KIFC1_HUMAN - dbPTM
KIFC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIFC1_HUMAN
UniProt AC Q9BW19
Protein Name Kinesin-like protein KIFC1
Gene Name KIFC1
Organism Homo sapiens (Human).
Sequence Length 673
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Early endosome . Associated with nucleus during interphase, centrosomes in early and spindle in later mitosis.
Protein Description Minus end-directed microtubule-dependent motor required for bipolar spindle formation. [PubMed: 15843429 May contribute to movement of early endocytic vesicles (By similarity Regulates cilium formation and structure (By similarity]
Protein Sequence MDPQRSPLLEVKGNIELKRPLIKAPSQLPLSGSRLKRRPDQMEDGLEPEKKRTRGLGATTKITTSHPRVPSLTTVPQTQGQTTAQKVSKKTGPRCSTAIATGLKNQKPVPAVPVQKSGTSGVPPMAGGKKPSKRPAWDLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKERRLQTSEAALSSSQAEVASLRQETVAQAALLTEREERLHGLEMERRRLHNQLQELKGNIRVFCRVRPVLPGEPTPPPGLLLFPSGPGGPSDPPTRLSLSRSDERRGTLSGAPAPPTRHDFSFDRVFPPGSGQDEVFEEIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPGGDPQLEGLIPRALRHLFSVAQELSGQGWTYSFVASYVEIYNETVRDLLATGTRKGQGGECEIRRAGPGSEELTVTNARYVPVSCEKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGAPLSLVDLAGSERLDPGLALGPGERERLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIGTAQANRK
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
6Phosphorylation--MDPQRSPLLEVKG
--CCCCCCCCEEECC		18.0429255136
23UbiquitinationELKRPLIKAPSQLPL
EECCCCCCCCCCCCC		63.03-
23MethylationELKRPLIKAPSQLPL
EECCCCCCCCCCCCC		63.03115972129
26PhosphorylationRPLIKAPSQLPLSGS
CCCCCCCCCCCCCCC		49.5725159151
31PhosphorylationAPSQLPLSGSRLKRR
CCCCCCCCCCHHCCC		32.5525159151
33PhosphorylationSQLPLSGSRLKRRPD
CCCCCCCCHHCCCCC		30.9425159151
54MethylationEPEKKRTRGLGATTK
CCHHHCCCCCCCCCE		42.23115481311
61AcetylationRGLGATTKITTSHPR
CCCCCCCEECCCCCC		33.4325953088
71PhosphorylationTSHPRVPSLTTVPQT
CCCCCCCCCCCCCCC		35.1819691289
73PhosphorylationHPRVPSLTTVPQTQG
CCCCCCCCCCCCCCC		30.0419691289
74PhosphorylationPRVPSLTTVPQTQGQ
CCCCCCCCCCCCCCC		35.1719691289
78PhosphorylationSLTTVPQTQGQTTAQ
CCCCCCCCCCCCCCH		28.7028555341
82PhosphorylationVPQTQGQTTAQKVSK
CCCCCCCCCCHHHHH		30.8118452278
83PhosphorylationPQTQGQTTAQKVSKK
CCCCCCCCCHHHHHH		21.1419691289
86AcetylationQGQTTAQKVSKKTGP
CCCCCCHHHHHHHCC		46.1125953088
88PhosphorylationQTTAQKVSKKTGPRC
CCCCHHHHHHHCCCC		35.1628555341
96PhosphorylationKKTGPRCSTAIATGL
HHHCCCCCHHHHHCC		23.3520860994
107AcetylationATGLKNQKPVPAVPV
HHCCCCCCCCCCCCC		58.3323236377
107UbiquitinationATGLKNQKPVPAVPV
HHCCCCCCCCCCCCC		58.33-
140UbiquitinationKRPAWDLKGQLCDLN
CCCCCCCCCCCCHHH		41.98-
151UbiquitinationCDLNAELKRCRERTQ
CHHHHHHHHHHHHHH		40.74-
151AcetylationCDLNAELKRCRERTQ
CHHHHHHHHHHHHHH		40.7425953088
159PhosphorylationRCRERTQTLDQENQQ
HHHHHHHHHHHHHHH		31.5228555341
179UbiquitinationRDAQQQVKALGTERT
HHHHHHHHHHCCCCC		33.29-
183PhosphorylationQQVKALGTERTTLEG
HHHHHHCCCCCHHHH		24.1224719451
194UbiquitinationTLEGHLAKVQAQAEQ
HHHHHHHHHHHHHHH		41.04-
194AcetylationTLEGHLAKVQAQAEQ
HHHHHHHHHHHHHHH		41.0425953088
207AcetylationEQGQQELKNLRACVL
HHHHHHHHHHHHHHH		53.8626051181
207UbiquitinationEQGQQELKNLRACVL
HHHHHHHHHHHHHHH		53.86-
232UbiquitinationGLVQELQKKQVELQE
HHHHHHHHHHHHHHH		58.77-
251UbiquitinationLMSQLEEKERRLQTS
HHHHHHHHHHHHHHH		47.33-
257PhosphorylationEKERRLQTSEAALSS
HHHHHHHHHHHHHHC		32.8820068231
258PhosphorylationKERRLQTSEAALSSS
HHHHHHHHHHHHHCC		16.5720068231
263PhosphorylationQTSEAALSSSQAEVA
HHHHHHHHCCHHHHH		24.1820068231
264PhosphorylationTSEAALSSSQAEVAS
HHHHHHHCCHHHHHH		27.5920068231
265PhosphorylationSEAALSSSQAEVASL
HHHHHHCCHHHHHHH		29.9920068231
271PhosphorylationSSQAEVASLRQETVA
CCHHHHHHHHHHHHH		29.3020068231
308UbiquitinationHNQLQELKGNIRVFC
HHHHHHHCCCEEEEE		49.5121890473
326PhosphorylationPVLPGEPTPPPGLLL
CCCCCCCCCCCCEEE		44.0926714015
336PhosphorylationPGLLLFPSGPGGPSD
CCEEECCCCCCCCCC		50.7327174698
342PhosphorylationPSGPGGPSDPPTRLS
CCCCCCCCCCCCCCC		67.0527174698
346PhosphorylationGGPSDPPTRLSLSRS
CCCCCCCCCCCCCCC		50.0227174698
349PhosphorylationSDPPTRLSLSRSDER
CCCCCCCCCCCCCCC		22.4723927012
351PhosphorylationPPTRLSLSRSDERRG
CCCCCCCCCCCCCCC		26.7717192257
359PhosphorylationRSDERRGTLSGAPAP
CCCCCCCCCCCCCCC		18.8821712546
361PhosphorylationDERRGTLSGAPAPPT
CCCCCCCCCCCCCCC		32.5220068231
373PhosphorylationPPTRHDFSFDRVFPP
CCCCCCCCCCEECCC		32.0921712546
475PhosphorylationTVRDLLATGTRKGQG
HHHHHHHCCCCCCCC		38.7721406692
477PhosphorylationRDLLATGTRKGQGGE
HHHHHCCCCCCCCCC		25.5021406692
479UbiquitinationLLATGTRKGQGGECE
HHHCCCCCCCCCCEE		56.26-
489MethylationGGECEIRRAGPGSEE
CCCEEEEECCCCCCE		49.94115481305
494PhosphorylationIRRAGPGSEELTVTN
EEECCCCCCEEEEEC		30.9126699800
498PhosphorylationGPGSEELTVTNARYV
CCCCCEEEEECEEEE		28.6726699800
500PhosphorylationGSEELTVTNARYVPV
CCCEEEEECEEEEEC		20.2326699800
504PhosphorylationLTVTNARYVPVSCEK
EEEECEEEEECCCHH		13.4926699800
508PhosphorylationNARYVPVSCEKEVDA
CEEEEECCCHHHHHH		15.5326699800
511UbiquitinationYVPVSCEKEVDALLH
EEECCCHHHHHHHHH		68.3221890473
540PhosphorylationERSSRSHSVFQLQIS
HHHHCCCEEEEEEEC		26.3524719451
551PhosphorylationLQISGEHSSRGLQCG
EEECCCCCCCCCCCC		19.8925332170
562PhosphorylationLQCGAPLSLVDLAGS
CCCCCCEEEEECCCC		25.8625332170
609UbiquitinationVIMALSNKESHVPYR
HHHHHHCCCCCCCCH		58.16-
619UbiquitinationHVPYRNSKLTYLLQN
CCCCHHHHHHHHHHH		48.6921890473
619AcetylationHVPYRNSKLTYLLQN
CCCCHHHHHHHHHHH		48.6925953088
621PhosphorylationPYRNSKLTYLLQNSL
CCHHHHHHHHHHHCC		18.8328152594
622PhosphorylationYRNSKLTYLLQNSLG
CHHHHHHHHHHHCCC		18.8228152594
641PhosphorylationMLMFVNISPLEENVS
EEEEEECCCCCCHHH		20.4429116813
648PhosphorylationSPLEENVSESLNSLR
CCCCCHHHHHHHHHH		32.8029116813
650PhosphorylationLEENVSESLNSLRFA
CCCHHHHHHHHHHHH		25.9129116813
653PhosphorylationNVSESLNSLRFASKV
HHHHHHHHHHHHHHH		26.6429116813
659UbiquitinationNSLRFASKVNQCVIG
HHHHHHHHHCEEHHH		41.60-
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
6SPhosphorylationKinaseCDK1P06493
PSP
26SPhosphorylationKinaseCDK1P06493
PSP
26SPhosphorylationKinaseCHEK1O14757
GPS
31SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIFC1_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 KIFC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 KIFC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-96, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND MASSSPECTROMETRY.

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