TBA1B_MOUSE - dbPTM
TBA1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA1B_MOUSE
UniProt AC P05213
Protein Name Tubulin alpha-1B chain
Gene Name Tuba1b
Organism Mus musculus (Mouse).
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 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
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
20.5015345747
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.512736326
40UbiquitinationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.51-
40MethylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5112692561
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8225521595
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7425521595
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.8524925903
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0225521595
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0025159016
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6819850273
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
73PhosphorylationVFVDLEPTVIDEVRT
EEECCCCEEEHHCCC
22.2522817900
80PhosphorylationTVIDEVRTGTYRQLF
EEEHHCCCCCCHHCC
38.7722006019
82PhosphorylationIDEVRTGTYRQLFHP
EHHCCCCCCHHCCCH
18.2126060331
83PhosphorylationDEVRTGTYRQLFHPE
HHCCCCCCHHCCCHH
9.5626060331
94PhosphorylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH
51.2827600695
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7127667366
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7123201123
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.4822817900
108PhosphorylationNNYARGHYTIGKEII
HHCCCCCCCCCHHHH
11.6825195567
109PhosphorylationNYARGHYTIGKEIID
HCCCCCCCCCHHHHH
19.9926824392
112UbiquitinationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.72-
124AcetylationLVLDRIRKLADQCTG
HHHHHHHHHHHHCCC
45.73156237
140UbiquitinationQGFLVFHSFGGGTGS
CCEEEEEECCCCCCC
17.7027667366
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.1127180971
161PhosphorylationMERLSVDYGKKSKLE
HHHHCCCCCCCCCEE
28.7929472430
163AcetylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.87129189
163UbiquitinationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8727667366
163SuccinylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8723954790
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.7527667366
165PhosphorylationSVDYGKKSKLEFSIY
CCCCCCCCCEEEEEE
46.06-
166UbiquitinationVDYGKKSKLEFSIYP
CCCCCCCCEEEEEEE
62.00-
207UbiquitinationCAFMVDNEAIYDICR
EEEEECHHHHHHHHH
31.7927667366
208UbiquitinationAFMVDNEAIYDICRR
EEEECHHHHHHHHHC
16.3427667366
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.3022817900
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCHHCHHHH
49.5522817900
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCHHCHHHHH
9.0522817900
225PhosphorylationDIERPTYTNLNRLIS
CCCCCCHHCHHHHHH
35.3922817900
232PhosphorylationTNLNRLISQIVSSIT
HCHHHHHHHHHHHHH
20.6026824392
236PhosphorylationRLISQIVSSITASLR
HHHHHHHHHHHHHCC
20.0423984901
237PhosphorylationLISQIVSSITASLRF
HHHHHHHHHHHHCCC
17.0523984901
271PhosphorylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0925159016
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.8725159016
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5225159016
277O-linked_GlycosylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5220547045
280UbiquitinationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.70-
282Nitrated tyrosineVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
282PhosphorylationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.5626745281
282NitrationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
287PhosphorylationKAYHEQLSVAEITNA
HHHHHHCCHHHHHHH
20.9825521595
292PhosphorylationQLSVAEITNACFEPA
HCCHHHHHHHHCCCH
14.3123984901
295S-nitrosocysteineVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.27-
295S-nitrosylationVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.2719101475
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.81-
311UbiquitinationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.23-
315S-nitrosocysteineRHGKYMACCLLYRGD
CCCCEEEEHHHCCCC
0.67-
315S-nitrosylationRHGKYMACCLLYRGD
CCCCEEEEHHHCCCC
0.6720925432
316S-nitrosocysteineHGKYMACCLLYRGDV
CCCEEEEHHHCCCCC
1.81-
316S-nitrosylationHGKYMACCLLYRGDV
CCCEEEEHHHCCCCC
1.8124926564
319PhosphorylationYMACCLLYRGDVVPK
EEEEHHHCCCCCCCC
10.2922817900
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.8027667366
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.8023201123
334PhosphorylationDVNAAIATIKTKRSI
CHHHHHHHCCCCCEE
19.5226824392
336UbiquitinationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.5727667366
337PhosphorylationAAIATIKTKRSIQFV
HHHHHCCCCCEEEEE
28.0426745281
338UbiquitinationAIATIKTKRSIQFVD
HHHHCCCCCEEEEEE
38.86-
339MethylationIATIKTKRSIQFVDW
HHHCCCCCEEEEEEE
44.20-
340PhosphorylationATIKTKRSIQFVDWC
HHCCCCCEEEEEEEC
23.4625521595
347S-nitrosocysteineSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.55-
347GlutathionylationSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5524333276
347S-nitrosylationSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5522588120
347S-palmitoylationSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5528526873
349PhosphorylationQFVDWCPTGFKVGIN
EEEEECCCCEEEEEE
52.7125159016
352AcetylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.6869933
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.0725521595
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH
40.6025159016
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3127667366
376S-nitrosocysteineAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.90-
376S-nitrosylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9020925432
376S-palmitoylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9028526873
379PhosphorylationQRAVCMLSNTTAIAE
HHHHHHHCCHHHHHH
12.7822817900
380UbiquitinationRAVCMLSNTTAIAEA
HHHHHHCCHHHHHHH
37.1727667366
381PhosphorylationAVCMLSNTTAIAEAW
HHHHHCCHHHHHHHH
17.7723984901
382PhosphorylationVCMLSNTTAIAEAWA
HHHHCCHHHHHHHHH
21.9523984901
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9927667366
394SuccinylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9923954790
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.1026745281
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11129185
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1127667366
401SuccinylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1123954790
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC
5.4525777480
414UbiquitinationWYVGEGMEEGEFSEA
HHCCCCCCCCCHHHH
73.9527667366
419PhosphorylationGMEEGEFSEAREDMA
CCCCCCHHHHHHHHH
26.5022817900
432PhosphorylationMAALEKDYEEVGVDS
HHHHHHCHHHHCCCC
25.6725619855
438UbiquitinationDYEEVGVDSVEGEGE
CHHHHCCCCCCCCCC
40.8227667366
439PhosphorylationYEEVGVDSVEGEGEE
HHHHCCCCCCCCCCC
21.4725521595
4455-glutamyl polyglutamateDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
445UbiquitinationDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.8827667366
445Formation of an isopeptide bondDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.881967194
451PhosphorylationGEEEGEEY-------
CCCCCCCC-------
21.3925619855
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 TBA1B_MOUSE !!

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

19564401
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 TBA1B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNJA1_HUMANDNAJA1physical
20360068

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA1B_MOUSE

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Related Literatures of Post-Translational Modification

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