dbPTM

TBA3E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBA3E_HUMAN
UniProt AC	Q6PEY2
Protein Name	Tubulin alpha-3E chain
Gene Name	TUBA3E
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 (By similarity)..
Protein Sequence	MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MRECISIHVGQAG --CCCEEEEEECCHH	20.50	-
24	Phosphorylation	GNACWELYCLEHGIQ CHHHHHCHHHHCCCC	5.40	-
38	Phosphorylation	QPDGQMPSDKTIGGG CCCCCCCCCCCCCCC	46.53	26074081
40	Acetylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	24906155
40	Ubiquitination	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	24906155
41	Phosphorylation	GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC	29.82	25463755
48	Phosphorylation	TIGGGDDSFNTFFSE CCCCCCCCHHHCCCC	25.74	19664994
51	Phosphorylation	GGDDSFNTFFSETGA CCCCCHHHCCCCCCC	24.85	29255136
54	Phosphorylation	DSFNTFFSETGAGKH CCHHHCCCCCCCCCC	30.02	25159151
56	Phosphorylation	FNTFFSETGAGKHVP HHHCCCCCCCCCCCC	31.00	23927012
60	Sumoylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	-
60	Neddylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	32015554
60	Ubiquitination	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	32142685
60	Sumoylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	-
60	Acetylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	19811121
79	Dimethylation	PTVVDEVRTGTYRQL CEEEECCCCCCCHHC	25.95	-
79	Methylation	PTVVDEVRTGTYRQL CEEEECCCCCCCHHC	25.95	-
80	Phosphorylation	TVVDEVRTGTYRQLF EEEECCCCCCCHHCC	38.77	23186163
82	Phosphorylation	VDEVRTGTYRQLFHP EECCCCCCCHHCCCH	18.21	24173317
83	Phosphorylation	DEVRTGTYRQLFHPE ECCCCCCCHHCCCHH	9.56	23917254
83	Nitrated tyrosine	DEVRTGTYRQLFHPE ECCCCCCCHHCCCHH	9.56	-
94	Phosphorylation	FHPEQLITGKEDAAS CCHHHHCCCCHHHHH	51.28	-
96	Ubiquitination	PEQLITGKEDAASNY HHHHCCCCHHHHHHC	43.71	16196087
105	Dimethylation	DAASNYARGHYTIGK HHHHHCCCCCCCCCH	23.28	-
105	Methylation	DAASNYARGHYTIGK HHHHHCCCCCCCCCH	23.28	18939037
108	Phosphorylation	SNYARGHYTIGKEIV HHCCCCCCCCCHHHH	11.68	25884760
109	Phosphorylation	NYARGHYTIGKEIVD HCCCCCCCCCHHHHH	19.99	28796482
156	Methylation	FASLLMERLSVDYSK HHHHHHHHHCCCCCC	20.49	24391021
158	Phosphorylation	SLLMERLSVDYSKKS HHHHHHHCCCCCCCC	21.11	29978859
161	Phosphorylation	MERLSVDYSKKSKLE HHHHCCCCCCCCCCE	21.89	29978859
162	Phosphorylation	ERLSVDYSKKSKLEF HHHCCCCCCCCCCEE	29.19	29978859
165	Phosphorylation	SVDYSKKSKLEFAIY CCCCCCCCCCEEEEE	46.33	20873877
185	Phosphorylation	STAVVEPYNSILTTH CEEEEECCCCCCCCC	14.18	22817900
187	Phosphorylation	AVVEPYNSILTTHTT EEEECCCCCCCCCCC	17.09	24275569
190	Phosphorylation	EPYNSILTTHTTLEH ECCCCCCCCCCCCCC	18.18	-
191	Phosphorylation	PYNSILTTHTTLEHS CCCCCCCCCCCCCCC	17.49	-
193	Phosphorylation	NSILTTHTTLEHSDC CCCCCCCCCCCCCCE	30.86	-
194	Phosphorylation	SILTTHTTLEHSDCA CCCCCCCCCCCCCEE	23.65	-
198	Phosphorylation	THTTLEHSDCAFMVD CCCCCCCCCEEEEEC	25.63	-
210	Phosphorylation	MVDNEAIYDICRRNL EECHHHHHHHHHCCC	13.30	25884760
223	Phosphorylation	NLDIERPTYTNLNRL CCCCCCCCCCCHHHH	49.55	28796482
224	Phosphorylation	LDIERPTYTNLNRLI CCCCCCCCCCHHHHH	9.05	19605366
225	Phosphorylation	DIERPTYTNLNRLIG CCCCCCCCCHHHHHH	35.39	28555341
236	Phosphorylation	RLIGQIVSSITASLR HHHHHHHHHHHHHCC	20.04	27732954
237	Phosphorylation	LIGQIVSSITASLRF HHHHHHHHHHHHCCC	17.05	27732954
239	Phosphorylation	GQIVSSITASLRFDG HHHHHHHHHHCCCCC	16.49	27732954
241	Phosphorylation	IVSSITASLRFDGAL HHHHHHHHCCCCCCC	16.07	-
253	Phosphorylation	GALNVDLTEFQTNLV CCCCCCCCEEECCCC	30.23	21712546
257	Phosphorylation	VDLTEFQTNLVPYPR CCCCEEECCCCCCCC	35.52	21712546
262	Phosphorylation	FQTNLVPYPRIHFPL EECCCCCCCCCCCCC	9.54	22817901
271	Phosphorylation	RIHFPLATYAPVISA CCCCCCCCCCCCCCH	28.09	21945579
272	Phosphorylation	IHFPLATYAPVISAE CCCCCCCCCCCCCHH	11.87	21945579
277	Phosphorylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	21945579
280	Ubiquitination	APVISAEKAYHEQLS CCCCCHHHHHHHHCC	54.70	21906983
282	Phosphorylation	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	25159151
282	Nitration	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	-
287	Phosphorylation	KAYHEQLSVAEITNA HHHHHHCCHHHHHHH	20.98	22322096
292	Phosphorylation	QLSVAEITNACFEPA HCCHHHHHHHHCCCH	14.31	30576142
304	Ubiquitination	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	21963094
304	Neddylation	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	32015554
311	Ubiquitination	KCDPRHGKYMACCML CCCCCCCCEEEEHHH	26.23	22817900
326	Sumoylation	YRGDVVPKDVNAAIA CCCCCCCCCCCHHHH	63.80	-
326	Ubiquitination	YRGDVVPKDVNAAIA CCCCCCCCCCCHHHH	63.80	27667366
326	Sumoylation	YRGDVVPKDVNAAIA CCCCCCCCCCCHHHH	63.80	-
326	Acetylation	YRGDVVPKDVNAAIA CCCCCCCCCCCHHHH	63.80	22632595
334	Phosphorylation	DVNAAIATIKTKRTI CCCHHHHHCCCCCEE	19.52	23401153
336	Acetylation	NAAIATIKTKRTIQF CHHHHHCCCCCEEEE	43.57	14497359
336	Sumoylation	NAAIATIKTKRTIQF CHHHHHCCCCCEEEE	43.57	-
336	Ubiquitination	NAAIATIKTKRTIQF CHHHHHCCCCCEEEE	43.57	21906983
336	Neddylation	NAAIATIKTKRTIQF CHHHHHCCCCCEEEE	43.57	32015554
336	Sumoylation	NAAIATIKTKRTIQF CHHHHHCCCCCEEEE	43.57	-
337	Phosphorylation	AAIATIKTKRTIQFV HHHHHCCCCCEEEEE	23.16	30266825
338	Methylation	AIATIKTKRTIQFVD HHHHCCCCCEEEEEE	42.41	14505319
338	Ubiquitination	AIATIKTKRTIQFVD HHHHCCCCCEEEEEE	42.41	21963094
340	Phosphorylation	ATIKTKRTIQFVDWC HHCCCCCEEEEEEEC	22.23	28857561
347	S-palmitoylation	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	29575903
349	Phosphorylation	QFVDWCPTGFKVGIN EEEEECCCCEEEEEE	52.71	21712546
352	Sumoylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
352	Ubiquitination	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	21963094
352	Acetylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	18529713
357	Phosphorylation	GFKVGINYQPPTVVP CEEEEEECCCCEECC	22.07	27273156
361	Phosphorylation	GINYQPPTVVPGGDL EEECCCCEECCCCCH	40.60	28152594
370	Sumoylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	-
370	Ubiquitination	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	27667366
370	Sumoylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	-
370	Neddylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	32015554
370	Acetylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	22632589
379	Phosphorylation	QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH	12.78	19664995
381	Phosphorylation	AVCMLSNTTAIAEAW HHHHHCCHHHHHHHH	17.77	30108239
382	Phosphorylation	VCMLSNTTAIAEAWA HHHHCCHHHHHHHHH	21.95	30108239
394	Ubiquitination	AWARLVHKFDLMYAK HHHHHHHHHHHHHHC	32.85	33845483
399	Phosphorylation	VHKFDLMYAKWAFVH HHHHHHHHHCHHHHH	16.60	25884760
401	Ubiquitination	KFDLMYAKWAFVHWY HHHHHHHCHHHHHHH	22.90	-
408	Phosphorylation	KWAFVHWYVGEGMEE CHHHHHHHCCCCCCC	5.45	28796482
419	Phosphorylation	GMEEGEFSEAREDLA CCCCCCHHHHHHHHH	26.50	-
439	Phosphorylation	CEEVGVDSVEAEAEE HHHHCCCCEEEHHHC	21.32	-
450	Nitration	EAEEGEAY------- HHHCCCCC-------	18.13	-

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 TBA3E_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
40	K	Acetylation	24906155
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen.
40	K	Methylation	24906155
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

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 TBA3E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIM50_HUMAN	TIMM50	physical	20360068
PFD4_HUMAN	PFDN4	physical	20360068
PFD2_HUMAN	PFDN2	physical	20360068
PFD6_HUMAN	PFDN6	physical	20360068
PFD5_HUMAN	PFDN5	physical	20360068
PFD3_HUMAN	VBP1	physical	20360068
AIFM1_HUMAN	AIFM1	physical	20360068
TCPH_HUMAN	CCT7	physical	26186194
TCPG_HUMAN	CCT3	physical	26186194
TCPB_HUMAN	CCT2	physical	26186194
T11L2_HUMAN	TCP11L2	physical	26186194
T11L2_HUMAN	TCP11L2	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442

Drug and Disease Associations

Kegg Disease
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.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TBA3E_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-60 AND LYS-326, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	16565220 [Abstract]

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