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Protein

Cullin-associated NEDD8-dissociated protein 1

Gene

CAND1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes.6 Publications

GO - Biological processi

  • cell differentiation Source: UniProtKB
  • negative regulation of catalytic activity Source: UniProtKB
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: Ensembl
  • protein ubiquitination Source: UniProtKB
  • SCF complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-associated NEDD8-dissociated protein 1
Alternative name(s):
Cullin-associated and neddylation-dissociated protein 1
TBP-interacting protein of 120 kDa A
Short name:
TBP-interacting protein 120A
p120 CAND1
Gene namesi
Name:CAND1
Synonyms:KIAA0829, TIP120, TIP120A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30688. CAND1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Predominantly cytoplasmic.

GO - Cellular componenti

  • cullin-RING ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi55832.
OpenTargetsiENSG00000111530.
PharmGKBiPA142672207.

Polymorphism and mutation databases

BioMutaiCAND1.
DMDMi67460541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000892932 – 1230Cullin-associated NEDD8-dissociated protein 1Add BLAST1229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei55N6-acetyllysineCombined sources1
Modified residuei335PhosphoserineCombined sources1
Modified residuei558PhosphoserineCombined sources1
Modified residuei971N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ86VP6.
MaxQBiQ86VP6.
PaxDbiQ86VP6.
PeptideAtlasiQ86VP6.
PRIDEiQ86VP6.

PTM databases

iPTMnetiQ86VP6.
PhosphoSitePlusiQ86VP6.
SwissPalmiQ86VP6.

Expressioni

Inductioni

Repressed by miR-148a.1 Publication

Gene expression databases

BgeeiENSG00000111530.
ExpressionAtlasiQ86VP6. baseline and differential.
GenevisibleiQ86VP6. HS.

Organism-specific databases

HPAiHPA055748.
HPA062833.
HPA069053.

Interactioni

Subunit structurei

Interacts with TBP (By similarity). Part of a complex that contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated CUL1. Interaction with cullins is abolished in presence of COMMD1, which antagonizes with CAND1 for interacting with cullins. Interacts with DCUN1D3.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL1Q1361619EBI-456077,EBI-359390
CUL2Q136173EBI-456077,EBI-456179
CUL3Q136182EBI-456077,EBI-456129
CUL4AQ136193EBI-456077,EBI-456106
CUL4BQ136204EBI-456077,EBI-456067

Protein-protein interaction databases

BioGridi120937. 699 interactors.
DIPiDIP-31608N.
IntActiQ86VP6. 29 interactors.
MINTiMINT-4999459.
STRINGi9606.ENSP00000299218.

Structurei

Secondary structure

11230
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 14Combined sources9
Helixi20 – 33Combined sources14
Beta strandi35 – 37Combined sources3
Helixi45 – 56Combined sources12
Helixi62 – 76Combined sources15
Helixi81 – 94Combined sources14
Beta strandi98 – 100Combined sources3
Helixi101 – 116Combined sources16
Helixi127 – 142Combined sources16
Helixi148 – 164Combined sources17
Turni170 – 172Combined sources3
Helixi173 – 180Combined sources8
Helixi181 – 185Combined sources5
Helixi189 – 202Combined sources14
Turni203 – 205Combined sources3
Helixi214 – 224Combined sources11
Helixi234 – 244Combined sources11
Helixi247 – 249Combined sources3
Helixi256 – 264Combined sources9
Turni269 – 271Combined sources3
Helixi272 – 284Combined sources13
Helixi291 – 301Combined sources11
Helixi348 – 361Combined sources14
Helixi368 – 372Combined sources5
Turni373 – 375Combined sources3
Helixi376 – 380Combined sources5
Beta strandi386 – 388Combined sources3
Helixi389 – 405Combined sources17
Helixi424 – 431Combined sources8
Helixi434 – 442Combined sources9
Helixi448 – 464Combined sources17
Turni466 – 469Combined sources4
Helixi470 – 472Combined sources3
Helixi473 – 483Combined sources11
Beta strandi487 – 489Combined sources3
Helixi491 – 506Combined sources16
Helixi510 – 513Combined sources4
Helixi514 – 517Combined sources4
Turni518 – 520Combined sources3
Helixi521 – 528Combined sources8
Helixi533 – 550Combined sources18
Beta strandi553 – 555Combined sources3
Helixi562 – 576Combined sources15
Beta strandi579 – 581Combined sources3
Helixi583 – 599Combined sources17
Helixi601 – 603Combined sources3
Helixi607 – 618Combined sources12
Beta strandi621 – 623Combined sources3
Helixi624 – 635Combined sources12
Helixi645 – 658Combined sources14
Helixi664 – 680Combined sources17
Helixi687 – 694Combined sources8
Helixi698 – 700Combined sources3
Helixi706 – 719Combined sources14
Helixi724 – 729Combined sources6
Turni730 – 734Combined sources5
Helixi735 – 742Combined sources8
Helixi749 – 763Combined sources15
Helixi772 – 779Combined sources8
Turni781 – 785Combined sources5
Helixi793 – 809Combined sources17
Helixi815 – 818Combined sources4
Turni819 – 824Combined sources6
Turni826 – 829Combined sources4
Helixi832 – 848Combined sources17
Helixi856 – 863Combined sources8
Helixi864 – 866Combined sources3
Helixi870 – 886Combined sources17
Helixi888 – 900Combined sources13
Helixi903 – 905Combined sources3
Helixi906 – 918Combined sources13
Turni923 – 925Combined sources3
Helixi926 – 936Combined sources11
Helixi947 – 960Combined sources14
Helixi963 – 965Combined sources3
Helixi967 – 970Combined sources4
Turni971 – 973Combined sources3
Beta strandi974 – 977Combined sources4
Helixi979 – 988Combined sources10
Helixi990 – 992Combined sources3
Helixi1001 – 1007Combined sources7
Turni1009 – 1014Combined sources6
Beta strandi1015 – 1019Combined sources5
Helixi1021 – 1036Combined sources16
Helixi1038 – 1040Combined sources3
Helixi1042 – 1044Combined sources3
Helixi1045 – 1054Combined sources10
Helixi1060 – 1062Combined sources3
Beta strandi1063 – 1068Combined sources6
Beta strandi1071 – 1076Combined sources6
Helixi1079 – 1094Combined sources16
Beta strandi1098 – 1100Combined sources3
Helixi1102 – 1111Combined sources10
Helixi1117 – 1132Combined sources16
Helixi1136 – 1139Combined sources4
Turni1140 – 1145Combined sources6
Helixi1146 – 1154Combined sources9
Helixi1163 – 1182Combined sources20
Beta strandi1190 – 1194Combined sources5
Helixi1200 – 1208Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U6GX-ray3.10C1-1230[»]
4A0CX-ray3.80A/B1-1230[»]
ProteinModelPortaliQ86VP6.
SMRiQ86VP6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86VP6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati2 – 39HEAT 1Add BLAST38
Repeati44 – 81HEAT 2Add BLAST38
Repeati83 – 119HEAT 3Add BLAST37
Repeati131 – 165HEAT 4Add BLAST35
Repeati171 – 208HEAT 5Add BLAST38
Repeati210 – 247HEAT 6Add BLAST38
Repeati248 – 282HEAT 7Add BLAST35
Repeati289 – 366HEAT 8Add BLAST78
Repeati370 – 407HEAT 9Add BLAST38
Repeati424 – 467HEAT 10Add BLAST44
Repeati471 – 510HEAT 11Add BLAST40
Repeati515 – 552HEAT 12Add BLAST38
Repeati563 – 602HEAT 13Add BLAST40
Repeati606 – 643HEAT 14Add BLAST38
Repeati646 – 683HEAT 15Add BLAST38
Repeati688 – 725HEAT 16Add BLAST38
Repeati729 – 768HEAT 17Add BLAST40
Repeati770 – 808HEAT 18Add BLAST39
Repeati809 – 845HEAT 19Add BLAST37
Repeati852 – 889HEAT 20Add BLAST38
Repeati890 – 927HEAT 21Add BLAST38
Repeati928 – 960HEAT 22Add BLAST33
Repeati961 – 998HEAT 23Add BLAST38
Repeati1002 – 1039HEAT 24Add BLAST38
Repeati1043 – 1097HEAT 25Add BLAST55
Repeati1099 – 1133HEAT 26Add BLAST35
Repeati1140 – 1189HEAT 27Add BLAST50

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi314 – 344Asp-richAdd BLAST31

Sequence similaritiesi

Belongs to the CAND family.Curated
Contains 27 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1824. Eukaryota.
ENOG410XPK4. LUCA.
GeneTreeiENSGT00390000017740.
HOVERGENiHBG053467.
InParanoidiQ86VP6.
KOiK17263.
OMAiTRPAQSW.
OrthoDBiEOG091G017Q.
PhylomeDBiQ86VP6.
TreeFamiTF300355.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013932. TATA-bd_TIP120.
[Graphical view]
PfamiPF08623. TIP120. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 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: Q86VP6-1) [UniParc]FASTAAdd to basket

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
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV
60 70 80 90 100
KMILKLLEDK NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE
110 120 130 140 150
QLRDISSIGL KTVIGELPPA SSGSALAANV CKKITGRLTS AIAKQEDVSV
160 170 180 190 200
QLEALDIMAD MLSRQGGLLV NFHPSILTCL LPQLTSPRLA VRKRTIIALG
210 220 230 240 250
HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA ISRQAGHRIG
260 270 280 290 300
EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI
310 320 330 340 350
CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR
360 370 380 390 400
RAAAKCLDAV VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS
410 420 430 440 450
LLKQTRPVQS WLCDPDAMEQ GETPLTMLQS QVPNIVKALH KQMKEKSVKT
460 470 480 490 500
RQCCFNMLTE LVNVLPGALT QHIPVLVPGI IFSLNDKSSS SNLKIDALSC
510 520 530 540 550
LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL LVTQQLVKVI
560 570 580 590 600
RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL
610 620 630 640 650
GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE
660 670 680 690 700
GVPILASFLR KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL
710 720 730 740 750
ISESDMHVSQ MAISFLTTLA KVYPSSLSKI SGSILNELIG LVRSPLLQGG
760 770 780 790 800
ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT GPVYSQSTAL THKQSYYSIA
810 820 830 840 850
KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL SLGEVGHHID
860 870 880 890 900
LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT
910 920 930 940 950
SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV
960 970 980 990 1000
VAECLGKLTL IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI
1010 1020 1030 1040 1050
DPLLKNCIGD FLKTLEDPDL NVRRVALVTF NSAAHNKPSL IRDLLDTVLP
1060 1070 1080 1090 1100
HLYNETKVRK ELIREVEMGP FKHTVDDGLD IRKAAFECMY TLLDSCLDRL
1110 1120 1130 1140 1150
DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ RLDRLVEPLR
1160 1170 1180 1190 1200
ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS
1210 1220 1230
QISSNPELAA IFESIQKDSS STNLESMDTS
Length:1,230
Mass (Da):136,376
Last modified:June 7, 2005 - v2
Checksum:iFE344558F72D79D8
GO
Isoform 2 (identifier: Q86VP6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     458-625: Missing.

Note: No experimental confirmation available.
Show »
Length:1,062
Mass (Da):117,889
Checksum:i2045EBFCEE84468B
GO
Isoform 3 (identifier: Q86VP6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.
     549-560: VIRPLDQPSSFD → AHHMPEAQWLRL
     561-1230: Missing.

Note: No experimental confirmation available.
Show »
Length:403
Mass (Da):45,539
Checksum:i4EC2B75A93D82663
GO

Sequence cautioni

The sequence BAA74852 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB55090 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti272R → K in BAB55365 (PubMed:14702039).Curated1
Sequence conflicti457M → I in BAB55090 (PubMed:14702039).Curated1
Sequence conflicti606S → P in AAF67492 (PubMed:10931946).Curated1
Sequence conflicti609P → S in AAF67492 (PubMed:10931946).Curated1
Sequence conflicti1047T → S in AAF67492 (PubMed:10931946).Curated1
Sequence conflicti1177M → T in BAB55090 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054041803V → A.Corresponds to variant rs12580996dbSNPEnsembl.1
Natural variantiVAR_025327952A → V.1 PublicationCorresponds to variant rs17854618dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0139471 – 157Missing in isoform 3. 1 PublicationAdd BLAST157
Alternative sequenceiVSP_013948458 – 625Missing in isoform 2. 1 PublicationAdd BLAST168
Alternative sequenceiVSP_013949549 – 560VIRPL…PSSFD → AHHMPEAQWLRL in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_013950561 – 1230Missing in isoform 3. 1 PublicationAdd BLAST670

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020636 mRNA. Translation: BAA74852.2. Different initiation.
AF157326 mRNA. Translation: AAF67492.1.
AL133560 mRNA. Translation: CAB63714.1.
AL136810 mRNA. Translation: CAB66744.1.
AL833880 mRNA. Translation: CAD38737.1.
CH471054 Genomic DNA. Translation: EAW97172.1.
BC004232 mRNA. Translation: AAH04232.1.
BC026220 mRNA. Translation: AAH26220.1.
BC050341 mRNA. Translation: AAH50341.1.
AK027404 mRNA. Translation: BAB55090.1. Different initiation.
AK027783 mRNA. Translation: BAB55365.1.
AK314358 mRNA. Translation: BAG36990.1.
CCDSiCCDS8977.1. [Q86VP6-1]
PIRiT43441.
RefSeqiNP_060918.2. NM_018448.4. [Q86VP6-1]
UniGeneiHs.546407.

Genome annotation databases

EnsembliENST00000545606; ENSP00000442318; ENSG00000111530. [Q86VP6-1]
GeneIDi55832.
KEGGihsa:55832.
UCSCiuc001stn.3. human. [Q86VP6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020636 mRNA. Translation: BAA74852.2. Different initiation.
AF157326 mRNA. Translation: AAF67492.1.
AL133560 mRNA. Translation: CAB63714.1.
AL136810 mRNA. Translation: CAB66744.1.
AL833880 mRNA. Translation: CAD38737.1.
CH471054 Genomic DNA. Translation: EAW97172.1.
BC004232 mRNA. Translation: AAH04232.1.
BC026220 mRNA. Translation: AAH26220.1.
BC050341 mRNA. Translation: AAH50341.1.
AK027404 mRNA. Translation: BAB55090.1. Different initiation.
AK027783 mRNA. Translation: BAB55365.1.
AK314358 mRNA. Translation: BAG36990.1.
CCDSiCCDS8977.1. [Q86VP6-1]
PIRiT43441.
RefSeqiNP_060918.2. NM_018448.4. [Q86VP6-1]
UniGeneiHs.546407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U6GX-ray3.10C1-1230[»]
4A0CX-ray3.80A/B1-1230[»]
ProteinModelPortaliQ86VP6.
SMRiQ86VP6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120937. 699 interactors.
DIPiDIP-31608N.
IntActiQ86VP6. 29 interactors.
MINTiMINT-4999459.
STRINGi9606.ENSP00000299218.

PTM databases

iPTMnetiQ86VP6.
PhosphoSitePlusiQ86VP6.
SwissPalmiQ86VP6.

Polymorphism and mutation databases

BioMutaiCAND1.
DMDMi67460541.

Proteomic databases

EPDiQ86VP6.
MaxQBiQ86VP6.
PaxDbiQ86VP6.
PeptideAtlasiQ86VP6.
PRIDEiQ86VP6.

Protocols and materials databases

DNASUi55832.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000545606; ENSP00000442318; ENSG00000111530. [Q86VP6-1]
GeneIDi55832.
KEGGihsa:55832.
UCSCiuc001stn.3. human. [Q86VP6-1]

Organism-specific databases

CTDi55832.
DisGeNETi55832.
GeneCardsiCAND1.
HGNCiHGNC:30688. CAND1.
HPAiHPA055748.
HPA062833.
HPA069053.
MIMi607727. gene.
neXtProtiNX_Q86VP6.
OpenTargetsiENSG00000111530.
PharmGKBiPA142672207.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1824. Eukaryota.
ENOG410XPK4. LUCA.
GeneTreeiENSGT00390000017740.
HOVERGENiHBG053467.
InParanoidiQ86VP6.
KOiK17263.
OMAiTRPAQSW.
OrthoDBiEOG091G017Q.
PhylomeDBiQ86VP6.
TreeFamiTF300355.

Enzyme and pathway databases

ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiCAND1. human.
EvolutionaryTraceiQ86VP6.
GeneWikiiCAND1.
GenomeRNAii55832.
PROiQ86VP6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111530.
ExpressionAtlasiQ86VP6. baseline and differential.
GenevisibleiQ86VP6. HS.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013932. TATA-bd_TIP120.
[Graphical view]
PfamiPF08623. TIP120. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCAND1_HUMAN
AccessioniPrimary (citable) accession number: Q86VP6
Secondary accession number(s): B2RAU3
, O94918, Q6PIY4, Q8NDJ4, Q96JZ9, Q96T19, Q9BTC4, Q9H0G2, Q9P0H7, Q9UF85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 143 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

Miscellaneous

A model has been proposed to explain the mechanisms of cullin-RING E3 ubiquitin ligase complexes assembly. According to this hypothesis, cullin-RING E3 ubiquitin ligase complexes exist in a 'stable' active state when saturated with substrate, occluding access to deneddylation by the COP9 signalosome (CSN) complex. The neddylation-conjugated cullin-RING E3 ubiquitin ligase complexes mediate ubiquitination of substrates and can recruit downstream factors involved in substrate degradation. Depletion of the substrate promotes the ability of CSN to bind the cullin-RING E3 ubiquitin ligase complex and mediate deneddylation. In this 'intermediate' deneddylated state, the complex can bind CAND1 and enter the 'exchange' state, resulting in high increase in dissociation rate of the substrate-recognition subunit. The resulting CAND1-cullin-RING complex rapidly assembles with another available substrate-recognition subunit to form an unstable ternary intermediate and yield a new cullin-RING E3 ubiquitin ligase complex. Subsequent neddylation of the cullin, which is stabilized by substrate, completes the cycle (PubMed:23453757).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.