KIF5C_HUMAN - dbPTM
KIF5C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF5C_HUMAN
UniProt AC O60282
Protein Name Kinesin heavy chain isoform 5C
Gene Name KIF5C
Organism Homo sapiens (Human).
Sequence Length 957
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, dendrite . Abundant in distal regions of dendrites.
Protein Description Involved in synaptic transmission. [PubMed: 24812067 Mediates dendritic trafficking of mRNAs (By similarity Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.]
Protein Sequence MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKTLKNVIQHLEMELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNIAPVVAGISTEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAIRGGGGSSSNSTHYQK
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
21 (in isoform 2)Ubiquitination-14.2021906983
47PhosphorylationVIGQGKPYVFDRVLP
EECCCCCEEECCCCC
19.7527811184
165PhosphorylationEDKNRVPYVKGCTER
CCCCCCCCCCCCCHH
16.3730631047
167AcetylationKNRVPYVKGCTERFV
CCCCCCCCCCCHHCC
42.2819608861
167MalonylationKNRVPYVKGCTERFV
CCCCCCCCCCCHHCC
42.2826320211
196PhosphorylationANRHVAVTNMNEHSS
CCCEEEEECCCCCCC
21.0021406692
202PhosphorylationVTNMNEHSSRSHSIF
EECCCCCCCCCCEEE
22.6721406692
203PhosphorylationTNMNEHSSRSHSIFL
ECCCCCCCCCCEEEE
39.4421406692
205PhosphorylationMNEHSSRSHSIFLIN
CCCCCCCCCEEEEEE
24.43-
225PhosphorylationVETEKKLSGKLYLVD
CCCHHHHCCEEEEEE
42.6429391485
227UbiquitinationTEKKLSGKLYLVDLA
CHHHHCCEEEEEECC
30.49-
229PhosphorylationKKLSGKLYLVDLAGS
HHHCCEEEEEECCCC
14.2528152594
238MalonylationVDLAGSEKVSKTGAE
EECCCCCCCCCCCCC
54.2126320211
238AcetylationVDLAGSEKVSKTGAE
EECCCCCCCCCCCCC
54.2125953088
241UbiquitinationAGSEKVSKTGAEGAV
CCCCCCCCCCCCCCH
54.70-
253MalonylationGAVLDEAKNINKSLS
CCHHHHHHHHHHHHH
57.2026320211
253 (in isoform 1)Ubiquitination-57.2021906983
253UbiquitinationGAVLDEAKNINKSLS
CCHHHHHHHHHHHHH
57.20-
274UbiquitinationSALAEGTKTHVPYRD
HHHHHCCCCCCCCCC
47.71-
316PhosphorylationFNEAETKSTLMFGQR
CCCCHHHCCCHHCCC
33.91-
317PhosphorylationNEAETKSTLMFGQRA
CCCHHHCCCHHCCCC
24.65-
326PhosphorylationMFGQRAKTIKNTVSV
HHCCCCCCCCCEEEE
35.88-
348AcetylationEWKKKYEKEKEKNKT
HHHHHHHHHHHHCHH
71.626568141
396PhosphorylationNLEPCDNTPIIDNIA
CCCCCCCCCCCCCCH
11.5627732954
501UbiquitinationLAVNYDQKSQEVEDK
HHCCCCCCCHHHHHH
51.73-
590PhosphorylationEFTMARLYISKMKSE
HHHHHHHHHHHHHHH
9.5223836654
593AcetylationMARLYISKMKSEVKS
HHHHHHHHHHHHHHH
40.5725953088
596PhosphorylationLYISKMKSEVKSLVN
HHHHHHHHHHHHHHH
44.0923836654
610PhosphorylationNRSKQLESAQMDSNR
HHHHHHHHHHHHHHH
32.1821406692
615PhosphorylationLESAQMDSNRKMNAS
HHHHHHHHHHCCCHH
32.9421406692
639AcetylationLISQHEAKIKSLTDY
HHHHHHHHHHHHHHH
47.9125953088
660PhosphorylationKRRQLEESQDSLSEE
HHHHHHHHHHHHHHH
29.88-
681PhosphorylationQEKMHEVSFQDKEKE
HHHHHHCCCCHHHHH
17.7627422710
692MethylationKEKEHLTRLQDAEEM
HHHHHHHHHHCHHHH
36.39115390063
692DimethylationKEKEHLTRLQDAEEM
HHHHHHHHHHCHHHH
36.39-
711DimethylationEQQMESHREAHQKQL
HHHHHHHHHHHHHHH
52.67-
711MethylationEQQMESHREAHQKQL
HHHHHHHHHHHHHHH
52.67115390069
753PhosphorylationQEKLSSDYNKLKIED
HHHHHHHHHCCCHHH
19.02-
797PhosphorylationTVSRELQTLHNLRKL
HHHHHHHHHHHHHHH
42.4821082442
814AcetylationQDLTTRVKKSVELDN
HHHHHHHHHHEECCC
35.727851115
816PhosphorylationLTTRVKKSVELDNDD
HHHHHHHHEECCCCC
18.33-
835PhosphorylationAAQKQKISFLENNLE
HHHHHHHHHHHHCHH
30.7125159151
846UbiquitinationNNLEQLTKVHKQLVR
HCHHHHHHHHHHHHH
51.43-
849UbiquitinationEQLTKVHKQLVRDNA
HHHHHHHHHHHHCCC
48.60-
864AcetylationDLRCELPKLEKRLRA
CCCCCHHHHHHHHHH
80.1925953088
903MethylationRYQQEVDRIKEAVRA
HHHHHHHHHHHHHHH
47.24-
919PhosphorylationNMARRAHSAQIAKPI
HHHHHHHHHCCCCCC
22.3822496350
931PhosphorylationKPIRPGHYPASSPTA
CCCCCCCCCCCCCCE
13.3521406692
934PhosphorylationRPGHYPASSPTAVHA
CCCCCCCCCCCEEEE
32.1429255136
935PhosphorylationPGHYPASSPTAVHAI
CCCCCCCCCCEEEEC
28.5129255136
937PhosphorylationHYPASSPTAVHAIRG
CCCCCCCCEEEECCC
43.1729255136

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
338TPhosphorylationKinaseCK2-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF5C_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 KIF5C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KINH_HUMANKIF5Bphysical
9624122
CBY1_HUMANCBY1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615282Cortical dysplasia, complex, with other brain malformations 2 (CDCBM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF5C_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP