General Information of Target

Target ID LDTP07141
Target Name Kinesin-like protein KIF24 (KIF24)
Gene Name KIF24
Gene ID 347240
Synonyms
C9orf48; Kinesin-like protein KIF24
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MASWLYECLCEAELAQYYSHFTALGLQKIDELAKITMKDYSKLGVHDMNDRKRLFQLIKI
IKIMQEEDKAVSIPERHLQTSSLRIKSQELRSGPRRQLNFDSPADNKDRNASNDGFEMCS
LSDFSANEQKSTYLKVLEHMLPDDSQYHTKTGILNATAGDSYVQTEISTSLFSPNYLSAI
LGDCDIPIIQRISHVSGYNYGIPHSCIRQNTSEKQNPWTEMEKIRVCVRKRPLGMREVRR
GEINIITVEDKETLLVHEKKEAVDLTQYILQHVFYFDEVFGEACTNQDVYMKTTHPLIQH
IFNGGNATCFAYGQTGAGKTYTMIGTHENPGLYALAAKDIFRQLEVSQPRKHLFVWISFY
EIYCGQLYDLLNRRKRLFAREDSKHMVQIVGLQELQVDSVELLLEVILKGSKERSTGATG
VNADSSRSHAVIQIQIKDSAKRTFGRISFIDLAGSERAADARDSDRQTKMEGAEINQSLL
ALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYA
DRVKELKKGIKCCTSVTSRNRTSGNSSPKRIQSSPGALSEDKCSPKKVKLGFQQSLTVAA
PGSTRGKVHPLTSHPPNIPFTSAPKVSGKRGGSRGSPSQEWVIHASPVKGTVRSGHVAKK
KPEESAPLCSEKNRMGNKTVLGWESRASGPGEGLVRGKLSTKCKKVQTVQPVQKQLVSRV
ELSFGNAHHRAEYSQDSQRGTPARPASEAWTNIPPHQKEREEHLRFYHQQFQQPPLLQQK
LKYQPLKRSLRQYRPPEGQLTNETPPLFHSYSENHDGAQVEELDDSDFSEDSFSHISSQR
ATKQRNTLENSEDSFFLHQTWGQGPEKQVAERQQSLFSSPRTGDKKDLTKSWVDSRDPIN
HRRAALDHSCSPSKGPVDWSRENSTSSGPSPRDSLAEKPYCSQVDFIYRQERGGGSSFDL
RKDASQSEVSGENEGNLPSPEEDGFTISLSHVAVPGSPDQRDTVTTPLREVSADGPIQVT
STVKNGHAVPGEDPRGQLGTHAEYASGLMSPLTMSLLENPDNEGSPPSEQLVQDGATHSL
VAESTGGPVVSHTVPSGDQEAALPVSSATRHLWLSSSPPDNKPGGDLPALSPSPIRQHPA
DKLPSREADLGEACQSRETVLFSHEHMGSEQYDADAEETGLDGSWGFPGKPFTTIHMGVP
HSGPTLTPRTGSSDVADQLWAQERKHPTRLGWQEFGLSTDPIKLPCNSENVTWLKPRPIS
RCLARPSSPLVPSCSPKTAGTLRQPTLEQAQQVVIRAHQEQLDEMAELGFKEETLMSQLA
SNDFEDFVTQLDEIMVLKSKCIQSLRSQLQLYLTCHGPTAAPEGTVPS
Target Bioclass
Enzyme
Family
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
Subcellular location
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole
Function
Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells, leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin, possibly to suppress aberrant cilia formation. Following activation by NEK2 involved in disassembly of primary cilium during G2/M phase but does not disassemble fully formed ciliary axonemes. As cilium assembly and disassembly is proposed to coexist in a dynamic equilibrium may suppress nascent cilium assembly and, potentially, ciliar re-assembly in cells that have already disassembled their cilia ensuring the completion of cilium removal in the later stages of the cell cycle. Plays an important role in recruiting MPHOSPH9, a negative regulator of cilia formation to the distal end of mother centriole.
Uniprot ID
Q5T7B8
Ensemble ID
ENST00000379174.7
HGNC ID
HGNC:19916
ChEMBL ID
CHEMBL3879840

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
CCLP1 Deletion: p.A430PfsTer19 .
HT115 SNV: p.F276V .
KMCH1 SNV: p.V556F .
LNCaP clone FGC SNV: p.L402F .
MFE319 SNV: p.D105V .
MOLT4 SNV: p.D264E .
REH SNV: p.C8R .
SUIT2 Substitution: p.A440V .

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 1 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
DBIA
 Probe Info 
C910(0.95)  LDD1513  [1]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0270  AC15 HEK-293T C910(0.95)  LDD1513  [1]
 LDCM0283  AC23 HEK-293T C910(1.07)  LDD1522  [1]
 LDCM0292  AC31 HEK-293T C910(0.93)  LDD1531  [1]
 LDCM0300  AC39 HEK-293T C910(1.24)  LDD1539  [1]
 LDCM0309  AC47 HEK-293T C910(0.89)  LDD1548  [1]
 LDCM0318  AC55 HEK-293T C910(1.03)  LDD1557  [1]
 LDCM0327  AC63 HEK-293T C910(0.99)  LDD1566  [1]
 LDCM0334  AC7 HEK-293T C910(0.96)  LDD1568  [1]
 LDCM0367  CL1 HEK-293T C910(0.75)  LDD1571  [1]
 LDCM0370  CL101 HEK-293T C910(1.36)  LDD1574  [1]
 LDCM0374  CL105 HEK-293T C910(1.09)  LDD1578  [1]
 LDCM0378  CL109 HEK-293T C910(1.24)  LDD1582  [1]
 LDCM0379  CL11 HEK-293T C910(1.03)  LDD1583  [1]
 LDCM0383  CL113 HEK-293T C910(0.91)  LDD1587  [1]
 LDCM0387  CL117 HEK-293T C910(0.90)  LDD1591  [1]
 LDCM0392  CL121 HEK-293T C910(0.71)  LDD1596  [1]
 LDCM0396  CL125 HEK-293T C910(0.83)  LDD1600  [1]
 LDCM0400  CL13 HEK-293T C910(1.49)  LDD1604  [1]
 LDCM0411  CL23 HEK-293T C910(1.16)  LDD1615  [1]
 LDCM0413  CL25 HEK-293T C910(0.85)  LDD1617  [1]
 LDCM0424  CL35 HEK-293T C910(0.87)  LDD1628  [1]
 LDCM0426  CL37 HEK-293T C910(0.79)  LDD1630  [1]
 LDCM0437  CL47 HEK-293T C910(0.92)  LDD1641  [1]
 LDCM0439  CL49 HEK-293T C910(0.76)  LDD1643  [1]
 LDCM0450  CL59 HEK-293T C910(1.08)  LDD1653  [1]
 LDCM0453  CL61 HEK-293T C910(1.45)  LDD1656  [1]
 LDCM0464  CL71 HEK-293T C910(0.83)  LDD1667  [1]
 LDCM0466  CL73 HEK-293T C910(0.57)  LDD1669  [1]
 LDCM0477  CL83 HEK-293T C910(0.87)  LDD1680  [1]
 LDCM0479  CL85 HEK-293T C910(0.90)  LDD1682  [1]
 LDCM0490  CL95 HEK-293T C910(1.19)  LDD1693  [1]
 LDCM0492  CL97 HEK-293T C910(0.98)  LDD1695  [1]

References

1 Accelerating multiplexed profiling of protein-ligand interactions: High-throughput plate-based reactive cysteine profiling with minimal input. Cell Chem Biol. 2024 Mar 21;31(3):565-576.e4. doi: 10.1016/j.chembiol.2023.11.015. Epub 2023 Dec 19.
Mass spectrometry data entry: PXD044402