Q62909 · KIF2C_RAT
- ProteinKinesin-like protein KIF2C
- GeneKif2c
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids671 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment.
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
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin-like protein KIF2C
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ62909
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1. Association with microtubule plus ends is also mediated by interaction with KIF18B. Centromeric localization requires the presence of BUB1 and SGO2.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000125421 | 1-671 | Kinesin-like protein KIF2C | |||
Sequence: MIDIDDVAAINPELVQLLPLRPKDSLPLQENVTIPKQKRKSVNSKIPGPKEGLRSRSTRISTVSEVRIPAQENEMEVELPVSTNSRKPFPIHTGHPRPSCSTVTELPLLMISEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSEIRIKRAQEYDNSFPNWEFARMIKEFRVTMDCNPLTVTDPIEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRSLNLEVYVTFFEIYNGKVFELLNKKAKLRVLEDSKQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRAKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKESIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQAVQMETEEMDASSHGASLTGNEEEELSSQMSSFNEAMTQIRELEERAMEELREIIQQGPSWLELSEMTDQPDYDLETFVNKAESALTQQAKQAKHFSALQEVIKALRLAMQLEEQASKQINSKKRHQ | ||||||
Modified residue | 41 | Phosphoserine; by AURKB | ||||
Sequence: S | ||||||
Modified residue | 55 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 57 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 61 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 112 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 121 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 133 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 138 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 465 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 576 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation by AURKB, regulates association with centromeres and kinetochores and the microtubule depolymerization activity.
Ubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Testis. Localized to the meiotically active cells of the seminiferous epithelia in the testis.
Interaction
Subunit
Interacts with CENPH. Interacts with MTUS2/TIP150; the interaction is direct. Interacts with MAPRE1; the interaction is direct, regulated by phosphorylation and is probably required for targeting to growing microtubule plus ends. Interacts with KIF18B at microtubule tips; this interaction increases the affinity of both partners for microtubule plus ends and is required for robust microtubule depolymerization. Phosphorylation by AURKA or AURKB strongly reduces KIF18B-binding.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif, domain, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-200 | Globular | ||||
Sequence: MIDIDDVAAINPELVQLLPLRPKDSLPLQENVTIPKQKRKSVNSKIPGPKEGLRSRSTRISTVSEVRIPAQENEMEVELPVSTNSRKPFPIHTGHPRPSCSTVTELPLLMISEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSEIRIKRAQEYDNSFPNWEFARMIKEFRVTMDCNPLTVTDPI | ||||||
Region | 37-58 | Disordered | ||||
Sequence: QKRKSVNSKIPGPKEGLRSRST | ||||||
Motif | 44-47 | Microtubule tip localization signal | ||||
Sequence: SKIP | ||||||
Region | 115-138 | Disordered | ||||
Sequence: AEEQAHSTRSTSSANPGNSVRRKS | ||||||
Region | 153-184 | Negative regulator of microtubule-binding | ||||
Sequence: EKRAQNSEIRIKRAQEYDNSFPNWEFARMIKE | ||||||
Domain | 204-534 | Kinesin motor | ||||
Sequence: RICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRSLNLEVYVTFFEIYNGKVFELLNKKAKLRVLEDSKQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRAKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKESIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKEL | ||||||
Region | 533-568 | Disordered | ||||
Sequence: ELSPHSGPSGEQAVQMETEEMDASSHGASLTGNEEE | ||||||
Compositional bias | 540-568 | Polar residues | ||||
Sequence: PSGEQAVQMETEEMDASSHGASLTGNEEE | ||||||
Coiled coil | 566-601 | |||||
Sequence: EEEELSSQMSSFNEAMTQIRELEERAMEELREIIQQ |
Domain
The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length671
- Mass (Da)75,572
- Last updated2010-04-20 v3
- ChecksumD3CE21F711F88506
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 540-568 | Polar residues | ||||
Sequence: PSGEQAVQMETEEMDASSHGASLTGNEEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U44979 EMBL· GenBank· DDBJ | AAC53528.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |