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Protein

Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial

Gene

CHCHD10

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

Functioni

May be involved in the maintenance of mitochondrial organization and mitochondrial cristae structure.1 Publication

GO - Biological processi

  • ATP biosynthetic process Source: BHF-UCL
  • mitochondrion organization Source: UniProtKB
  • negative regulation of ATP citrate synthase activity Source: BHF-UCL
  • oxidative phosphorylation Source: BHF-UCL

Enzyme and pathway databases

ReactomeiR-HSA-1268020 Mitochondrial protein import

Names & Taxonomyi

Protein namesi
Recommended name:
Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial
Alternative name(s):
Protein N27C7-4
Gene namesi
Name:CHCHD10
Synonyms:C22orf16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

EuPathDBiHostDB:ENSG00000250479.8
HGNCiHGNC:15559 CHCHD10
MIMi615903 gene
neXtProtiNX_Q8WYQ3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Frontotemporal dementia and/or amyotrophic lateral sclerosis 2 (FTDALS2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. The pathological events leading to disease involve fragmentation of the mitochondrial network, mitochondrial ultrastructural abnormalities including loss, disorganization and dilatation of cristae, and mitochondrial dysfunction associated with respiratory chain deficiency (PubMed:24934289).1 Publication
Disease descriptionA neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis.
See also OMIM:615911
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07180534P → S in FTDALS2. 1 PublicationCorresponds to variant dbSNP:rs551521196EnsemblClinVar.1
Natural variantiVAR_07180659S → L in FTDALS2; results in disorganization of mitochondrial cristae. 1 PublicationCorresponds to variant dbSNP:rs587777574EnsemblClinVar.1
Spinal muscular atrophy, Jokela type (SMAJ)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant, slowly progressive, lower motor neuron disease. SMAJ is characterized by adult-onset of muscle cramps and fasciculations affecting the proximal and distal muscles of the upper and lower limbs. The disorder results in weakness and mild muscle atrophy later in life.
See also OMIM:615048
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07328566G → V in SMAJ. 1 PublicationCorresponds to variant dbSNP:rs730880031EnsemblClinVar.1
Myopathy, isolated mitochondrial, autosomal dominant (IMMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA mitochondrial myopathy presenting with severe exercise intolerance, progressive proximal weakness, and lactic acidemia. The disorder is slowly progressive, with later involvement of facial muscles, muscles of the upper limbs, and distal muscles.
See also OMIM:616209
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07328315R → S in IMMD; associated in cis with R-58 in a IMMD family; unknown pathological significance; does not affect mitochondrial structure and organization. 1 PublicationCorresponds to variant dbSNP:rs730880032EnsemblClinVar.1
Natural variantiVAR_07328458G → R in IMMD; associated in cis with S-15 in a IMMD family; causes mitochondrial fragmentation. 1 PublicationCorresponds to variant dbSNP:rs730880033EnsemblClinVar.1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi400916
MalaCardsiCHCHD10
MIMi615048 phenotype
615911 phenotype
616209 phenotype
OpenTargetsiENSG00000250479
Orphaneti803 Amyotrophic lateral sclerosis
275872 Frontotemporal dementia with motor neuron disease
PharmGKBiPA162382225

Polymorphism and mutation databases

BioMutaiCHCHD10
DMDMi74731006

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 16MitochondrionSequence analysisAdd BLAST16
ChainiPRO_000025403817 – 142Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrialAdd BLAST126

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi102 ↔ 132PROSITE-ProRule annotation
Disulfide bondi112 ↔ 122PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ8WYQ3
PaxDbiQ8WYQ3
PeptideAtlasiQ8WYQ3
PRIDEiQ8WYQ3

PTM databases

iPTMnetiQ8WYQ3
PhosphoSitePlusiQ8WYQ3

Expressioni

Tissue specificityi

Ubiquitously expressed. Higher expression is observed in heart and liver.1 Publication

Gene expression databases

BgeeiENSG00000250479
CleanExiHS_CHCHD10
ExpressionAtlasiQ8WYQ3 baseline and differential
GenevisibleiQ8WYQ3 HS

Organism-specific databases

HPAiHPA003440

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi134810, 73 interactors
IntActiQ8WYQ3, 3 interactors
STRINGi9606.ENSP00000418428

Structurei

3D structure databases

ProteinModelPortaliQ8WYQ3
SMRiQ8WYQ3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini99 – 140CHCHPROSITE-ProRule annotationAdd BLAST42

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi102 – 112Cx9C motif 1PROSITE-ProRule annotationAdd BLAST11
Motifi122 – 132Cx9C motif 2PROSITE-ProRule annotationAdd BLAST11

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4090 Eukaryota
ENOG41126E7 LUCA
GeneTreeiENSGT00440000038159
HOGENOMiHOG000194088
HOVERGENiHBG059852
InParanoidiQ8WYQ3
PhylomeDBiQ8WYQ3
TreeFamiTF318060

Family and domain databases

InterProiView protein in InterPro
IPR010625 CHCH
PfamiView protein in Pfam
PF06747 CHCH, 1 hit
PROSITEiView protein in PROSITE
PS51808 CHCH, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q8WYQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRGSRSAAS RPASRPAAPS AHPPAHPPPS AAAPAPAPSG QPGLMAQMAT
60 70 80 90 100
TAAGVAVGSA VGHVMGSALT GAFSGGSSEP SQPAVQQAPT PAAPQPLQMG
110 120 130 140
PCAYEIRQFL DCSTTQSDLS LCEGFSEALK QCKYYHGLSS LP
Length:142
Mass (Da):14,149
Last modified:March 1, 2002 - v1
Checksum:iA3AA3894CBEC0137
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07328315R → S in IMMD; associated in cis with R-58 in a IMMD family; unknown pathological significance; does not affect mitochondrial structure and organization. 1 PublicationCorresponds to variant dbSNP:rs730880032EnsemblClinVar.1
Natural variantiVAR_07180534P → S in FTDALS2. 1 PublicationCorresponds to variant dbSNP:rs551521196EnsemblClinVar.1
Natural variantiVAR_07328458G → R in IMMD; associated in cis with S-15 in a IMMD family; causes mitochondrial fragmentation. 1 PublicationCorresponds to variant dbSNP:rs730880033EnsemblClinVar.1
Natural variantiVAR_07180659S → L in FTDALS2; results in disorganization of mitochondrial cristae. 1 PublicationCorresponds to variant dbSNP:rs587777574EnsemblClinVar.1
Natural variantiVAR_07328566G → V in SMAJ. 1 PublicationCorresponds to variant dbSNP:rs730880031EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050774 Genomic DNA Translation: BAB83036.1
AK289560 mRNA Translation: BAF82249.1
CH471095 Genomic DNA Translation: EAW59602.1
BC065232 mRNA Translation: AAH65232.1
CCDSiCCDS13815.1
RefSeqiNP_001288268.1, NM_001301339.1
NP_998885.1, NM_213720.2
UniGeneiHs.66915

Genome annotation databases

EnsembliENST00000484558; ENSP00000418428; ENSG00000250479
ENST00000629095; ENSP00000487006; ENSG00000273607
GeneIDi400916
KEGGihsa:400916
UCSCiuc002zxw.4 human

Similar proteinsi

Entry informationi

Entry nameiCHC10_HUMAN
AccessioniPrimary (citable) accession number: Q8WYQ3
Secondary accession number(s): A8K0J5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2002
Last modified: March 28, 2018
This is version 111 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

Complete proteome, Reference proteome

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