CBLC

Protein-coding gene in the species Homo sapiens
CBLC
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3OP0, 3VRN, 3VRO, 3VRP, 3VRQ, 3VRR

Identifiers
AliasesCBLC, CBL-3, CBL-SL, RNF57, Cbl proto-oncogene C
External IDsOMIM: 608453; MGI: 1931457; HomoloGene: 8108; GeneCards: CBLC; OMA:CBLC - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for CBLC
Genomic location for CBLC
Band19q13.32Start44,777,869 bp[1]
End44,800,652 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for CBLC
Genomic location for CBLC
Band7|7 A3Start19,512,806 bp[2]
End19,530,734 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • skin of abdomen

  • skin of leg

  • duodenum

  • right lobe of liver

  • body of pancreas

  • jejunal mucosa

  • rectum

  • olfactory zone of nasal mucosa

  • minor salivary glands
Top expressed in
  • duodenum

  • intestinal villus

  • right kidney

  • epithelium of stomach

  • jejunum

  • lip

  • proximal tubule

  • colon

  • esophagus

  • lumbar spinal ganglion
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • SH3 domain binding
  • phosphotyrosine residue binding
  • calcium ion binding
  • epidermal growth factor receptor binding
  • ubiquitin protein ligase activity
  • metal ion binding
  • ubiquitin-protein transferase activity
  • transferase activity
  • receptor tyrosine kinase binding
  • zinc ion binding
  • protein binding
Cellular component
  • plasma membrane
  • membrane raft
Biological process
  • negative regulation of epidermal growth factor-activated receptor activity
  • cell surface receptor signaling pathway
  • negative regulation of epidermal growth factor receptor signaling pathway
  • negative regulation of MAP kinase activity
  • protein ubiquitination
  • regulation of signaling
  • ubiquitin-dependent protein catabolic process
  • signal transduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23624

80794

Ensembl

ENSG00000142273

ENSMUSG00000040525

UniProt

Q9ULV8

Q80XL1

RefSeq (mRNA)

NM_001130852
NM_012116

NM_001161844
NM_023224

RefSeq (protein)

NP_001124324
NP_036248

NP_001155316
NP_075713

Location (UCSC)Chr 19: 44.78 – 44.8 MbChr 7: 19.51 – 19.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Signal transduction protein CBL-C is a protein that in humans is encoded by the CBLC gene.[5][6][7]

CBL proteins, such as CBLC, are phosphorylated upon activation of a variety of receptors that signal via protein tyrosine kinases. Through interactions with proteins containing SRC (MIM 190090) homology-2 (SH2) and SH3 domains, CBL proteins modulate downstream cell signaling (Keane et al., 1999).[supplied by OMIM][7]

Interactions

CBLC has been shown to interact with FYN[8] and Epidermal growth factor receptor.[6][9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142273 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040525 – 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. ^ Keane MM, Ettenberg SA, Nau MM, Banerjee P, Cuello M, Penninger J, Lipkowitz S (Jun 1999). "cbl-3: a new mammalian cbl family protein". Oncogene. 18 (22): 3365–75. doi:10.1038/sj.onc.1202753. PMID 10362357. S2CID 28195948.
  6. ^ a b Kim M, Tezuka T, Suziki Y, Sugano S, Hirai M, Yamamoto T (Dec 1999). "Molecular cloning and characterization of a novel cbl-family gene, cbl-c". Gene. 239 (1): 145–54. doi:10.1016/S0378-1119(99)00356-X. PMID 10571044.
  7. ^ a b "Entrez Gene: CBLC Cas-Br-M (murine) ecotropic retroviral transforming sequence c".
  8. ^ Kim M, Tezuka T, Suziki Y, Sugano S, Hirai M, Yamamoto T (Oct 1999). "Molecular cloning and characterization of a novel cbl-family gene, cbl-c". Gene. 239 (1). NETHERLANDS: 145–54. doi:10.1016/S0378-1119(99)00356-X. ISSN 0378-1119. PMID 10571044.
  9. ^ Keane MM, Ettenberg S A, Nau M M, Banerjee P, Cuello M, Penninger J, Lipkowitz S (Jun 1999). "cbl-3: a new mammalian cbl family protein". Oncogene. 18 (22). ENGLAND: 3365–75. doi:10.1038/sj.onc.1202753. ISSN 0950-9232. PMID 10362357. S2CID 28195948.

External links

Further reading

  • Ollendorff V, Mattei M, Fournier E, et al. (1999). "A third human CBL gene is on chromosome 19". Int. J. Oncol. 13 (6): 1159–61. doi:10.3892/ijo.13.6.1159. PMID 9824625.
  • Irby RB, Mao W, Coppola D, et al. (1999). "Activating SRC mutation in a subset of advanced human colon cancers". Nat. Genet. 21 (2): 187–90. doi:10.1038/5971. PMID 9988270. S2CID 27129630.
  • Ettenberg SA, Keane MM, Nau MM, et al. (1999). "Cbl-b inhibits epidermal growth factor receptor signaling". Oncogene. 18 (10): 1855–66. doi:10.1038/sj.onc.1202499. PMID 10086340.
  • Loreto MP, Berry DM, McGlade CJ (2002). "Functional Cooperation between c-Cbl and Src-Like Adaptor Protein 2 in the Negative Regulation of T-Cell Receptor Signaling". Mol. Cell. Biol. 22 (12): 4241–55. doi:10.1128/MCB.22.12.4241-4255.2002. PMC 133880. PMID 12024036.
  • Szymkiewicz I, Kowanetz K, Soubeyran P, et al. (2002). "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases". J. Biol. Chem. 277 (42): 39666–72. doi:10.1074/jbc.M205535200. PMID 12177062.
  • Courbard JR, Fiore F, Adélaïde J, et al. (2003). "Interaction between two ubiquitin-protein isopeptide ligases of different classes, CBLC and AIP4/ITCH". J. Biol. Chem. 277 (47): 45267–75. doi:10.1074/jbc.M206460200. PMID 12226085.
  • Wong ES, Fong CW, Lim J, et al. (2002). "Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling". EMBO J. 21 (18): 4796–808. doi:10.1093/emboj/cdf493. PMC 126289. PMID 12234920.
  • Taher TE, Tjin EP, Beuling EA, et al. (2002). "C-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination". J. Immunol. 169 (7): 3793–800. doi:10.4049/jimmunol.169.7.3793. PMID 12244174.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Nau MM, Lipkowitz S (2003). "Comparative genomic organization of the cbl genes". Gene. 308: 103–13. doi:10.1016/S0378-1119(03)00471-2. PMID 12711395.
  • Kim M, Tezuka T, Tanaka K, Yamamoto T (2004). "Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation". Oncogene. 23 (9): 1645–55. doi:10.1038/sj.onc.1207298. PMID 14661060. S2CID 24925646.
  • Kassenbrock CK, Anderson SM (2004). "Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations". J. Biol. Chem. 279 (27): 28017–27. doi:10.1074/jbc.M404114200. PMID 15117950.
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.


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