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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