TBA3C_HUMAN - dbPTM
TBA3C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA3C_HUMAN
UniProt AC Q13748
Protein Name Tubulin alpha-3C/D chain
Gene Name TUBA3C
Organism Homo sapiens (Human).
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..
Protein Sequence MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY
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
6Phosphorylation--MRECISIHVGQAG
--CCCEEEEEECCHH
20.50-
24PhosphorylationGNACWELYCLEHGIQ
CHHHHHCHHHHCCCC
5.40-
38PhosphorylationQPDGQMPSDKTIGGG
CCCCCCCCCCCCCCC
46.53-
40UbiquitinationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.82-
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7417924679
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.85-
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.02-
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.00-
60SumoylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6819811027
60 (in isoform 1)Ubiquitination-40.6821890473
60 (in isoform 2)Ubiquitination-40.6821890473
79MethylationPTVVDEVRTGTYRQL
CEEEECCCCCCCHHC
25.95-
94PhosphorylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH
51.28-
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7130582473
96 (in isoform 1)Ubiquitination-43.7121890473
96 (in isoform 2)Ubiquitination-43.7121890473
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.48-
108PhosphorylationNNYARGHYTIGKEIV
HHCCCCCCCCCHHHH
11.68-
109PhosphorylationNYARGHYTIGKEIVD
HCCCCCCCCCHHHHH
19.99-
112AcetylationRGHYTIGKEIVDLVL
CCCCCCCHHHHHHHH
40.1825038526
156MethylationFASLLMERLSVDYGK
HHHHHHHHHCCCCCC
20.49-
156MethylationFASLLMERLSVDYGK
HHHHHHHHHCCCCCC
20.4924390935
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.11-
161PhosphorylationMERLSVDYGKKSKLE
HHHHCCCCCCCCCCE
28.79-
163MethylationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.87-
163UbiquitinationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.87-
163AcetylationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.87-
163AcetylationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.87130867
163MethylationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.87130867
163UbiquitinationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.8721890473
163 (in isoform 1)Ubiquitination-47.8721890473
163 (in isoform 2)Ubiquitination-47.8721890473
164UbiquitinationLSVDYGKKSKLEFAI
HCCCCCCCCCCEEEE
48.75-
164UbiquitinationLSVDYGKKSKLEFAI
HCCCCCCCCCCEEEE
48.7520972266
164 (in isoform 1)Ubiquitination-48.7521890473
164 (in isoform 2)Ubiquitination-48.7521890473
165PhosphorylationSVDYGKKSKLEFAIY
CCCCCCCCCCEEEEE
46.06-
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.30-
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCCCCHHHH
49.55-
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCCCCHHHHH
9.05-
225PhosphorylationDIERPTYTNLNRLIG
CCCCCCCCCHHHHHH
35.39-
253PhosphorylationGALNVDLTEFQTNLV
CCCCCCCCEEECCCC
30.23-
257PhosphorylationVDLTEFQTNLVPYPR
CCCCEEECCCCCCCC
35.52-
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.87-
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.52-
280UbiquitinationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.70-
280AcetylationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.7088229
280UbiquitinationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.7021906983
280 (in isoform 1)Ubiquitination-54.7021890473
280 (in isoform 2)Ubiquitination-54.7021890473
282PhosphorylationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.5617016520
282NitrationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
287PhosphorylationKAYHEQLSVAEITNA
HHHHHHCCHHHHHHH
20.98-
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.81-
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8121890473
304 (in isoform 1)Ubiquitination-27.8121890473
304 (in isoform 2)Ubiquitination-27.8121890473
311AcetylationKCDPRHGKYMACCML
CCCCCCCCEEEEHHH
26.2325038526
326SumoylationYRGDVVPKDVNAAIA
CCCCCCCCCCCHHHH
63.80-
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCCCHHHH
63.80-
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCCCHHHH
63.80-
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCCCHHHH
63.8022632571
326 (in isoform 1)Ubiquitination-63.8021890473
326 (in isoform 2)Ubiquitination-63.8021890473
334PhosphorylationDVNAAIATIKTKRTI
CCCHHHHHCCCCCEE
19.52-
336SumoylationNAAIATIKTKRTIQF
CHHHHHCCCCCEEEE
43.57-
336UbiquitinationNAAIATIKTKRTIQF
CHHHHHCCCCCEEEE
43.57-
336AcetylationNAAIATIKTKRTIQF
CHHHHHCCCCCEEEE
43.57-
336AcetylationNAAIATIKTKRTIQF
CHHHHHCCCCCEEEE
43.5723749302
336UbiquitinationNAAIATIKTKRTIQF
CHHHHHCCCCCEEEE
43.5720639865
336 (in isoform 1)Ubiquitination-43.5721890473
336 (in isoform 2)Ubiquitination-43.5721890473
337PhosphorylationAAIATIKTKRTIQFV
HHHHHCCCCCEEEEE
23.16-
338MethylationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.41-
338UbiquitinationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.41-
338MethylationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.41184311
338UbiquitinationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.4121890473
338 (in isoform 1)Ubiquitination-42.4121890473
338 (in isoform 2)Ubiquitination-42.4121890473
340PhosphorylationATIKTKRTIQFVDWC
HHCCCCCEEEEEEEC
22.23-
347S-palmitoylationTIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5529575903
349PhosphorylationQFVDWCPTGFKVGIN
EEEEECCCCEEEEEE
52.71-
352SumoylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
352AcetylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68130869
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.07-
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH
40.60-
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370AcetylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370AcetylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31184313
370 (in isoform 1)Ubiquitination-46.3121890473
370 (in isoform 2)Ubiquitination-46.3121890473
379PhosphorylationQRAVCMLSNTTAIAE
HHHHHHHCCHHHHHH
12.78-
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99134085
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9921890473
394 (in isoform 1)Ubiquitination-39.9921890473
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.10-
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11130865
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1121890473
401 (in isoform 1)Ubiquitination-27.1121890473
419PhosphorylationGMEEGEFSEAREDLA
CCCCCCHHHHHHHHH
26.50-
439PhosphorylationYEEVGVDSVEAEAEE
HHHHCCCCCCCHHHC
21.32-
450NitrationEAEEGEEY-------
HHHCCCCC-------
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 TBA3C_HUMAN !!

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

24906155
40KMethylation

24906155

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 TBA3C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NMI_HUMANNMIphysical
16189514
TCPG_HUMANCCT3physical
26186194
TTC5_HUMANTTC5physical
26186194
TXND9_HUMANTXNDC9physical
26186194
T11L2_HUMANTCP11L2physical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
TBA1C_HUMANTUBA1Cphysical
26186194
MFS4B_HUMANKIAA1919physical
26186194
TBB4B_HUMANTUBB4Bphysical
26344197
T11L2_HUMANTCP11L2physical
28514442
TXND9_HUMANTXNDC9physical
28514442
TTC5_HUMANTTC5physical
28514442
TBA1A_HUMANTUBA1Aphysical
28514442
MFS4B_HUMANKIAA1919physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPG_HUMANCCT3physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA3C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND THR-51, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.

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