KI18A_HUMAN - dbPTM
KI18A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KI18A_HUMAN
UniProt AC Q8NI77
Protein Name Kinesin-like protein KIF18A
Gene Name KIF18A
Organism Homo sapiens (Human).
Sequence Length 898
Subcellular Localization Cell projection, ruffle. Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Description Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression..
Protein Sequence MSVTEEDLCHHMKVVVRVRPENTKEKAAGFHKVVHVVDKHILVFDPKQEEVSFFHGKKTTNQNVIKKQNKDLKFVFDAVFDETSTQSEVFEHTTKPILRSFLNGYNCTVLAYGATGAGKTHTMLGSADEPGVMYLTMLHLYKCMDEIKEEKICSTAVSYLEVYNEQIRDLLVNSGPLAVREDTQKGVVVHGLTLHQPKSSEEILHLLDNGNKNRTQHPTDMNATSSRSHAVFQIYLRQQDKTASINQNVRIAKMSLIDLAGSERASTSGAKGTRFVEGTNINRSLLALGNVINALADSKRKNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSVFYDDTYNTLKYANRAKDIKSSLKSNVLNVNNHITQYVKICNEQKAEILLLKEKLKAYEEQKAFTNENDQAKLMISNPQEKEIERFQEILNCLFQNREEIRQEYLKLEMLLKENELKSFYQQQCHKQIEMMCSEDKVEKATGKRDHRLAMLKTRRSYLEKRREEELKQFDENTNWLHRVEKEMGLLSQNGHIPKELKKDLHCHHLHLQNKDLKAQIRHMMDLACLQEQQHRQTEAVLNALLPTLRKQYCTLKEAGLSNAAFESDFKEIEHLVERKKVVVWADQTAEQPKQNDLPGISVLMTFPQLGPVQPIPCCSSSGGTNLVKIPTEKRTRRKLMPSPLKGQHTLKSPPSQSVQLNDSLSKELQPIVYTPEDCRKAFQNPSTVTLMKPSSFTTSFQAISSNINSDNCLKMLCEVAIPHNRRKECGQEDLDSTFTICEDIKSSKCKLPEQESLPNDNKDILQRLDPSSFSTKHSMPVPSMVPSYMAMTTAAKRKRKLTSSTSNSSLTADVNSGFAKRVRQDNSSEKHLQENKPTMEHKRNICKINPSMVRKFGRNISKGNLR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSVTEEDLC
------CCCCHHHHH		37.4330108239
4Phosphorylation----MSVTEEDLCHH
----CCCCHHHHHHC		26.7527732954
24SumoylationRVRPENTKEKAAGFH
EECCCCCHHHHHCCE		69.6525755297
57UbiquitinationEVSFFHGKKTTNQNV
CEEEECCCCCCCCHH		38.0729967540
57AcetylationEVSFFHGKKTTNQNV
CEEEECCCCCCCCHH		38.0725953088
58UbiquitinationVSFFHGKKTTNQNVI
EEEECCCCCCCCHHH		66.2429967540
126PhosphorylationKTHTMLGSADEPGVM
CCCCCCCCCCCCCHH		28.6922210691
134PhosphorylationADEPGVMYLTMLHLY
CCCCCHHHHHHHHHH		9.1622210691
241UbiquitinationIYLRQQDKTASINQN
EEEECCCCCCCCCCC		41.47-
242PhosphorylationYLRQQDKTASINQNV
EEECCCCCCCCCCCH		33.6519691289
244PhosphorylationRQQDKTASINQNVRI
ECCCCCCCCCCCHHE		27.5719691289
253UbiquitinationNQNVRIAKMSLIDLA
CCCHHEEEEEEEHHC		27.0129967540
279PhosphorylationGTRFVEGTNINRSLL
CCCCCCCCCCCHHHH		21.3020068231
284PhosphorylationEGTNINRSLLALGNV
CCCCCCHHHHHHHHH		24.2124719451
298PhosphorylationVINALADSKRKNQHI
HHHHHHHCHHHCCCC		28.8420860994
299AcetylationINALADSKRKNQHIP
HHHHHHCHHHCCCCC		68.8624431523
299UbiquitinationINALADSKRKNQHIP
HHHHHHCHHHCCCCC		68.86-
356UbiquitinationANRAKDIKSSLKSNV
HHHHHHHHHHHHHCC		44.0929967540
357PhosphorylationNRAKDIKSSLKSNVL
HHHHHHHHHHHHCCC		41.0322817900
360UbiquitinationKDIKSSLKSNVLNVN
HHHHHHHHHCCCCCC		41.7629967540
388UbiquitinationKAEILLLKEKLKAYE
HHHHHHHHHHHHHHH		53.4229967540
398SumoylationLKAYEEQKAFTNEND
HHHHHHHHHCCCCCH		49.07-
398UbiquitinationLKAYEEQKAFTNEND
HHHHHHHHHCCCCCH		49.0729967540
398SumoylationLKAYEEQKAFTNEND
HHHHHHHHHCCCCCH		49.07-
408UbiquitinationTNENDQAKLMISNPQ
CCCCHHHHHECCCHH		32.7129967540
412PhosphorylationDQAKLMISNPQEKEI
HHHHHECCCHHHHHH		28.6125690035
440PhosphorylationREEIRQEYLKLEMLL
HHHHHHHHHHHHHHH		10.7824043423
453UbiquitinationLLKENELKSFYQQQC
HHHHHHHHHHHHHHH		32.1329967540
503UbiquitinationKRREEELKQFDENTN
HHHHHHHHHHHHCCC		52.8029967540
517MethylationNWLHRVEKEMGLLSQ
CHHHHHHHHHCHHHC		50.5823644510
534MethylationHIPKELKKDLHCHHL
CCCHHHHHHHCCHHH		77.4823644510
534UbiquitinationHIPKELKKDLHCHHL
CCCHHHHHHHCCHHH		77.4829967540
546UbiquitinationHHLHLQNKDLKAQIR
HHHHCCCHHHHHHHH		52.0229967540
549UbiquitinationHLQNKDLKAQIRHMM
HCCCHHHHHHHHHHH		48.6729967540
588UbiquitinationRKQYCTLKEAGLSNA
HHHCCCHHHHCCCCH		27.6229967540
602UbiquitinationAAFESDFKEIEHLVE
HHHHCCHHHHHHHHH		63.8729967540
612UbiquitinationEHLVERKKVVVWADQ
HHHHHHCCEEEECCC		46.6229967540
674PhosphorylationTRRKLMPSPLKGQHT
CCCCCCCCCCCCCCC		28.9730266825
681PhosphorylationSPLKGQHTLKSPPSQ
CCCCCCCCCCCCCCC		28.1718669648
683SumoylationLKGQHTLKSPPSQSV
CCCCCCCCCCCCCCE		63.1728112733
684PhosphorylationKGQHTLKSPPSQSVQ
CCCCCCCCCCCCCEE		45.1925159151
687PhosphorylationHTLKSPPSQSVQLND
CCCCCCCCCCEECCC		38.1720873877
689PhosphorylationLKSPPSQSVQLNDSL
CCCCCCCCEECCCCC		19.0320873877
695PhosphorylationQSVQLNDSLSKELQP
CCEECCCCCCCCCCC		33.2125159151
697PhosphorylationVQLNDSLSKELQPIV
EECCCCCCCCCCCCE		28.2125159151
705PhosphorylationKELQPIVYTPEDCRK
CCCCCCEECHHHHHH		19.8030266825
706PhosphorylationELQPIVYTPEDCRKA
CCCCCEECHHHHHHH		14.8730266825
712UbiquitinationYTPEDCRKAFQNPST
ECHHHHHHHHCCCCC		60.9429967540
727PhosphorylationVTLMKPSSFTTSFQA
EEEECCCCCCCCHHH		34.8323403867
729PhosphorylationLMKPSSFTTSFQAIS
EECCCCCCCCHHHHH		24.3923403867
737PhosphorylationTSFQAISSNINSDNC
CCHHHHHCCCCCCHH		35.3023403867
741PhosphorylationAISSNINSDNCLKML
HHHCCCCCCHHHHHH		26.8023403867
769PhosphorylationGQEDLDSTFTICEDI
CCCCHHHCEEEEHHH		25.1922468782
771PhosphorylationEDLDSTFTICEDIKS
CCHHHCEEEEHHHHH		25.4722468782
788PhosphorylationCKLPEQESLPNDNKD
CCCCCHHCCCCCCHH		49.1528555341
794UbiquitinationESLPNDNKDILQRLD
HCCCCCCHHHHHHCC		49.3529967540
794SumoylationESLPNDNKDILQRLD
HCCCCCCHHHHHHCC		49.35-
794SumoylationESLPNDNKDILQRLD
HCCCCCCHHHHHHCC		49.3528112733
810PhosphorylationSSFSTKHSMPVPSMV
CCCCCCCCCCCCCCC		26.7422210691
815PhosphorylationKHSMPVPSMVPSYMA
CCCCCCCCCCHHHHH		32.4222210691
819PhosphorylationPVPSMVPSYMAMTTA
CCCCCCHHHHHHHHH		19.0122210691
825PhosphorylationPSYMAMTTAAKRKRK
HHHHHHHHHHHHHHC		16.1320068231
834PhosphorylationAKRKRKLTSSTSNSS
HHHHHCCCCCCCCCC		24.5427273156
835PhosphorylationKRKRKLTSSTSNSSL
HHHHCCCCCCCCCCC		41.8920068231
836PhosphorylationRKRKLTSSTSNSSLT
HHHCCCCCCCCCCCC		30.5320068231
837PhosphorylationKRKLTSSTSNSSLTA
HHCCCCCCCCCCCCE		31.5220068231
838PhosphorylationRKLTSSTSNSSLTAD
HCCCCCCCCCCCCEE		36.3428112733
840PhosphorylationLTSSTSNSSLTADVN
CCCCCCCCCCCEECC		26.8825159151
841PhosphorylationTSSTSNSSLTADVNS
CCCCCCCCCCEECCC		33.7125159151
843PhosphorylationSTSNSSLTADVNSGF
CCCCCCCCEECCCCH		23.8220068231
848PhosphorylationSLTADVNSGFAKRVR
CCCEECCCCHHHHHC		34.8320068231
868SumoylationEKHLQENKPTMEHKR
HHHHHHCCCCHHHHH		40.90-
868SumoylationEKHLQENKPTMEHKR
HHHHHHCCCCHHHHH		40.9028112733
874SumoylationNKPTMEHKRNICKIN
CCCCHHHHHHHHHCC		33.5628112733
883O-linked_GlycosylationNICKINPSMVRKFGR
HHHHCCHHHHHHHCC		25.9730379171
893PhosphorylationRKFGRNISKGNLR--
HHHCCCCCCCCCC--		37.7528857561
894SumoylationKFGRNISKGNLR---
HHCCCCCCCCCC---		48.28-
894SumoylationKFGRNISKGNLR---
HHCCCCCCCCCC---		48.28-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 KI18A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KI18A_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 KI18A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO2_HUMANCSE1Lphysical
26496610
FOXM1_HUMANFOXM1physical
26496610
PSMD5_HUMANPSMD5physical
26496610
TFE2_HUMANTCF3physical
26496610
ICAM5_HUMANICAM5physical
26496610
TTC3_HUMANTTC3physical
26496610
MKNK1_HUMANMKNK1physical
26496610
ITM2B_HUMANITM2Bphysical
26496610
NCOR1_HUMANNCOR1physical
26496610
KBP_HUMANKIAA1279physical
26496610
RRP7A_HUMANRRP7Aphysical
26496610
KNL1_HUMANCASC5physical
26496610
S39AA_HUMANSLC39A10physical
26496610
GKAP1_HUMANGKAP1physical
26496610
CR021_HUMANC18orf21physical
26496610
EME1_HUMANEME1physical
26496610
PP1R7_HUMANPPP1R7physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KI18A_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-684, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-706, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory