P46863 · KL61_DROME
- ProteinKinesin-like protein Klp61F
- GeneKlp61F
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1066 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Important role in mitotic dividing cells (PubMed:8227131).
Microtubule motor required for spindle body separation (PubMed:8918872).
Slow plus-end directed microtubule motor capable of cross-linking and sliding apart antiparallel microtubules, thereby pushing apart the associated spindle poles during spindle assembly and function (PubMed:19062285, PubMed:8589456, PubMed:8918872).
Forms cross-links between microtubules within interpolar microtubule bundles (PubMed:19158379, PubMed:9885249).
Contributes to the length of the metaphase spindle, maintains the prometaphase spindle by antagonizing Ncd, drives anaphase B, and also contributes to normal chromosome congression, kinetochore spacing, and anaphase A rates (PubMed:19158379).
Displays microtubule-stimulated ATPase activity (PubMed:8589456).
Required for normal fusome organization (PubMed:10469596).
Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface (PubMed:23857769).
Microtubule motor required for spindle body separation (PubMed:8918872).
Slow plus-end directed microtubule motor capable of cross-linking and sliding apart antiparallel microtubules, thereby pushing apart the associated spindle poles during spindle assembly and function (PubMed:19062285, PubMed:8589456, PubMed:8918872).
Forms cross-links between microtubules within interpolar microtubule bundles (PubMed:19158379, PubMed:9885249).
Contributes to the length of the metaphase spindle, maintains the prometaphase spindle by antagonizing Ncd, drives anaphase B, and also contributes to normal chromosome congression, kinetochore spacing, and anaphase A rates (PubMed:19158379).
Displays microtubule-stimulated ATPase activity (PubMed:8589456).
Required for normal fusome organization (PubMed:10469596).
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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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKinesin-like protein Klp61F
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP46863
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In somatic cells, cytoplasmic during interphase, localized to centrosomal asters at the onset of mitosis in prophase and associated with spindle structures during the remainder of mitosis (PubMed:10469596).
In male and female germ cells, associates with fusomes during interphase, then localizes to centrosomal asters during prophase and to spindles in metaphase (PubMed:10469596).
Coincident with spindle microtubules from prophase to metaphase and, as mitosis proceeds, found both at the spindle poles and along the spindle fibers (PubMed:8589456).
In male and female germ cells, associates with fusomes during interphase, then localizes to centrosomal asters during prophase and to spindles in metaphase (PubMed:10469596).
Coincident with spindle microtubules from prophase to metaphase and, as mitosis proceeds, found both at the spindle poles and along the spindle fibers (PubMed:8589456).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 23 | Spindle defects and greatly reduced phosphorylation by Wee1 in vitro; when associated with F-152 and F-207. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 152 | Spindle defects and greatly reduced phosphorylation by Wee1 in vitro; when associated with F-23 and F-207. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 207 | Spindle defects and greatly reduced phosphorylation by Wee1 in vitro; when associated with F-23 and F-152. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 669 | Remains tetrameric. | ||||
Sequence: F → E | ||||||
Mutagenesis | 726 | Mainly tetrameric. Mainly dimeric; when associated with R-775. | ||||
Sequence: L → D | ||||||
Mutagenesis | 726 | Mainly tetrameric. | ||||
Sequence: L → K | ||||||
Mutagenesis | 729-730 | Mainly monomeric. | ||||
Sequence: MM → EE | ||||||
Mutagenesis | 740 | Formation of tetramers, dimers and monomers. | ||||
Sequence: R → A | ||||||
Mutagenesis | 761 | Formation of tetramers and dimers. | ||||
Sequence: R → A | ||||||
Mutagenesis | 775 | Mainly tetrameric with formation of some monomers. Mainly dimeric; when associated with D-726. | ||||
Sequence: Y → R |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000125371 | 1-1066 | Kinesin-like protein Klp61F | |||
Sequence: MDISGGNTSRQPQKKSNQNIQVYVRVRPLNSRERCIRSAEVVDVVGPREVVTRHTLDSKLTKKFTFDRSFGPESKQCDVYSVVVSPLIEEVLNGYNCTVFAYGQTGTGKTHTMVGNETAELKSSWEDDSDIGIIPRALSHLFDELRMMEVEYTMRISYLELYNEELCDLLSTDDTTKIRIFDDSTKKGSVIIQGLEEIPVHSKDDVYKLLEKGKERRKTATTLMNAQSSRSHTVFSIVVHIRENGIEGEDMLKIGKLNLVDLAGSENVSKAGNEKGIRVRETVNINQSLLTLGRVITALVDRAPHVPYRESKLTRLLQESLGGRTKTSIIATISPGHKDIEETLSTLEYAHRAKNIQNKPEVNQKLTKKTVLKEYTEEIDKLKRDLMAARDKNGIYLAEETYGEITLKLESQNRELNEKMLLLKALKDELQNKEKIFSEVSMSLVEKTQELKKTEENLLNTKGTLLLTKKVLTKTKRRYKEKKELVASHMKTEQVLTTQAQEILAAADLATDDTHQLHGTIERRRELDEKIRRSCDQFKDRMQDNLEMIGGSLNLYQDQQAALKEQLSQEMVNSSYVSQRLALNSSKSIEMLKEMCAQSLQDQTNLHNKLIGEVMKISDQHSQAFVAKLMEQMQQQQLLMSKEIQTNLQVIEENNQRHKAMLDSMQEKFATIIDSSLQSVEEHAKQMHKKLEQLGAMSLPDAEELQNLQEELANERALAQQEDALLESMMMQMEQIKNLRSKNSISMSVHLNKMEESRLTRNHRIDDIKSGIQDYQKLGIEASQSAQAELTSQMEAGMLCLDQGVANCSMLQVHMKNLNQKYEKETNENVGSVRVHHNQVEIICQESKQQLEAVQEKTEVNLEQMVDARQQLITEDRQRFIGHATVATDLVQESNRQFSEHAEHQRQQLQICEQELVRFQQSELKTYAPTGTTPSKRDFVYPRTLVATSPHQEIVRRYRQELDWSDLDTTATIDECSEGEHDVSMHSVQELSETETIMNSTPIEPVDGVTVKRGCGTTRNSNSNALKPPVATGGKRSSSLSRSLTPSKTSPRGSPAFVRHNKENVA | ||||||
Modified residue | 520 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 933 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 949 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1043 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1045 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1050 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1054 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation is required for localization to mitotic spindles (PubMed:9885249).
Phosphorylation of Thr-933 during mitosis controls association with the spindle apparatus (By similarity).
Phosphorylated in vitro by Wee1 (PubMed:19800237).
Phosphorylation of Thr-933 during mitosis controls association with the spindle apparatus (By similarity).
Phosphorylated in vitro by Wee1 (PubMed:19800237).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Specifically expressed in proliferating tissues during embryonic and larval development.
Gene expression databases
Interaction
Subunit
Homotetramer (PubMed:24714498, PubMed:8538794, PubMed:9885249).
Consists of two pairs of polypeptides associated by coiled-coil interactions to form two homodimers (PubMed:8538794).
The homodimers are linked by lateral interactions between their coiled-coil regions to form a bipolar homotetramer consisting of a central rod with two motor domains projecting from either end (PubMed:8538794).
Parallel coiled coils extend from each pair of motor heads, switch to two antiparallel coiled coils in the central region and then back to parallel coiled coils (PubMed:24714498).
Interacts with Wee1 (PubMed:19800237).
Consists of two pairs of polypeptides associated by coiled-coil interactions to form two homodimers (PubMed:8538794).
The homodimers are linked by lateral interactions between their coiled-coil regions to form a bipolar homotetramer consisting of a central rod with two motor domains projecting from either end (PubMed:8538794).
Parallel coiled coils extend from each pair of motor heads, switch to two antiparallel coiled coils in the central region and then back to parallel coiled coils (PubMed:24714498).
Interacts with Wee1 (PubMed:19800237).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-356 | Kinesin motor | ||||
Sequence: NIQVYVRVRPLNSRERCIRSAEVVDVVGPREVVTRHTLDSKLTKKFTFDRSFGPESKQCDVYSVVVSPLIEEVLNGYNCTVFAYGQTGTGKTHTMVGNETAELKSSWEDDSDIGIIPRALSHLFDELRMMEVEYTMRISYLELYNEELCDLLSTDDTTKIRIFDDSTKKGSVIIQGLEEIPVHSKDDVYKLLEKGKERRKTATTLMNAQSSRSHTVFSIVVHIRENGIEGEDMLKIGKLNLVDLAGSENVSKAGNEKGIRVRETVNINQSLLTLGRVITALVDRAPHVPYRESKLTRLLQESLGGRTKTSIIATISPGHKDIEETLSTLEYAHRAKNI | ||||||
Coiled coil | 362-462 | |||||
Sequence: VNQKLTKKTVLKEYTEEIDKLKRDLMAARDKNGIYLAEETYGEITLKLESQNRELNEKMLLLKALKDELQNKEKIFSEVSMSLVEKTQELKKTEENLLNTK | ||||||
Coiled coil | 540-569 | |||||
Sequence: DRMQDNLEMIGGSLNLYQDQQAALKEQLSQ | ||||||
Coiled coil | 639-738 | |||||
Sequence: LMSKEIQTNLQVIEENNQRHKAMLDSMQEKFATIIDSSLQSVEEHAKQMHKKLEQLGAMSLPDAEELQNLQEELANERALAQQEDALLESMMMQMEQIKN | ||||||
Coiled coil | 808-875 | |||||
Sequence: CSMLQVHMKNLNQKYEKETNENVGSVRVHHNQVEIICQESKQQLEAVQEKTEVNLEQMVDARQQLITE | ||||||
Coiled coil | 889-918 | |||||
Sequence: DLVQESNRQFSEHAEHQRQQLQICEQELVR | ||||||
Region | 990-1009 | Disordered | ||||
Sequence: ELSETETIMNSTPIEPVDGV | ||||||
Compositional bias | 1016-1054 | Polar residues | ||||
Sequence: GTTRNSNSNALKPPVATGGKRSSSLSRSLTPSKTSPRGS | ||||||
Region | 1016-1066 | Disordered | ||||
Sequence: GTTRNSNSNALKPPVATGGKRSSSLSRSLTPSKTSPRGSPAFVRHNKENVA |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,066
- Mass (Da)121,163
- Last updated2002-11-28 v2
- Checksum363647366EE0721F
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 962 | in Ref. 1; AAA03718 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 983 | in Ref. 1; AAA03718 | ||||
Sequence: V → D | ||||||
Compositional bias | 1016-1054 | Polar residues | ||||
Sequence: GTTRNSNSNALKPPVATGGKRSSSLSRSLTPSKTSPRGS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U01842 EMBL· GenBank· DDBJ | AAA03718.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF47458.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY069442 EMBL· GenBank· DDBJ | AAL39587.1 EMBL· GenBank· DDBJ | mRNA | ||
M74428 EMBL· GenBank· DDBJ | AAA28655.1 EMBL· GenBank· DDBJ | Genomic DNA |