TBB3_RAT - dbPTM
TBB3_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBB3_RAT
UniProt AC Q4QRB4
Protein Name Tubulin beta-3 chain
Gene Name Tubb3
Organism Rattus norvegicus (Rat).
Sequence Length 450
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and mantainance (By similarity)..
Protein Sequence MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDDEESEAQGPK
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
55PhosphorylationSVYYNEASSHKYVPR
EEEECCCCCCCCCCE
27.1422673903
56PhosphorylationVYYNEASSHKYVPRA
EEECCCCCCCCCCEE
30.9222673903
58AcetylationYNEASSHKYVPRAIL
ECCCCCCCCCCEEEE
50.3022902405
58UbiquitinationYNEASSHKYVPRAIL
ECCCCCCCCCCEEEE
50.30-
72PhosphorylationLVDLEPGTMDSVRSG
EEECCCCCCHHHHCC
28.6423984901
75PhosphorylationLEPGTMDSVRSGAFG
CCCCCCHHHHCCCCC
14.4927097102
106PhosphorylationNNWAKGHYTEGAELV
CCCCCCCCCCHHHHH
18.37-
115PhosphorylationEGAELVDSVLDVVRK
CHHHHHHHHHHHHHH
19.6623984901
136PhosphorylationCLQGFQLTHSLGGGT
CCCCEEEEEECCCCC
9.9130240740
138PhosphorylationQGFQLTHSLGGGTGS
CCEEEEEECCCCCCC
24.3930240740
143PhosphorylationTHSLGGGTGSGMGTL
EEECCCCCCCCHHHH
31.3023984901
145PhosphorylationSLGGGTGSGMGTLLI
ECCCCCCCCHHHHHH
25.9930240740
168PhosphorylationDRIMNTFSVVPSPKV
CCCCCCEECCCCCCC
21.8423984901
172PhosphorylationNTFSVVPSPKVSDTV
CCEECCCCCCCCCCE
26.2430240740
216UbiquitinationDICFRTLKLATPTYG
HHHHHHCCCCCCCCH
35.15-
274PhosphorylationMPGFAPLTARGSQQY
CCCCCCCCCCCCHHH
17.1623984901
278PhosphorylationAPLTARGSQQYRALT
CCCCCCCCHHHEEEE
14.4623984901
281PhosphorylationTARGSQQYRALTVPE
CCCCCHHHEEEEHHH
7.1023984901
290PhosphorylationALTVPELTQQMFDAK
EEEHHHHHHHHHCCC
18.32-
310PhosphorylationCDPRHGRYLTVATVF
CCCCCCCEEEHEEEE
16.0026022182
315PhosphorylationGRYLTVATVFRGRMS
CCEEEHEEEEECCCC
18.8126022182
324AcetylationFRGRMSMKEVDEQML
EECCCCHHHHHHHHH
47.4872588455
338PhosphorylationLAIQSKNSSYFVEWI
HHHHHCCCCCEEEEC
30.1027097102
339PhosphorylationAIQSKNSSYFVEWIP
HHHHCCCCCEEEECC
31.8023984901
340PhosphorylationIQSKNSSYFVEWIPN
HHHCCCCCEEEECCC
16.0927097102
362UbiquitinationDIPPRGLKMSSTFIG
CCCCCCCCCCCCCCC
39.29-
379AcetylationTAIQELFKRISEQFT
HHHHHHHHHHHHHHH
62.54134801
409PhosphorylationGMDEMEFTEAESNMN
CCCHHCCCHHHHHHH
22.4512631274
420PhosphorylationSNMNDLVSEYQQYQD
HHHHHHHHHHHHHHC
37.5712631274
438Formation of an isopeptide bondEEEGEMYEDDDEESE
HHHCCCCCCCCHHHH
54.37-
4385-glutamyl polyglutamateEEEGEMYEDDDEESE
HHHCCCCCCCCHHHH
54.37-
444PhosphorylationYEDDDEESEAQGPK-
CCCCCHHHHHCCCC-
35.8622817900

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
172SPhosphorylationKinaseCDK1P39951
Uniprot
444SPhosphorylationKinaseCSNK2A1P19139
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
172SPhosphorylation

-

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 TBB3_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPYL2_RATDpysl2physical
12134159

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBB3_RAT

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Related Literatures of Post-Translational Modification

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