UniProt ID | KL61_DROME | |
---|---|---|
UniProt AC | P46863 | |
Protein Name | Kinesin-like protein Klp61F {ECO:0000303|PubMed:8227131} | |
Gene Name | Klp61F {ECO:0000312|FlyBase:FBgn0004378} | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1066 | |
Subcellular Localization | Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm . In somatic cells, cytoplasmic during interphase, localized to centrosomal asters at the onset of mitosis in prophase and associated with spindle structures during | |
Protein Description | Important role in mitotic dividing cells. [PubMed: 8227131 Microtubule motor required for spindle body separation] | |
Protein Sequence | MDISGGNTSRQPQKKSNQNIQVYVRVRPLNSRERCIRSAEVVDVVGPREVVTRHTLDSKLTKKFTFDRSFGPESKQCDVYSVVVSPLIEEVLNGYNCTVFAYGQTGTGKTHTMVGNETAELKSSWEDDSDIGIIPRALSHLFDELRMMEVEYTMRISYLELYNEELCDLLSTDDTTKIRIFDDSTKKGSVIIQGLEEIPVHSKDDVYKLLEKGKERRKTATTLMNAQSSRSHTVFSIVVHIRENGIEGEDMLKIGKLNLVDLAGSENVSKAGNEKGIRVRETVNINQSLLTLGRVITALVDRAPHVPYRESKLTRLLQESLGGRTKTSIIATISPGHKDIEETLSTLEYAHRAKNIQNKPEVNQKLTKKTVLKEYTEEIDKLKRDLMAARDKNGIYLAEETYGEITLKLESQNRELNEKMLLLKALKDELQNKEKIFSEVSMSLVEKTQELKKTEENLLNTKGTLLLTKKVLTKTKRRYKEKKELVASHMKTEQVLTTQAQEILAAADLATDDTHQLHGTIERRRELDEKIRRSCDQFKDRMQDNLEMIGGSLNLYQDQQAALKEQLSQEMVNSSYVSQRLALNSSKSIEMLKEMCAQSLQDQTNLHNKLIGEVMKISDQHSQAFVAKLMEQMQQQQLLMSKEIQTNLQVIEENNQRHKAMLDSMQEKFATIIDSSLQSVEEHAKQMHKKLEQLGAMSLPDAEELQNLQEELANERALAQQEDALLESMMMQMEQIKNLRSKNSISMSVHLNKMEESRLTRNHRIDDIKSGIQDYQKLGIEASQSAQAELTSQMEAGMLCLDQGVANCSMLQVHMKNLNQKYEKETNENVGSVRVHHNQVEIICQESKQQLEAVQEKTEVNLEQMVDARQQLITEDRQRFIGHATVATDLVQESNRQFSEHAEHQRQQLQICEQELVRFQQSELKTYAPTGTTPSKRDFVYPRTLVATSPHQEIVRRYRQELDWSDLDTTATIDECSEGEHDVSMHSVQELSETETIMNSTPIEPVDGVTVKRGCGTTRNSNSNALKPPVATGGKRSSSLSRSLTPSKTSPRGSPAFVRHNKENVA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
189 | Phosphorylation | DDSTKKGSVIIQGLE ECCCCCCEEEEECCE | 21.01 | 21082442 | |
282 | Phosphorylation | KGIRVRETVNINQSL CCCCEEEEEECCHHH | 14.32 | 21082442 | |
461 | Phosphorylation | TEENLLNTKGTLLLT HHHHHCCCCCHHHHH | 30.71 | 21082442 | |
464 | Phosphorylation | NLLNTKGTLLLTKKV HHCCCCCHHHHHHHH | 18.78 | 21082442 | |
511 | Phosphorylation | LAAADLATDDTHQLH HHHHCCCCCCCCHHC | 41.53 | 19429919 | |
514 | Phosphorylation | ADLATDDTHQLHGTI HCCCCCCCCHHCHHH | 17.84 | 19429919 | |
520 | Phosphorylation | DTHQLHGTIERRREL CCCHHCHHHHHHHHH | 14.66 | 19429919 | |
534 | Phosphorylation | LDEKIRRSCDQFKDR HHHHHHHHHHHHHHH | 16.52 | 22817900 | |
618 | Phosphorylation | IGEVMKISDQHSQAF HHHHHHCCHHHHHHH | 26.21 | 22817900 | |
932 | Phosphorylation | KTYAPTGTTPSKRDF CCCCCCCCCCCCCCC | 37.70 | 28490779 | |
933 | Phosphorylation | TYAPTGTTPSKRDFV CCCCCCCCCCCCCCC | 27.23 | 28490779 | |
944 | Phosphorylation | RDFVYPRTLVATSPH CCCCCCCCEEECCHH | 22.53 | 27626673 | |
948 | Phosphorylation | YPRTLVATSPHQEIV CCCCEEECCHHHHHH | 35.00 | 19429919 | |
949 | Phosphorylation | PRTLVATSPHQEIVR CCCEEECCHHHHHHH | 15.62 | 19429919 | |
1021 | Phosphorylation | GCGTTRNSNSNALKP CCCCCCCCCCCCCCC | 38.04 | 19429919 | |
1023 | Phosphorylation | GTTRNSNSNALKPPV CCCCCCCCCCCCCCC | 24.25 | 19429919 | |
1038 | Phosphorylation | ATGGKRSSSLSRSLT CCCCCCCCCCCCCCC | 39.05 | 22817900 | |
1043 | Phosphorylation | RSSSLSRSLTPSKTS CCCCCCCCCCCCCCC | 32.97 | 25749252 | |
1045 | Phosphorylation | SSLSRSLTPSKTSPR CCCCCCCCCCCCCCC | 27.11 | 25749252 | |
1047 | Phosphorylation | LSRSLTPSKTSPRGS CCCCCCCCCCCCCCC | 43.24 | 19429919 | |
1049 | Phosphorylation | RSLTPSKTSPRGSPA CCCCCCCCCCCCCCC | 48.58 | 19429919 | |
1050 | Phosphorylation | SLTPSKTSPRGSPAF CCCCCCCCCCCCCCC | 19.14 | 19429919 | |
1054 | Phosphorylation | SKTSPRGSPAFVRHN CCCCCCCCCCCCCCC | 17.84 | 25749252 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of KL61_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KL61_DROME !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KL61_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NCD_DROME | ncd | genetic | 15367580 | |
FOJO_DROME | fj | physical | 24114784 | |
KL61_DROME | Klp61F | physical | 23299893 | |
WARTS_DROME | wts | physical | 24114784 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-933; SER-949; SER-1043;THR-1045; SER-1050 AND SER-1054, AND MASS SPECTROMETRY. | |
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-520 AND SER-949, ANDMASS SPECTROMETRY. |