Q8TC05 · MDM1_HUMAN
- ProteinNuclear protein MDM1
- GeneMDM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids714 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules (PubMed:26337392).
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 | centriolar satellite | |
Cellular Component | centriole | |
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Cellular Component | microtubule | |
Cellular Component | nucleus | |
Molecular Function | microtubule binding | |
Biological Process | negative regulation of centriole replication | |
Biological Process | retina development in camera-type eye |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear protein MDM1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TC05
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the centriole lumen.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 9-15 | Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 189-A--A-195; 232-A--A-238 and 306-A--A-312. | ||||
Sequence: SEYQRNF → AAAQRNA | ||||||
Natural variant | VAR_034782 | 103 | in dbSNP:rs962976 | |||
Sequence: T → I | ||||||
Mutagenesis | 189-195 | Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 9-A--A-15; 232-A--A-238 and 306-A--A-312. | ||||
Sequence: SEYQRQF → AAAQRQA | ||||||
Mutagenesis | 232-238 | Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 9-A--A-15; 189-A--A-195 and 306-A--A-312. | ||||
Sequence: TEYKRNF → AAAKRNA | ||||||
Mutagenesis | 306-312 | Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 9-A--A-15; 189-A--A-195 and 232-A--A-238. | ||||
Sequence: SEYRAKF → AAARAKA | ||||||
Natural variant | VAR_034783 | 383 | in dbSNP:rs17224810 | |||
Sequence: V → I | ||||||
Natural variant | VAR_034784 | 489 | in dbSNP:rs2306393 | |||
Sequence: R → H | ||||||
Natural variant | VAR_034785 | 552 | in dbSNP:rs2306392 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 862 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000299059 | 1-714 | UniProt | Nuclear protein MDM1 | |||
Sequence: MPVRFKGLSEYQRNFLWKKSYLSESCNSSVGRKYPWAGLRSDQLGITKEPSFISKRRVPYHDPQISKSLEWNGAISESNVVASPEPEAPETPKSQEAEQKDVTQERVHSLEASRVPKRTRSHSADSRAEGASDVENNEGVTNHTPVNENVELEHSTKVLSENVDNGLDRLLRKKAGLTVVPSYNALRNSEYQRQFVWKTSKETAPAFAANQVFHNKSQFVPPFKGNSVIHETEYKRNFKGLSPVKEPKLRNDLRENRNLETVSPERKSNKIDDRLKLEAEMELKDLHQPKRKLTPWKHQRLGKVNSEYRAKFLSPAQYLYKAGAWTHVKGNMPNQVKELREKAEFYRKRVQGTHFSRDHLNQILSDSNCCWDVSSTTSSEGTVSSNIRALDLAGDPTSHKTLQKCPSTEPEEKGNIVEEQPQKNTTEKLGVSAPTIPVRRRLAWDTENTSEDVQKQPGEKEEEDDNEEEGDRKTGKQAFMGEQEKLDVREKSKADKMKEGSDSSVSSEKGGRLPTPKLRELGGIQRTHHDLTTPAVGGAVLVSPSKMKPPAPEQRKRMTSQDCLETSKNDFTKKESRAVSLLTSPAAGIKTVDPLPLREDSEDNIHKFAEATLPVSKIPKYPTNPPGQLPSPPHVPSYWHPSRRIQGSLRDPEFQHNVGKARMNNLQLPQHEAFNDEDEDRLSEISARSAASSLRAFQTLARAKKRKENFWGKT | |||||||
Modified residue | 83 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 123 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 126 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 242 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 263 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 314 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 543 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 560 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 584 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 631 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 648 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 648 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 683 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 686 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TC05 | CCDC57 Q2TAC2-2 | 3 | EBI-3951677, EBI-10961624 | |
BINARY | Q8TC05 | HOMER3 Q9NSC5 | 3 | EBI-3951677, EBI-748420 | |
BINARY | Q8TC05 | POC1A Q8NBT0 | 2 | EBI-3951677, EBI-2557132 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 9-15 | ST]-E-Y-X3-F motif 1; required for efficient microtubule binding and stabilization | ||||
Sequence: SEYQRNF | ||||||
Region | 79-152 | Disordered | ||||
Sequence: NVVASPEPEAPETPKSQEAEQKDVTQERVHSLEASRVPKRTRSHSADSRAEGASDVENNEGVTNHTPVNENVEL | ||||||
Compositional bias | 91-132 | Basic and acidic residues | ||||
Sequence: TPKSQEAEQKDVTQERVHSLEASRVPKRTRSHSADSRAEGAS | ||||||
Compositional bias | 135-152 | Polar residues | ||||
Sequence: ENNEGVTNHTPVNENVEL | ||||||
Motif | 189-195 | ST]-E-Y-X3-F motif 2; required for efficient microtubule binding and stabilization | ||||
Sequence: SEYQRQF | ||||||
Motif | 232-238 | ST]-E-Y-X3-F motif 3; required for efficient microtubule binding and stabilization | ||||
Sequence: TEYKRNF | ||||||
Motif | 306-312 | ST]-E-Y-X3-F motif 4; required for efficient microtubule binding and stabilization | ||||
Sequence: SEYRAKF | ||||||
Region | 391-571 | Disordered | ||||
Sequence: DLAGDPTSHKTLQKCPSTEPEEKGNIVEEQPQKNTTEKLGVSAPTIPVRRRLAWDTENTSEDVQKQPGEKEEEDDNEEEGDRKTGKQAFMGEQEKLDVREKSKADKMKEGSDSSVSSEKGGRLPTPKLRELGGIQRTHHDLTTPAVGGAVLVSPSKMKPPAPEQRKRMTSQDCLETSKNDF | ||||||
Compositional bias | 444-460 | Basic and acidic residues | ||||
Sequence: WDTENTSEDVQKQPGEK | ||||||
Compositional bias | 469-505 | Basic and acidic residues | ||||
Sequence: EGDRKTGKQAFMGEQEKLDVREKSKADKMKEGSDSSV | ||||||
Compositional bias | 550-571 | Basic and acidic residues | ||||
Sequence: PAPEQRKRMTSQDCLETSKNDF | ||||||
Region | 616-637 | Disordered | ||||
Sequence: SKIPKYPTNPPGQLPSPPHVPS | ||||||
Compositional bias | 619-637 | Pro residues | ||||
Sequence: PKYPTNPPGQLPSPPHVPS |
Sequence similarities
Belongs to the MDM1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8TC05-1
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
- Length714
- Mass (Da)80,735
- Last updated2007-08-21 v2
- Checksum301E3A89A5BFF13B
Q8TC05-2
- Name2
Q8TC05-3
- Name3
Q8TC05-4
- Name4
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YGX6 | H0YGX6_HUMAN | MDM1 | 121 | ||
H0Y301 | H0Y301_HUMAN | MDM1 | 30 | ||
A0A804HIJ5 | A0A804HIJ5_HUMAN | MDM1 | 724 | ||
F5H804 | F5H804_HUMAN | MDM1 | 46 | ||
F5H529 | F5H529_HUMAN | MDM1 | 280 |
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 42 | in Ref. 2; BAG59777 | ||||
Sequence: D → Y | ||||||
Alternative sequence | VSP_027544 | 46-69 | in isoform 3 | |||
Sequence: ITKEPSFISKRRVPYHDPQISKSL → NQGRCRTKIQHSDISSLLILVCST | ||||||
Alternative sequence | VSP_027545 | 70-714 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 91-132 | Basic and acidic residues | ||||
Sequence: TPKSQEAEQKDVTQERVHSLEASRVPKRTRSHSADSRAEGAS | ||||||
Compositional bias | 135-152 | Polar residues | ||||
Sequence: ENNEGVTNHTPVNENVEL | ||||||
Alternative sequence | VSP_046400 | 167-211 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_027546 | 167-222 | in isoform 2 | |||
Sequence: LDRLLRKKAGLTVVPSYNALRNSEYQRQFVWKTSKETAPAFAANQVFHNKSQFVPP → VGIFTAFLFKSIEFFIGFIVISVILHFVFQNFPLLFSCLMSIRIVDNRLLTLVIVN | ||||||
Alternative sequence | VSP_027547 | 223-714 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_046401 | 335 | in isoform 4 | |||
Sequence: Q → QGSLNAMWYAE | ||||||
Compositional bias | 444-460 | Basic and acidic residues | ||||
Sequence: WDTENTSEDVQKQPGEK | ||||||
Sequence conflict | 458 | in Ref. 2; BAG59777 | ||||
Sequence: G → E | ||||||
Compositional bias | 469-505 | Basic and acidic residues | ||||
Sequence: EGDRKTGKQAFMGEQEKLDVREKSKADKMKEGSDSSV | ||||||
Compositional bias | 550-571 | Basic and acidic residues | ||||
Sequence: PAPEQRKRMTSQDCLETSKNDF | ||||||
Compositional bias | 619-637 | Pro residues | ||||
Sequence: PKYPTNPPGQLPSPPHVPS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF267851 EMBL· GenBank· DDBJ | AAF78952.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297311 EMBL· GenBank· DDBJ | BAG59777.1 EMBL· GenBank· DDBJ | mRNA | ||
AC022511 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC022042 EMBL· GenBank· DDBJ | AAH22042.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028355 EMBL· GenBank· DDBJ | AAH28355.1 EMBL· GenBank· DDBJ | mRNA | ||
AF007130 EMBL· GenBank· DDBJ | AAC19149.1 EMBL· GenBank· DDBJ | mRNA |