KBP_MOUSE - dbPTM
KBP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KBP_MOUSE
UniProt AC Q6ZPU9
Protein Name KIF1-binding protein {ECO:0000250|UniProtKB:Q96EK5}
Gene Name Kif1bp {ECO:0000250|UniProtKB:Q96EK5}
Organism Mus musculus (Mouse).
Sequence Length 617
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description Required for neuronal development and differentiation. Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development..
Protein Sequence MANAPGPEIREKFQAALALSRVELHKNPEKEPYKSKYGARALLEEVRALLGPAPEDEDEPAADDGPGDQALGAGEPREAEGPGAQRALRLAVVEFHLGVNHIDTEELSAGEEHLVRCLSLLRPYRLSLGCVSLYIQAQNNLGILWSEREEIETARTYLESSEALYSQYMKEIGSPPLDPTEHFLPEEEKLTEQERSKRFEKVYTHNLYYLAQVYQHMEMFEKAAHYCHSTLKRQLEHNAYHPMEWAINAATLSQFYINKLCFMEARHCLSAANVIFGQTGKIPATEDTPEVEGDVPELYHQRKGEIARCWIKYCLTLMQNAQLSMQDNIGELDLDKQSELRALRKKELDEEESVRKRAVQFGTGELCDAISAVEEKVRYLRPLDFEEARELFLLGQHYVCEAKEFFQIDGYVTDHIEVVQDHSALFKVLSFFEADMERRCKMHKRRIAMLEPLTVDLNPQYYLLVSRQIQFEIAHAYYDMMDLKVAIADKLRDPDSHIVKKINSLNKSALKYYQLFLDSLRDPNKVFPEHIGEDVLRPAMLAKFRVARLYGKIITADPKKELENLATSLEHYKFIVDYCETHPEAAQEIEVELELSKEMVSLLPTKMERFRAKMALT
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
161PhosphorylationARTYLESSEALYSQY
HHHHHHCHHHHHHHH
19.95-
166PhosphorylationESSEALYSQYMKEIG
HCHHHHHHHHHHHHC
18.71-
168PhosphorylationSEALYSQYMKEIGSP
HHHHHHHHHHHHCCC
12.29-
174PhosphorylationQYMKEIGSPPLDPTE
HHHHHHCCCCCCCCC
29.0728066266
477PhosphorylationQFEIAHAYYDMMDLK
HHHHHHHHHHHHHHH
7.0728507225
490UbiquitinationLKVAIADKLRDPDSH
HHHHHHHHCCCCCCH
36.0822790023
496PhosphorylationDKLRDPDSHIVKKIN
HHCCCCCCHHHHHHH
22.0926824392
504PhosphorylationHIVKKINSLNKSALK
HHHHHHHHCCHHHHH
36.4725338131
507UbiquitinationKKINSLNKSALKYYQ
HHHHHCCHHHHHHHH
42.2627667366
543UbiquitinationLRPAMLAKFRVARLY
HHHHHHHHHHHHHHH
29.7322790023
552UbiquitinationRVARLYGKIITADPK
HHHHHHCCEECCCCH
19.8522790023
559UbiquitinationKIITADPKKELENLA
CEECCCCHHHHHHHH
60.4727667366
560UbiquitinationIITADPKKELENLAT
EECCCCHHHHHHHHH
73.2922790023
606UbiquitinationMVSLLPTKMERFRAK
HHHHCCHHHHHHHHH
36.5022790023

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 KBP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KBP_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 KBP_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTB_HUMANACTBphysical
26496610
AP2B1_HUMANAP2B1physical
26496610
ERCC5_HUMANERCC5physical
26496610
MYL6_HUMANMYL6physical
26496610
MYPT1_HUMANPPP1R12Aphysical
26496610
SPG7_HUMANSPG7physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
TAF1_HUMANTAF1physical
26496610
TPM1_HUMANTPM1physical
26496610
TPM4_HUMANTPM4physical
26496610
AK17A_HUMANAKAP17Aphysical
26496610
SC16A_HUMANSEC16Aphysical
26496610
KIF14_HUMANKIF14physical
26496610
TMOD3_HUMANTMOD3physical
26496610
FEM1A_HUMANFEM1Aphysical
26496610
MIER1_HUMANMIER1physical
26496610
CHD9_HUMANCHD9physical
26496610
KI18A_HUMANKIF18Aphysical
26496610
KLC3_HUMANKLC3physical
26496610
CA052_HUMANC1orf52physical
26496610
MY18A_HUMANMYO18Aphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KBP_MOUSE

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Related Literatures of Post-Translational Modification

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