RBCK1

RBCK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CRC, 2LGY, 4DBG
Identifiers
Aliases	RBCK1, C20orf18, HOIL-1, HOIL1, PBMEI, RBCK2, RNF54, UBCE7IP3, XAP3, XAP4, ZRANB4, PGBM1, RANBP2-type and C3HC4-type zinc finger containing 1
External IDs	OMIM: 610924; MGI: 1344372; HomoloGene: 32448; GeneCards: RBCK1; OMA:RBCK1 - orthologs
Gene location (Human) Chr. Chromosome 20 (human) Band 20p13 Start 407,498 bp End 432,139 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 G3 Start 152,158,254 bp End 152,174,573 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum anterior pituitary right uterine tube right lobe of liver granulocyte right adrenal gland left adrenal cortex right adrenal cortex right lobe of thyroid gland mucosa of transverse colon Top expressed in neural layer of retina superior frontal gyrus ankle joint thymus lip dentate gyrus of hippocampal formation granule cell primary visual cortex granulocyte mesenteric lymph nodes genital tubercle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity metal ion binding ubiquitin binding protein binding ubiquitin-protein transferase activity transferase activity identical protein binding Cellular component cytosol LUBAC complex Biological process negative regulation of necroptotic process regulation of tumor necrosis factor-mediated signaling pathway positive regulation of NF-kappaB transcription factor activity positive regulation of apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of extrinsic apoptotic signaling pathway viral process I-kappaB kinase/NF-kappaB signaling negative regulation of NF-kappaB transcription factor activity T cell receptor signaling pathway protein linear polyubiquitination proteasome-mediated ubiquitin-dependent protein catabolic process protein polyubiquitination positive regulation of NIK/NF-kappaB signaling regulation of transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10616 24105 Ensembl ENSG00000125826 ENSMUSG00000027466 UniProt Q9BYM8 Q9WUB0 RefSeq (mRNA) NM_006462 NM_031227 NM_031228 NM_031229 NM_001323956 NM_001323958 NM_001323960 NM_001083921 NM_019705 NM_001355282 RefSeq (protein) NP_001310885 NP_001310887 NP_001310889 NP_006453 NP_112506 NP_001077390 NP_062679 NP_001342211 Location (UCSC) Chr 20: 0.41 – 0.43 Mb Chr 2: 152.16 – 152.17 Mb PubMed search
Wikidata
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RanBP-type and C3HC4-type zinc finger-containing protein 1 is a protein that in humans is encoded by the RBCK1 gene.

The protein encoded by this gene is similar to mouse UIP28/UbcM4 interacting protein. Alternative splicing has been observed at this locus, resulting in distinct isoforms.

Clinical significance

A family quartet was found with two children, both affected with a previously unreported disease, characterized by progressive muscular weakness and cardiomyopathy, with normal intelligence. During the course of the study, one additional unrelated patient was found with a comparable phenotype. From whole-genome sequence data, RBCK1, a gene encoding an E3 ubiquitin-protein ligase, was identified as the most likely candidate gene, with two protein-truncating mutations in probands in the first family. Sanger sequencing identified a private homozygous splice variant in RBCK1 in the proband in the second family, yet SNP genotyping revealed a 1.2Mb copy-neutral region of homozygosity covering RBCK1. RNA-Seq confirmed aberrant splicing of RBCK1 transcripts, resulting in truncated protein products. Ten other individuals with mutations in RBCK1 and overlapping phenotypes have been identified.

Further reading

• Martinez-Noel G, Niedenthal R, Tamura T, Harbers K (Jul 1999). "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4". FEBS Letters. 454 (3): 257–61. doi:10.1016/S0014-5793(99)00823-6. PMID 10431818.
• Yamanaka K, Ishikawa H, Megumi Y, Tokunaga F, Kanie M, Rouault TA, Morishima I, Minato N, Ishimori K, Iwai K (Apr 2003). "Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2". Nature Cell Biology. 5 (4): 336–40. doi:10.1038/ncb952. PMID 12629548.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biology. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Tatematsu K, Yoshimoto N, Koyanagi T, Tokunaga C, Tachibana T, Yoneda Y, Yoshida M, Okajima T, Tanizawa K, Kuroda S (Jun 2005). "Nuclear-cytoplasmic shuttling of a RING-IBR protein RBCK1 and its functional interaction with nuclear body proteins". The Journal of Biological Chemistry. 280 (24): 22937–44. doi:10.1074/jbc.M413476200. PMID 15833741.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM (Sep 2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Molecular & Cellular Proteomics. 4 (9): 1240–50. doi:10.1074/mcp.M500089-MCP200. PMID 15951569.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Yoshimoto N, Tatematsu K, Koyanagi T, Okajima T, Tanizawa K, Kuroda S (Sep 2005). "Cytoplasmic tethering of a RING protein RBCK1 by its splice variant lacking the RING domain". Biochemical and Biophysical Research Communications. 335 (2): 550–7. doi:10.1016/j.bbrc.2005.07.104. PMID 16083853.
• Bayle J, Lopez S, Iwaï K, Dubreuil P, De Sepulveda P (May 2006). "The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins". FEBS Letters. 580 (11): 2609–14. doi:10.1016/j.febslet.2006.03.093. PMID 16643902.
• Tian Y, Zhang Y, Zhong B, Wang YY, Diao FC, Wang RP, Zhang M, Chen DY, Zhai ZH, Shu HB (Jun 2007). "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation". The Journal of Biological Chemistry. 282 (23): 16776–82. doi:10.1074/jbc.M701913200. PMID 17449468.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Wang K, Kim C, Bradfield J, Guo Y, Toskala E, Otieno FG, Hou C, Thomas K, Cardinale C, Lyon GJ, Golhar R, Hakonarson H (2013). "Whole-genome DNA/RNA sequencing identifies truncating mutations in RBCK1 in a novel Mendelian disease with neuromuscular and cardiac involvement". Genome Medicine. 5 (7): 67. doi:10.1186/gm471. PMC 3971341. PMID 23889995.{{cite journal}}: CS1 maint: unflagged free DOI (link)