Q9ULC4 · MCTS1_HUMAN
- ProteinMalignant T-cell-amplified sequence 1
- GeneMCTS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids181 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Translation regulator forming a complex with DENR to promote translation reinitiation. Translation reinitiation is the process where the small ribosomal subunit remains attached to the mRNA following termination of translation of a regulatory upstream ORF (uORF), and resume scanning on the same mRNA molecule to initiate translation of a downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is pivotal to two linked mechanisms essential for translation reinitiation. Firstly, the dissociation of deacylated tRNAs from post-termination 40S ribosomal complexes during ribosome recycling. Secondly, the recruitment in an EIF2-independent manner of aminoacylated initiator tRNA to P site of 40S ribosomes for a new round of translation (PubMed:16982740, PubMed:20713520, PubMed:37875108).
This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent (PubMed:16982740, PubMed:20713520, PubMed:37875108).
Consequently, modulates various unrelated biological processes including cell cycle regulation and DNA damage signaling and repair (PubMed:10440924, PubMed:11709712, PubMed:12637315, PubMed:15897892, PubMed:16322206, PubMed:17016429, PubMed:17416211, PubMed:9766643).
Notably, it positively regulates interferon gamma immunity to mycobacteria by enhancing the translation of JAK2 (PubMed:37875108).
This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent (PubMed:16982740, PubMed:20713520, PubMed:37875108).
Consequently, modulates various unrelated biological processes including cell cycle regulation and DNA damage signaling and repair (PubMed:10440924, PubMed:11709712, PubMed:12637315, PubMed:15897892, PubMed:16322206, PubMed:17016429, PubMed:17416211, PubMed:9766643).
Notably, it positively regulates interferon gamma immunity to mycobacteria by enhancing the translation of JAK2 (PubMed:37875108).
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 | cytoplasm | |
Molecular Function | ribosomal small subunit binding | |
Molecular Function | RNA cap binding | |
Molecular Function | translation factor activity, non-nucleic acid binding | |
Molecular Function | translation initiation factor activity | |
Biological Process | DNA damage response | |
Biological Process | formation of translation preinitiation complex | |
Biological Process | IRES-dependent viral translational initiation | |
Biological Process | ribosome disassembly | |
Biological Process | translation reinitiation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMalignant T-cell-amplified sequence 1
- Short namesMCT-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULC4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear relocalization after DNA damage.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Immunodeficiency 118 (IMD118)
- Note
- DescriptionAn X-linked recessive disorder characterized by increased susceptibility to disseminated mycobacterial infections in infancy, notably after Bacillus Calmette-Guerin (BCG) vaccination. Initial clinical features include fever, lymphadenopathy, hepatosplenomegaly, abscesses, and osteomyelitis. Affected males usually recover with treatment, have no other infections, and show normal growth and development.
- See alsoMIM:301115
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 81 | No phosphorylation by MAPK1; decreased stability of MCTS1 protein; Significant cell growth reduction. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_045632 | 106 | in dbSNP:rs2233110 | |||
Sequence: L → H | ||||||
Mutagenesis | 118 | No phosphorylation by CDK1; No cell growth alteration. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 119 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000344786 | 1-181 | UniProt | Malignant T-cell-amplified sequence 1 | |||
Sequence: MFKKFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQIMPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYPAAVDTIVAIMAEGKQHALCVGVMKMSAEDIEKVNKGIGIENIHYLNDGLWHMKTYK | |||||||
Modified residue | 81 | UniProt | Phosphothreonine; by MAPK1 and MAPK3 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 118 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation is critical for stabilization and promotion of cell proliferation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Over-expressed in T-cell lymphoid cell lines and in non-Hodgkin lymphoma cell lines as well as in a subset of primary large B-cell lymphomas.
Induction
By DNA damaging agents such as gamma irradiation, adriamycin or taxol in lymphoid cells, but not by stress stimuli such as heat shock. This induction of protein expression does not occur at the RNA level, and does not require new protein synthesis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via PUA domain) with DENR; the complex regulates translation reinitiation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ULC4 | DENR O43583 | 10 | EBI-716076, EBI-716083 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 92-171 | PUA | ||||
Sequence: LPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYPAAVDTIVAIMAEGKQHALCVGVMKMSAEDIEKVNKGIGIENIHYLN |
Domain
The PUA RNA-binding domain is critical for cap binding, but not sufficient for translation enhancer function. MCT1 N-terminal region is required to enhance translation possibly through interaction with other proteins.
Sequence similarities
Belongs to the MCTS1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9ULC4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length181
- Mass (Da)20,555
- Last updated2000-05-01 v1
- Checksum2FC00C7A992E24EB
Q9ULC4-2
- Name2
- Differences from canonical
- 1-22: MFKKFDEKENVSNCIQLKTSVI → MENYSFLDKE
Q9ULC4-3
- Name3
- Differences from canonical
- 1-4: MFKK → MGKGR
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB034206 EMBL· GenBank· DDBJ | BAA86055.1 EMBL· GenBank· DDBJ | mRNA | ||
AY364258 EMBL· GenBank· DDBJ | AAQ76817.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294834 EMBL· GenBank· DDBJ | BAG57943.1 EMBL· GenBank· DDBJ | mRNA | ||
AK311993 EMBL· GenBank· DDBJ | BAG34931.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011890 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471107 EMBL· GenBank· DDBJ | EAX11874.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001013 EMBL· GenBank· DDBJ | AAH01013.1 EMBL· GenBank· DDBJ | mRNA | ||
BC095461 EMBL· GenBank· DDBJ | AAH95461.1 EMBL· GenBank· DDBJ | mRNA |