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HUMAN:CISD3

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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

PMID:17376863[1]

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

PMID:17376863[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:29259115[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051537

2 iron, 2 sulfur cluster binding

PMID:29259115[2]

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

PMID:29259115[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0043231

intracellular membrane-bounded organelle

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018967

C

Seeded From UniProt

complete

enables

GO:0051537

2 iron, 2 sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018967

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496
UniProtKB-SubCell:SL-0173

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0051537

2 iron, 2 sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0001

F

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0411

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 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. ↑ 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