TBA1C_RAT - dbPTM
TBA1C_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA1C_RAT
UniProt AC Q6AYZ1
Protein Name Tubulin alpha-1C chain
Gene Name Tuba1c
Organism Rattus norvegicus (Rat).
Sequence Length 449
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 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLARVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSAEGDDEGEEY
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
46.513325293
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8227097102
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7427097102
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.8527097102
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0223984901
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0023984901
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6820679923
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
80PhosphorylationTVIDEVRTGTYRQLF
EEEHHCCCCCCHHCC
38.7723984901
82PhosphorylationIDEVRTGTYRQLFHP
EHHCCCCCCHHCCCH
18.2123984901
83PhosphorylationDEVRTGTYRQLFHPE
HHCCCCCCHHCCCHH
9.5623984901
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7130595941
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.4827097102
108PhosphorylationNNYARGHYTIGKEII
HHCCCCCCCCCHHHH
11.6827097102
109PhosphorylationNYARGHYTIGKEIID
HCCCCCCCCCHHHHH
19.9927097102
140PhosphorylationQGFLVFHSFGGGTGS
CCEEEEEECCCCCCC
17.7030240740
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.1130240740
163UbiquitinationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.87-
163AcetylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.873325305
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.75-
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.30-
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCHHCHHHH
49.5527097102
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCHHCHHHHH
9.0527097102
225PhosphorylationDIERPTYTNLNRLIS
CCCCCCHHCHHHHHH
35.3927097102
232PhosphorylationTNLNRLISQIVSSIT
HCHHHHHHHHHHHHH
20.6028689409
237PhosphorylationLISQIVSSITASLRF
HHHHHHHHHHHHCCC
17.0523984901
271PhosphorylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0930240740
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.87-
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5223984901
282Nitrated tyrosineVISAEKAYHEQLTVA
CCCHHHHHHHCCCHH
19.56-
282NitrationVISAEKAYHEQLTVA
CCCHHHHHHHCCCHH
19.56-
311UbiquitinationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.23-
312PhosphorylationCDPRHGKYMACCLLY
CCCCCCCEEEEHHHC
8.44-
319PhosphorylationYMACCLLYRGDVVPK
EEEEHHHCCCCCCCC
10.29-
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.80-
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.8022632561
334PhosphorylationDVNAAIATIKTKRTI
CCHHHHHHCCCCCEE
19.5227097102
336UbiquitinationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.57-
336AcetylationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.573325315
337PhosphorylationAAIATIKTKRTIQFV
HHHHHCCCCCEEEEE
23.1623984901
338UbiquitinationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.41-
340PhosphorylationATIKTKRTIQFVDWC
HHCCCCCEEEEEEEC
22.2323984901
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCCCCC
22.07-
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCCCCCCCHH
40.60-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.993325343
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.10-
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.113325341
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC
5.4525403869
432PhosphorylationMAALEKDYEEVGADS
HHHHHHHHHHHCCCC
25.6728689409
439PhosphorylationYEEVGADSAEGDDEG
HHHHCCCCCCCCCCC
27.9029779826
449NitrationGDDEGEEY-------
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 TBA1C_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 TBA1C_RAT !!

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

Oops, there are no PPI records of TBA1C_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA1C_RAT

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Related Literatures of Post-Translational Modification

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