A0A8I5KTA5 · A0A8I5KTA5_HUMAN
- ProteinRAF proto-oncogene serine/threonine-protein kinase
- GeneRAF1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids611 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]This reaction proceeds in the forward direction.
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 | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | positive regulation of macromolecule metabolic process | |
Biological Process | protein modification process | |
Biological Process | regulation of protein modification process | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRAF proto-oncogene serine/threonine-protein kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A8I5KTA5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,705 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 210 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 256 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 324 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 575 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 582 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 587 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 604 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-131 | RBD | ||||
Sequence: NTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFL | ||||||
Domain | 138-184 | Phorbol-ester/DAG-type | ||||
Sequence: THNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMC | ||||||
Region | 205-234 | Disordered | ||||
Sequence: FTFNTSSPSSEGSLSQRQRSTSTPNVHMVS | ||||||
Region | 248-301 | Disordered | ||||
Sequence: IRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRG | ||||||
Compositional bias | 251-277 | Polar residues | ||||
Sequence: HSESASPSALSSSPNNLSPTGWSQPKT | ||||||
Domain | 316-572 | Protein kinase | ||||
Sequence: VMLSTRIGSGSFGTVYKGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length611
- Mass (Da)69,005
- Last updated2022-05-25 v1
- ChecksumBDF56A69B899DFE1
Computationally mapped potential isoform sequences
There are 26 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P04049 | RAF1_HUMAN | RAF1 | 648 | ||
A0A8I5QJG5 | A0A8I5QJG5_HUMAN | RAF1 | 78 | ||
A0A8I5QKZ6 | A0A8I5QKZ6_HUMAN | RAF1 | 589 | ||
A0A8I5QKU8 | A0A8I5QKU8_HUMAN | RAF1 | 499 | ||
A0A0S2Z4L5 | A0A0S2Z4L5_HUMAN | RAF1 | 615 | ||
H7C155 | H7C155_HUMAN | RAF1 | 421 | ||
A0A8I5KQ33 | A0A8I5KQ33_HUMAN | RAF1 | 346 | ||
A0A8I5KS16 | A0A8I5KS16_HUMAN | RAF1 | 494 | ||
A0A8I5KSM4 | A0A8I5KSM4_HUMAN | RAF1 | 152 | ||
A0A8I5KSI1 | A0A8I5KSI1_HUMAN | RAF1 | 156 | ||
A0A8I5KSB0 | A0A8I5KSB0_HUMAN | RAF1 | 573 | ||
A0A8I5KQV4 | A0A8I5KQV4_HUMAN | RAF1 | 611 | ||
A0A8I5KR46 | A0A8I5KR46_HUMAN | RAF1 | 193 | ||
A0A0B4J1W9 | A0A0B4J1W9_HUMAN | RAF1 | 87 | ||
A0A8I5KRD1 | A0A8I5KRD1_HUMAN | RAF1 | 109 | ||
A0A8I5KSV6 | A0A8I5KSV6_HUMAN | RAF1 | 644 | ||
A0A8I5KT32 | A0A8I5KT32_HUMAN | RAF1 | 341 | ||
A0A8I5KTK4 | A0A8I5KTK4_HUMAN | RAF1 | 374 | ||
A0A8I5KWA9 | A0A8I5KWA9_HUMAN | RAF1 | 287 | ||
A0A8I5KWS9 | A0A8I5KWS9_HUMAN | RAF1 | 91 | ||
A0A8I5KX50 | A0A8I5KX50_HUMAN | RAF1 | 69 | ||
A0A8I5KWF7 | A0A8I5KWF7_HUMAN | RAF1 | 273 | ||
A0A8I5KUW4 | A0A8I5KUW4_HUMAN | RAF1 | 80 | ||
A0A8I5KW44 | A0A8I5KW44_HUMAN | RAF1 | 278 | ||
A0A8I5KYC4 | A0A8I5KYC4_HUMAN | RAF1 | 486 | ||
A0A8I5KYP5 | A0A8I5KYP5_HUMAN | RAF1 | 382 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 251-277 | Polar residues | ||||
Sequence: HSESASPSALSSSPNNLSPTGWSQPKT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC018500 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC026170 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |