MAP6_HUMAN - dbPTM
MAP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAP6_HUMAN
UniProt AC Q96JE9
Protein Name Microtubule-associated protein 6
Gene Name MAP6
Organism Homo sapiens (Human).
Sequence Length 813
Subcellular Localization Cytoplasm, cytoskeleton . Golgi apparatus . Cell projection, axon . Cell projection, dendrite . Cytoplasmic vesicle, secretory vesicle membrane
Lipid-anchor
Cytoplasmic side . Localizes predominantly in the proximal part of the axon (By similarit
Protein Description Involved in microtubule stabilization in many cell types, including neuronal cells (By similarity). Specifically has microtubule cold stabilizing activity (By similarity). Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B. [PubMed: 24357581 Regulates KIF5A-mediated axonal cargo transport (By similarity Regulates axonal growth during neuron polarization (By similarity]
Protein Sequence MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPPPQQQAQPALAPPSARAVAIETQPAQGELDAVARATGPAPGPTGEREPAAGPGRSGPGPGLGSGSTSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQISAASQASAPILGAPKRRPQSQERWPVQAAAEAREQEAAPGGAGGLAAGKASGADERDTRRKAGPAWIVRRAEGLGHEQTPLPAAQAQVQATGPEAGRGRAAADALNRQIREEVASAVSSSYRNEFRAWTDIKPVKPIKAKPQYKPPDDKMVHETSYSAQFKGEASKPTTADNKVIDRRRIRSLYSEPFKEPPKVEKPSVQSSKPKKTSASHKPTRKAKDKQAVSGQAAKKKSAEGPSTTKPDDKEQSKEMNNKLAEAKESLAQPVSDSSKTQGPVATEPDKDQGSVVPGLLKGQGPMVQEPLKKQGSVVPGPPKDLGPMIPLPVKDQDHTVPEPLKNESPVISAPVKDQGPSVPVPPKNQSPMVPAKVKDQGSVVPESLKDQGPRIPEPVKNQAPMVPAPVKDEGPMVSASVKDQGPMVSAPVKDQGPIVPAPVKGEGPIVPAPVKDEGPMVSAPIKDQDPMVPEHPKDESAMATAPIKNQGSMVSEPVKNQGLVVSGPVKDQDVVVPEHAKVHDSAVVAPVKNQGPVVPESVKNQDPILPVLVKDQGPTVLQPPKNQGRIVPEPLKNQVPIVPVPLKDQDPLVPVPAKDQGPAVPEPLKTQGPRDPQLPTVSPLPRVMIPTAPHTEYIESSP
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
5S-palmitoylation---MAWPCITRACCI
---CCCHHHHHHHHH
3.28-
10S-palmitoylationWPCITRACCIARFWN
CHHHHHHHHHHHHHH
1.23-
11S-palmitoylationPCITRACCIARFWNQ
HHHHHHHHHHHHHHH
2.38-
31O-linked_GlycosylationIAVPLVFTKYSEATE
CEEEEEEEECHHHCC
22.9230379171
90PhosphorylationTGPAPGPTGEREPAA
HCCCCCCCCCCCCCC
58.55-
102PhosphorylationPAAGPGRSGPGPGLG
CCCCCCCCCCCCCCC
56.0821955146
110PhosphorylationGPGPGLGSGSTSGPA
CCCCCCCCCCCCCCC
34.3121955146
112PhosphorylationGPGLGSGSTSGPADS
CCCCCCCCCCCCCHH
22.5423684312
113PhosphorylationPGLGSGSTSGPADSV
CCCCCCCCCCCCHHH
41.0321955146
114PhosphorylationGLGSGSTSGPADSVM
CCCCCCCCCCCHHHH
44.4721955146
119PhosphorylationSTSGPADSVMRQDYR
CCCCCCHHHHHHHHH
21.6621955146
143PhosphorylationSCRPRSEYQPSDAPF
CCCCCCCCCCCCCCC
27.2825884760
181PhosphorylationIPKPVQISAASQASA
CCCCEEECCCCCCCC
10.7427174698
184PhosphorylationPVQISAASQASAPIL
CEEECCCCCCCCCCC
26.4627174698
187PhosphorylationISAASQASAPILGAP
ECCCCCCCCCCCCCC
27.2627174698
200PhosphorylationAPKRRPQSQERWPVQ
CCCCCCCCCCCCHHH
36.3727174698
229UbiquitinationAGGLAAGKASGADER
CCHHHHHHCCCCCHH
34.3530230243
295PhosphorylationQIREEVASAVSSSYR
HHHHHHHHHHHHHHH
34.0929449344
298PhosphorylationEEVASAVSSSYRNEF
HHHHHHHHHHHHHCC
17.1829449344
299PhosphorylationEVASAVSSSYRNEFR
HHHHHHHHHHHHCCC
25.4529449344
300PhosphorylationVASAVSSSYRNEFRA
HHHHHHHHHHHCCCC
22.1729449344
301PhosphorylationASAVSSSYRNEFRAW
HHHHHHHHHHCCCCC
21.2929449344
329AcetylationQYKPPDDKMVHETSY
CCCCCCCCCCCCCCC
50.6419826911
336PhosphorylationKMVHETSYSAQFKGE
CCCCCCCCCEEECCC
18.5525884760
346AcetylationQFKGEASKPTTADNK
EECCCCCCCCCCCCC
54.1319826595
362PhosphorylationIDRRRIRSLYSEPFK
ECHHHHHHHHCCCCC
29.3232142685
364PhosphorylationRRRIRSLYSEPFKEP
HHHHHHHHCCCCCCC
16.5425884760
369UbiquitinationSLYSEPFKEPPKVEK
HHHCCCCCCCCCCCC
78.8732142685
396AcetylationASHKPTRKAKDKQAV
CCCCCCCHHHHHHCC
63.3769859
398AcetylationHKPTRKAKDKQAVSG
CCCCCHHHHHHCCCH
69.3769863
438AcetylationNNKLAEAKESLAQPV
HHHHHHHHHHHCCCC
39.0619818113
446O-linked_GlycosylationESLAQPVSDSSKTQG
HHHCCCCCCCCCCCC
38.1630379171
457O-linked_GlycosylationKTQGPVATEPDKDQG
CCCCCCCCCCCCCCC
48.5730379171
487PhosphorylationEPLKKQGSVVPGPPK
CCHHHCCCCCCCCCH
19.9024719451
519PhosphorylationPEPLKNESPVISAPV
CCCCCCCCCCEECCC
33.5826657352
523PhosphorylationKNESPVISAPVKDQG
CCCCCCEECCCCCCC
27.1025332170
541PhosphorylationPVPPKNQSPMVPAKV
CCCCCCCCCCCCCEE
25.1024719451
553PhosphorylationAKVKDQGSVVPESLK
CEECCCCCCCCHHHH
17.8229759185
651PhosphorylationPEHPKDESAMATAPI
CCCCCCCCCCCCCCC
33.2128270605
655PhosphorylationKDESAMATAPIKNQG
CCCCCCCCCCCCCCC
21.6328270605
663PhosphorylationAPIKNQGSMVSEPVK
CCCCCCCCCCCCCCC
13.2728270605
666PhosphorylationKNQGSMVSEPVKNQG
CCCCCCCCCCCCCCC
27.7828270605
791PhosphorylationPRDPQLPTVSPLPRV
CCCCCCCCCCCCCCE
42.0628348404
793PhosphorylationDPQLPTVSPLPRVMI
CCCCCCCCCCCCEEC
24.1724719451
811PhosphorylationPHTEYIESSP-----
CCCHHHCCCC-----
38.0527732954
812PhosphorylationHTEYIESSP------
CCHHHCCCC------
23.1018510355

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 MAP6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAP6_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 MAP6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MAP6_HUMAN !!

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 MAP6_HUMAN

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Related Literatures of Post-Translational Modification

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