Q5PRF9 · SMAG2_HUMAN
- ProteinProtein Smaug homolog 2
- GeneSAMD4B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids694 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A.
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 | cytosol | |
Cellular Component | nucleus | |
Cellular Component | P-body | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | translation repressor activity | |
Biological Process | nuclear-transcribed mRNA poly(A) tail shortening |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein Smaug homolog 2
- Short namesSmaug 2; hSmaug2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5PRF9
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 680 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_0000260080 | 1-694 | UniProt | Protein Smaug homolog 2 | |||
Sequence: MMFRDQVGILAGWFKGWNECEQTVALLSLLKRVTRTQARFLQLCLEHSLADCNDIHLLESEANSAAIVSQWQQESKEKVVSLLLSHLPLLQPGNTEAKSEYMRLLQKVLAYSIESNAFIEESRQLLSYALIHPATTLEDRNALALWLSHLEERLASGFRSRPEPSYHSRQGSDEWGGPAELGPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSNANTGLPCQIHPSPLKRSMSLIPTSPQVPGEWPSPEELGARAAFTTPDHAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRERQSVLKSLEKDVLEGGNLRNALQELQQIIITPIKAYSVLQATVAAATTTPTAKDGAPGEPPLPGAEPPLAHPGTDKGTEAKDPPAVENYPPPPAPAPTDGSEPAPAPVADGDIPSQFTRVMGKVCTQLLVSRPDEENITSYLQLIEKCLTHEAFTETQKKRLLSWKQQVLKLLRTFPRKAALEMQNYRQQKGWAFGSNSLPIAGSVGMGVARRTQRQFPMPPRALPPGRMGLLSPSGIGGVSPRHALTSPSLGGQGRQNLWFANPGGSNSMPSQSRSSVQRTHSLPVHSSPQAILMFPPDCPVPGPDLEINPTLESLCLSMTEHALGDGTDKTSTI | |||||||
Modified residue | 172 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 242 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 243 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 271 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 278 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 281 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 407 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 555 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 555 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 557 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 557 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 563 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 592 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 600 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 602 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 606 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 607 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 626 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 628 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 628 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed in embryonic and adult tissues.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5PRF9 | BCL2L10 Q9HD36 | 3 | EBI-1047489, EBI-2126349 | |
BINARY | Q5PRF9 | CCDC179 H3BU77 | 3 | EBI-1047489, EBI-17766379 | |
BINARY | Q5PRF9 | LRRC8E Q6NSJ5 | 3 | EBI-1047489, EBI-8647013 | |
BINARY | Q5PRF9 | RSRC2 Q7L4I2 | 3 | EBI-1047489, EBI-953753 | |
BINARY | Q5PRF9 | USP53 Q70EK8 | 3 | EBI-1047489, EBI-742050 | |
BINARY | Q5PRF9 | YWHAE P62258 | 6 | EBI-1047489, EBI-356498 | |
BINARY | Q5PRF9 | YWHAZ P63104 | 3 | EBI-1047489, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 158-301 | Disordered | ||||
Sequence: FRSRPEPSYHSRQGSDEWGGPAELGPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSNANTGLPCQIHPSPLKRSMSLIPTSPQVPGEWPSPEELGARAAFTTPDHAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGSGM | ||||||
Compositional bias | 208-226 | Polar residues | ||||
Sequence: SVPPAINSIGSNANTGLPC | ||||||
Compositional bias | 267-299 | Polar residues | ||||
Sequence: HAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGS | ||||||
Domain | 299-372 | SAM | ||||
Sequence: SGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRERQSVLKSLEKDVLE | ||||||
Region | 407-471 | Disordered | ||||
Sequence: TPTAKDGAPGEPPLPGAEPPLAHPGTDKGTEAKDPPAVENYPPPPAPAPTDGSEPAPAPVADGDI | ||||||
Compositional bias | 443-460 | Pro residues | ||||
Sequence: AVENYPPPPAPAPTDGSE | ||||||
Region | 607-643 | Disordered | ||||
Sequence: SPSLGGQGRQNLWFANPGGSNSMPSQSRSSVQRTHSL |
Sequence similarities
Belongs to the SMAUG family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length694
- Mass (Da)75,483
- Last updated2005-01-04 v1
- Checksum4AA4769F38494E56
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 208-226 | Polar residues | ||||
Sequence: SVPPAINSIGSNANTGLPC | ||||||
Compositional bias | 267-299 | Polar residues | ||||
Sequence: HAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGS | ||||||
Compositional bias | 443-460 | Pro residues | ||||
Sequence: AVENYPPPPAPAPTDGSE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EF601121 EMBL· GenBank· DDBJ | ABQ85549.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471126 EMBL· GenBank· DDBJ | EAW56877.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC054518 EMBL· GenBank· DDBJ | AAH54518.1 EMBL· GenBank· DDBJ | mRNA | ||
BC065211 EMBL· GenBank· DDBJ | AAH65211.1 EMBL· GenBank· DDBJ | mRNA |