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Protein

CDGSH iron-sulfur domain-containing protein 1

Gene

CISD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

Cofactori

[2Fe-2S] cluster5 PublicationsNote: Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is redox-active and pH labile and is significantly less stable at pH 4.5 as compared with pH 7.0.5 Publications

Redox potential

E is 0 +/- 10 mV for 2Fe-2S at pH 7.5.1 Publication

Manual assertion based on experiment ini

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi72Iron-sulfur (2Fe-2S)1
Metal bindingi74Iron-sulfur (2Fe-2S)1
Metal bindingi83Iron-sulfur (2Fe-2S)1
Metal bindingi87Iron-sulfur (2Fe-2S); via pros nitrogen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122873-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CDGSH iron-sulfur domain-containing protein 1
Alternative name(s):
MitoNEET
Gene namesi
Name:CISD1
Synonyms:C10orf70, ZCD1
ORF Names:MDS029
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:30880. CISD1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei14 – 31Helical; Signal-anchor for type III membrane proteinSequence analysisAdd BLAST18
Topological domaini32 – 108CytoplasmicSequence analysisAdd BLAST77

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72C → S: Abolishes absorption in the 300-500 nm range. 1 Publication1
Mutagenesisi74C → S: Abolishes absorption in the 300-500 nm range. 1 Publication1
Mutagenesisi83C → S: Abolishes absorption in the 300-500 nm range. 1 Publication1
Mutagenesisi84D → N: Does not affect absorption in the 300-500 nm range. 1 Publication1
Mutagenesisi87H → C: Affects absorption in the 300-500 nm range but it is not reduced. Increased stability of the 2Fe-2S cluster at low pH. 1 Publication1
Mutagenesisi87H → Q: Abolishes absorption in the 300-500 nm range. 1 Publication1

Organism-specific databases

DisGeNETi55847.
OpenTargetsiENSG00000122873.
PharmGKBiPA162382289.

Chemistry databases

ChEMBLiCHEMBL1795168.

Polymorphism and mutation databases

BioMutaiCISD1.
DMDMi25453105.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000898032 – 108CDGSH iron-sulfur domain-containing protein 1Add BLAST107

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei55N6-acetyllysine; alternateBy similarity1
Cross-linki55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei68N6-acetyllysine; alternateBy similarity1
Cross-linki68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei104N6-acetyllysine; alternateBy similarity1
Cross-linki104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9NZ45.
MaxQBiQ9NZ45.
PaxDbiQ9NZ45.
PeptideAtlasiQ9NZ45.
PRIDEiQ9NZ45.
TopDownProteomicsiQ9NZ45.

PTM databases

iPTMnetiQ9NZ45.
PhosphoSitePlusiQ9NZ45.
SwissPalmiQ9NZ45.

Expressioni

Tissue specificityi

Expression is reduced in cells derived from cystic fibrosis patients.1 Publication

Inductioni

Expression is down-regulated by glibenclamide and 5-[(4-carboxyphenyl)methylene]-2-thioxo-3-(3-trifluoromethyl)phenyl-4-thiazolidinone (CFTR(inh)172), and up-regulated by cAMP/isoproterenol/IBMX, components that inhibit and stimulate chloride transport activity respectively.1 Publication

Gene expression databases

BgeeiENSG00000122873.
CleanExiHS_CISD1.
ExpressionAtlasiQ9NZ45. baseline and differential.
GenevisibleiQ9NZ45. HS.

Organism-specific databases

HPAiCAB045965.
HPA074383.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi120949. 30 interactors.
DIPiDIP-46446N.
IntActiQ9NZ45. 3 interactors.
STRINGi9606.ENSP00000363041.

Chemistry databases

BindingDBiQ9NZ45.

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 49Combined sources3
Beta strandi53 – 66Combined sources14
Beta strandi68 – 71Combined sources4
Beta strandi73 – 75Combined sources3
Turni78 – 81Combined sources4
Helixi86 – 94Combined sources9
Beta strandi98 – 104Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QD0X-ray1.81A/B32-108[»]
2QH7X-ray1.50A/B33-108[»]
2R13X-ray1.80A33-108[»]
3EW0X-ray1.40A/B33-108[»]
3LPQX-ray1.70A/B33-107[»]
3REEX-ray1.76A32-108[»]
4EZFX-ray1.19A/B33-108[»]
4F1EX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R33-108[»]
4F28X-ray1.55A/B33-108[»]
4F2CX-ray1.35A/B33-108[»]
ProteinModelPortaliQ9NZ45.
SMRiQ9NZ45.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZ45.

Family & Domainsi

Sequence similaritiesi

Belongs to the CISD protein family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3461. Eukaryota.
ENOG41122II. LUCA.
GeneTreeiENSGT00390000001233.
HOGENOMiHOG000242301.
HOVERGENiHBG052444.
InParanoidiQ9NZ45.
OMAiKDHRNKS.
OrthoDBiEOG091G0XB4.
PhylomeDBiQ9NZ45.
TreeFamiTF324661.

Family and domain databases

InterProiIPR018967. FeS-contain_CDGSH-typ.
IPR019610. FeS-contain_mitoNEET_N.
[Graphical view]
PfamiPF10660. MitoNEET_N. 1 hit.
PF09360. zf-CDGSH. 1 hit.
[Graphical view]
SMARTiSM00704. ZnF_CDGSH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NZ45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTSSSSVR VEWIAAVTIA AGTAAIGYLA YKRFYVKDHR NKAMINLHIQ
60 70 80 90 100
KDNPKIVHAF DMEDLGDKAV YCRCWRSKKF PFCDGAHTKH NEETGDNVGP

LIIKKKET
Length:108
Mass (Da):12,199
Last modified:October 1, 2000 - v1
Checksum:i2E47000F0635CBB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY960578 mRNA. Translation: AAY32336.1.
AF220049 mRNA. Translation: AAF67642.1.
AK312017 mRNA. Translation: BAG34955.1.
CH471083 Genomic DNA. Translation: EAW54163.1.
BC005962 mRNA. Translation: AAH05962.1.
BC007043 mRNA. Translation: AAH07043.1.
BC008474 mRNA. Translation: AAH08474.1.
BC059168 mRNA. Translation: AAH59168.1.
CCDSiCCDS7251.1.
RefSeqiNP_060934.1. NM_018464.4.
UniGeneiHs.370102.

Genome annotation databases

EnsembliENST00000333926; ENSP00000363041; ENSG00000122873.
GeneIDi55847.
KEGGihsa:55847.
UCSCiuc001jkc.6. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY960578 mRNA. Translation: AAY32336.1.
AF220049 mRNA. Translation: AAF67642.1.
AK312017 mRNA. Translation: BAG34955.1.
CH471083 Genomic DNA. Translation: EAW54163.1.
BC005962 mRNA. Translation: AAH05962.1.
BC007043 mRNA. Translation: AAH07043.1.
BC008474 mRNA. Translation: AAH08474.1.
BC059168 mRNA. Translation: AAH59168.1.
CCDSiCCDS7251.1.
RefSeqiNP_060934.1. NM_018464.4.
UniGeneiHs.370102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QD0X-ray1.81A/B32-108[»]
2QH7X-ray1.50A/B33-108[»]
2R13X-ray1.80A33-108[»]
3EW0X-ray1.40A/B33-108[»]
3LPQX-ray1.70A/B33-107[»]
3REEX-ray1.76A32-108[»]
4EZFX-ray1.19A/B33-108[»]
4F1EX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R33-108[»]
4F28X-ray1.55A/B33-108[»]
4F2CX-ray1.35A/B33-108[»]
ProteinModelPortaliQ9NZ45.
SMRiQ9NZ45.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120949. 30 interactors.
DIPiDIP-46446N.
IntActiQ9NZ45. 3 interactors.
STRINGi9606.ENSP00000363041.

Chemistry databases

BindingDBiQ9NZ45.
ChEMBLiCHEMBL1795168.

PTM databases

iPTMnetiQ9NZ45.
PhosphoSitePlusiQ9NZ45.
SwissPalmiQ9NZ45.

Polymorphism and mutation databases

BioMutaiCISD1.
DMDMi25453105.

Proteomic databases

EPDiQ9NZ45.
MaxQBiQ9NZ45.
PaxDbiQ9NZ45.
PeptideAtlasiQ9NZ45.
PRIDEiQ9NZ45.
TopDownProteomicsiQ9NZ45.

Protocols and materials databases

DNASUi55847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333926; ENSP00000363041; ENSG00000122873.
GeneIDi55847.
KEGGihsa:55847.
UCSCiuc001jkc.6. human.

Organism-specific databases

CTDi55847.
DisGeNETi55847.
GeneCardsiCISD1.
H-InvDBHIX0201471.
HGNCiHGNC:30880. CISD1.
HPAiCAB045965.
HPA074383.
MIMi611932. gene.
neXtProtiNX_Q9NZ45.
OpenTargetsiENSG00000122873.
PharmGKBiPA162382289.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3461. Eukaryota.
ENOG41122II. LUCA.
GeneTreeiENSGT00390000001233.
HOGENOMiHOG000242301.
HOVERGENiHBG052444.
InParanoidiQ9NZ45.
OMAiKDHRNKS.
OrthoDBiEOG091G0XB4.
PhylomeDBiQ9NZ45.
TreeFamiTF324661.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122873-MONOMER.

Miscellaneous databases

ChiTaRSiCISD1. human.
EvolutionaryTraceiQ9NZ45.
GenomeRNAii55847.
PROiQ9NZ45.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122873.
CleanExiHS_CISD1.
ExpressionAtlasiQ9NZ45. baseline and differential.
GenevisibleiQ9NZ45. HS.

Family and domain databases

InterProiIPR018967. FeS-contain_CDGSH-typ.
IPR019610. FeS-contain_mitoNEET_N.
[Graphical view]
PfamiPF10660. MitoNEET_N. 1 hit.
PF09360. zf-CDGSH. 1 hit.
[Graphical view]
SMARTiSM00704. ZnF_CDGSH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCISD1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ45
Secondary accession number(s): Q1X902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Binds pioglitazone, an anti-diabetes drug. Binding increases the stability of the 2Fe-2S cluster.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.