CAND1

CAND1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1U6G, 4A0C
Identifiers
Aliases	CAND1 , TIP120, TIP120A, cullin associated and neddylation dissociated 1
External IDs	OMIM: 607727 MGI: 1261820 HomoloGene: 10202 GeneCards: CAND1
Gene location (Human)
Chr.	Chromosome 12 (human)
End	67,319,953 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	119,075,960 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; stromal cell of endometrium; ; Achilles tendon; ; islet of Langerhans; ; endothelial cell; ; appendix; ; parietal pleura; ; germinal epithelium; ; thymus; ; body of pancreas;
	Top expressed in
	spermatocyte; ; spermatid; ; somite; ; maxillary prominence; ; cumulus cell; ; morula; ; primitive streak; ; abdominal wall; ; seminiferous tubule; ; supraoptic nucleus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	TBP-class protein binding ; protein binding ;
Cellular component	cytoplasm ; cullin-RING ubiquitin ligase complex ; Golgi apparatus ; extracellular exosome ; membrane ; nucleus ; ubiquitin ligase complex ; extracellular region ; secretory granule lumen ; ficolin-1-rich granule lumen ; nucleoplasm ; cytosol ;
Biological process	positive regulation of transcription, DNA-templated ; SCF complex assembly ; cell differentiation ; positive regulation of RNA polymerase II transcription preinitiation complex assembly ; negative regulation of catalytic activity ; protein ubiquitination ; neutrophil degranulation ; cellular iron ion homeostasis ; post-translational protein modification ;
	Sources:Amigo / QuickGO
Orthologs
	55832
	71902
	ENSG00000111530
	ENSMUSG00000020114
	Q86VP6
	Q6ZQ38
	NM_001329674 ; NM_001329675 ; NM_001329676 ; NM_018448
	NM_027994
	NP_001316603 ; NP_001316604 ; NP_001316605 ; NP_060918
	NP_082270
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 03, 2023

Cullin-associated NEDD8-dissociated protein 1 is a protein that in humans is encoded by the CAND1 gene.^[5]^[6]^[7]

Interactions

CAND1 has been shown to interact with:

Related Research Articles

Cullin 1, also known as CUL1, is a human protein and gene from cullin family. This protein plays an important role in protein degradation and protein ubiquitination.

NEDD8 is a protein that in humans is encoded by the NEDD8 gene. This ubiquitin-like (UBL) protein becomes covalently conjugated to a limited number of cellular proteins, in a process called NEDDylation similar to ubiquitination. Human NEDD8 shares 60% amino acid sequence identity to ubiquitin. The primary known substrates of NEDD8 modification are the cullin subunits of cullin-based E3 ubiquitin ligases, which are active only when NEDDylated. Their NEDDylation is critical for the recruitment of E2 to the ligase complex, thus facilitating ubiquitin conjugation. NEDD8 modification has therefore been implicated in cell cycle progression and cytoskeletal regulation.

RING-box protein 1 is a protein that in humans is encoded by the RBX1 gene.

Cullin-4A is a protein that in humans is encoded by the CUL4A gene. CUL4A belongs to the cullin family of ubiquitin ligase proteins and is highly homologous to the CUL4B protein. CUL4A regulates numerous key processes such as DNA repair, chromatin remodeling, spermatogenesis, haematopoiesis and the mitotic cell cycle. As a result, CUL4A has been implicated in several cancers and the pathogenesis of certain viruses including HIV. A component of a CUL4A complex, Cereblon, was discovered to be a major target of the teratogenic agent thalidomide.

F-box/WD repeat-containing protein 1A (FBXW1A) also known as βTrCP1 or Fbxw1 or hsSlimb or pIkappaBalpha-E3 receptor subunit is a protein that in humans is encoded by the BTRC gene.

Cullin-5 is a protein that in humans is encoded by the CUL5 gene.

COP9 signalosome complex subunit 2 is a protein that in humans is encoded by the COPS2 gene. It encodes a subunit of the COP9 signalosome.

Cullin-2 is a protein that in humans is encoded by the CUL2 gene.

Cullin-4B is a protein that in humans is encoded by the CUL4B gene which is located on the X chromosome. CUL4B has high sequence similarity with CUL4A, with which it shares certain E3 ubiquitin ligase functions. CUL4B is largely expressed in the nucleus and regulates several key functions including: cell cycle progression, chromatin remodeling and neurological and placental development in mice. In humans, CUL4B has been implicated in X-linked intellectual disability and is frequently mutated in pancreatic adenocarcinomas and a small percentage of various lung cancers. Viruses such as HIV can also co-opt CUL4B-based complexes to promote viral pathogenesis. CUL4B complexes containing Cereblon are also targeted by the teratogenic drug thalidomide.

Cullin 3 is a protein that in humans is encoded by the CUL3 gene.

RING-box protein 2 is a protein that in humans is encoded by the RNF7 gene.

COP9 signalosome complex subunit 8 is a protein that in humans is encoded by the COPS8 gene.

Ubiquitin/ISG15-conjugating enzyme E2 L6 is a protein that in humans is encoded by the UBE2L6 gene.

The human gene UBR1 encodes the enzyme ubiquitin-protein ligase E3 component n-recognin 1.

COP9 signalosome complex subunit 7a is a protein that in humans is encoded by the COPS7A gene.

βTrCP2 is a protein that in humans is encoded by the FBXW11 gene.

E3 ubiquitin-protein ligase RNF19A is an enzyme that in humans is encoded by the RNF19A gene.

Sentrin-specific protease 8 is an enzyme that in humans is encoded by the SENP8 gene.

Cullins are a family of hydrophobic scaffold proteins which provide support for ubiquitin ligases (E3). All eukaryotes appear to have cullins. They combine with RING proteins to form Cullin-RING ubiquitin ligases (CRLs) that are highly diverse and play a role in myriad cellular processes, most notably protein degradation by ubiquitination.

S-phase kinase-associated protein 1 is an enzyme that in humans is encoded by the SKP1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000111530 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020114 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "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". DNA Research. 5 (6): 355–64. doi: 10.1093/dnares/5.6.355 . PMID 10048485.
↑ Yogosawa S, Makino Y, Yoshida T, Kishimoto T, Muramatsu M, Tamura T (Dec 1996). "Molecular cloning of a novel 120-kDa TBP-interacting protein". Biochemical and Biophysical Research Communications. 229 (2): 612–7. doi:10.1006/bbrc.1996.1852. PMID 8954946.
↑ "Entrez Gene: CAND1 cullin-associated and neddylation-dissociated 1".
1 2 3 4 5 6 Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi: 10.1074/jbc.M213070200 . PMID 12609982.
1 2 Menon S, Tsuge T, Dohmae N, Takio K, Wei N (2008). "Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome". BMC Biochemistry. 9: 1. doi: 10.1186/1471-2091-9-1 . PMC 2265268 . PMID 18173839.
1 2 Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". The Journal of Biological Chemistry. 283 (48): 33211–20. doi: 10.1074/jbc.M804440200 . PMC 2586271 . PMID 18826954.

External links

Human CAND1 genome location and CAND1 gene details page in the UCSC Genome Browser .

Yogosawa S, Kayukawa K, Kawata T, Makino Y, Inoue S, Okuda A, Muramatsu M, Tamura T (Dec 1999). "Induced expression, localization, and chromosome mapping of a gene for the TBP-interacting protein 120A". Biochemical and Biophysical Research Communications. 266 (1): 123–8. doi:10.1006/bbrc.1999.1773. PMID 10581176.
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (Aug 2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi: 10.1073/pnas.160270997 . PMC 16901 . PMID 10931946.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072 . PMID 11230166.
Liu J, Furukawa M, Matsumoto T, Xiong Y (Dec 2002). "NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases". Molecular Cell. 10 (6): 1511–8. doi: 10.1016/S1097-2765(02)00783-9 . PMID 12504025. S2CID 28959307.
Zheng J, Yang X, Harrell JM, Ryzhikov S, Shim EH, Lykke-Andersen K, Wei N, Sun H, Kobayashi R, Zhang H (Dec 2002). "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex". Molecular Cell. 10 (6): 1519–26. doi: 10.1016/S1097-2765(02)00784-0 . PMID 12504026.
Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi: 10.1074/jbc.M213070200 . PMID 12609982.
Feng S, Shen Y, Sullivan JA, Rubio V, Xiong Y, Sun TP, Deng XW (Jul 2004). "Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein Degradation". The Plant Cell. 16 (7): 1870–82. doi:10.1105/tpc.021949. PMC 514167 . PMID 15208391.
Goldenberg SJ, Cascio TC, Shumway SD, Garbutt KC, Liu J, Xiong Y, Zheng N (Nov 2004). "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases". Cell. 119 (4): 517–28. doi: 10.1016/j.cell.2004.10.019 . PMID 15537541. S2CID 1606360.
Min KW, Kwon MJ, Park HS, Park Y, Yoon SK, Yoon JB (Sep 2005). "CAND1 enhances deneddylation of CUL1 by COP9 signalosome". Biochemical and Biophysical Research Communications. 334 (3): 867–74. doi:10.1016/j.bbrc.2005.06.188. PMID 16036220.
Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Research. 12 (2): 117–26. doi: 10.1093/dnares/12.2.117 . PMID 16303743.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000111530 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020114 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10048485-5] Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "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". DNA Research. 5 (6): 355–64. doi: 10.1093/dnares/5.6.355 . PMID 10048485.

[pmid8954946-6] Yogosawa S, Makino Y, Yoshida T, Kishimoto T, Muramatsu M, Tamura T (Dec 1996). "Molecular cloning of a novel 120-kDa TBP-interacting protein". Biochemical and Biophysical Research Communications. 229 (2): 612–7. doi:10.1006/bbrc.1996.1852. PMID 8954946.

[entrez-7] "Entrez Gene: CAND1 cullin-associated and neddylation-dissociated 1".

[pmid12609982-8] 1 2 3 4 5 6 Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi: 10.1074/jbc.M213070200 . PMID 12609982.

[pmid18173839-9] 1 2 Menon S, Tsuge T, Dohmae N, Takio K, Wei N (2008). "Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome". BMC Biochemistry. 9: 1. doi: 10.1186/1471-2091-9-1 . PMC 2265268 . PMID 18173839.

[pmid18826954-10] 1 2 Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". The Journal of Biological Chemistry. 283 (48): 33211–20. doi: 10.1074/jbc.M804440200 . PMC 2586271 . PMID 18826954.

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CAND1

Contents

Interactions

Related Research Articles

References

External links

Further reading