KIF5C_MOUSE - dbPTM
KIF5C_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF5C_MOUSE
UniProt AC P28738
Protein Name Kinesin heavy chain isoform 5C
Gene Name Kif5c
Organism Mus musculus (Mouse).
Sequence Length 956
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, dendrite . Abundant in distal regions of dendrites.
Protein Description Involved in synaptic transmission (By similarity). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs..
Protein Sequence MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVLQHLEMELNRWRNGEAVPEDEQISAKDQKSLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGGSSNSTHYQK
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
45UbiquitinationTVVIGQGKPYVFDRV
EEEECCCCCEEECCC		25.8627667366
99UbiquitinationKTHTMEGKLHDPQLM
CEEEEECEECCHHHH		29.37-
167UbiquitinationKNRVPYVKGCTERFV
CCCCCCCCCCCHHCC		42.28-
176PhosphorylationCTERFVSSPEEVMDV
CCHHCCCCHHHHHHH		30.91-
220PhosphorylationIKQENVETEKKLSGK
EEECCCCCHHHHCCE		49.15-
227UbiquitinationTEKKLSGKLYLVDLA
CHHHHCCEEEEEECC		30.49-
238UbiquitinationVDLAGSEKVSKTGAE
EECCCCCCCCCCCCC		54.2127667366
241AcetylationAGSEKVSKTGAEGAV
CCCCCCCCCCCCCCH		54.7023806337
241UbiquitinationAGSEKVSKTGAEGAV
CCCCCCCCCCCCCCH		54.70-
253UbiquitinationGAVLDEAKNINKSLS
CCHHHHHHHHHHHHH		57.20-
258PhosphorylationEAKNINKSLSALGNV
HHHHHHHHHHHHHHH		24.0629899451
326PhosphorylationMFGQRAKTIKNTVSV
HHCCCCCCCCCEEEE		35.88-
338PhosphorylationVSVNLELTAEEWKKK
EEEEEEECHHHHHHH		23.7317203969
348AcetylationEWKKKYEKEKEKNKA
HHHHHHHHHHHHHHH		71.626567333
385UbiquitinationEDEQISAKDQKSLEP
HHHCCCHHHCCCCCC		54.6327667366
389PhosphorylationISAKDQKSLEPCDNT
CCHHHCCCCCCCCCC		32.1224925903
396PhosphorylationSLEPCDNTPIIDNIT
CCCCCCCCCCCCCCC		11.5625521595
403PhosphorylationTPIIDNITPVVDGIS
CCCCCCCCCCCCCCC		19.1124925903
413UbiquitinationVDGISAEKEKYDEEI
CCCCCHHHHHHHHHH		60.26-
415UbiquitinationGISAEKEKYDEEITS
CCCHHHHHHHHHHHH		69.90-
445UbiquitinationSQLAEKLKQQMLDQD
HHHHHHHHHHCCCHH		49.94-
497PhosphorylationLEELAVNYDQKSQEV
HHHHHCCCCCCCHHH		17.1029899451
539PhosphorylationLSQLQELSNHQKKRA
HHHHHHHHHHHHHHH		31.3622006019
547PhosphorylationNHQKKRATEILNLLL
HHHHHHHHHHHHHHH		27.8220495213
592UbiquitinationMARLYISKMKSEVKS
HHHHHHHHHHHHHHH		40.5727667366
609PhosphorylationNRSKQLESAQMDSNR
HHHHHHHHHHHHHHH		32.1820139300
621PhosphorylationSNRKMNASERELAAC
HHHCCCHHHHHHHHH		31.9820139300
652UbiquitinationYMQNMEQKRRQLEES
HHHHHHHHHHHHHHH		35.92-
662PhosphorylationQLEESQDSLSEELAK
HHHHHHHHHHHHHHH		26.5929899451
669UbiquitinationSLSEELAKLRAQEKM
HHHHHHHHHHHHHHH		51.64-
715UbiquitinationSHREAHQKQLSRLRD
HHHHHHHHHHHHHHH		43.2527667366
765UbiquitinationEDQEREVKLEKLLLL
HHHHHHHHHHHHHHH		46.29-
768UbiquitinationEREVKLEKLLLLNDK
HHHHHHHHHHHHCHH		55.67-
775UbiquitinationKLLLLNDKREQARED
HHHHHCHHHHHHHHH		57.6827667366
784AcetylationEQAREDLKGLEETVS
HHHHHHHHHHHHHHH		74.0019819415
796PhosphorylationTVSRELQTLHNLRKL
HHHHHHHHHHHHHHH		42.4817203969
809PhosphorylationKLFVQDLTTRVKKSV
HHHHHHHHHHHHHHE		22.35-
810PhosphorylationLFVQDLTTRVKKSVE
HHHHHHHHHHHHHEE		40.54-
815PhosphorylationLTTRVKKSVELDSDD
HHHHHHHHEECCCCC		18.33-
820PhosphorylationKKSVELDSDDGGGSA
HHHEECCCCCCCCCH		50.6725521595
826PhosphorylationDSDDGGGSAAQKQKI
CCCCCCCCHHHHHHH		24.5729899451
832UbiquitinationGSAAQKQKISFLENN
CCHHHHHHHHHHHHC		47.56-
845UbiquitinationNNLEQLTKVHKQLVR
HCHHHHHHHHHHHHH		51.43-
848UbiquitinationEQLTKVHKQLVRDNA
HHHHHHHHHHHHCCC		48.6027667366
871PhosphorylationLEKRLRATAERVKAL
HHHHHHHHHHHHHHH		23.7118779572
918PhosphorylationNMARRAHSAQIAKPI
HHHHHHHHHCCCCCC		22.3829899451
930PhosphorylationKPIRPGHYPASSPTA
CCCCCCCCCCCCCCE		13.3529233185
933PhosphorylationRPGHYPASSPTAVHA
CCCCCCCCCCCEEEE		32.1421930439
934PhosphorylationPGHYPASSPTAVHAV
CCCCCCCCCCEEEEC		28.5126824392
936PhosphorylationHYPASSPTAVHAVRG
CCCCCCCCEEEECCC		43.1722817900
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
176SPhosphorylationKinaseMAPK10P53779
GPS
176SPhosphorylationKinaseJNK3Q61831
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF5C_MOUSE !!
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 KIF5C_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KINH_MOUSEKif5bphysical
15834408
KIF5C_MOUSEKif5cphysical
15834408
KINH_MOUSEKif5bphysical
10964943
KIF5A_MOUSEKif5aphysical
10964943
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF5C_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-338 AND THR-796, ANDMASS SPECTROMETRY.

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