Q92585 · MAML1_HUMAN
- ProteinMastermind-like protein 1
- GeneMAML1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1016 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions.
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 | MAML1-RBP-Jkappa- ICN1 complex | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | peptide antigen binding | |
Molecular Function | protein kinase binding | |
Molecular Function | transcription coactivator activity | |
Biological Process | atrioventricular node cell development | |
Biological Process | atrioventricular node development | |
Biological Process | myoblast differentiation | |
Biological Process | Notch signaling pathway | |
Biological Process | positive regulation of myotube differentiation | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription of Notch receptor target | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMastermind-like protein 1
- Short namesMam-1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92585
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear, in a punctate manner.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_061335 | 583 | in dbSNP:rs41285557 | |||
Sequence: S → N | ||||||
Natural variant | VAR_029010 | 1007 | in dbSNP:rs6895902 | |||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,027 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_0000129493 | 1-1016 | UniProt | Mastermind-like protein 1 | |||
Sequence: MVLPTCPMAEFALPRHSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQAKAKRAGKHRQPPAATAPAPAAPAPRLDAADGPEHGRPATHLHDTVKRNLDSATSPQNGDQQNGYGDLFPGHKKTRREAPLGVAISSNGLPPASPLGQSDKPSGADALQSSGKHSLGLDSLNKKRLADSSLHLNGGSNPSESFPLSLNKELKQEPVEDLPCMITGTVGSISQSNLMPDLNLNEQEWKELIEELNRSVPDEDMKDLFNEDFEEKKDPESSGSATQTPLAQDINIKTEFSPAAFEQEQLGSPQVRAGSAGQTFLGPSSAPVSTDSPSLGGSQTLFHTSGQPRADNPSPNLMPASAQAQNAQRALAGVVLPSQGPGGASELSSAHQLQQIAAKQKREQMLQNPQQATPAPAPGQMSTWQQTGPSHSSLDVPYPMEKPASPSSYKQDFTNSKLLMMPSVNKSSPRPGGPYLQPSHVNLLSHQPPSNLNQNSANNQGSVLDYGNTKPLSHYKADCGQGSPGSGQSKPALMAYLPQQLSHISHEQNSLFLMKPKPGNMPFRSLVPPGQEQNPSSVPVQAQATSVGTQPPAVSVASSHNSSPYLSSQQQAAVMKQHQLLLDQQKQREQQQKHLQQQQFLQRQQHLLAEQEKQQFQRHLTRPPPQYQDPTQGSFPQQVGQFTGSSAAVPGMNTLGPSNSSCPRVFPQAGNLMPMGPGHASVSSLPTNSGQQDRGVAQFPGSQNMPQSSLYGMASGITQIVAQPPPQATNGHAHIPRQTNVGQNTSVSAAYGQNSLGSSGLSQQHNKGTLNPGLTKPPVPRVSPAMGGQNSSWQHQGMPNLSGQTPGNSNVSPFTAASSFHMQQQAHLKMSSPQFSQAVPNRPMAPMSSAAAVGSLLPPVSAQQRTSAPAPAPPPTAPQQGLPGLSPAGPELGAFSQSPASQMGGRAGLHCTQAYPVRTAGQELPFAYSGQPGGSGLSSVAGHTDLIDSLLKNRTSEEWMSDLDDLLGSQ | |||||||
Modified residue | 45 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 120 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 303 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 303 | 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) | 321 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 360 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 360 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 822 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 932 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1015 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1015 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via N-terminus) with NOTCH1, NOTCH2, NOTCH3 and NOTCH4 (via ankyrin repeat region). Interacts (via N-terminus) with p53 (via DNA-binding region). Forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1. Also binds CREBBP/CBP and CDK8.Forms a complex with PRAG1, NOTCH1 and MAML1, in a MAML1-dependent manner (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q92585 | NOTCH1 P46531 | 15 | EBI-908250, EBI-636374 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-123 | Required for interaction with NOTCH proteins | ||||
Sequence: MVLPTCPMAEFALPRHSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQAKAKRAGKHRQPPAATAPAPAAPAPRLDAADGPEHGRPATHLHDTVKRNLDSATSPQN | ||||||
Region | 65-184 | Disordered | ||||
Sequence: QAKAKRAGKHRQPPAATAPAPAAPAPRLDAADGPEHGRPATHLHDTVKRNLDSATSPQNGDQQNGYGDLFPGHKKTRREAPLGVAISSNGLPPASPLGQSDKPSGADALQSSGKHSLGLD | ||||||
Compositional bias | 95-113 | Basic and acidic residues | ||||
Sequence: ADGPEHGRPATHLHDTVKR | ||||||
Compositional bias | 114-129 | Polar residues | ||||
Sequence: NLDSATSPQNGDQQNG | ||||||
Compositional bias | 168-182 | Polar residues | ||||
Sequence: SGADALQSSGKHSLG | ||||||
Compositional bias | 263-283 | Basic and acidic residues | ||||
Sequence: PDEDMKDLFNEDFEEKKDPES | ||||||
Region | 263-487 | Disordered | ||||
Sequence: PDEDMKDLFNEDFEEKKDPESSGSATQTPLAQDINIKTEFSPAAFEQEQLGSPQVRAGSAGQTFLGPSSAPVSTDSPSLGGSQTLFHTSGQPRADNPSPNLMPASAQAQNAQRALAGVVLPSQGPGGASELSSAHQLQQIAAKQKREQMLQNPQQATPAPAPGQMSTWQQTGPSHSSLDVPYPMEKPASPSSYKQDFTNSKLLMMPSVNKSSPRPGGPYLQPSHV | ||||||
Compositional bias | 307-374 | Polar residues | ||||
Sequence: FEQEQLGSPQVRAGSAGQTFLGPSSAPVSTDSPSLGGSQTLFHTSGQPRADNPSPNLMPASAQAQNAQ | ||||||
Compositional bias | 388-439 | Polar residues | ||||
Sequence: GGASELSSAHQLQQIAAKQKREQMLQNPQQATPAPAPGQMSTWQQTGPSHSS | ||||||
Compositional bias | 453-469 | Polar residues | ||||
Sequence: SSYKQDFTNSKLLMMPS | ||||||
Region | 561-617 | Disordered | ||||
Sequence: KPKPGNMPFRSLVPPGQEQNPSSVPVQAQATSVGTQPPAVSVASSHNSSPYLSSQQQ | ||||||
Compositional bias | 573-617 | Polar residues | ||||
Sequence: VPPGQEQNPSSVPVQAQATSVGTQPPAVSVASSHNSSPYLSSQQQ | ||||||
Region | 658-681 | Disordered | ||||
Sequence: EKQQFQRHLTRPPPQYQDPTQGSF | ||||||
Compositional bias | 664-681 | Polar residues | ||||
Sequence: RHLTRPPPQYQDPTQGSF | ||||||
Compositional bias | 796-817 | Polar residues | ||||
Sequence: AYGQNSLGSSGLSQQHNKGTLN | ||||||
Region | 796-953 | Disordered | ||||
Sequence: AYGQNSLGSSGLSQQHNKGTLNPGLTKPPVPRVSPAMGGQNSSWQHQGMPNLSGQTPGNSNVSPFTAASSFHMQQQAHLKMSSPQFSQAVPNRPMAPMSSAAAVGSLLPPVSAQQRTSAPAPAPPPTAPQQGLPGLSPAGPELGAFSQSPASQMGGRA | ||||||
Compositional bias | 831-889 | Polar residues | ||||
Sequence: AMGGQNSSWQHQGMPNLSGQTPGNSNVSPFTAASSFHMQQQAHLKMSSPQFSQAVPNRP |
Domain
The C-terminal region is required for transcriptional activation.
Sequence similarities
Belongs to the mastermind family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,016
- Mass (Da)108,054
- Last updated2005-07-05 v3
- ChecksumC683CB81B73A2A61
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 95-113 | Basic and acidic residues | ||||
Sequence: ADGPEHGRPATHLHDTVKR | ||||||
Compositional bias | 114-129 | Polar residues | ||||
Sequence: NLDSATSPQNGDQQNG | ||||||
Compositional bias | 168-182 | Polar residues | ||||
Sequence: SGADALQSSGKHSLG | ||||||
Compositional bias | 263-283 | Basic and acidic residues | ||||
Sequence: PDEDMKDLFNEDFEEKKDPES | ||||||
Compositional bias | 307-374 | Polar residues | ||||
Sequence: FEQEQLGSPQVRAGSAGQTFLGPSSAPVSTDSPSLGGSQTLFHTSGQPRADNPSPNLMPASAQAQNAQ | ||||||
Compositional bias | 388-439 | Polar residues | ||||
Sequence: GGASELSSAHQLQQIAAKQKREQMLQNPQQATPAPAPGQMSTWQQTGPSHSS | ||||||
Compositional bias | 453-469 | Polar residues | ||||
Sequence: SSYKQDFTNSKLLMMPS | ||||||
Compositional bias | 573-617 | Polar residues | ||||
Sequence: VPPGQEQNPSSVPVQAQATSVGTQPPAVSVASSHNSSPYLSSQQQ | ||||||
Compositional bias | 664-681 | Polar residues | ||||
Sequence: RHLTRPPPQYQDPTQGSF | ||||||
Compositional bias | 796-817 | Polar residues | ||||
Sequence: AYGQNSLGSSGLSQQHNKGTLN | ||||||
Compositional bias | 831-889 | Polar residues | ||||
Sequence: AMGGQNSSWQHQGMPNLSGQTPGNSNVSPFTAASSFHMQQQAHLKMSSPQFSQAVPNRP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D83785 EMBL· GenBank· DDBJ | BAA12114.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF221759 EMBL· GenBank· DDBJ | AAF34658.1 EMBL· GenBank· DDBJ | mRNA |