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Q13618

- CUL3_HUMAN

UniProt

Q13618 - CUL3_HUMAN

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Protein
Cullin-3
Gene
CUL3, KIAA0617
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 TIP120A/CAND1 By similarity. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. 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 SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4. The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination (1 Publication, 1 Publication, 1 Publication, 1 Publication). The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1). Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM.21 Publications

Pathwayi

GO - Molecular functioni

  1. POZ domain binding Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. COPII vesicle coating Source: UniProtKB
  2. ER to Golgi vesicle-mediated transport Source: UniProtKB
  3. G1/S transition of mitotic cell cycle Source: ProtInc
  4. Wnt signaling pathway Source: Ensembl
  5. anaphase Source: UniProtKB
  6. cell cycle arrest Source: ProtInc
  7. cell migration Source: UniProtKB
  8. cyclin catabolic process Source: MGI
  9. cytokinesis Source: UniProtKB
  10. embryonic cleavage Source: UniProtKB
  11. gastrulation Source: Ensembl
  12. integrin-mediated signaling pathway Source: UniProtKB
  13. intrinsic apoptotic signaling pathway Source: ProtInc
  14. mitotic anaphase Source: UniProtKB
  15. negative regulation of Rho protein signal transduction Source: UniProtKB
  16. positive regulation of cell proliferation Source: ProtInc
  17. positive regulation of cytokinesis Source: UniProtKB
  18. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  19. protein monoubiquitination Source: UniProtKB
  20. protein polyubiquitination Source: UniProtKB
  21. protein ubiquitination Source: UniProtKB
  22. stem cell division Source: UniProtKB
  23. stress fiber assembly Source: UniProtKB
  24. trophectodermal cellular morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Transport, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_200841. degradation of DVL.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13618.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-3
Short name:
CUL-3
Gene namesi
Name:CUL3
Synonyms:KIAA0617
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2553. CUL3.

Subcellular locationi

Nucleus. Golgi apparatus 2 Publications

GO - Cellular componenti

  1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
  2. Golgi membrane Source: GOC
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProtKB-SubCell
  5. polar microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pseudohypoaldosteronism 2E (PHA2E) [MIM:614496]: An autosomal dominant disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti413 – 4131D → G in PHA2E. 1 Publication
VAR_067532
Natural varianti459 – 4591K → R in PHA2E. 1 Publication
VAR_067533

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614496. phenotype.
Orphaneti300530. Pseudohypoaldosteronism type 2E.
PharmGKBiPA27049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 768767Cullin-3
PRO_0000119793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Cross-linki712 – 712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Post-translational modificationi

Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-protein ligase activity of the BCR complex. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ13618.
PaxDbiQ13618.
PRIDEiQ13618.

PTM databases

PhosphoSiteiQ13618.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

ArrayExpressiQ13618.
BgeeiQ13618.
CleanExiHS_CUL3.
GenevestigatoriQ13618.

Organism-specific databases

HPAiCAB002678.

Interactioni

Subunit structurei

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 TIP120A/CAND1. Part of the BCR(SPOP) containing SPOP, and of BCR containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL. Part of the probable BCR(KLHL9-KLHL13) complex with BTB domain proteins KLHL9 and KLHL13. Part of the BCR(KLHL41) complex containing KLHL41. 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 Inferred. Part of the BCR(ENC1) complex containing ENC1. Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of a complex consisting of BRMS1, CUL3 and SPOP. Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1. Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1. Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL25 and RBX1. Part of a complex consisting of H2AFY, CUL3 and SPOP. Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL42. Interacts with KLHL42 (via the BTB domain). Interacts with KATNA1; the interaction is enhanced by KLHL42. Interacts with KCTD5, KLHL9, KLHL11, KLHL13, GAN, ZBTB16, KLHL3, KLHL15, KLHL20, KLHL36, GMCL1P1, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with KLHL17; the interaction regulates surface GRIK2 expression. Interacts with KCTD7. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KEAP1) complex containing KEAP1. Interacts with KLHL10 By similarity. Interacts with KAT5 and ATF2.27 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAND1Q86VP62EBI-456129,EBI-456077
CASP8Q147906EBI-456129,EBI-78060
HSP90AB1P082382EBI-456129,EBI-352572
KLHL20Q9Y2M52EBI-456129,EBI-714379
SPOPO437912EBI-456129,EBI-743549
TNFSF10P505912EBI-456129,EBI-495373

Protein-protein interaction databases

BioGridi114030. 1152 interactions.
DIPiDIP-31611N.
IntActiQ13618. 38 interactions.
MINTiMINT-3028280.
STRINGi9606.ENSP00000264414.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 4520
Helixi49 – 513
Helixi54 – 6613
Helixi70 – 8718
Helixi89 – 946
Turni95 – 984
Helixi101 – 12222
Helixi124 – 1296
Helixi132 – 1343
Helixi139 – 15012
Turni151 – 1533
Helixi155 – 17319
Helixi180 – 19213
Beta strandi195 – 1984
Helixi199 – 2046
Helixi206 – 22722
Helixi230 – 25122
Helixi254 – 2563
Helixi257 – 26812
Turni269 – 2724
Helixi273 – 2775
Turni280 – 2823
Helixi284 – 2874
Turni288 – 2914
Helixi293 – 30311
Helixi309 – 32315
Helixi339 – 35820
Helixi364 – 38017

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AP2X-ray2.80B1-388[»]
4APFX-ray3.10B23-388[»]
4EOZX-ray2.40B/D20-381[»]
4HXIX-ray3.51B20-381[»]
ProteinModelPortaliQ13618.
SMRiQ13618. Positions 17-768.

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.

Phylogenomic databases

eggNOGiCOG5647.
HOVERGENiHBG003619.
InParanoidiQ13618.
KOiK03869.
OMAiAMGKATQ.
OrthoDBiEOG7C5M7H.
PhylomeDBiQ13618.
TreeFamiTF105858.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13618-1) [UniParc]FASTAAdd to Basket

Also known as: Cul-3 Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS    50
GLSFEELYRN AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN 100
FLQTLNQAWN DHQTAMVMIR DILMYMDRVY VQQNNVENVY NLGLIIFRDQ 150
VVRYGCIRDH LRQTLLDMIA RERKGEVVDR GAIRNACQML MILGLEGRSV 200
YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR INEEIERVMH 250
CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLGCMY 300
KLFSRVPNGL KTMCECMSSY LREQGKALVS EEGEGKNPVD YIQGLLDLKS 350
RFDRFLLESF NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV 400
KGLTEQEVET ILDKAMVLFR FMQEKDVFER YYKQHLARRL LTNKSVSDDS 450
EKNMISKLKT ECGCQFTSKL EGMFRDMSIS NTTMDEFRQH LQATGVSLGG 500
VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL AKHSGRQLTL 550
QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT 600
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS 650
KEIENGHIFT VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK 700
HEIEAAIVRI MKSRKKMQHN VLVAEVTQQL KARFLPSPVV IKKRIEGLIE 750
REYLARTPED RKVYTYVA 768
Length:768
Mass (Da):88,930
Last modified:January 24, 2001 - v2
Checksum:iA1A02022480BF099
GO
Isoform 2 (identifier: Q13618-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Show »
Length:744
Mass (Da):86,234
Checksum:iAD845C2516117B9F
GO
Isoform 3 (identifier: Q13618-3) [UniParc]FASTAAdd to Basket

Also known as: Cul-3 Short

The sequence of this isoform differs from the canonical sequence as follows:
     23-88: Missing.

Show »
Length:702
Mass (Da):81,093
Checksum:i2CDE8E7AF43C898A
GO

Sequence cautioni

The sequence AAC28621.1 differs from that shown. Reason: Frameshift at position 452.
The sequence AAC36682.1 differs from that shown. Reason: Frameshift at positions 159 and 179.
The sequence BAA31592.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131D → H.
Corresponds to variant rs2969802 [ dbSNP | Ensembl ].
VAR_017194
Natural varianti184 – 1841R → S.
Corresponds to variant rs17480168 [ dbSNP | Ensembl ].
VAR_048839
Natural varianti413 – 4131D → G in PHA2E. 1 Publication
VAR_067532
Natural varianti459 – 4591K → R in PHA2E. 1 Publication
VAR_067533
Natural varianti567 – 5671V → I.
Corresponds to variant rs3738952 [ dbSNP | Ensembl ].
VAR_017195

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424Missing in isoform 2.
VSP_008824Add
BLAST
Alternative sequencei23 – 8866Missing in isoform 3.
VSP_008825Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131D → G in AAC36682. 1 Publication
Sequence conflicti397 – 3971K → T in AAQ01660. 1 Publication
Sequence conflicti481 – 4811N → T in AAQ01660. 1 Publication
Sequence conflicti609 – 6091E → G in AAH31844. 1 Publication
Sequence conflicti666 – 6661T → I in AAQ01660. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064087 mRNA. Translation: AAC36304.1.
AB014517 mRNA. Translation: BAA31592.2. Different initiation.
AF062537 mRNA. Translation: AAC36682.1. Frameshift.
AY337761 mRNA. Translation: AAQ01660.1.
AK291151 mRNA. Translation: BAF83840.1.
AC073052 Genomic DNA. No translation available.
AC092679 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70828.1.
BC031844 mRNA. Translation: AAH31844.1.
BC039598 mRNA. Translation: AAH39598.1.
BC092409 mRNA. Translation: AAH92409.1.
U58089 mRNA. Translation: AAC50546.1.
AF052147 mRNA. Translation: AAC28621.1. Frameshift.
CCDSiCCDS2462.1. [Q13618-1]
CCDS58751.1. [Q13618-3]
RefSeqiNP_001244126.1. NM_001257197.1. [Q13618-3]
NP_001244127.1. NM_001257198.1.
NP_003581.1. NM_003590.4. [Q13618-1]
UniGeneiHs.372286.

Genome annotation databases

EnsembliENST00000264414; ENSP00000264414; ENSG00000036257. [Q13618-1]
ENST00000344951; ENSP00000343601; ENSG00000036257. [Q13618-3]
ENST00000409096; ENSP00000387200; ENSG00000036257. [Q13618-2]
ENST00000409777; ENSP00000386525; ENSG00000036257. [Q13618-2]
GeneIDi8452.
KEGGihsa:8452.
UCSCiuc002vny.3. human. [Q13618-1]
uc010zls.2. human. [Q13618-3]

Polymorphism databases

DMDMi12643396.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064087 mRNA. Translation: AAC36304.1 .
AB014517 mRNA. Translation: BAA31592.2 . Different initiation.
AF062537 mRNA. Translation: AAC36682.1 . Frameshift.
AY337761 mRNA. Translation: AAQ01660.1 .
AK291151 mRNA. Translation: BAF83840.1 .
AC073052 Genomic DNA. No translation available.
AC092679 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70828.1 .
BC031844 mRNA. Translation: AAH31844.1 .
BC039598 mRNA. Translation: AAH39598.1 .
BC092409 mRNA. Translation: AAH92409.1 .
U58089 mRNA. Translation: AAC50546.1 .
AF052147 mRNA. Translation: AAC28621.1 . Frameshift.
CCDSi CCDS2462.1. [Q13618-1 ]
CCDS58751.1. [Q13618-3 ]
RefSeqi NP_001244126.1. NM_001257197.1. [Q13618-3 ]
NP_001244127.1. NM_001257198.1.
NP_003581.1. NM_003590.4. [Q13618-1 ]
UniGenei Hs.372286.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AP2 X-ray 2.80 B 1-388 [» ]
4APF X-ray 3.10 B 23-388 [» ]
4EOZ X-ray 2.40 B/D 20-381 [» ]
4HXI X-ray 3.51 B 20-381 [» ]
ProteinModelPortali Q13618.
SMRi Q13618. Positions 17-768.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114030. 1152 interactions.
DIPi DIP-31611N.
IntActi Q13618. 38 interactions.
MINTi MINT-3028280.
STRINGi 9606.ENSP00000264414.

PTM databases

PhosphoSitei Q13618.

Polymorphism databases

DMDMi 12643396.

Proteomic databases

MaxQBi Q13618.
PaxDbi Q13618.
PRIDEi Q13618.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264414 ; ENSP00000264414 ; ENSG00000036257 . [Q13618-1 ]
ENST00000344951 ; ENSP00000343601 ; ENSG00000036257 . [Q13618-3 ]
ENST00000409096 ; ENSP00000387200 ; ENSG00000036257 . [Q13618-2 ]
ENST00000409777 ; ENSP00000386525 ; ENSG00000036257 . [Q13618-2 ]
GeneIDi 8452.
KEGGi hsa:8452.
UCSCi uc002vny.3. human. [Q13618-1 ]
uc010zls.2. human. [Q13618-3 ]

Organism-specific databases

CTDi 8452.
GeneCardsi GC02M225298.
HGNCi HGNC:2553. CUL3.
HPAi CAB002678.
MIMi 603136. gene.
614496. phenotype.
neXtProti NX_Q13618.
Orphaneti 300530. Pseudohypoaldosteronism type 2E.
PharmGKBi PA27049.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5647.
HOVERGENi HBG003619.
InParanoidi Q13618.
KOi K03869.
OMAi AMGKATQ.
OrthoDBi EOG7C5M7H.
PhylomeDBi Q13618.
TreeFami TF105858.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_200841. degradation of DVL.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki Q13618.

Miscellaneous databases

ChiTaRSi CUL3. human.
GeneWikii CUL3.
GenomeRNAii 8452.
NextBioi 31630.
PROi Q13618.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13618.
Bgeei Q13618.
CleanExi HS_CUL3.
Genevestigatori Q13618.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view ]
SMARTi SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view ]
SUPFAMi SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEi PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression analysis of a novel salicylate suppressible gene, Hs-CUL-3, a member of cullin/Cdc53 family."
    Du M., Sansores-Garcia L., Zu Z., Wu K.K.
    J. Biol. Chem. 273:24289-24292(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A."
    Michel J.J., Xiong Y.
    Cell Growth Differ. 9:435-449(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon carcinoma.
  4. "Cloning and characterization of a new isoform of CUL3 gene in testis."
    Xu M., Huang X.Y., Yin L.L., Xu Z.Y., Lu L., Zhou Z.M., Sha J.H.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Ovary, Skin and Uterus.
  9. "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family."
    Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.
    Cell 85:829-839(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 192-768.
  10. Yu W., Sarginson J., Gibbs R.A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 398-768.
    Tissue: Brain.
  11. "Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cells."
    Singer J.D., Gurian-West M., Clurman B., Roberts J.M.
    Genes Dev. 13:2375-2387(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CYCE, NEDDYLATION.
  12. "In vitro ubiquitination of cyclin D1 by ROC1-CUL1 and ROC1-CUL3."
    Maeda I., Ohta T., Koizumi H., Fukuda M.
    FEBS Lett. 494:181-185(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Covalent modification of all members of human cullin family proteins by NEDD8."
    Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
    Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION.
  14. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
    Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
    Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBX1 AND RNF7.
  15. "TIP120A associates with cullins and modulates ubiquitin ligase activity."
    Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.
    J. Biol. Chem. 278:15905-15910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIP120A.
  16. "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases."
    Furukawa M., He Y.J., Borchers C., Xiong Y.
    Nat. Cell Biol. 5:1001-1007(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN; ZBTB16; KLHL9; KLHL13; KLHL21; KLHL3; KLHL15; KLHL20; KLHL36; GMCL1P1; BTBD1 AND SPOP.
  17. "Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway."
    Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.
    J. Biol. Chem. 280:30091-30099(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE BCR(KLHL41) COMPLEX, IDENTIFICATION IN THE BCR(ENC1) COMPLEX, IDENTIFICATION IN THE BCR(KEAP1) COMPLEX, IDENTIFICATION IN THE BCR(GAN) COMPLEX.
  18. "Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
    Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.
    Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SPOP AND BMI1, IDENTIFICATION IN A COMPLEX WITH SPOP AND H2AFY, FUNCTION.
  19. "BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase."
    Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.
    J. Biol. Chem. 281:12664-12672(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BCR(SPOP) COMPLEX, INTERACTION WITH SPOP, FUNCTION IN UBIQUITINATION OF DAXX.
  20. "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells."
    Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.
    Dev. Cell 12:887-900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KLHL9 AND KLHL13.
  21. "Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization."
    Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T.
    Cell. Signal. 19:1071-1080(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION.
  22. "The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer."
    Wimuttisuk W., Singer J.D.
    Mol. Biol. Cell 18:899-909(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: BCR COMPLEX HOMODIMERIZATION.
  23. Cited for: INTERACTION WITH KCTD5.
  24. "Regulation of TIP60 by ATF2 modulates ATM activation."
    Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.
    J. Biol. Chem. 283:17605-17614(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATF2 AND KAT5.
  25. "The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal mitosis in mammalian cells."
    Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.
    J. Biol. Chem. 284:11663-11675(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BCR(KLHL42) COMPLEX, FUNCTION IN UBIQUITINATION OF KATNA1, INTERACTION WITH KATNA1 AND KLHL42.
  26. "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis."
    Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M., Sumara I., Peter M.
    J. Cell Biol. 187:791-800(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BCR(KLHL21) COMPLEX, FUNCTION.
  27. "The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses."
    Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.
    EMBO J. 29:1748-1761(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex."
    Kim B., Nam H.J., Pyo K.E., Jang M.J., Kim I.S., Kim D., Boo K., Lee S.H., Yoon J.B., Baek S.H., Kim J.H.
    Biochem. Biophys. Res. Commun. 415:720-726(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH SPOP AND BRMS1.
  30. "A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression."
    Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C., Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H., Gu D.L., Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.
    Cancer Cell 20:214-228(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX.
  31. "PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-induced neurite outgrowth."
    Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.
    J. Cell Biol. 193:985-994(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX.
  32. Cited for: INTERACTION WITH KCTD7.
  33. Cited for: IDENTIFICATION IN THE BCR(KLHL25) COMPLEX, FUNCTION.
  34. "Ubiquitin-dependent regulation of COPII coat size and function."
    Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M.
    Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BCR(KLHL12) COMPLEX, FUNCTION.
  35. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  36. "The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction."
    Ohta A., Schumacher F.R., Mehellou Y., Johnson C., Knebel A., Macartney T.J., Wood N.T., Alessi D.R., Kurz T.
    Biochem. J. 451:111-122(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KLHL3.
  37. Cited for: FUNCTION, IDENTIFICATION IN THE BCR(KLHL3) COMPLEX.
  38. Cited for: IDENTIFICATION IN THE BCR(KLHL22) COMPLEX, FUNCTION.
  39. "Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4."
    Shibata S., Zhang J., Puthumana J., Stone K.L., Lifton R.P.
    Proc. Natl. Acad. Sci. U.S.A. 110:7838-7843(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE BCR(KLHL3) COMPLEX.
  40. "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
    Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
    Mol. Cell 54:586-600(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX.
  41. "Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase."
    Errington W.J., Khan M.Q., Bueler S.A., Rubinstein J.L., Chakrabartty A., Prive G.G.
    Structure 20:1141-1153(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-381 IN COMPLEX WITH SPOP, FUNCTION, IDENTIFICATION IN UBIQUITIN LIGASE COMPLEXES WITH SPOP AND SPOPL, SUBUNIT.
  42. "Crystal structure of KLHL3 in complex with Cullin3."
    Ji A.X., Prive G.G.
    PLoS ONE 8:E60445-E60445(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 20-381 IN COMPLEX WITH KLHL3.
  43. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-388 IN COMPLEX WITH KLHL11, INTERACTION WITH KLHL11.
  44. Cited for: VARIANTS PHA2E GLY-413 AND ARG-459.

Entry informationi

Entry nameiCUL3_HUMAN
AccessioniPrimary (citable) accession number: Q13618
Secondary accession number(s): A8K536
, B8ZZC3, O75415, Q569L3, Q9UBI8, Q9UET7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 24, 2001
Last modified: September 3, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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