Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (ASAP1)
The protein contains 1129 amino acids for an estimated molecular weight of 125498 Da.
Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Plays a role in ciliogenesis. (updated: April 1, 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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
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| Variant | Description |
|---|---|
| dbSNP:rs966185 |
Biological Process
Cilium assembly
Negative regulation of dendritic spine development
Organelle organization
Positive regulation of membrane tubulation
Positive regulation of podosome assembly
Cellular Component
Cell projection membrane
Cytosol
Dendritic spine
Membrane
Plasma membrane
Podosome
The reference OMIM entry for this protein is 605953
Development- and differentiation-enhancing factor 1; ddef1
Adp-ribosylation factor-directed gtpase-activating protein
Arf gtpase-activating protein 1; asap1
CLONING
Membrane trafficking is regulated in part by small GTP-binding proteins of the ADP-ribosylation factor (ARF) family (see 600464). ARF function depends on the controlled exchange and hydrolysis of GTP. Brown et al. (1998) purified a 130-kD phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent ARF GTPase-associated protein (GAP), termed ASAP1, from bovine brain. Using peptide sequences, the authors cloned the corresponding mouse gene. They found 2 alternatively spliced forms of the cDNA, termed ASAP1a and ASAP1b, encoding 1,147-amino acid and 1,090-amino acid polypeptides, respectively. The protein sequence contains a pleckstrin homology (PH) domain, a zinc finger motif, 3 ankyrin repeats, a proline-rich region containing several SH3 ligand motifs, and an SH3 domain. Northern blot analysis of mouse tissues revealed expression in a variety of tissues. Western blot analysis detected crossreacting proteins, suggesting that ASAP1 is part of a gene family. Studies of the expressed ASAP1 protein showed that it has GAP activity on ARF1 (103180) and ARF5 (103188) substrates. ASAP1 binds to SH3 domains, including those of SRC (190090) and CRK (164762). Both isoforms of ASAP1 became tyrosine phosphorylated by active SRC.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DDEF1 gene to chromosome 8q24.1-q24.2 (TMAP WI-8901). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605953 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed