Josephin-1 (JOSD1)
The protein contains 202 amino acids for an estimated molecular weight of 23198 Da.
Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance membrane dynamics and cell motility independently of its catalytic activity. (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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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| Variant | Description |
|---|---|
| dbSNP:rs6001200 |
The reference OMIM entry for this protein is 615323
Josephin domain-containing protein 1; josd1
Kiaa0063
DESCRIPTION
JOSD1 belongs to a family of Josephin domain-containing deubiquitinating enzymes related to ATXN3 (607047). JOSD1 is activated by monoubiquitination and functions in cytoskeletal dynamics, cell motility, and endocytosis (Seki et al., 2013).CLONING
By sequencing clones obtained from a size-fractionated KG-1 human immature myeloid cell line cDNA library, (Nomura et al., 1994) obtained a partial JOSD1 clone, which they designated KIAA0063. The 3-prime untranslated region contains an Alu element and its 202-amino acid sequence was predicted to include a transmembrane domain. Northern blot analysis detected JOSD1 in all human tissues and cell lines examined. Seki et al. (2013) stated that the deduced 202-amino acid JOSD1 protein is made up almost entirely of an approximately 180-amino acid Josephin catalytic domain, including a catalytic cys36. Western blot analysis detected robust Josd1 expression in all mouse tissues examined: anterior and posterior brain, heart, kidney, liver, skeletal muscle, and spleen. In transfected HEK293 cells, epitope- or fluorescence-tagged JOSD1 localized predominantly at the plasma membrane and cytoplasmic puncta. In fractionated cells, JOSD1 localized to the cytoskeletal, cytosolic, and membrane fractions, but not to the nuclear fraction. Database analysis revealed 2 JOSD genes in vertebrates, JOSD1 and JOSD2 (615324), but only a single Josd gene in C. elegans and Drosophila.GENE FUNCTION
Seki et al. (2013) found that recombinant human JOSD1 deubiquitinated a monoubiquitinated probe. However, monoubiquitinated JOSD1 showed activity against both lys48- and lys63-linked polyubiquitin chains, which are associated with protein degradative and regulatory pathways, respectively. A substantial proportion of JOSD1 appeared to be monoubiquitinated in cultured cells. In contrast, JOSD2 did not require monoubiquitination for activity against either lys48- or lys63-linked ubiquitin chains. Monoubiquitination of JOSD1 caused its relocalization from the cytoskeletal fraction to the membrane fraction in transfected cells. Time-lapse microscopy revealed that catalytically inactive JOSD1 altered membrane dynamics and cell motility; monoubiquitinated and catalytic active JOSD1 also enhanced macropinocytosis and suppressed clathrin- and caveolae-mediated endocytosis. Seki et al. (2013) concluded that the activity of JOSD1 is regulated by monoubiquitination and that it has a role in membrane dynamics and endocytosis.MAPPING
By PCR of a human-rodent hybrid panel, Nomura et al. (1994) mapped the JOSD1 gene to chromosome 22. Hartz (2013) mapped the JOSD1 gene to chromosome 22q13.1 based on an alignment of the JOSD1 sequence (GenBank GENBANK D31884) with the genomic sequence (GRCh37). ... 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 25, 2017: Additional information
No protein expression data in P. Mayeux work for JOSD1
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 615323 was added.