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Q86VP6

- CAND1_HUMAN

UniProt

Q86VP6 - CAND1_HUMAN

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Protein
Cullin-associated NEDD8-dissociated protein 1
Gene
CAND1, KIAA0829, TIP120, TIP120A
Organism
Homo sapiens (Human)
Status
Reviewed - 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 - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

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

Keywords - Biological processi

Ubl conjugation pathway

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:30688. CAND1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Predominantly cytoplasmic.1 Publication

GO - Cellular componenti

  1. cullin-RING ubiquitin ligase complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. intracellular membrane-bounded organelle Source: HPA
  5. nucleus Source: UniProtKB
  6. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672207.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 12301229Cullin-associated NEDD8-dissociated protein 1
PRO_0000089293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei335 – 3351Phosphoserine1 Publication
Modified residuei971 – 9711N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ86VP6.
PaxDbiQ86VP6.
PRIDEiQ86VP6.

PTM databases

PhosphoSiteiQ86VP6.

Expressioni

Inductioni

Repressed by miR-148a.1 Publication

Gene expression databases

ArrayExpressiQ86VP6.
BgeeiQ86VP6.
GenevestigatoriQ86VP6.

Organism-specific databases

HPAiHPA055748.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL1Q1361619EBI-456077,EBI-359390
CUL2Q136173EBI-456077,EBI-456179
CUL3Q136182EBI-456077,EBI-456129
CUL4AQ136193EBI-456077,EBI-456106
CUL4BQ136203EBI-456077,EBI-456067

Protein-protein interaction databases

BioGridi120937. 674 interactions.
DIPiDIP-31608N.
IntActiQ86VP6. 15 interactions.
MINTiMINT-4999459.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 149
Helixi20 – 3314
Beta strandi35 – 373
Helixi45 – 5612
Helixi62 – 7615
Helixi81 – 9414
Beta strandi98 – 1003
Helixi101 – 11616
Helixi127 – 14216
Helixi148 – 16417
Turni170 – 1723
Helixi173 – 1808
Helixi181 – 1855
Helixi189 – 20214
Turni203 – 2053
Helixi214 – 22411
Helixi234 – 24411
Helixi247 – 2493
Helixi256 – 2649
Turni269 – 2713
Helixi272 – 28413
Helixi291 – 30111
Helixi348 – 36114
Helixi368 – 3725
Turni373 – 3753
Helixi376 – 3805
Beta strandi386 – 3883
Helixi389 – 40517
Helixi424 – 4318
Helixi434 – 4429
Helixi448 – 46417
Turni466 – 4694
Helixi470 – 4723
Helixi473 – 48311
Beta strandi487 – 4893
Helixi491 – 50616
Helixi510 – 5134
Helixi514 – 5174
Turni518 – 5203
Helixi521 – 5288
Helixi533 – 55018
Beta strandi553 – 5553
Helixi562 – 57615
Beta strandi579 – 5813
Helixi583 – 59917
Helixi601 – 6033
Helixi607 – 61812
Beta strandi621 – 6233
Helixi624 – 63512
Helixi645 – 65814
Helixi664 – 68017
Helixi687 – 6948
Helixi698 – 7003
Helixi706 – 71914
Helixi724 – 7296
Turni730 – 7345
Helixi735 – 7428
Helixi749 – 76315
Helixi772 – 7798
Turni781 – 7855
Helixi793 – 80917
Helixi815 – 8184
Turni819 – 8246
Turni826 – 8294
Helixi832 – 84817
Helixi856 – 8638
Helixi864 – 8663
Helixi870 – 88617
Helixi888 – 90013
Helixi903 – 9053
Helixi906 – 91813
Turni923 – 9253
Helixi926 – 93611
Helixi947 – 96014
Helixi963 – 9653
Helixi967 – 9704
Turni971 – 9733
Beta strandi974 – 9774
Helixi979 – 98810
Helixi990 – 9923
Helixi1001 – 10077
Turni1009 – 10146
Beta strandi1015 – 10195
Helixi1021 – 103616
Helixi1038 – 10403
Helixi1042 – 10443
Helixi1045 – 105410
Helixi1060 – 10623
Beta strandi1063 – 10686
Beta strandi1071 – 10766
Helixi1079 – 109416
Beta strandi1098 – 11003
Helixi1102 – 111110
Helixi1117 – 113216
Helixi1136 – 11394
Turni1140 – 11456
Helixi1146 – 11549
Helixi1163 – 118220
Beta strandi1190 – 11945
Helixi1200 – 12089

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U6GX-ray3.10C1-1230[»]
4A0CX-ray3.80A/B1-1230[»]
ProteinModelPortaliQ86VP6.

Miscellaneous databases

EvolutionaryTraceiQ86VP6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 3938HEAT 1
Add
BLAST
Repeati44 – 8138HEAT 2
Add
BLAST
Repeati83 – 11937HEAT 3
Add
BLAST
Repeati131 – 16535HEAT 4
Add
BLAST
Repeati171 – 20838HEAT 5
Add
BLAST
Repeati210 – 24738HEAT 6
Add
BLAST
Repeati248 – 28235HEAT 7
Add
BLAST
Repeati289 – 36678HEAT 8
Add
BLAST
Repeati370 – 40738HEAT 9
Add
BLAST
Repeati424 – 46744HEAT 10
Add
BLAST
Repeati471 – 51040HEAT 11
Add
BLAST
Repeati515 – 55238HEAT 12
Add
BLAST
Repeati563 – 60240HEAT 13
Add
BLAST
Repeati606 – 64338HEAT 14
Add
BLAST
Repeati646 – 68338HEAT 15
Add
BLAST
Repeati688 – 72538HEAT 16
Add
BLAST
Repeati729 – 76840HEAT 17
Add
BLAST
Repeati770 – 80839HEAT 18
Add
BLAST
Repeati809 – 84537HEAT 19
Add
BLAST
Repeati852 – 88938HEAT 20
Add
BLAST
Repeati890 – 92738HEAT 21
Add
BLAST
Repeati928 – 96033HEAT 22
Add
BLAST
Repeati961 – 99838HEAT 23
Add
BLAST
Repeati1002 – 103938HEAT 24
Add
BLAST
Repeati1043 – 109755HEAT 25
Add
BLAST
Repeati1099 – 113335HEAT 26
Add
BLAST
Repeati1140 – 118950HEAT 27
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi314 – 34431Asp-rich
Add
BLAST

Sequence similaritiesi

Belongs to the CAND family.
Contains 27 HEAT repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG278162.
HOVERGENiHBG053467.
InParanoidiQ86VP6.
KOiK17263.
OMAiTRPAQSW.
OrthoDBiEOG77HDCZ.
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. Align

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

MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV     50
KMILKLLEDK NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE 100
QLRDISSIGL KTVIGELPPA SSGSALAANV CKKITGRLTS AIAKQEDVSV 150
QLEALDIMAD MLSRQGGLLV NFHPSILTCL LPQLTSPRLA VRKRTIIALG 200
HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA ISRQAGHRIG 250
EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI 300
CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR 350
RAAAKCLDAV VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS 400
LLKQTRPVQS WLCDPDAMEQ GETPLTMLQS QVPNIVKALH KQMKEKSVKT 450
RQCCFNMLTE LVNVLPGALT QHIPVLVPGI IFSLNDKSSS SNLKIDALSC 500
LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL LVTQQLVKVI 550
RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL 600
GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE 650
GVPILASFLR KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL 700
ISESDMHVSQ MAISFLTTLA KVYPSSLSKI SGSILNELIG LVRSPLLQGG 750
ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT GPVYSQSTAL THKQSYYSIA 800
KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL SLGEVGHHID 850
LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT 900
SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV 950
VAECLGKLTL IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI 1000
DPLLKNCIGD FLKTLEDPDL NVRRVALVTF NSAAHNKPSL IRDLLDTVLP 1050
HLYNETKVRK ELIREVEMGP FKHTVDDGLD IRKAAFECMY TLLDSCLDRL 1100
DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ RLDRLVEPLR 1150
ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS 1200
QISSNPELAA IFESIQKDSS STNLESMDTS 1230
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 BAA74852.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAB55090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti803 – 8031V → A.
Corresponds to variant rs12580996 [ dbSNP | Ensembl ].
VAR_054041
Natural varianti952 – 9521A → V.1 Publication
Corresponds to variant rs17854618 [ dbSNP | Ensembl ].
VAR_025327

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 157157Missing in isoform 3.
VSP_013947Add
BLAST
Alternative sequencei458 – 625168Missing in isoform 2.
VSP_013948Add
BLAST
Alternative sequencei549 – 56012VIRPL…PSSFD → AHHMPEAQWLRL in isoform 3.
VSP_013949Add
BLAST
Alternative sequencei561 – 1230670Missing in isoform 3.
VSP_013950Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2721R → K in BAB55365. 1 Publication
Sequence conflicti457 – 4571M → I in BAB55090. 1 Publication
Sequence conflicti606 – 6061S → P in AAF67492. 1 Publication
Sequence conflicti609 – 6091P → S in AAF67492. 1 Publication
Sequence conflicti1047 – 10471T → S in AAF67492. 1 Publication
Sequence conflicti1177 – 11771M → T in BAB55090. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_018448.3. [Q86VP6-1]
UniGeneiHs.546407.

Genome annotation databases

EnsembliENST00000544619; ENSP00000444089; ENSG00000111530.
ENST00000545606; ENSP00000442318; ENSG00000111530. [Q86VP6-1]
GeneIDi55832.
KEGGihsa:55832.
UCSCiuc001stn.2. human. [Q86VP6-1]
uc001sto.2. human. [Q86VP6-2]

Polymorphism databases

DMDMi67460541.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8977.1. [Q86VP6-1 ]
PIRi T43441.
RefSeqi NP_060918.2. NM_018448.3. [Q86VP6-1 ]
UniGenei Hs.546407.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U6G X-ray 3.10 C 1-1230 [» ]
4A0C X-ray 3.80 A/B 1-1230 [» ]
ProteinModelPortali Q86VP6.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120937. 674 interactions.
DIPi DIP-31608N.
IntActi Q86VP6. 15 interactions.
MINTi MINT-4999459.

PTM databases

PhosphoSitei Q86VP6.

Polymorphism databases

DMDMi 67460541.

Proteomic databases

MaxQBi Q86VP6.
PaxDbi Q86VP6.
PRIDEi Q86VP6.

Protocols and materials databases

DNASUi 55832.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000544619 ; ENSP00000444089 ; ENSG00000111530 .
ENST00000545606 ; ENSP00000442318 ; ENSG00000111530 . [Q86VP6-1 ]
GeneIDi 55832.
KEGGi hsa:55832.
UCSCi uc001stn.2. human. [Q86VP6-1 ]
uc001sto.2. human. [Q86VP6-2 ]

Organism-specific databases

CTDi 55832.
GeneCardsi GC12P067663.
HGNCi HGNC:30688. CAND1.
HPAi HPA055748.
MIMi 607727. gene.
neXtProti NX_Q86VP6.
PharmGKBi PA142672207.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG278162.
HOVERGENi HBG053467.
InParanoidi Q86VP6.
KOi K17263.
OMAi TRPAQSW.
OrthoDBi EOG77HDCZ.
PhylomeDBi Q86VP6.
TreeFami TF300355.

Miscellaneous databases

ChiTaRSi CAND1. human.
EvolutionaryTracei Q86VP6.
GeneWikii CAND1.
GenomeRNAii 55832.
NextBioi 61049.
PROi Q86VP6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86VP6.
Bgeei Q86VP6.
Genevestigatori Q86VP6.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013932. TATA-bd_TIP120.
[Graphical view ]
Pfami PF08623. TIP120. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANT VAL-952.
    Tissue: Cervix, Testis and Uterus.
  7. "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] (ISOFORMS 1 AND 3).
    Tissue: Placenta.
  8. Bienvenut W.V., Ramsay A., Leung H.Y.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  9. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14; 535-548; 668-679; 730-743; 859-873; 958-969 AND 983-990, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  10. "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex."
    Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.
    Mol. Cell 10:1519-1526(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1.
  11. "NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases."
    Liu J., Furukawa M., Matsumoto T., Xiong Y.
    Mol. Cell 10:1511-1518(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, INTERACTION WITH UNNEDDYLATED CUL1; CUL4A AND CUL5.
  12. "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: FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "CAND1-mediated substrate adaptor recycling is required for efficient repression of Nrf2 by Keap1."
    Lo S.C., Hannink M.
    Mol. Cell. Biol. 26:1235-1244(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL3.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression."
    Murata T., Takayama K., Katayama S., Urano T., Horie-Inoue K., Ikeda K., Takahashi S., Kawazu C., Hasegawa A., Ouchi Y., Homma Y., Hayashizaki Y., Inoue S.
    Prostate Cancer Prostatic Dis. 13:356-361(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding."
    Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N., Burstein E.
    J. Biol. Chem. 286:32355-32365(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL2.
  21. "Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo."
    Chua Y.S., Boh B.K., Ponyeam W., Hagen T.
    PLoS ONE 6:E16071-E16071(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, SUBCELLULAR LOCATION.
  22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins."
    Pierce N.W., Lee J.E., Liu X., Sweredoski M.J., Graham R.L., Larimore E.A., Rome M., Zheng N., Clurman B.E., Hess S., Shan S.O., Deshaies R.J.
    Cell 153:206-215(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REACTION MECHANISM.
  25. "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases."
    Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., Zheng N.
    Cell 119:517-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1.
  26. "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation."
    Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., Sugasawa K., Thoma N.H.
    Cell 147:1024-1039(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1.

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: September 3, 2014
This is version 117 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 (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

External Data

Dasty 3

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