TBA8_HUMAN - dbPTM
TBA8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA8_HUMAN
UniProt AC Q9NY65
Protein Name Tubulin alpha-8 chain
Gene Name TUBA8
Organism Homo sapiens (Human).
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 MRECISVHVGQAGVQIGNACWELFCLEHGIQADGTFDAQASKINDDDSFTTFFSETGNGKHVPRAVMIDLEPTVVDEVRAGTYRQLFHPEQLITGKEDAANNYARGHYTVGKESIDLVLDRIRKLTDACSGLQGFLIFHSFGGGTGSGFTSLLMERLSLDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLSVAEITSSCFEPNSQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGTDSFEEENEGEEF
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--MRECISVHVGQAG
--CCCEEEEEECCHH		20.1615345747
30UbiquitinationLFCLEHGIQADGTFD
HHHHHHCCCCCCCEE		3.0932142685
48PhosphorylationSKINDDDSFTTFFSE
HCCCCCCCCEECEEE		31.3330622161
50PhosphorylationINDDDSFTTFFSETG
CCCCCCCEECEEECC		27.0130622161
51PhosphorylationNDDDSFTTFFSETGN
CCCCCCEECEEECCC		22.2230622161
56PhosphorylationFTTFFSETGNGKHVP
CEECEEECCCCCEEC		34.45-
82PhosphorylationVDEVRAGTYRQLFHP
EHHHHCCCHHHHCCH		17.97-
83PhosphorylationDEVRAGTYRQLFHPE
HHHHCCCHHHHCCHH		8.7422210691
94PhosphorylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH		51.2828152594
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC		43.7130585421
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC		43.71-
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC		43.7127667366
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC		43.71-
103PhosphorylationKEDAANNYARGHYTV
CHHHHHHCCCCCCCC		9.4827155012
112AcetylationRGHYTVGKESIDLVL
CCCCCCCHHHHHHHH		43.9118529257
124MethylationLVLDRIRKLTDACSG
HHHHHHHHHHHHHCC		54.06-
124"N6,N6-dimethyllysine"LVLDRIRKLTDACSG
HHHHHHHHHHHHHCC		54.06-
151PhosphorylationGTGSGFTSLLMERLS
CCCCCHHHHHHHHHC		19.76-
163AcetylationRLSLDYGKKSKLEFA
HHCCCCCCCCCCEEE		47.8725953088
165PhosphorylationSLDYGKKSKLEFAIY
CCCCCCCCCCEEEEE		46.0617855441
185PhosphorylationSTAVVEPYNSILTTH
CEEEEECCCCCCCCC		14.1822817900
187PhosphorylationAVVEPYNSILTTHTT
EEEECCCCCCCCCCC		17.0924275569
190PhosphorylationEPYNSILTTHTTLEH
ECCCCCCCCCCCCCC		18.18-
191PhosphorylationPYNSILTTHTTLEHS
CCCCCCCCCCCCCCC		17.49-
193PhosphorylationNSILTTHTTLEHSDC
CCCCCCCCCCCCCCE		30.86-
194PhosphorylationSILTTHTTLEHSDCA
CCCCCCCCCCCCCEE		23.65-
198PhosphorylationTHTTLEHSDCAFMVD
CCCCCCCCCEEEEEC		25.63-
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC		13.3025884760
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCHHCHHHH		49.5528796482
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCHHCHHHHH		9.0519605366
225PhosphorylationDIERPTYTNLNRLIS
CCCCCCHHCHHHHHH		35.3928555341
232PhosphorylationTNLNRLISQIVSSIT
HCHHHHHHHHHHHHH		20.6021712546
236PhosphorylationRLISQIVSSITASLR
HHHHHHHHHHHHHCC		20.0423403867
237PhosphorylationLISQIVSSITASLRF
HHHHHHHHHHHHCCC		17.0523403867
239PhosphorylationSQIVSSITASLRFDG
HHHHHHHHHHCCCCC		16.4923403867
241PhosphorylationIVSSITASLRFDGAL
HHHHHHHHCCCCCCC		16.0723403867
245UbiquitinationITASLRFDGALNVDL
HHHHCCCCCCCCCCC		34.7122817900
253PhosphorylationGALNVDLTEFQTNLV
CCCCCCCCEEECCCC		30.2321712546
257PhosphorylationVDLTEFQTNLVPYPR
CCCCEEECCCCCCCC		35.5221712546
262PhosphorylationFQTNLVPYPRIHFPL
EECCCCCCCCCCCCE		9.5423532336
282PhosphorylationIISAEKAYHEQLSVA
CCCHHHHHHHCCCHH		19.5628270605
283PhosphorylationISAEKAYHEQLSVAE
CCHHHHHHHCCCHHH		22.6132142685
286UbiquitinationEKAYHEQLSVAEITS
HHHHHHCCCHHHHHH		3.9621963094
287PhosphorylationKAYHEQLSVAEITSS
HHHHHCCCHHHHHHC		20.9830576142
292PhosphorylationQLSVAEITSSCFEPN
CCCHHHHHHCCCCCC		13.1928270605
293PhosphorylationLSVAEITSSCFEPNS
CCHHHHHHCCCCCCC		30.6728270605
294PhosphorylationSVAEITSSCFEPNSQ
CHHHHHHCCCCCCCC		17.7428270605
300PhosphorylationSSCFEPNSQMVKCDP
HCCCCCCCCCEECCC		30.3030576142
304UbiquitinationEPNSQMVKCDPRHGK
CCCCCCEECCCCCCC		27.8121890473
304UbiquitinationEPNSQMVKCDPRHGK
CCCCCCEECCCCCCC		27.8127667366
304NeddylationEPNSQMVKCDPRHGK
CCCCCCEECCCCCCC		27.8132015554
311AcetylationKCDPRHGKYMACCML
ECCCCCCCEEEEHHH		26.237961041
311UbiquitinationKCDPRHGKYMACCML
ECCCCCCCEEEEHHH		26.2322817900
328UbiquitinationGDVVPKDVNVAIAAI
CCCCCCCCHHHHHCC		8.5132142685
335UbiquitinationVNVAIAAIKTKRTIQ
CHHHHHCCCCCCEEE		4.2621963094
337PhosphorylationVAIAAIKTKRTIQFV
HHHHCCCCCCEEEEE		21.46-
340PhosphorylationAAIKTKRTIQFVDWC
HCCCCCCEEEEEEEC		22.2328857561
349PhosphorylationQFVDWCPTGFKVGIN
EEEEECCCCEEEEEE		52.7121712546
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC		40.6821963094
352SumoylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC		40.68-
352AcetylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC		40.687212415
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC		22.0727273156
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH		40.6028152594
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH		46.31-
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH		46.3121906983
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH		46.31-
370AcetylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH		46.3122632609
370NeddylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH		46.3132015554
379PhosphorylationQRAVCMLSNTTAIAE
HHHHHHHCCHHHHHH		12.7819664995
381PhosphorylationAVCMLSNTTAIAEAW
HHHHHCCHHHHHHHH		17.7730108239
382PhosphorylationVCMLSNTTAIAEAWA
HHHHCCHHHHHHHHH		21.9530108239
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE		39.99-
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE		39.9932142685
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE		39.99-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE		39.997215613
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH		19.1028674151
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH		27.11-
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH		27.1121906983
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH		27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH		27.117675705
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC		5.4528796482
419PhosphorylationGMEEGEFSEAREDLA
CCCCCCHHHHHHHHH		26.50-
439PhosphorylationYEEVGTDSFEEENEG
HHHHCCCCCCCCCCC		34.1018452278
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 TBA8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBA8_HUMAN !!
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 TBA8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI18_HUMANMID1physical
25416956
TRI27_HUMANTRIM27physical
25416956
TPP2_HUMANTPP2physical
25416956
TRAF1_HUMANTRAF1physical
25416956
BHE40_HUMANBHLHE40physical
25416956
SSNA1_HUMANSSNA1physical
25416956
PNMA1_HUMANPNMA1physical
25416956
TNIP1_HUMANTNIP1physical
25416956
NECA2_HUMANNECAB2physical
25416956
KCTD9_HUMANKCTD9physical
25416956
TRI54_HUMANTRIM54physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
LZTS2_HUMANLZTS2physical
25416956
TRI41_HUMANTRIM41physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
FUND1_HUMANFUNDC1physical
25416956
KCTD6_HUMANKCTD6physical
25416956
ZBTB9_HUMANZBTB9physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
OMIM Disease
613180Polymicrogyria, with optic nerve hypoplasia (PMGONH)
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 TBA8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-370, AND MASS SPECTROMETRY.

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