulation of cullin-RING E3 ubiquitin ligase-dependent ubiquitination by small molecule compounds
J. Biol. Chem.
300
105752
2024
Homo sapiens (Q13619 AND Q13620 AND P62877)
brenda
Wu, K.; Hopkins, B.D.; Sanchez, R.; DeVita, R.J.; Pan, Z.Q.
Targeting cullin-RING E3 ubiquitin ligase 4 by small molecule modulators
J. Cell. Signal.
2
195-205
2021
Homo sapiens (Q13619 AND Q13620)
brenda
Wu, K.; Huynh, K.Q.; Lu, I.; Moustakim, M.; Miao, H.; Yu, C.; Haeusgen, M.J.; Hopkins, B.D.; Huang, L.; Zheng, N.; Sanchez, R.; DeVita, R.J.; Pan, Z.Q.
Inhibitors of cullin-RING E3 ubiquitin ligase 4 with antitumor potential
Proc. Natl. Acad. Sci. USA
118
e2007328118
2021
Homo sapiens (Q13619 AND Q13620 AND P62877)
brenda
Scholtes, G.K.; Sawyer, A.M.; Vaca, C.C.; Clerc, I.; Roh, M.; Song, C.; D'Aquila, R.T.
The von Hippel-Lindau cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases
Transl. Res.
237
1-15
2021
Homo sapiens (P40337), Homo sapiens (Q93034), Homo sapiens (Q15370), Homo sapiens (Q9UBF6), Homo sapiens (Q15369), Homo sapiens (Q95376)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.2.B13)
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