| + |
HSPA9 | up-regulates activity 
relocalization
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262131 |
|
|
|
|
| pmid |
sentence |
| 27714045 |
Cluster transfer from ISCU to recipient apoproteins is assisted by a dedicated chaperone/cochaperone (HSPA9/HSC20) system that facilitates cluster release from the primary scaffold ISCU and transfer to recipient apoproteins or to intermediate carriers |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
Succinate dehydrogenase-Mitochondrial respiratory chain complex II |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262136 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
CoQ-cytochrome c reductase-Mitochondrial respiratory chain complex III |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262137 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
Mitochondrial Fe-S Cluster Assembly Complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262129 |
|
|
in vitro |
|
| pmid |
sentence |
| 27519411 |
As the architecture of the human machinery remains undefined, we co-expressed in Escherichia coli the following four proteins involved in the initial step of Fe-S cluster synthesis: FXN42-210 (iron donor); [NFS1]·[ISD11] (sulfur donor); and ISCU (scaffold upon which new clusters are assembled). We purified a stable, active complex consisting of all four proteins with 1:1:1:1 stoichiometry. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
SDHB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262133 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Succinate dehydrogenase subunit B contains three Fe-S clusters |The enzymatic activity of both proteins depends on the presence of intact Fe-S clusters |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates quantity
precursor of
|
D-threo-isocitrate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262132 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Mitochondrial aconitase and succinate dehydrogenase were among the earliest mammalian Fe-S proteins identified.|The enzymatic activity of both proteins depends on the presence of intact Fe-S clusters |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262135 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
CIAO2B cytosolic iron-sulfur protein assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281027 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23585563 |
The MMS19 complex consists of a core complex (MMS19-MIP18-CIAO1) and an external component (IOP1). The core complex catches and holds IOP1 via interaction with CIAO1. MMS19 in the core complex binds apoproteins. MIP18 connects CIAO1 and MMS19. IOP1 protein is an external component of the human cytosolic iron-sulfur cluster assembly (CIA) machinery and functions in the MMS19 protein-dependent CIA pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CIAO1-CIAO2A-CIAO3 cytosolic iron-sulfur protein assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281031 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32222833 |
This work shows, for the first time, via size exclusion chromatography coupled with multiangle light scattering, UV-vis absorption and electron paramagnetic resonance (EPR) spectroscopies, the formation of a stable, [4Fe-4S]-bound, complex, composed by CIAO3 and the hetero-CIA2A-CIAO1 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Mitochondrial BOLA1-GLRX5 iron-sulfur cluster assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281054 |
|
|
|
|
| pmid |
sentence |
| 27532772 |
Here, we characterize the BOLA family proteins Bol1 and Bol3 as specific mitochondrial ISC assembly factors that facilitate [4Fe-4S] cluster insertion into a subset of mitochondrial proteins such as lipoate synthase and succinate dehydrogenase. Bol1-Bol3 perform largely overlapping functions, yet cannot replace the ISC protein Nfu1 that also participates in this phase of Fe/S protein biogenesis. Bol1 and Bol3 form dimeric complexes with both monothiol glutaredoxin Grx5 and Nfu1. Complex formation differentially influences the stability of the Grx5-Bol-shared Fe/S clusters. |
|
| Publications: |
1 |
| + |
Mitochondrial BOLA3-GLRX5 iron-sulfur cluster assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281057 |
|
|
|
|
| pmid |
sentence |
| 27532772 |
Here, we characterize the BOLA family proteins Bol1 and Bol3 as specific mitochondrial ISC assembly factors that facilitate [4Fe-4S] cluster insertion into a subset of mitochondrial proteins such as lipoate synthase and succinate dehydrogenase. Bol1-Bol3 perform largely overlapping functions, yet cannot replace the ISC protein Nfu1 that also participates in this phase of Fe/S protein biogenesis. Bol1 and Bol3 form dimeric complexes with both monothiol glutaredoxin Grx5 and Nfu1. Complex formation differentially influences the stability of the Grx5-Bol-shared Fe/S clusters. |
|
| Publications: |
1 |
| + |
ISCA2-IBA57 mitochondrial iron-sulfur protein assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281060 |
|
|
|
|
| pmid |
sentence |
| 31831856 |
In mitochondria, a complex protein machinery is devoted to the maturation of iron-sulfur cluster proteins. Structural information on the last steps of the machinery, which involve ISCA1, ISCA2 and IBA57 proteins, needs to be acquired in order to define how these proteins cooperate each other. We report here the use of an integrative approach, utilizing information from small-angle X-ray scattering (SAXS) and bioinformatics-driven docking prediction, to determine a low-resolution structural model of the human mitochondrial [2Fe-2S]2+ ISCA2-IBA57 complex. |
|
| Publications: |
1 |
| + |
NUBP1-NUBP2 iron-sulfur cluster assembly scaffold complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281063 |
|
|
|
|
| pmid |
sentence |
| 18573874 |
HuNbp35 formed a complex with its close homologue huCfd1 (also known as Nubp2) in vivo, suggesting the existence of a heteromeric P-loop NTPase complex that is required for both cytosolic Fe/S protein assembly and cellular iron homeostasis. |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
PRIM2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262134 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Human DNA primase, are Fe-S proteins. The loss of an iron-sulfur cluster in RAD3 helicase results in a failure to unwind DNA1 |
|
| Publications: |
1 |
| + |
ISCA1-ISCA2 mitochondrial iron-sulfur protein assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281066 |
|
|
|
|
| pmid |
sentence |
| 25347204 |
We found that (i) ISCA2 binds either [2Fe-2S] or [4Fe-4S] cluster in a dimeric state, and (ii) two molecules of [2Fe-2S](2+) GRX5 donate their cluster to a heterodimeric ISCA1/ISCA2 complex. This complex acts as an "assembler" of [4Fe-4S] clusters; i.e., the two GRX5-donated [2Fe-2S](2+) clusters generate a [4Fe-4S](2+) cluster. The formation of the same [4Fe-4S](2+) cluster-bound heterodimeric species is also observed by having first one [2Fe-2S](2+) cluster transferred from GRX5 to each individual ISCA1 and ISCA2 proteins to form [2Fe-2S](2+) ISCA2 and [2Fe-2S](2+) ISCA1, and then mixing them together. |
|
| Publications: |
1 |
| + |
BOLA2-GLRX3 iron-sulfur cluster assembly complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281069 |
|
|
|
|
| pmid |
sentence |
| 22309771 |
Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. Furthermore, we demonstrate that apo BolA2 binds to each Grx domain in the [2Fe-2S] Glrx3 homodimer forming a [2Fe-2S] BolA2-Glrx3 heterotrimer. Taken together, these results suggest that the unusual [2Fe-2S]-bridging Grx-BolA interaction is conserved in higher eukaryotes and may play a role in signaling cellular iron status in humans. |
|
| Publications: |
1 |
| + |
HSCB | up-regulates activity
relocalization
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262130 |
|
|
|
|
| pmid |
sentence |
| 27714045 |
Cluster transfer from ISCU to recipient apoproteins is assisted by a dedicated chaperone/cochaperone (HSPA9/HSC20) system that facilitates cluster release from the primary scaffold ISCU and transfer to recipient apoproteins or to intermediate carriers |
|
| Publications: |
1 |
4.0
iron-sulfur cluster