Q92845 · KIFA3_HUMAN
- ProteinKinesin-associated protein 3
- GeneKIFAP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids792 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex (By similarity).
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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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin-associated protein 3
- Short namesKAP-3; KAP3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92845
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
- axoneme
- centrosome
- ciliary basal body
- ciliary tip
- ciliary transition zone
- cilium
- condensed nuclear chromosome
- cytosol
- endoplasmic reticulum
- Golgi apparatus
- kinesin II complex
- microtubule cytoskeleton
- periciliary membrane compartment
- photoreceptor connecting cilium
- photoreceptor inner segment
- photoreceptor outer segment
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051081 | 513 | in dbSNP:rs12075833 | |||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 736 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_0000084302 | 1-792 | UniProt | Kinesin-associated protein 3 | |||
Sequence: MQGEDARYLKRKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQLLYYLQNRRDSLSGKEKKEKSSKPKDPPPFEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELLLNETALGALARVLREDWKQSVELATNIIYIFFCFSSFSQFHGLITHYKIGALCMNIIDHELKRHELWQEELSKKKKAVDEDPENQTLRKDYEKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMRNKNIVHMLVKALDRDNFELLILVVSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNDNYKQIAMCVLYHISMDDRFKSMFAYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKFKDPLLMKMIRNISQHDGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTIPDLDWELVLKEYKLVPYLKDKLKPGAAEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIRKVCDNTLDIIAEYDEEWAKKIQSEKFRWHNSQWLEMVESRQMDESEQYLYGDDRIEPYIHEGDILERPDLFYNSDGLIASEGAISPDFFNDYHLQNGDVVGQHSFPGSLGMDGFGQPVGILGRPATAYGFRPDEPYYYGYGS | |||||||
Modified residue | 60 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on tyrosine residues by SRC in vitro; this reduces the binding affinity of the protein for RAP1GDS1.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterotrimer of KIFAP3, KIF3A and KIF3B. Interacts with RAP1GDS1/SMG GDS. Interacts with SMC3 subunit of the cohesin complex.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q92845 | C19orf44 Q9H6X5-2 | 3 | EBI-954040, EBI-12061599 | |
BINARY | Q92845 | HOXB5 P09067 | 3 | EBI-954040, EBI-3893317 | |
BINARY | Q92845 | KANK2 Q63ZY3 | 3 | EBI-954040, EBI-2556193 | |
BINARY | Q92845 | KIF3A Q9Y496 | 11 | EBI-954040, EBI-1104844 | |
BINARY | Q92845 | KIF3B O15066 | 10 | EBI-954040, EBI-3931791 | |
BINARY | Q92845 | MOS P00540 | 3 | EBI-954040, EBI-1757866 | |
BINARY | Q92845 | MYPOP Q86VE0 | 3 | EBI-954040, EBI-2858213 | |
BINARY | Q92845 | NAA10 P41227 | 7 | EBI-954040, EBI-747693 | |
BINARY | Q92845 | NAA11 Q9BSU3 | 3 | EBI-954040, EBI-2585120 | |
BINARY | Q92845 | NCF2 P19878 | 14 | EBI-954040, EBI-489611 | |
BINARY | Q92845 | RTP5 Q14D33 | 3 | EBI-954040, EBI-10217913 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 103-123 | Basic and acidic residues | ||||
Sequence: LSGKEKKEKSSKPKDPPPFEG | ||||||
Region | 103-124 | Disordered | ||||
Sequence: LSGKEKKEKSSKPKDPPPFEGM | ||||||
Repeat | 333-373 | ARM 1 | ||||
Sequence: FMENKNDMVEMDIVEKLVKMIPCEHEDLLNITLRLLLNLSF | ||||||
Repeat | 374-412 | ARM 2 | ||||
Sequence: DTGLRNKMVQVGLLPKLTALLGNDNYKQIAMCVLYHISM | ||||||
Repeat | 494-533 | ARM 3 | ||||
Sequence: DGPTKNLFIDYVGDLAAQISNDEEEEFVIECLGTLANLTI | ||||||
Repeat | 578-620 | ARM 4 | ||||
Sequence: DDSCAALLAKSGIIPALIELLNAQQEDDEFVCQIIYVFYQMVF | ||||||
Repeat | 621-662 | ARM 5 | ||||
Sequence: HQATRDVIIKETQAPAYLIDLMHDKNNEIRKVCDNTLDIIAE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q92845-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length792
- Mass (Da)91,205
- Last updated2005-08-30 v2
- Checksum1887A75D811DF56A
Q92845-2
- Name2
- Differences from canonical
- 11-55: RKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKI → S
Q92845-3
- Name3
- Differences from canonical
- 1-40: Missing
Q92845-4
- Name4
- Differences from canonical
- 1-106: MQGEDARYLKRKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQLLYYLQNRRDSLSGK → MSIALGNTYRRSLSDSETVSVLQASLCE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAQ5BGI3 | A0AAQ5BGI3_HUMAN | KIFAP3 | 807 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047133 | 1-40 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047132 | 1-106 | in isoform 4 | |||
Sequence: MQGEDARYLKRKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQLLYYLQNRRDSLSGK → MSIALGNTYRRSLSDSETVSVLQASLCE | ||||||
Alternative sequence | VSP_044505 | 11-55 | in isoform 2 | |||
Sequence: RKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKI → S | ||||||
Sequence conflict | 91 | in Ref. 1; AAC50788 | ||||
Sequence: Q → L | ||||||
Compositional bias | 103-123 | Basic and acidic residues | ||||
Sequence: LSGKEKKEKSSKPKDPPPFEG | ||||||
Sequence conflict | 734 | in Ref. 2; BAH13889 | ||||
Sequence: I → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U59919 EMBL· GenBank· DDBJ | AAC50788.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297368 EMBL· GenBank· DDBJ | BAH12562.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303052 EMBL· GenBank· DDBJ | BAH13889.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315586 EMBL· GenBank· DDBJ | BAG37958.1 EMBL· GenBank· DDBJ | mRNA | ||
AL356475 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL121714 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471067 EMBL· GenBank· DDBJ | EAW90872.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471067 EMBL· GenBank· DDBJ | EAW90873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471067 EMBL· GenBank· DDBJ | EAW90871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC028679 EMBL· GenBank· DDBJ | AAH28679.1 EMBL· GenBank· DDBJ | mRNA |