CAND1

CAND1

Identifiers

CAND1, TIP120, TIP120A, cullin associated and neddylation dissociated 1

External IDs

OMIM: 607727; MGI: 1261820; GeneCards: CAND1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1U6G, 4A0C

Gene location (Human)

Chr.	Chromosome 12 (human)

Band	12q14.3-q15	Start	67,269,358 bp
Band	12q14.3-q15	End	67,319,953 bp

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)

Band	10 D2\|10 67.08 cM	Start	119,035,160 bp
Band	10 D2\|10 67.08 cM	End	119,075,960 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

ventricular zone

ganglionic eminence

stromal cell of endometrium

Achilles tendon

islet of Langerhans

endothelial cell

appendix

left ovary

right ovary

parietal pleura

Top expressed in

spermatocyte

spermatid

tail of embryo

somite

mandibular prominence

maxillary prominence

Gonadal ridge

epiblast

cumulus cell

morula

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

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


55832


71902


ENSG00000111530


ENSMUSG00000020114


Q86VP6


Q6ZQ38

RefSeq (mRNA)


NM_001329674 NM_001329675 NM_001329676 NM_018448


NM_027994

RefSeq (protein)


NP_001316603 NP_001316604 NP_001316605 NP_060918


NP_082270

Location (UCSC)

Chr 12: 67.27 – 67.32 Mb

Chr 10: 119.04 – 119.08 Mb

PubMed search

View/Edit Human

View/Edit Mouse

Cullin-associated NEDD8-dissociated protein 1 is a protein that in humans is encoded by the CAND1 gene.

Interactions

CAND1 has been shown to interact with:

CUL1,
CUL2,
CUL3,
CUL4A,
CUL4B,
DCUN1D1, and
RBX1.

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.

Further reading

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.

v t e PDB gallery
1u6g: Crystal Structure of The Cand1-Cul1-Roc1 Complex

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