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UniProtKB - Q13618 (CUL3_HUMAN)

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Protein

Cullin-3

Gene

CUL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:27565346). 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. 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) (PubMed:22358839, PubMed:27716508). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4 (PubMed:23387299, PubMed:23453970, PubMed:23576762). 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 (PubMed:19995937). 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 (PubMed:23455478). The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway (PubMed:29769719). The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1) (PubMed:22578813). The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). 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). The BCR(KLHL24) E3 ubiquitin ligase complex mediates ubiquitination of KRT14, controls KRT14 levels during keratinocytes differentiation, and is essential for skin integrity (PubMed:27798626).27 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

  • cyclin binding Source: Ensembl
  • Notch binding Source: MGI
  • POZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: Ensembl
  • protein homodimerization activity Source: Ensembl
  • ubiquitin protein ligase binding Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • anaphase-promoting complex-dependent catabolic process Source: MGI
  • 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 Rho protein signal transduction Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: Ensembl
  • nuclear protein quality control by the ubiquitin-proteasome system Source: UniProtKB
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  • positive regulation of protein ubiquitination Source: BHF-UCL
  • post-translational protein modification Source: Reactome
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein destabilization Source: BHF-UCL
  • protein monoubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • stem cell division Source: UniProtKB
  • stress fiber assembly Source: UniProtKB
  • trophectodermal cellular morphogenesis Source: Ensembl
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
  • Wnt signaling pathway Source: Ensembl
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processCilium 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-8951664 Neddylation
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000036257.12
HGNCiHGNC:2553 CUL3
MIMi603136 gene
neXtProtiNX_Q13618

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Flagellum, 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_067532413D → G in PHA2E. 1 PublicationCorresponds to variant dbSNP:rs199469656EnsemblClinVar.1
Natural variantiVAR_067533459K → R in PHA2E. 1 PublicationCorresponds to variant dbSNP:rs199469658EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi8452
MalaCardsiCUL3
MIMi614496 phenotype
OpenTargetsiENSG00000036257
Orphaneti300530 Pseudohypoaldosteronism type 2E
PharmGKBiPA27049

Polymorphism and mutation databases

BioMutaiCUL3
DMDMi12643396

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001197932 – 768Cullin-3Add BLAST767

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei585PhosphoserineCombined sources1
Cross-linki712Glycyl 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.4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13618
MaxQBiQ13618
PaxDbiQ13618
PeptideAtlasiQ13618
PRIDEiQ13618
ProteomicsDBi59606
59607 [Q13618-2]
59608 [Q13618-3]

PTM databases

iPTMnetiQ13618
PhosphoSitePlusiQ13618

Expressioni

Tissue specificityi

Brain, spermatozoa, and testis (at protein level). Widely expressed.1 Publication

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. Component of the BCR(KBTBD8) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD8 and RBX1 (PubMed:26399832). Interacts with KCTD5, KLHL9, KLHL11, KLHL13, GAN, ZBTB16, KLHL3, KLHL15, KLHL20, KLHL36, GMCL2, 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). Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (PubMed:24076655, PubMed:27565346). Interacts with COPS9 isoform 2 (PubMed:23776465). Interacts with PPP2R5B; this interaction is indirect and mediated through KLHL15-binding and leads to PPP2R5B proteasomal degradation (PubMed:23135275). Interacts with RBBP8/CtIP; this interaction is indirect and mediated through KLHL15-binding and leads to RBBP8 proteasomal degradation (PubMed:27561354). Interacts with KLHL24 in the BCR(KLHL24) E3 ubiquitin ligase complex, composed of CUL3, RBX1 and KLHL24 (PubMed:27798626).By similarityCurated36 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cyclin binding Source: Ensembl
  • Notch binding Source: MGI
  • POZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: Ensembl
  • protein homodimerization activity Source: Ensembl
  • ubiquitin protein ligase binding Source: GO_Central
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114030, 1219 interactors
CORUMiQ13618
DIPiDIP-31611N
IntActiQ13618, 72 interactors
MINTiQ13618
STRINGi9606.ENSP00000264414

Structurei

Secondary structure

1768
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 45Combined sources20
Helixi49 – 51Combined sources3
Helixi54 – 66Combined sources13
Helixi70 – 87Combined sources18
Helixi89 – 94Combined sources6
Turni95 – 98Combined sources4
Helixi101 – 122Combined sources22
Helixi124 – 129Combined sources6
Helixi132 – 134Combined sources3
Helixi139 – 150Combined sources12
Turni151 – 153Combined sources3
Helixi155 – 173Combined sources19
Helixi180 – 192Combined sources13
Beta strandi195 – 198Combined sources4
Helixi199 – 204Combined sources6
Helixi206 – 227Combined sources22
Helixi230 – 251Combined sources22
Helixi254 – 256Combined sources3
Helixi257 – 268Combined sources12
Turni269 – 272Combined sources4
Helixi273 – 277Combined sources5
Turni280 – 282Combined sources3
Helixi284 – 287Combined sources4
Turni288 – 291Combined sources4
Helixi293 – 303Combined sources11
Helixi309 – 323Combined sources15
Helixi339 – 358Combined sources20
Helixi364 – 380Combined sources17

3D structure databases

ProteinModelPortaliQ13618
SMRiQ13618
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2167 Eukaryota
COG5647 LUCA
GeneTreeiENSGT00760000119212
HOVERGENiHBG003619
InParanoidiQ13618
KOiK03869
OMAiTSTFWPM
OrthoDBiEOG091G02DP
PhylomeDBiQ13618
TreeFamiTF105858

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016157 Cullin_CS
IPR016158 Cullin_homology
IPR036317 Cullin_homology_sf
IPR001373 Cullin_N
IPR019559 Cullin_neddylation_domain
IPR016159 Cullin_repeat-like_dom_sf
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00888 Cullin, 1 hit
PF10557 Cullin_Nedd8, 1 hit
SMARTiView protein in SMART
SM00182 CULLIN, 1 hit
SM00884 Cullin_Nedd8, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF74788 SSF74788, 1 hit
SSF75632 SSF75632, 1 hit
PROSITEiView protein in PROSITE
PS01256 CULLIN_1, 1 hit
PS50069 CULLIN_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti13D → G in AAC36682 (PubMed:9663463).Curated1
Sequence conflicti397K → T in AAQ01660 (Ref. 4) Curated1
Sequence conflicti481N → T in AAQ01660 (Ref. 4) Curated1
Sequence conflicti609E → G in AAH31844 (PubMed:15489334).Curated1
Sequence conflicti666T → I in AAQ01660 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01719413D → H. Corresponds to variant dbSNP:rs2969802Ensembl.1
Natural variantiVAR_048839184R → S. Corresponds to variant dbSNP:rs17480168Ensembl.1
Natural variantiVAR_067532413D → G in PHA2E. 1 PublicationCorresponds to variant dbSNP:rs199469656EnsemblClinVar.1
Natural variantiVAR_067533459K → R in PHA2E. 1 PublicationCorresponds to variant dbSNP:rs199469658EnsemblClinVar.1
Natural variantiVAR_017195567V → I. Corresponds to variant dbSNP:rs3738952EnsemblClinVar.1
Natural variantiVAR_078688719H → R Found in a patient with autism spectrum disorder; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs763087632Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0088241 – 24Missing in isoform 2. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_00882523 – 88Missing in isoform 3. CuratedAdd BLAST66

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

Similar proteinsi

Entry informationi

Entry nameiCUL3_HUMAN
AccessioniPrimary (citable) accession number: Q13618
Secondary accession number(s): A8K536
, B8ZZC3, O75415, Q569L3, Q9UBI8, Q9UET7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 24, 2001
Last modified: July 18, 2018
This is version 188 of the entry and version 2 of the sequence. See 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

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