TBA1A_RAT - dbPTM
TBA1A_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA1A_RAT
UniProt AC P68370
Protein Name Tubulin alpha-1A chain
Gene Name Tuba1a
Organism Rattus norvegicus (Rat).
Sequence Length 451
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..
Protein Sequence MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
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
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5125786129
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8227097102
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7427097102
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.8527097102
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0223984901
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0023984901
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60"N6,N6-dimethyllysine"FSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60MethylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6822902405
61MethylationSETGAGKHVPRAVFV
CCCCCCCCCCEEEEE
33.624207429
64MethylationGAGKHVPRAVFVDLE
CCCCCCCEEEEECCC
42.154207423
64DimethylationGAGKHVPRAVFVDLE
CCCCCCCEEEEECCC
42.15-
80PhosphorylationTVIDEVRTGTYRQLF
EEEHHCCCCCCHHCC
38.7723984901
82PhosphorylationIDEVRTGTYRQLFHP
EHHCCCCCCHHCCCH
18.2123984901
83PhosphorylationDEVRTGTYRQLFHPE
HHCCCCCCHHCCCHH
9.5623984901
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7122902405
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.4827097102
103NitrationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.48-
108PhosphorylationNNYARGHYTIGKEII
HHCCCCCCCCCHHHH
11.6827097102
109PhosphorylationNYARGHYTIGKEIID
HCCCCCCCCCHHHHH
19.9927097102
140PhosphorylationQGFLVFHSFGGGTGS
CCEEEEEECCCCCCC
17.7030240740
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.1130240740
163AcetylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8713667149
163UbiquitinationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.87-
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.75-
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.30-
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCCCCHHHH
49.5527097102
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCCCCHHHHH
9.0527097102
225PhosphorylationDIERPTYTNLNRLIG
CCCCCCCCCHHHHHH
35.3927097102
271PhosphorylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0930240740
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.87-
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5223984901
282PhosphorylationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.5623984901
282Nitrated tyrosineVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
282NitrationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
287PhosphorylationKAYHEQLSVAEITNA
HHHHHHCCHHHHHHH
20.9823984901
292PhosphorylationQLSVAEITNACFEPA
HCCHHHHHHHHCCCH
14.3123984901
295S-nitrosylationVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.2722178444
295S-nitrosocysteineVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.27-
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.81-
311UbiquitinationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.23-
312PhosphorylationCDPRHGKYMACCLLY
CCCCCCCEEEEHHHC
8.44-
315S-nitrosylationRHGKYMACCLLYRGD
CCCCEEEEHHHCCCC
0.6722178444
315S-nitrosocysteineRHGKYMACCLLYRGD
CCCCEEEEHHHCCCC
0.67-
316S-nitrosylationHGKYMACCLLYRGDV
CCCEEEEHHHCCCCC
1.8122178444
316S-nitrosocysteineHGKYMACCLLYRGDV
CCCEEEEHHHCCCCC
1.81-
319PhosphorylationYMACCLLYRGDVVPK
EEEEHHHCCCCCCCC
10.29-
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.80-
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.8022902405
334PhosphorylationDVNAAIATIKTKRTI
CCHHHHHHCCCCCEE
19.5227097102
336UbiquitinationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.57-
336AcetylationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.5714497325
337PhosphorylationAAIATIKTKRTIQFV
HHHHHCCCCCEEEEE
23.1623984901
338UbiquitinationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.41-
340PhosphorylationATIKTKRTIQFVDWC
HHCCCCCEEEEEEEC
22.2323984901
347S-nitrosylationTIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5522178444
347S-nitrosocysteineTIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.55-
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.0723984901
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH
40.6023984901
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370AcetylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3125786129
376S-nitrosocysteineAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.90-
376S-nitrosylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9022178444
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9922902405
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.10-
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1122902405
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC
5.4525403869
432PhosphorylationMAALEKDYEEVGVDS
HHHHHHCHHHHCCCC
25.6728689409
439PhosphorylationYEEVGVDSVEGEGEE
HHHHCCCCCCCCCCC
21.4729779826
4455-glutamyl polyglutamateDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
445Formation of an isopeptide bondDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
451NitrationGEEEGEEY-------
CCCCCCCC-------
21.39-

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 TBA1A_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
40KAcetylation

-
40KMethylation

-

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 TBA1A_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPN1_RATEpn1physical
12750376
EPN2_RATEpn2physical
12750376
GRM7_RATGrm7physical
11953448
ATX3_RATAtxn3physical
19666135
HDAC6_HUMANHDAC6physical
19961433
DPYL2_RATDpysl2physical
12134159

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA1A_RAT

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Related Literatures of Post-Translational Modification

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