AP-1 complex subunit mu-1 (AP1M1)
The protein contains 423 amino acids for an estimated molecular weight of 48587 Da.
Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. (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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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 |
|---|---|
| a breast cancer sample |
Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Endosome to melanosome transport
Intracellular protein transport
Melanosome organization
Membrane organization
Neutrophil degranulation
Post-Golgi vesicle-mediated transport
Regulation of defense response to virus by virus
Vesicle-mediated transport
Viral process
Cellular Component
Clathrin adaptor complex
Clathrin-coated endocytic vesicle membrane
Clathrin-coated vesicle
Clathrin-coated vesicle membrane
Cytoplasmic vesicle
Cytoplasmic vesicle membrane
Cytosol
Extracellular exosome
Golgi membrane
Intracellular membrane-bounded organelle
Lysosomal membrane
Membrane
Plasma membrane
Specific granule membrane
Trans-Golgi network membrane
The reference OMIM entry for this protein is 603535
Adaptor-related protein complex 1, mu-1 subunit; ap1m1
Clathrin assembly protein complex ap1, mu subunit
Clathrin adaptor protein ap47; ap47
Mu-1a
DESCRIPTION
Heterotetrameric adaptor complexes promote the formation of clathrin-coated pits and vesicles. The AP1 adaptor complex, localized at the trans-Golgi network, is composed of 2 approximately 100-kD subunits, beta-prime adaptin (600157) and gamma-adaptin (603533); a medium subunit, AP47; and a small subunit, AP19 (603531) (summary by Peyrard et al., 1998).CLONING
Nakayama et al. (1991) isolated a mouse brain cDNA encoding AP47. By Northern blot analysis, Peyrard et al. (1998) demonstrated that the 2.5-kb AP47 mRNA is expressed ubiquitously in human tissues.GENE FUNCTION
Doray et al. (2002) demonstrated that the Golgi-localized, gamma-ear-containing adenosine diphosphate ribosylation factor-binding proteins (GGA1, 606004 and GGA3, 606006) and the AP1 complex colocalize in clathrin-coated buds of the trans-Golgi networks of mouse L cells and human HeLa cells. Binding studies revealed a direct interaction between the hinge domains of the GGAs and the gamma-ear domain of AP1. Further, AP1 contained bound casein kinase-2 (see CSNK2A1, 115440) that phosphorylated GGA1 and GGA3, thereby causing autoinhibition. Doray et al. (2002) demonstrated that this autoinhibition could induce the directed transfer of mannose 6-phosphate receptors (see 154540) from the GGAs to AP1. Mannose 6-phosphate receptors that were defective in binding to GGAs were poorly incorporated into adaptor protein complex containing clathrin coated vesicles. Thus, Doray et al. (2002) concluded that GGAs and the AP1 complex interact to package mannose 6-phosphate receptors into AP1-containing coated vesicles.MAPPING
By analyzing a somatic cell hybrid panel with a mouse AP47 cDNA probe (Peyrard, 1999), Peyrard et al. (1998) mapped the AP47 gene to human chromosome 19. ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603535 was added.