CAND1

Protein-coding gene in humans
CAND1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1U6G, 4A0C

Identifiers
AliasesCAND1, TIP120, TIP120A, cullin associated and neddylation dissociated 1
External IDsOMIM: 607727; MGI: 1261820; HomoloGene: 10202; GeneCards: CAND1; OMA:CAND1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for CAND1
Genomic location for CAND1
Band12q14.3-q15Start67,269,358 bp[1]
End67,319,953 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for CAND1
Genomic location for CAND1
Band10 D2|10 67.08 cMStart119,035,160 bp[2]
End119,075,960 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
BioGPS




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
SpeciesHumanMouse
Entrez

55832

71902

Ensembl

ENSG00000111530

ENSMUSG00000020114

UniProt

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 MbChr 10: 119.04 – 119.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000111530 – Ensembl, May 2017
  2. ^ a b c 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.
  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.
  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.
  7. ^ "Entrez Gene: CAND1 cullin-associated and neddylation-dissociated 1".
  8. ^ a b c d e f 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.
  9. ^ a b 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.
  10. ^ a b 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.

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
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  • 1u6g: Crystal Structure of The Cand1-Cul1-Roc1 Complex
    1u6g: Crystal Structure of The Cand1-Cul1-Roc1 Complex
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