Q9Y512 · SAM50_HUMAN
- ProteinSorting and assembly machinery component 50 homolog
- GeneSAMM50
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes (PubMed:22252321, PubMed:25781180).
Required for the assembly of TOMM40 into the TOM complex (PubMed:15644312).
Required for the assembly of TOMM40 into the TOM complex (PubMed:15644312).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | membrane | |
Cellular Component | MIB complex | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Cellular Component | SAM complex | |
Biological Process | cristae formation | |
Biological Process | inner mitochondrial membrane organization | |
Biological Process | mitochondrial respiratory chain complex assembly | |
Biological Process | protein insertion into mitochondrial outer membrane |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSorting and assembly machinery component 50 homolog
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y512
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Multi-pass membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057338 | 110 | in dbSNP:rs3761472 | |||
Sequence: D → G | ||||||
Natural variant | VAR_013768 | 345 | in dbSNP:rs8418 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 510 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000215939 | 1-469 | UniProt | Sorting and assembly machinery component 50 homolog | |||
Sequence: MGTVHARSLEPLPSSGPDFGGLGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLGRTKDDIIICEIGDVFKAKNLIEVMRKSHEAREKLLRLGIFRQVDVLIDTCQGDDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPRPGNFERNFSVNLYKVTGQFPWSSLRETDRGMSAEYSFPIWKTSHTVKWEGVWRELGCLSRTASFAVRKESGHSLKSSLSHAMVIDSRNSSILPRRGALLKVNQELAGYTGGDVSFIKEDFELQLNKQLIFDSVFSASFWGGMLVPIGDKPSSIADRFYLGGPTSIRGFSMHSIGPQSEGDYLGGEAYWAGGLHLYTPLPFRPGQGGFGELFRTHFFLNAGNLCNLNYGEGPKAHIRKLAECIRWSYGAGIVLRLGNIARLELNYCVPMGVQTGDRICDGVQFGAGIRFL | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 255 | UniProt | N6-methyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13 (PubMed:25781180, PubMed:25997101).
This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9 (PubMed:25781180, PubMed:25997101).
The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex (PubMed:25997101).
Interacts with CHCHD3/MIC19 (PubMed:21081504).
Interacts with ARMC1 (PubMed:31644573).
This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together described as components of the mitochondrial outer membrane sorting assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9 (PubMed:25781180, PubMed:25997101).
The MICOS and SAM complexes together with DNAJC11 are part of a large protein complex spanning both membranes termed the mitochondrial intermembrane space bridging (MIB) complex (PubMed:25997101).
Interacts with CHCHD3/MIC19 (PubMed:21081504).
Interacts with ARMC1 (PubMed:31644573).
(Microbial infection) Interacts with parasite T.gondii RH strain MAF1b1; the interaction is probably indirect and results in the disruption of the MIB complex and the formation of SPOTs (structures positive for outer mitochondrial membrane (OMM)), a cellular response to OMM stress, which leads to the constitutive shedding of OMM vesicles.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y512 | CHCHD3 Q9NX63 | 7 | EBI-748409, EBI-743375 | |
BINARY | Q9Y512 | CHCHD6 Q9BRQ6 | 3 | EBI-748409, EBI-2557895 | |
BINARY | Q9Y512 | DNM1L O00429 | 3 | EBI-748409, EBI-724571 | |
BINARY | Q9Y512 | MFN2 O95140 | 2 | EBI-748409, EBI-3324756 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MGTVHARSLEPLPSSGPDFG | ||||||
Domain | 45-125 | POTRA | ||||
Sequence: VVVQHVHFDGLGRTKDDIIICEIGDVFKAKNLIEVMRKSHEAREKLLRLGIFRQVDVLIDTCQGDDALPNGLDVTFEVTEL |
Domain
Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane beta-barrel type structure.
Sequence similarities
Belongs to the SAM50/omp85 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)51,976
- Last updated2006-11-28 v3
- Checksum4F686FB7ACB08DEF
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10 | in Ref. 5; BAD96377 | ||||
Sequence: E → G | ||||||
Sequence conflict | 368-372 | in Ref. 1; AAD34046 | ||||
Sequence: WAGGL → LGRRW | ||||||
Sequence conflict | 371 | in Ref. 8; AAH07830 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF151809 EMBL· GenBank· DDBJ | AAD34046.1 EMBL· GenBank· DDBJ | mRNA | ||
AY189688 EMBL· GenBank· DDBJ | AAO85221.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001087 EMBL· GenBank· DDBJ | BAA91498.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456483 EMBL· GenBank· DDBJ | CAG30369.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222657 EMBL· GenBank· DDBJ | BAD96377.1 EMBL· GenBank· DDBJ | mRNA | ||
AL035398 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471138 EMBL· GenBank· DDBJ | EAW73326.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007830 EMBL· GenBank· DDBJ | AAH07830.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011681 EMBL· GenBank· DDBJ | AAH11681.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015200 EMBL· GenBank· DDBJ | AAH15200.1 EMBL· GenBank· DDBJ | mRNA |