KIF5A_HUMAN - dbPTM
KIF5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF5A_HUMAN
UniProt AC Q12840
Protein Name Kinesin heavy chain isoform 5A
Gene Name KIF5A
Organism Homo sapiens (Human).
Sequence Length 1032
Subcellular Localization Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Concentrated in the cell body of the neurons, particularly in the perinuclear region..
Protein Description Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons..
Protein Sequence MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQATPSSTSDMYFANSCTSSGATSSGGPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS
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
2Acetylation------MAETNNECS
------CCCCCCCCE		43.5619413330
138UbiquitinationIKVSYFEIYLDKIRD
EEEEEEEHHHHHHHH		2.7232142685
152UbiquitinationDLLDVTKTNLSVHED
HHHHHHCCCCCCCCC		31.8433845483
152PhosphorylationDLLDVTKTNLSVHED
HHHHHHCCCCCCCCC		31.84-
155PhosphorylationDVTKTNLSVHEDKNR
HHHCCCCCCCCCCCC		24.4125159151
1602-HydroxyisobutyrylationNLSVHEDKNRVPFVK
CCCCCCCCCCCCCCC		43.60-
160AcetylationNLSVHEDKNRVPFVK
CCCCCCCCCCCCCCC		43.6023236377
160UbiquitinationNLSVHEDKNRVPFVK
CCCCCCCCCCCCCCC		43.60-
164UbiquitinationHEDKNRVPFVKGCTE
CCCCCCCCCCCCCHH		25.6933845483
170PhosphorylationVPFVKGCTERFVSSP
CCCCCCCHHHHCCCH		38.57-
196PhosphorylationSNRHVAVTNMNEHSS
CCCEEEEECCCCCCC		21.0021406692
202PhosphorylationVTNMNEHSSRSHSIF
EECCCCCCCCCCEEE		22.6721406692
203PhosphorylationTNMNEHSSRSHSIFL
ECCCCCCCCCCEEEE		39.4421406692
205PhosphorylationMNEHSSRSHSIFLIN
CCCCCCCCCEEEEEE		24.43-
223UbiquitinationENMETEQKLSGKLYL
HHHHHHHHHCCEEEE		38.0923000965
225PhosphorylationMETEQKLSGKLYLVD
HHHHHHHCCEEEEEE		40.7029391485
227UbiquitinationTEQKLSGKLYLVDLA
HHHHHCCEEEEEECC		30.4923000965
229PhosphorylationQKLSGKLYLVDLAGS
HHHCCEEEEEECCCC		14.2528152594
241UbiquitinationAGSEKVSKTGAEGAV
CCCCCCCCCCCCCCH		54.7033845483
253UbiquitinationGAVLDEAKNINKSLS
CCHHHHHHHHHHHHH		57.2022817900
257UbiquitinationDEAKNINKSLSALGN
HHHHHHHHHHHHHHH		49.3122817900
291PhosphorylationMTRILQDSLGGNCRT
HHHHHHHHCCCCCEE		18.8925954137
298PhosphorylationSLGGNCRTTMFICCS
HCCCCCEEEEEEEEC		25.4725954137
299PhosphorylationLGGNCRTTMFICCSP
CCCCCEEEEEEEECC		7.25-
305PhosphorylationTTMFICCSPSSYNDA
EEEEEEECCHHCCCH		24.3325954137
308PhosphorylationFICCSPSSYNDAETK
EEEECCHHCCCHHHC		31.1925954137
309PhosphorylationICCSPSSYNDAETKS
EEECCHHCCCHHHCH		22.7725954137
314PhosphorylationSSYNDAETKSTLMFG
HHCCCHHHCHHHHHC		31.8329759185
316PhosphorylationYNDAETKSTLMFGQR
CCCHHHCHHHHHCHH		33.91-
317PhosphorylationNDAETKSTLMFGQRA
CCHHHCHHHHHCHHC		24.65-
326PhosphorylationMFGQRAKTIKNTASV
HHCHHCCCCCCCCCC		35.88-
348AcetylationQWKKKYEKEKEKTKA
HHHHHHHHHHHHHHH		71.626570425
368PhosphorylationAKLEAELSRWRNGEN
HHHHHHHHHHHCCCC		22.6924702127
397PhosphorylationGAELCEETPVNDNSS
CHHHCCCCCCCCCCC		15.39-
417PhosphorylationAPEERQKYEEEIRRL
CHHHHHHHHHHHHHH		21.8927642862
644PhosphorylationEAKIRSLTEYMQSVE
HHHHHHHHHHHHHHH		26.7328509920
646PhosphorylationKIRSLTEYMQSVELK
HHHHHHHHHHHHHHH		8.6728509920
649PhosphorylationSLTEYMQSVELKKRH
HHHHHHHHHHHHHHH		10.8828509920
660PhosphorylationKKRHLEESYDSLSDE
HHHHHHHHHHHHHHH		25.5122210691
665PhosphorylationEESYDSLSDELAKLQ
HHHHHHHHHHHHHHH		32.7522210691
705PhosphorylationALELQMESHREAHHR
HHHHHHHHHHHHHHH		23.6221406692
753UbiquitinationQADYEKLKSEEHEKS
HHHHHHHCCHHHHHH		67.8832015554
793PhosphorylationTVARELQTLHNLRKL
HHHHHHHHHHHHHHH		42.4821082442
806PhosphorylationKLFVQDVTTRVKKSA
HHHHHHHHHHHHHHC		19.7128509920
807PhosphorylationLFVQDVTTRVKKSAE
HHHHHHHHHHHHHCC		33.0628509920
831PhosphorylationHSQKQKISFLENNLE
CCHHHHHHHHHHHHH		30.7125159151
838PhosphorylationSFLENNLEQLTKVHK
HHHHHHHHHHHHHHH		45.7432142685
842UbiquitinationNNLEQLTKVHKQLVR
HHHHHHHHHHHHHHH		51.4332015554
845UbiquitinationEQLTKVHKQLVRDNA
HHHHHHHHHHHHCCC		48.6029967540
863UbiquitinationCELPKLEKRLRATAE
CCHHHHHHHHHHHHH		68.1424816145
883AcetylationEGALKEAKEGAMKDK
HHHHHHHHHHHHHCH		58.747369499
888AcetylationEAKEGAMKDKRRYQQ
HHHHHHHHCHHHHHH		60.617369509
890AcetylationKEGAMKDKRRYQQEV
HHHHHHCHHHHHHHH		33.007693111
899MethylationRYQQEVDRIKEAVRY
HHHHHHHHHHHHHHH		47.24-
915PhosphorylationSSGKRGHSAQIAKPV
CCCCCCCCCEECCCC		25.3728348404
927PhosphorylationKPVRPGHYPASSPTN
CCCCCCCCCCCCCCC		13.3532142685
930PhosphorylationRPGHYPASSPTNPYG
CCCCCCCCCCCCCCC		32.1428152594
931PhosphorylationPGHYPASSPTNPYGT
CCCCCCCCCCCCCCC		37.5428152594
933PhosphorylationHYPASSPTNPYGTRS
CCCCCCCCCCCCCCC		51.2628152594
936PhosphorylationASSPTNPYGTRSPEC
CCCCCCCCCCCCHHH		32.9527732954
938PhosphorylationSPTNPYGTRSPECIS
CCCCCCCCCCHHHHH		23.3328152594
1032PhosphorylationLHQETAAS-------
CCHHHCCC-------		37.9929759185
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 KIF5A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF5A_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 KIF5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DTNB_HUMANDTNBphysical
14600269
KLC2_HUMANKLC2physical
22939629
KLC1_HUMANKLC1physical
22939629
KLC4_HUMANKLC4physical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604187Spastic paraplegia 10, autosomal dominant (SPG10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF5A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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