Q9Y496 · KIF3A_HUMAN
- ProteinKinesin-like protein KIF3A
- GeneKIF3A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids699 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation. Plays a role in centriole cohesion and subdistal appendage organization and function. Regulates the formation of the subdistal appendage via recruitment of DCTN1 to the centriole. Also required for ciliary basal feet formation and microtubule anchoring to mother centriole.
Features
Showing features for binding site.
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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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin-like protein KIF3A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y496
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the subdistal appendage region of the centriole.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055319 | 172 | in dbSNP:rs17854353 | |||
Sequence: K → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 615 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000125393 | 1-699 | UniProt | Kinesin-like protein KIF3A | |||
Sequence: MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKEKDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 386 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 633 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 687 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 687 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Heterodimer of KIF3A and KIF3B (By similarity).
Interacts with CIMAP3 (PubMed:20643351).
Interacts with CLN3 (PubMed:22261744).
Interacts with DCTN1 (By similarity).
Interacts with FLCN (PubMed:27072130).
Interacts with AP3B1 (PubMed:19934039).
Interacts with CIMAP3 (PubMed:20643351).
Interacts with CLN3 (PubMed:22261744).
Interacts with DCTN1 (By similarity).
Interacts with FLCN (PubMed:27072130).
Interacts with AP3B1 (PubMed:19934039).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y496 | AP3B1 O00203-1 | 5 | EBI-1104844, EBI-15816315 | |
BINARY | Q9Y496 | DISC1 Q9NRI5 | 5 | EBI-1104844, EBI-529989 | |
BINARY | Q9Y496 | KIFAP3 Q92845 | 11 | EBI-1104844, EBI-954040 | |
BINARY | Q9Y496 | RAB11FIP5 Q9BXF6 | 2 | EBI-1104844, EBI-1387068 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-345 | Kinesin motor | ||||
Sequence: NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNI | ||||||
Coiled coil | 355-590 | |||||
Sequence: PKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQML | ||||||
Region | 372-421 | Disordered | ||||
Sequence: KKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIE | ||||||
Compositional bias | 382-398 | Acidic residues | ||||
Sequence: GSDISGSEEDDDEEGEV | ||||||
Region | 663-699 | Disordered | ||||
Sequence: SLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ | ||||||
Region | 697-699 | Globular | ||||
Sequence: LLQ |
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length699
- Mass (Da)80,041
- Last updated2010-05-18 v4
- ChecksumA0BF5BB1F699DF12
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J9X2 | C9J9X2_HUMAN | KIF3A | 169 | ||
J3KPF9 | J3KPF9_HUMAN | KIF3A | 702 | ||
H7C2F6 | H7C2F6_HUMAN | KIF3A | 185 | ||
E9PES4 | E9PES4_HUMAN | KIF3A | 726 | ||
A0A087X011 | A0A087X011_HUMAN | KIF3A | 725 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 151 | in Ref. 4; AAH45542 | ||||
Sequence: E → G | ||||||
Sequence conflict | 170 | in Ref. 1; AAC72294 | ||||
Sequence: E → A | ||||||
Compositional bias | 382-398 | Acidic residues | ||||
Sequence: GSDISGSEEDDDEEGEV | ||||||
Sequence conflict | 409 | in Ref. 2; BAD93017 | ||||
Sequence: R → RDQA | ||||||
Sequence conflict | 409 | in Ref. 4; AAH45542 | ||||
Sequence: R → RDQT | ||||||
Sequence conflict | 409 | in Ref. 1; AAC72294 | ||||
Sequence: R → RIQI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF041853 EMBL· GenBank· DDBJ | AAC72294.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209780 EMBL· GenBank· DDBJ | BAD93017.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC004039 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004237 EMBL· GenBank· DDBJ | AAC04475.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC045542 EMBL· GenBank· DDBJ | AAH45542.1 EMBL· GenBank· DDBJ | mRNA |