UniProt Accession

 CISD1_HUMAN; Q9NZ45; Q1X902 

Genbank Protein ID

 AY960578; AF220049; AK312017; CH471083; BC005962; BC007043; BC008474; BC059168 

Genbank Nucleotide ID

 AAY32336.1; AAF67642.1; BAG34955.1; EAW54163.1; AAH05962.1; AAH07043.1; AAH08474.1; AAH59168.1 

Protein Name

 CDGSH iron-sulfur domain-containing protein 1 

Protein Synonyms/Alias

 MitoNEET 

Gene Name

 CISD1 

Gene Synonyms/Alias

 C10orf70; ZCD1; MDS029 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
37	AYKRFYVKDHRNKAM	ubiquitination	[1]
51	MINLHIQKDNPKIVH	ubiquitination	[1]
55	HIQKDNPKIVHAFDM	acetylation	[2, 3]
55	HIQKDNPKIVHAFDM	ubiquitination	[1, 4]
68	DMEDLGDKAVYCRCW	acetylation	[2, 3]
68	DMEDLGDKAVYCRCW	ubiquitination	[1, 3, 4]
78	YCRCWRSKKFPFCDG	ubiquitination	[1]
79	CRCWRSKKFPFCDGA	ubiquitination	[1]
104	NVGPLIIKKKET***	acetylation	[2]
104	NVGPLIIKKKET***	ubiquitination	[4]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions. 

Sequence Annotation

 METAL 72 72 Iron-sulfur (2Fe-2S).
 METAL 74 74 Iron-sulfur (2Fe-2S).
 METAL 83 83 Iron-sulfur (2Fe-2S).
 METAL 87 87 Iron-sulfur (2Fe-2S); via pros nitrogen.
 MOD_RES 104 104 N6-acetyllysine (By similarity).  

Keyword

 2Fe-2S; 3D-structure; Acetylation; Complete proteome; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 108 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; ISS:UniProtKB.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0043457; P:regulation of cellular respiration; IEA:Compara. 

Interpro

 IPR018967; FeS-contain_CDGSH-typ.
 IPR006622; FeS-contain_CDGSH-typ_subfam.
 IPR019610; FeS-contain_mitoNEET_N. 

Pfam

 PF10660; MitoNEET_N
 PF09360; zf-CDGSH 

SMART

 SM00704; ZnF_CDGSH 

PROSITE

  

PRINTS