Probable cytosolic iron-sulfur protein assembly protein CIAO1 (CIAO1)
The protein contains 339 amino acids for an estimated molecular weight of 37840 Da.
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (PubMed:17937914, PubMed:23891004). As a CIA complex component, interacts specifically with CIAO2A or CIAO2B and MMS19 to assist different branches of iron-sulfur protein assembly, depending of its interactors. The complex CIAO1:CIAO2B:MMS19 binds to and facilitates the assembly of most cytosolic-nuclear Fe/S proteins. CIAO1:CIAO2A specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). Seems to specifically modulate the transactivation activity of WT1 (PubMed:9556563). As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (PubMed:20797633). (updated: Nov. 7, 2018)
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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
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Biological Process
Chromosome segregation
Iron-sulfur cluster assembly
Positive regulation of cell population proliferation
Protein maturation by iron-sulfur cluster transfer
Regulation of transcription by RNA polymerase II
Small molecule metabolic process
Molecular Function
The reference OMIM entry for this protein is 604333
Wd40 repeat-containing protein ciao1; ciao1
Wd repeat-containing protein 39; wdr39
DESCRIPTION
CIAO1 is a subunit of a protein complex involved in the biosynthesis of Fe-S proteins. Other subunits of this complex are MMS19 (614777), FAM96B (614778), and NARFL (611118) (Stehling et al., 2012; Gari et al., 2012).CLONING
The Wilms tumor gene (WT1; 607102) on 11p13 is involved in regulating cell cycle progression and apoptosis. In an attempt to dissect the molecular mechanisms of transcriptional activation and repression by WT1, and to identify other proteins that may be involved in kidney and hematopoietic cell tumorigenesis, several groups have studied WT1-interacting proteins. WT1 binds in vivo and in vitro to p53 (191170), resulting in WT1 functioning as a transcriptional repressor. Mutations in p53 increase the aggressiveness of Wilms tumors, resulting in poorer patient prognosis, but are not thought to be a primary genetic cause of Wilms tumor formation. WT1 also interacts with and regulates the transcriptional activity of steroidogenic factor-1 (184757), a key molecule in gonadal development. Johnstone et al. (1996) identified a protein called PAWR (601936), the gene for which maps to 12q21, that is capable of modulating the transcriptional activities of WT1. Johnstone et al. (1998) identified a second protein, which they named CIAO1 after the Chinese word for 'bridge,' that is also capable of modulating the transcriptional activities of WT1. CIAO1 is a 339-amino acid polypeptide containing 7 WD40 or beta-transducin repeats. It can inhibit the transcriptional activation function of WT1, but does not affect WT1-mediated transcriptional repression. Johnstone et al. (1998) demonstrated that the yeast Ciao1 homolog is an essential protein that appears to be highly evolutionarily conserved.GENE STRUCTURE
Johnstone et al. (1999) described the structural organization of the CIAO1 gene, with the intron/exon boundaries closely matching the consensus 5-prime donor/3-prime acceptor splice site sequences. The gene contains 7 exons.GENE FUNCTION
Ito et al. (2010) showed that CIAO1 coprecipitated with ANT2 (SLC25A5; 300150), XPD (ERCC2; 126340), MIP18 (FAM96B), and MMS19 in a protein complex that was required for chromosome segregation in human cell lines. In HEK293 cells, Stehling et al. (2012) identified and confirmed a protein complex made up of several known or putative proteins involved in the biosynthesis of Fe-S proteins: MMS19, CIAO1, and IOP1 (NARFL). Inactivation of MMS19, FAM96B, or IOP1 reduced HEK293 cell survival following UV irradiation or methyl methanesulfonate treatment. Stehling et al. (2012) hypothesized that the complex acts late in Fe-S protein biogenesis to facilitate Fe-S cluster transfer from the CIA scaffold complex CFD1 (NUBP2; 610779)-NBP35 (NUBP1; 600280) to Fe-S target proteins. Using coimmunoprecipitation and gel filtration studies, Gari et al. (2012) independently identified a stable complex that involved MMS19, CIAO1, IOP1, and FAM96B.MAPPING
By FISH and radiation hybrid analysis, Johnstone et al. (1999) mapped the WDR39 gene to the pericentric region of chromosome 2. They stated that the probable location is 2q11.2 based on the gene's inclusion within a previously mapped BAC clone (GenBank GENBANK AC004020). ... More on the omim web site
Nov. 16, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 604333 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed