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HUMAN:CISD3
Contents
| Species (Taxon ID) | Homo sapiens (Human). (9606) | |
| Gene Name(s) | CISD3 | |
| Protein Name(s) | CDGSH iron-sulfur domain-containing protein 3, mitochondrial
MitoNEET-related protein 2 Miner2 | |
| External Links | ||
| UniProt | P0C7P0 | |
| EMBL | AC006449 BM546511 | |
| CCDS | CCDS45662.1 | |
| RefSeq | NP_001129970.1 | |
| UniGene | Hs.713595 | |
| ProteinModelPortal | P0C7P0 | |
| SMR | P0C7P0 | |
| BioGrid | 129759 | |
| STRING | 9606.ENSP00000391402 | |
| PhosphoSite | P0C7P0 | |
| DMDM | 190358744 | |
| MaxQB | P0C7P0 | |
| PaxDb | P0C7P0 | |
| PRIDE | P0C7P0 | |
| Ensembl | ENST00000613478 ENST00000620783 | |
| GeneID | 284106 | |
| KEGG | hsa:284106 | |
| UCSC | uc010wds.1 | |
| CTD | 284106 | |
| GeneCards | GC17P036886 | |
| H-InvDB | HIX0202460 | |
| HGNC | HGNC:27578 | |
| HPA | HPA053436 HPA054400 | |
| MIM | 611933 | |
| neXtProt | NX_P0C7P0 | |
| PharmGKB | PA162382311 | |
| eggNOG | NOG87526 | |
| GeneTree | ENSGT00390000004574 | |
| HOGENOM | HOG000060282 | |
| HOVERGEN | HBG107689 | |
| InParanoid | P0C7P0 | |
| OMA | THKSERV | |
| OrthoDB | EOG71RXND | |
| PhylomeDB | P0C7P0 | |
| TreeFam | TF313111 | |
| GenomeRNAi | 284106 | |
| NextBio | 94542 | |
| PRO | PR:P0C7P0 | |
| Proteomes | UP000005640 UP000005640 | |
| Bgee | P0C7P0 | |
| CleanEx | HS_CISD3 | |
| Genevestigator | P0C7P0 | |
| GO | GO:0005739 GO:0051537 GO:0046872 | |
| InterPro | IPR018967 IPR006622 | |
| Pfam | PF09360 | |
| SMART | SM00704 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0005739 |
mitochondrion |
ECO:0000314 |
C |
mito-NEET is suited to communicate signals between the mitochondria and the rest of the cell as seen in Figure 3. It is characterized by a CDGSH-type zinc finger domain(Figure 1), even though it does not contain any zinc. It is more likely iron containing (Table 1). This protein plays a role in regulating the ETC and oxidative phosphorylation (Figure 5). Yet it's actual role in the etiology of type 2 diabetes and mediating some of the insulin sensitizing thiazolidinediene drugs is yet to be determined. |
complete | |||||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051537 |
2 iron, 2 sulfur cluster binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0106034 |
protein maturation by [2Fe-2S] cluster transfer |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
|
Seeded From UniProt |
complete | ||
|
part_of |
GO:0043231 |
intracellular membrane-bounded organelle |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051537 |
2 iron, 2 sulfur cluster binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051537 |
2 iron, 2 sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051536 |
iron-sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Wiley, SE et al. (2007) MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. Proc. Natl. Acad. Sci. U.S.A. 104 5318-23 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Lipper, CH et al. (2018) Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells. Proc. Natl. Acad. Sci. U.S.A. 115 272-277 PubMed GONUTS page
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