P52732 · KIF11_HUMAN
- ProteinKinesin-like protein KIF11
- GeneKIF11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1056 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Motor protein required for establishing a bipolar spindle and thus contributing to chromosome congression during mitosis (PubMed:19001501, PubMed:37728657).
Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769).
Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769).
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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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | kinesin complex | |
Cellular Component | membrane | |
Cellular Component | microtubule | |
Cellular Component | mitotic spindle | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Cellular Component | spindle | |
Cellular Component | spindle pole | |
Molecular Function | ATP binding | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule motor activity | |
Molecular Function | plus-end-directed microtubule motor activity | |
Molecular Function | protein kinase binding | |
Biological Process | cell division | |
Biological Process | microtubule-based movement | |
Biological Process | mitotic cell cycle | |
Biological Process | mitotic centrosome separation | |
Biological Process | mitotic spindle assembly | |
Biological Process | mitotic spindle organization | |
Biological Process | regulation of mitotic centrosome separation | |
Biological Process | spindle elongation | |
Biological Process | spindle organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin-like protein KIF11
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP52732
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Microcephaly with or without chorioretinopathy, lymphedema, or impaired intellectual development (MCLMR)
- Note
- DescriptionAn autosomal dominant disorder that involves an overlapping but variable spectrum of central nervous system and ocular developmental anomalies. Microcephaly ranges from mild to severe and is often associated with mild to moderate developmental delay and a characteristic facial phenotype with upslanting palpebral fissures, broad nose with rounded tip, long philtrum with thin upper lip, prominent chin, and prominent ears. Chorioretinopathy is the most common eye abnormality, but retinal folds, microphthalmia, and myopic and hypermetropic astigmatism have also been reported, and some individuals have no overt ocular phenotype. Congenital lymphedema, when present, is typically confined to the dorsa of the feet, and lymphoscintigraphy reveals the absence of radioactive isotope uptake from the webspaces between the toes.
- See alsoMIM:152950
Natural variants in MCLMR
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067829 | 144 | F>L | in MCLMR | |
VAR_067830 | 234 | R>C | in MCLMR | |
VAR_067831 | 235 | S>C | in MCLMR; dbSNP:rs387906643 | |
VAR_067832 | 944 | R>C | in MCLMR; dbSNP:rs387906642 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067829 | 144 | in MCLMR | |||
Sequence: F → L | ||||||
Natural variant | VAR_067830 | 234 | in MCLMR | |||
Sequence: R → C | ||||||
Natural variant | VAR_067831 | 235 | in MCLMR; dbSNP:rs387906643 | |||
Sequence: S → C | ||||||
Mutagenesis | 926 | No mitotic phosphorylation. No binding to spindle apparatus. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_067832 | 944 | in MCLMR; dbSNP:rs387906642 | |||
Sequence: R → C | ||||||
Mutagenesis | 1033 | Still binds to the mitotic spindle but mitotic progression is impaired. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1033 | Still binds to the mitotic spindle but mitotic progression is impaired. | ||||
Sequence: S → D | ||||||
Mutagenesis | 1034 | Significantly diminished interaction with TPX2. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_049682 | 1042 | in dbSNP:rs34417963 | |||
Sequence: L → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 863 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000125372 | 1-1056 | UniProt | Kinesin-like protein KIF11 | |||
Sequence: MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 146 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 399 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 458 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 458 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 477 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 540 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 925 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 925 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 926 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 926 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 931 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1033 | UniProt | Phosphoserine; by NEK6 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1033 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 1034 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Phosphorylated exclusively on serine during S phase, but on both serine and Thr-926 during mitosis, so controlling the association of KIF11 with the spindle apparatus (probably during early prophase).
A subset of this protein primarily localized at the spindle pole is phosphorylated by NEK6 during mitosis; phosphorylation is required for mitotic function.
Ubiquitinated at Lys-1034 by UHRF1 via 'Lys-63'-linked ubiquitin chains, leading to interaction with spindle assembly factor TPX2, thereby ensuring accurate distribution to the spindles during metaphase.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with the thyroid hormone receptor in the presence of thyroid hormone. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Interacts (via C-terminus) with the kinase NEK6 in both interphase and mitosis. Interacts with RARRES1 and AGBL2 (PubMed:21303978).
Interacts with TPX2 (PubMed:37728657).
Interacts with TPX2 (PubMed:37728657).
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-359 | Kinesin motor | ||||
Sequence: NIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNI | ||||||
Coiled coil | 364-480 | |||||
Sequence: EVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEY | ||||||
Coiled coil | 736-763 | |||||
Sequence: LEEKCENIQKPLSSVQENIQQKSKDIVN |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,056
- Mass (Da)119,159
- Last updated2006-10-17 v2
- ChecksumC7F2606FE68DA8EA
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7I2YQY4 | A0A7I2YQY4_HUMAN | KIF11 | 673 | ||
A0A7I2V3A9 | A0A7I2V3A9_HUMAN | KIF11 | 987 | ||
A0A7I2V3V3 | A0A7I2V3V3_HUMAN | KIF11 | 533 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 674-675 | in Ref. 1; CAA59449 | ||||
Sequence: EL → RNS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X85137 EMBL· GenBank· DDBJ | CAA59449.1 EMBL· GenBank· DDBJ | mRNA | ||
U37426 EMBL· GenBank· DDBJ | AAA86132.1 EMBL· GenBank· DDBJ | mRNA | ||
AL360222 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL356128 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC126211 EMBL· GenBank· DDBJ | AAI26212.1 EMBL· GenBank· DDBJ | mRNA | ||
BC136474 EMBL· GenBank· DDBJ | AAI36475.1 EMBL· GenBank· DDBJ | mRNA | ||
L40372 EMBL· GenBank· DDBJ | AAC41739.1 EMBL· GenBank· DDBJ | mRNA |