Q9NYF3 · FA53C_HUMAN
- ProteinProtein FAM53C
- GeneFAM53C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids392 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
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 | nucleus | |
Biological Process | protein import into nucleus |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein FAM53C
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NYF3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053089 | 21 | in dbSNP:rs35360938 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 502 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000189546 | 1-392 | UniProt | Protein FAM53C | |||
Sequence: MITLITEQLQKQTLDELKCTRFSISLPLPDHADISNCGNSFQLVSEGASWRGLPHCSCAEFQDSLNFSYHPSGLSLHLRPPSRGNSPKEQPFSQVLRPEPPDPEKLPVPPAPPSKRHCRSLSVPVDLSRWQPVWRPAPSKLWTPIKHRGSGGGGGPQVPHQSPPKRVSSLRFLQAPSASSQCAPAHRPYSPPFFSLALAQDSSRPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPASSPELPWRPRGLRNLPRSRSQPCDLDARKTGVKRRHEEDPRRLRPSLDFDKMNQKPYSGGLCLQETAREGSSISPPWFMACSPPPLSASCSPTGGSSQVLSESEEEEEGAVRWGRQALSKRTLCQRDFGDLDLNLIEEN | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 122 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 254 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 273 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 273 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 299 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NYF3 | DYRK1A Q13627 | 5 | EBI-1644252, EBI-1053596 | |
BINARY | Q9NYF3 | HEL2 V9HW98 | 3 | EBI-1644252, EBI-10190883 | |
BINARY | Q9NYF3 | MEOX2 Q6FHY5 | 3 | EBI-1644252, EBI-16439278 | |
BINARY | Q9NYF3 | NCK2 O43639 | 8 | EBI-1644252, EBI-713635 | |
BINARY | Q9NYF3 | SFN P31947 | 3 | EBI-1644252, EBI-476295 | |
BINARY | Q9NYF3 | SORBS3 O60504 | 3 | EBI-1644252, EBI-741237 | |
BINARY | Q9NYF3 | YWHAG P61981 | 9 | EBI-1644252, EBI-359832 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 78-119 | Disordered | ||||
Sequence: LRPPSRGNSPKEQPFSQVLRPEPPDPEKLPVPPAPPSKRHCR | ||||||
Compositional bias | 94-114 | Pro residues | ||||
Sequence: QVLRPEPPDPEKLPVPPAPPS | ||||||
Region | 141-167 | Disordered | ||||
Sequence: LWTPIKHRGSGGGGGPQVPHQSPPKRV | ||||||
Compositional bias | 204-254 | Polar residues | ||||
Sequence: RPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPAS | ||||||
Region | 204-294 | Disordered | ||||
Sequence: RPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPASSPELPWRPRGLRNLPRSRSQPCDLDARKTGVKRRHEEDPR | ||||||
Compositional bias | 275-294 | Basic and acidic residues | ||||
Sequence: PCDLDARKTGVKRRHEEDPR | ||||||
Region | 341-364 | Disordered | ||||
Sequence: ASCSPTGGSSQVLSESEEEEEGAV |
Sequence similarities
Belongs to the FAM53 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length392
- Mass (Da)43,091
- Last updated2000-10-01 v1
- Checksum28ED288D94D81073
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 94-114 | Pro residues | ||||
Sequence: QVLRPEPPDPEKLPVPPAPPS | ||||||
Compositional bias | 204-254 | Polar residues | ||||
Sequence: RPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPAS | ||||||
Compositional bias | 275-294 | Basic and acidic residues | ||||
Sequence: PCDLDARKTGVKRRHEEDPR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF251040 EMBL· GenBank· DDBJ | AAF63766.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315567 EMBL· GenBank· DDBJ | BAG37942.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62143.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471062 EMBL· GenBank· DDBJ | EAW62144.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000259 EMBL· GenBank· DDBJ | AAH00259.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052993 EMBL· GenBank· DDBJ | AAH52993.1 EMBL· GenBank· DDBJ | mRNA |