TBA3_MOUSE - dbPTM
TBA3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA3_MOUSE
UniProt AC P05214
Protein Name Tubulin alpha-3 chain
Gene Name Tuba3a
Organism Mus musculus (Mouse).
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
20.5015345747
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.518275617
40UbiquitinationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.51-
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8225521595
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7425521595
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.8524925903
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0225521595
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0025159016
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6819850279
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
82PhosphorylationVDEVRTGTYRQLFHP
EECCCCCCCHHCCCH
18.21-
83NitrationDEVRTGTYRQLFHPE
ECCCCCCCHHCCCHH
9.56-
83PhosphorylationDEVRTGTYRQLFHPE
ECCCCCCCHHCCCHH
9.56-
83Nitrated tyrosineDEVRTGTYRQLFHPE
ECCCCCCCHHCCCHH
9.56-
94PhosphorylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH
51.2827600695
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.4822817900
108PhosphorylationNNYARGHYTIGKEIV
HHCCCCCCCCCHHHH
11.6825195567
109PhosphorylationNYARGHYTIGKEIVD
HCCCCCCCCCHHHHH
19.9919854140
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.1127180971
161PhosphorylationMERLSVDYGKKSKLE
HHHHCCCCCCCCCCE
28.7929472430
163AcetylationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.877609119
163UbiquitinationRLSVDYGKKSKLEFA
HHCCCCCCCCCCEEE
47.87-
164UbiquitinationLSVDYGKKSKLEFAI
HCCCCCCCCCCEEEE
48.75-
165PhosphorylationSVDYGKKSKLEFAIY
CCCCCCCCCCEEEEE
46.06-
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.3022817900
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCCCCHHHH
49.5520415495
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCCCCHHHHH
9.0520415495
225PhosphorylationDIERPTYTNLNRLIG
CCCCCCCCCHHHHHH
35.3920415495
237PhosphorylationLIGQIVSSITASLRF
HHHHHHHHHHHHCCC
17.05-
271PhosphorylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0925159016
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.8725159016
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5225159016
277O-linked_GlycosylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5230813383
280UbiquitinationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.70-
282PhosphorylationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.5626745281
287PhosphorylationKAYHEQLSVAEITNA
HHHHHHCCHHHHHHH
20.9825521595
292PhosphorylationQLSVAEITNACFEPA
HCCHHHHHHHHCCCH
14.3123984901
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.81-
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCCCHHHH
63.80-
334PhosphorylationDVNAAIATIKTKRTI
CCCHHHHHCCCCCEE
19.5226824392
336UbiquitinationNAAIATIKTKRTIQF
CHHHHHCCCCCEEEE
43.57-
337PhosphorylationAAIATIKTKRTIQFV
HHHHHCCCCCEEEEE
23.1627600695
338UbiquitinationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.41-
340PhosphorylationATIKTKRTIQFVDWC
HHCCCCCEEEEEEEC
22.2322817900
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
352AcetylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.687969707
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.0725521595
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH
40.6025159016
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
379PhosphorylationQRAVCMLSNTTAIAE
HHHHHHHCCHHHHHH
12.7822817900
381PhosphorylationAVCMLSNTTAIAEAW
HHHHHCCHHHHHHHH
17.7723984901
382PhosphorylationVCMLSNTTAIAEAWA
HHHHCCHHHHHHHHH
21.9523984901
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.1026745281
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.117675323
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC
5.4525777480
432PhosphorylationLAALEKDYEEVGVDS
HHHHHHHHHHHCCCC
25.67-
439PhosphorylationYEEVGVDSVEAEAEE
HHHHCCCCCCCHHHC
21.3223140645
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 TBA3_MOUSE !!

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 TBA3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL7A_HUMANBCL7Aphysical
26496610
BLMH_HUMANBLMHphysical
26496610
TCPZ_HUMANCCT6Aphysical
26496610
CATC_HUMANCTSCphysical
26496610
CO5A1_HUMANCOL5A1physical
26496610
FKB1A_HUMANFKBP1Aphysical
26496610
GTF2I_HUMANGTF2Iphysical
26496610
HEXA_HUMANHEXAphysical
26496610
HEXB_HUMANHEXBphysical
26496610
DNJA1_HUMANDNAJA1physical
26496610
HS90B_HUMANHSP90AB1physical
26496610
I5P2_HUMANINPP5Bphysical
26496610
LG3BP_HUMANLGALS3BPphysical
26496610
OXA1L_HUMANOXA1Lphysical
26496610
PFD1_HUMANPFDN1physical
26496610
PFD2_HUMANPFDN2physical
26496610
SPAST_HUMANSPASTphysical
26496610
TCPA_HUMANTCP1physical
26496610
ENPL_HUMANHSP90B1physical
26496610
TCPG_HUMANCCT3physical
26496610
TRPS1_HUMANTRPS1physical
26496610
TTC3_HUMANTTC3physical
26496610
TYSY_HUMANTYMSphysical
26496610
SF01_HUMANSF1physical
26496610
TBA1A_HUMANTUBA1Aphysical
26496610
REEP5_HUMANREEP5physical
26496610
IFT88_HUMANIFT88physical
26496610
PKP4_HUMANPKP4physical
26496610
PIAS2_HUMANPIAS2physical
26496610
TRIPB_HUMANTRIP11physical
26496610
CRIPT_HUMANCRIPTphysical
26496610
SC22B_HUMANSEC22Bphysical
26496610
CMC2_HUMANSLC25A13physical
26496610
TXND9_HUMANTXNDC9physical
26496610
DNJA2_HUMANDNAJA2physical
26496610
TBA1B_HUMANTUBA1Bphysical
26496610
TBB4B_HUMANTUBB4Bphysical
26496610
PRDX4_HUMANPRDX4physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
CTCF_HUMANCTCFphysical
26496610
TCPQ_HUMANCCT8physical
26496610
SRCAP_HUMANSRCAPphysical
26496610
GCN1_HUMANGCN1L1physical
26496610
TCPE_HUMANCCT5physical
26496610
SYNEM_HUMANSYNMphysical
26496610
TRI29_HUMANTRIM29physical
26496610
APOL2_HUMANAPOL2physical
26496610
UNC50_HUMANUNC50physical
26496610
PI3R4_HUMANPIK3R4physical
26496610
ASCC1_HUMANASCC1physical
26496610
SPN90_HUMANNCKIPSDphysical
26496610
S38A2_HUMANSLC38A2physical
26496610
CCHCR_HUMANCCHCR1physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
EMSY_HUMANC11orf30physical
26496610
T126A_HUMANTMEM126Aphysical
26496610
SPIR2_HUMANSPIRE2physical
26496610
LRCH3_HUMANLRCH3physical
26496610
TM209_HUMANTMEM209physical
26496610
ESCO1_HUMANESCO1physical
26496610
ERIC3_HUMANERICH3physical
26496610
TATD3_HUMANTATDN3physical
26496610
RBM33_HUMANRBM33physical
26496610
TBB5_HUMANTUBBphysical
26496610
TTC9C_HUMANTTC9Cphysical
26496610
1C07_HUMANHLA-Cphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA3_MOUSE

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Related Literatures of Post-Translational Modification

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