Cytosolic Fe-S cluster assembly factor NUBP1 (NUBP1)
The protein contains 320 amino acids for an estimated molecular weight of 34534 Da.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery (PubMed:18573874). Required for maturation of extramitochondrial Fe-S proteins (PubMed:18573874). The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (PubMed:18573874). Implicated in the regulation of centrosome duplication (By similarity). Negatively regulates cilium formation and structure (By similarity). (updated: Sept. 27, 2017)
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.
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:rs2233531 |
Biological Process
Cell growth
Cell projection organization
Cellular iron ion homeostasis
Centrosome localization
Iron-sulfur cluster assembly
Negative regulation of centrosome duplication
Protein localization to cell cortex
Regulation of cell growth
Small molecule metabolic process
Cellular Component
Centriole
Cilium
Cytoplasm
Cytosol
Extracellular exosome
Nucleus
Obsolete cell
Plasma membrane
The reference OMIM entry for this protein is 600280
Nucleotide-binding protein 1; nubp1
Nbp
Nbp35
DESCRIPTION
NUBP1 is a member of the NUBP/MRP subfamily of ATP-binding proteins (Nakashima et al., 1999).CLONING
By screening a human neuroblastoma library, Shahrestanifar et al. (1994) cloned NUBP1, which they called NBP. The deduced 320-amino acid protein has a molecular mass of 34.5 kD. NBP displays sequence similarity with the product of the MinD gene from Escherichia coli. MinD is involved in the proper placement of the division septum and has ATPase activity. Both NBP and MinD contain consensus nucleotide-binding domains. The NBP mRNA is approximately 1,500 nucleotides long and was expressed in several human cell lines and in all rat tissues examined, with the highest levels in lung and testis. Shahrestanifar et al. (1994) indicated that the yeast homolog of the NBP gene had been isolated and found to exhibit 40% identity with human NBP. Furthermore, mutation of the gene was found to be lethal in yeast, indicating that NBP plays a vital role in cell function. Nakashima et al. (1999) showed that NUBP1 contains a conserved ATP/GTP binding motif A (P-loop), an ATP/GTP binding motif A-prime, and NUBP/MRP alpha and beta motifs. NUBP1 has an additional N-terminal sequence with 4 cysteine residues that is not present in NUBP2 (610779). Stehling et al. (2008) noted that the N and C termini of human NBP35 have several conserved cysteines that may form iron-binding sites. Using ultraviolet and visible spectroscopy and low-temperature electron paramagnetic resonance, they showed that NBP35 likely coordinated a 4Fe-4S cluster. Both fluorescence-tagged and endogenous HeLa cell NBP35 localized to the cytosol, which was verified by cell fractionation.GENE FUNCTION
Stehling et al. (2008) found that depletion of NBP35 in HeLa cells via RNA interference impaired maturation of the cytosolic Fe-S proteins GPAT (PPAT; 172450) and IRP1 (ACO1; 100880). IRP1 is a bifunctional protein; in the presence of a 4Fe-4S cluster, it functions as a cytosolic aconitase, and in the absence of a 4Fe-4S cluster, it regulates cellular iron homeostasis by binding iron regulatory elements (IREs) in target mRNAs, influencing mRNA translation. Depletion of NBP35 in HeLa cells resulted in a time-dependent decrease in IRP1 cytosolic aconitase activity and a concomitant increase in IRP1 binding to IREs. Binding of IRP1 to a 5-prime IRE in ferritin heavy chain (FTH1; 134770) mRNA inhibits translation and thereby reduces cytosolic iron storage capacity, whereas binding of IRP1 to 3-prime IREs in transferrin receptor (TFRC; 190010) mRNA stabilizes the mRNA, leading to increased translation and increased uptake of transferrin (190000). Increased IRE binding by IRP1 in NBP35-depleted cells led to decreased levels of ferritin heavy chain, increased levels of transferrin receptor, and increased transferrin uptake. NBP35 also interacted with coexpressed CFD1 (NUBP2; 610779) in transfected HeLa cells, suggesting that the 2 proteins may function in a complex for regulation of cellular iron homeostasis and cytosolic Fe-S protein assembly.MAPPING
Hartz (2012) mapped the NUBP1 gene to chromosome 16p13.13 based on an alignment of the NUBP1 sequence (GenBank GENBANK AK223204) with the genomic sequence (GRCh37). Nakashima et al. (1999) mapped the mouse Nubp1 gene to the t-complex region of mouse chromosome 16, which shows homology of synteny with human chromosome 16p13.1. ... More on the omim web site
Feb. 10, 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600280 was added.