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HUMAN:CAND1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) CAND1 (synonyms: KIAA0829, TIP120, TIP120A)
Protein Name(s) Cullin-associated NEDD8-dissociated protein 1

Cullin-associated and neddylation-dissociated protein 1 TBP-interacting protein of 120 kDa A TBP-interacting protein 120A p120 CAND1

External Links
UniProt Q86VP6
EMBL AB020636
AF157326
AL133560
AL136810
AL833880
CH471054
BC004232
BC026220
BC050341
AK027404
AK027783
AK314358
CCDS CCDS8977.1
PIR T43441
RefSeq NP_060918.2
UniGene Hs.546407
PDB 1U6G
4A0C
PDBsum 1U6G
4A0C
ProteinModelPortal Q86VP6
BioGrid 120937
DIP DIP-31608N
IntAct Q86VP6
MINT MINT-4999459
PhosphoSite Q86VP6
DMDM 67460541
MaxQB Q86VP6
PaxDb Q86VP6
PRIDE Q86VP6
DNASU 55832
Ensembl ENST00000544619
ENST00000545606
GeneID 55832
KEGG hsa:55832
UCSC uc001stn.2
uc001sto.2
CTD 55832
GeneCards GC12P067663
HGNC HGNC:30688
HPA HPA055748
MIM 607727
neXtProt NX_Q86VP6
PharmGKB PA142672207
eggNOG NOG278162
GeneTree ENSGT00390000017740
HOVERGEN HBG053467
InParanoid Q86VP6
KO K17263
OMA TRPAQSW
OrthoDB EOG77HDCZ
PhylomeDB Q86VP6
TreeFam TF300355
ChiTaRS CAND1
EvolutionaryTrace Q86VP6
GeneWiki CAND1
GenomeRNAi 55832
NextBio 61049
PRO PR:Q86VP6
Proteomes UP000005640
Bgee Q86VP6
ExpressionAtlas Q86VP6
Genevestigator Q86VP6
GO GO:0031461
GO:0005737
GO:0070062
GO:0043231
GO:0016020
GO:0005634
GO:0000151
GO:0030154
GO:0043086
GO:0045899
GO:0016567
GO:0010265
Gene3D 1.25.10.10
InterPro IPR011989
IPR016024
IPR013932
Pfam PF08623
SUPFAM SSF48371

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0031396

regulation of protein ubiquitination

PMID:24130483[1]

ECO:0000316

UniProtKB:BZLF1_EBVB9 UniProtKB:EBNA1_EBVB9


P

Figure 5

complete
CACAO 9154

part_of

GO:0070062

extracellular exosome

PMID:23533145[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:19946888[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19056867[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001088)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:20458337[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0000639)

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21630459[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0000019)

Seeded From UniProt

complete

involved_in

GO:0043086

negative regulation of catalytic activity

PMID:12609982[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0031461

cullin-RING ubiquitin ligase complex

PMID:21249194[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0031461

cullin-RING ubiquitin ligase complex

PMID:15537541[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0030154

cell differentiation

PMID:10581176[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

PMID:21249194[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

PMID:15537541[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

PMID:12609982[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0010265

SCF complex assembly

PMID:21249194[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0010265

SCF complex assembly

PMID:15537541[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21249194[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21249194[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:10581176[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000151

ubiquitin ligase complex

PMID:12609982[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000294436
UniProtKB:Q86VP6

P

Seeded From UniProt

complete

involved_in

GO:0010265

SCF complex assembly

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000294436
UniProtKB:Q86VP6

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1914338
PANTHER:PTN000294436
RGD:620479
RGD:620480
UniProtKB:C8VP82
UniProtKB:Q5BAH2
UniProtKB:Q86VP6
WB:WBGene00013606

C

Seeded From UniProt

complete

part_of

GO:0031461

cullin-RING ubiquitin ligase complex

PMID:22405651[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045899

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P97536
ensembl:ENSRNOP00000010720

P

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P97536
ensembl:ENSRNOP00000010720

P

Seeded From UniProt

complete

enables

GO:0017025

TBP-class protein binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P97536
ensembl:ENSRNOP00000010720

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P97536
ensembl:ENSRNOP00000010720

C

Seeded From UniProt

complete

involved_in

GO:0010265

SCF complex assembly

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR039852

P

Seeded From UniProt

complete

part_of

GO:1904813

ficolin-1-rich granule lumen

Reactome:R-HSA-6800434

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0043687

post-translational protein modification

Reactome:R-HSA-597592

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043312

neutrophil degranulation

Reactome:R-HSA-6798695

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0034774

secretory granule lumen

Reactome:R-HSA-6798748

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

Reactome:R-HSA-917937

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-8955289
Reactome:R-HSA-8955241
Reactome:R-HSA-5691131

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-8955285
Reactome:R-HSA-8955245

ECO:0000304

author statement supported by traceable reference used in manual assertion


C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

Reactome:R-HSA-6800434
Reactome:R-HSA-6798748

ECO:0000304

author statement supported by traceable reference used in manual assertion


C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Gastaldello, S et al. (2013) Caspase-1 promotes Epstein-Barr virus replication by targeting the large tegument protein deneddylase to the nucleus of productively infected cells. PLoS Pathog. 9 e1003664 PubMed GONUTS page
  2. Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  3. Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
  4. Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
  5. Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
  6. de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
  7. 7.0 7.1 7.2 Min, KW et al. (2003) TIP120A associates with cullins and modulates ubiquitin ligase activity. J. Biol. Chem. 278 15905-10 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 8.4 Chua, YS et al. (2011) Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo. PLoS ONE 6 e16071 PubMed GONUTS page
  9. 9.0 9.1 9.2 Goldenberg, SJ et al. (2004) Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases. Cell 119 517-28 PubMed GONUTS page
  10. 10.0 10.1 Yogosawa, S et al. (1999) Induced expression, localization, and chromosome mapping of a gene for the TBP-interacting protein 120A. Biochem. Biophys. Res. Commun. 266 123-8 PubMed GONUTS page
  11. 11.0 11.1 11.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  12. Tron, AE et al. (2012) The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. Mol. Cell 46 67-78 PubMed GONUTS page