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Protein

Cullin-3

Gene

CUL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:20389280, PubMed:21840486, PubMed:21670212, PubMed:24768539). 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. The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis (PubMed:25270598).By similarity22 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • POZ domain binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

  • cell cycle arrest Source: ProtInc
  • cell migration Source: UniProtKB
  • cell projection organization Source: UniProtKB-KW
  • COPII vesicle coating Source: UniProtKB
  • embryonic cleavage Source: UniProtKB
  • ER to Golgi vesicle-mediated transport Source: UniProtKB
  • fibroblast apoptotic process Source: Ensembl
  • G1/S transition of mitotic cell cycle Source: ProtInc
  • gastrulation Source: Ensembl
  • integrin-mediated signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway Source: ProtInc
  • liver morphogenesis Source: Ensembl
  • MAPK cascade Source: Reactome
  • mitotic metaphase plate congression Source: UniProtKB
  • negative regulation of canonical Wnt signaling pathway Source: Reactome
  • negative regulation of cyclin-dependent protein serine/threonine kinase by cyclin degradation Source: MGI
  • negative regulation of Rho protein signal transduction Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein monoubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
  • stem cell division Source: UniProtKB
  • stress fiber assembly Source: UniProtKB
  • trophectodermal cellular morphogenesis Source: Ensembl
  • Wnt signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, ER-Golgi transport, Transport, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-4641258. Degradation of DVL.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13618.
SIGNORiQ13618.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2553. CUL3.

Subcellular locationi

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: GOC
  • membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
  • polar microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pseudohypoaldosteronism 2E (PHA2E)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics.
See also OMIM:614496
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti413 – 4131D → G in PHA2E. 1 Publication
Corresponds to variant rs199469656 [ dbSNP | Ensembl ].
VAR_067532
Natural varianti459 – 4591K → R in PHA2E. 1 Publication
Corresponds to variant rs199469658 [ dbSNP | Ensembl ].
VAR_067533

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiCUL3.
MIMi614496. phenotype.
Orphaneti300530. Pseudohypoaldosteronism type 2E.
PharmGKBiPA27049.

Polymorphism and mutation databases

BioMutaiCUL3.
DMDMi12643396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 768767Cullin-3PRO_0000119793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei585 – 5851PhosphoserineCombined sources
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.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13618.
MaxQBiQ13618.
PaxDbiQ13618.
PeptideAtlasiQ13618.
PRIDEiQ13618.

PTM databases

iPTMnetiQ13618.
PhosphoSiteiQ13618.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000036257.
CleanExiHS_CUL3.
ExpressionAtlasiQ13618. baseline and differential.
GenevisibleiQ13618. HS.

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 (Probable). 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. Interacts with DCUN1D3. Interacts with KCTD17 in the BCR(KCTD17) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD17 and RBX1 (PubMed:25270598).By similarityCurated29 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABTB1Q969K43EBI-456129,EBI-7223971
CAND1Q86VP62EBI-456129,EBI-456077
CASP8Q147906EBI-456129,EBI-78060
CCDC22O608262EBI-456129,EBI-3943153
FLJ13057Q53SE73EBI-456129,EBI-10172181
HSP90AB1P082382EBI-456129,EBI-352572
KCTD13Q8WZ193EBI-456129,EBI-742916
KCTD6Q8NC693EBI-456129,EBI-2511344
KCTD9Q7L2733EBI-456129,EBI-4397613
KLHL12Q53G593EBI-456129,EBI-740929
KLHL2O951983EBI-456129,EBI-746999
KLHL20Q9Y2M52EBI-456129,EBI-714379
KLHL3Q8N4I83EBI-456129,EBI-10230467
KLHL7Q8IXQ57EBI-456129,EBI-6153160
SPOPO437912EBI-456129,EBI-743549
TNFAIP1Q138293EBI-456129,EBI-2505861
TNFSF10P505912EBI-456129,EBI-495373
ZMAT4Q9H8983EBI-456129,EBI-2548542

GO - Molecular functioni

  • POZ domain binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: GO_Central

Protein-protein interaction databases

BioGridi114030. 1204 interactions.
DIPiDIP-31611N.
IntActiQ13618. 54 interactions.
MINTiMINT-3028280.
STRINGi9606.ENSP00000264414.

Structurei

Secondary structure

1
768
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 4520Combined sources
Helixi49 – 513Combined sources
Helixi54 – 6613Combined sources
Helixi70 – 8718Combined sources
Helixi89 – 946Combined sources
Turni95 – 984Combined sources
Helixi101 – 12222Combined sources
Helixi124 – 1296Combined sources
Helixi132 – 1343Combined sources
Helixi139 – 15012Combined sources
Turni151 – 1533Combined sources
Helixi155 – 17319Combined sources
Helixi180 – 19213Combined sources
Beta strandi195 – 1984Combined sources
Helixi199 – 2046Combined sources
Helixi206 – 22722Combined sources
Helixi230 – 25122Combined sources
Helixi254 – 2563Combined sources
Helixi257 – 26812Combined sources
Turni269 – 2724Combined sources
Helixi273 – 2775Combined sources
Turni280 – 2823Combined sources
Helixi284 – 2874Combined sources
Turni288 – 2914Combined sources
Helixi293 – 30311Combined sources
Helixi309 – 32315Combined sources
Helixi339 – 35820Combined sources
Helixi364 – 38017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MYLNMR-A49-68[»]
2MYMNMR-A49-68[»]
4AP2X-ray2.80B1-388[»]
4APFX-ray3.10B23-388[»]
4EOZX-ray2.40B/D20-381[»]
4HXIX-ray3.51B20-381[»]
ProteinModelPortaliQ13618.
SMRiQ13618. Positions 17-768.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2167. Eukaryota.
COG5647. LUCA.
GeneTreeiENSGT00760000119212.
HOVERGENiHBG003619.
InParanoidiQ13618.
KOiK03869.
OMAiHKIRAPR.
OrthoDBiEOG091G02DP.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. 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. AlignAdd to basket

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

        10         20         30         40         50
MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS
60 70 80 90 100
GLSFEELYRN AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN
110 120 130 140 150
FLQTLNQAWN DHQTAMVMIR DILMYMDRVY VQQNNVENVY NLGLIIFRDQ
160 170 180 190 200
VVRYGCIRDH LRQTLLDMIA RERKGEVVDR GAIRNACQML MILGLEGRSV
210 220 230 240 250
YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR INEEIERVMH
260 270 280 290 300
CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLGCMY
310 320 330 340 350
KLFSRVPNGL KTMCECMSSY LREQGKALVS EEGEGKNPVD YIQGLLDLKS
360 370 380 390 400
RFDRFLLESF NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV
410 420 430 440 450
KGLTEQEVET ILDKAMVLFR FMQEKDVFER YYKQHLARRL LTNKSVSDDS
460 470 480 490 500
EKNMISKLKT ECGCQFTSKL EGMFRDMSIS NTTMDEFRQH LQATGVSLGG
510 520 530 540 550
VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL AKHSGRQLTL
560 570 580 590 600
QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
610 620 630 640 650
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS
660 670 680 690 700
KEIENGHIFT VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK
710 720 730 740 750
HEIEAAIVRI MKSRKKMQHN VLVAEVTQQL KARFLPSPVV IKKRIEGLIE
760
REYLARTPED RKVYTYVA
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 differs from that shown. Reason: Frameshift at position 452. Curated
The sequence AAC36682 differs from that shown. Reason: Frameshift at positions 159 and 179. Curated
The sequence BAA31592 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131D → G in AAC36682 (PubMed:9663463).Curated
Sequence conflicti397 – 3971K → T in AAQ01660 (Ref. 4) Curated
Sequence conflicti481 – 4811N → T in AAQ01660 (Ref. 4) Curated
Sequence conflicti609 – 6091E → G in AAH31844 (PubMed:15489334).Curated
Sequence conflicti666 – 6661T → I in AAQ01660 (Ref. 4) Curated

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
Corresponds to variant rs199469656 [ dbSNP | Ensembl ].
VAR_067532
Natural varianti459 – 4591K → R in PHA2E. 1 Publication
Corresponds to variant rs199469658 [ dbSNP | Ensembl ].
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. 1 PublicationVSP_008824Add
BLAST
Alternative sequencei23 – 8866Missing in isoform 3. CuratedVSP_008825Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q13618-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MYLNMR-A49-68[»]
2MYMNMR-A49-68[»]
4AP2X-ray2.80B1-388[»]
4APFX-ray3.10B23-388[»]
4EOZX-ray2.40B/D20-381[»]
4HXIX-ray3.51B20-381[»]
ProteinModelPortaliQ13618.
SMRiQ13618. Positions 17-768.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114030. 1204 interactions.
DIPiDIP-31611N.
IntActiQ13618. 54 interactions.
MINTiMINT-3028280.
STRINGi9606.ENSP00000264414.

PTM databases

iPTMnetiQ13618.
PhosphoSiteiQ13618.

Polymorphism and mutation databases

BioMutaiCUL3.
DMDMi12643396.

Proteomic databases

EPDiQ13618.
MaxQBiQ13618.
PaxDbiQ13618.
PeptideAtlasiQ13618.
PRIDEiQ13618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4. human. [Q13618-1]

Organism-specific databases

CTDi8452.
GeneCardsiCUL3.
HGNCiHGNC:2553. CUL3.
HPAiCAB002678.
MalaCardsiCUL3.
MIMi603136. gene.
614496. phenotype.
neXtProtiNX_Q13618.
Orphaneti300530. Pseudohypoaldosteronism type 2E.
PharmGKBiPA27049.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2167. Eukaryota.
COG5647. LUCA.
GeneTreeiENSGT00760000119212.
HOVERGENiHBG003619.
InParanoidiQ13618.
KOiK03869.
OMAiHKIRAPR.
OrthoDBiEOG091G02DP.
PhylomeDBiQ13618.
TreeFamiTF105858.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-4641258. Degradation of DVL.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13618.
SIGNORiQ13618.

Miscellaneous databases

ChiTaRSiCUL3. human.
GeneWikiiCUL3.
GenomeRNAii8452.
PROiQ13618.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000036257.
CleanExiHS_CUL3.
ExpressionAtlasiQ13618. baseline and differential.
GenevisibleiQ13618. HS.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 7, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.