Sorbin and SH3 domain-containing protein 1 (SORBS1)
The protein contains 1292 amino acids for an estimated molecular weight of 142513 Da.
Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity). (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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Biological Process
Cell-matrix adhesion
Cellular response to insulin stimulus
Focal adhesion assembly
Glucose transport
Insulin receptor signaling pathway
Muscle contraction
Obsolete positive regulation of glucose import in response to insulin stimulus
Positive regulation of establishment of protein localization to plasma membrane
Positive regulation of glucose import
Positive regulation of glycogen biosynthetic process
Positive regulation of insulin receptor signaling pathway
Positive regulation of lipid biosynthetic process
Positive regulation of protein localization to plasma membrane
Positive regulation of signal transduction
Stress fiber assembly
The reference OMIM entry for this protein is 605264
Sorbin and sh3-domains containing protein 1; sorbs1
Sh3 domain protein 5; sh3d5
Cbl-associated protein; cap
Sh3 domain-containing protein 12; sh3p12
Ponsin
Sorb1
CLONING
The protein product of the CBL protooncogene (165360) is prominently tyrosine phosphorylated in response to insulin (176730) in 3T3-L1 adipocytes but not in 3T3-L1 fibroblasts. After insulin-dependent tyrosine phosphorylation, CBL specifically associates with endogenous CRK (164762) and FYN (137025). These results suggest a role for tyrosine-phosphorylated CBL in adipocyte activation by insulin. Ribon et al. (1998) used full-length CBL as a target protein to screen a fully differentiated 3T3-L1 adipocyte cDNA library using the yeast 2-hybrid system. They isolated cDNAs encompassing the entire coding region of Cap (CBL-associated protein) from a mouse embryo cDNA expression library by using a functional screen with a defined SH3 ligand peptide. The unique structure of Cap includes 3 adjacent Src homology-3 (SH3) domains in the C terminus and a region showing significant sequence similarity with the peptide hormone sorbin. Both Cap mRNA and proteins were expressed predominantly in 3T3-L1 adipocytes and not in 3T3-L1 fibroblasts. By Northern blot analysis of mouse tissues, Cap expression was detected in greatest abundance in heart, liver, skeletal muscle, and kidney; lesser amounts were detected in brain and lung, and expression in spleen and testis was not detected. Scott (2000) considered the mouse Cap protein to be the probable ortholog of human SH3P12 (GenBank GENBANK AF136380). Spinocerebellar ataxia-7 (SCA7; 164500) is a neurodegenerative disease caused by expansion of a CAG repeat in the coding region of the SCA7 gene. Ataxin-7, encoded by the SCA7 gene, is a protein expressed in many tissues, including the CNS. Lebre et al. (2001) used a 2-hybrid approach to screen a human retina cDNA library for ataxin-7-binding proteins and isolated R85, a splice variant of SH3P12. SH3P12 gene products were expressed in Purkinje cells in the cerebellum.GENE FUNCTION
Ribon et al. (1998) found that Cap associated with CBL in 3T3-L1 adipocytes independently of insulin stimulation in vivo and in vitro in an SH3 domain-mediated manner. Furthermore, Ribon et al. (1998) detected the association of Cap with insulin receptor (147670). Insulin stimulation resulted in the dissociation of Cap from the insulin receptor. Taken together, Ribon et al. (1998) concluded that CAP represents a novel CBL-binding protein in adipocytes likely to participate in insulin signaling. Insulin stimulates the transport of glucose into fat and muscle cells and initiates its actions by binding to its tyrosine kinase receptor, leading to the phosphorylation of intracellular substrates. One such substrate is the CBL protooncogene product. CBL is recruited to the insulin receptor by interaction with the adaptor protein CAP, through 1 of 3 adjacent SH3 domains in the C terminus of CAP. Upon phosphorylation of CBL, the CAP-CBL complex dissociates from the insulin receptor and moves to a caveolin (see 601047)-enriched triton-insoluble membrane fraction (Mastick et al., 1995). To identify a molecular mechanism underlying this subcellular redistribution, Baumann et al. (2000) screened a yeast 2-hybrid library using the N-terminal region of CAP and identified the caveolar protein flotillin (131560). Flotillin forms a ternary complex with CAP and CBL, directing the localization of the CAP-CBL complex to a lipid raft subdomain of the plasma membrane. Expression of the N-terminal domain of CAP in 3T3-L1 adipocytes blocks the stimulation of glucose transport by ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605264 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed