dbPTM

TBA1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBA1A_MOUSE
UniProt AC	P68369
Protein Name	Tubulin alpha-1A chain
Gene Name	Tuba1a
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	MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MRECISIHVGQAG --CCCEEEEEECCHH	20.50	15345747
25	Glutathionylation	NACWELYCLEHGIQP HHHHHCHHHHCCCCC	5.86	24333276
40	Ubiquitination	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	-
40	Acetylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	66191
41	Phosphorylation	GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC	29.82	25521595
48	Phosphorylation	TIGGGDDSFNTFFSE CCCCCCCCHHHCCCC	25.74	25521595
51	Phosphorylation	GGDDSFNTFFSETGA CCCCCHHHCCCCCCC	24.85	24925903
54	Phosphorylation	DSFNTFFSETGAGKH CCHHHCCCCCCCCCC	30.02	25521595
56	Phosphorylation	FNTFFSETGAGKHVP HHHCCCCCCCCCCCC	31.00	25159016
60	Ubiquitination	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	22790023
60	Acetylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	19850435
73	Phosphorylation	VFVDLEPTVIDEVRT EEECCCCEEEHHCCC	22.25	22817900
80	Phosphorylation	TVIDEVRTGTYRQLF EEEHHCCCCCCHHCC	38.77	22006019
82	Phosphorylation	IDEVRTGTYRQLFHP EHHCCCCCCHHCCCH	18.21	26060331
83	Phosphorylation	DEVRTGTYRQLFHPE HHCCCCCCHHCCCHH	9.56	26060331
94	Phosphorylation	FHPEQLITGKEDAAN CCHHHHCCCCHHHHH	51.28	27600695
96	Ubiquitination	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	22790023
103	Phosphorylation	KEDAANNYARGHYTI CHHHHHHCCCCCCCC	9.48	22817900
108	Phosphorylation	NNYARGHYTIGKEII HHCCCCCCCCCHHHH	11.68	25195567
109	Phosphorylation	NYARGHYTIGKEIID HCCCCCCCCCHHHHH	19.99	26824392
112	Ubiquitination	RGHYTIGKEIIDLVL CCCCCCCHHHHHHHH	41.72	-
124	Acetylation	LVLDRIRKLADQCTG HHHHHHHHHHHHCCC	45.73	15611747
158	Phosphorylation	SLLMERLSVDYGKKS HHHHHHHCCCCCCCC	21.11	27180971
161	Phosphorylation	MERLSVDYGKKSKLE HHHHCCCCCCCCCEE	28.79	29472430
163	Acetylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	129737
163	Ubiquitination	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	22790023
164	Ubiquitination	LSVDYGKKSKLEFSI HCCCCCCCCCEEEEE	48.75	27667366
165	Phosphorylation	SVDYGKKSKLEFSIY CCCCCCCCCEEEEEE	46.06	-
166	Ubiquitination	VDYGKKSKLEFSIYP CCCCCCCCEEEEEEE	62.00	-
210	Phosphorylation	MVDNEAIYDICRRNL EECHHHHHHHHHCCC	13.30	22817900
223	Phosphorylation	NLDIERPTYTNLNRL CCCCCCCCCCCHHHH	49.55	20415495
224	Phosphorylation	LDIERPTYTNLNRLI CCCCCCCCCCHHHHH	9.05	20415495
225	Phosphorylation	DIERPTYTNLNRLIG CCCCCCCCCHHHHHH	35.39	20415495
237	Phosphorylation	LIGQIVSSITASLRF HHHHHHHHHHHHCCC	17.05	-
271	Phosphorylation	RIHFPLATYAPVISA CCCCCCCCCCCCCCH	28.09	25159016
272	Phosphorylation	IHFPLATYAPVISAE CCCCCCCCCCCCCHH	11.87	25159016
277	Phosphorylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	25159016
277	O-linked_Glycosylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	30813311
280	Ubiquitination	APVISAEKAYHEQLS CCCCCHHHHHHHHCC	54.70	-
282	Nitration	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	-
282	Nitrated tyrosine	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	-
282	Phosphorylation	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	26745281
287	Phosphorylation	KAYHEQLSVAEITNA HHHHHHCCHHHHHHH	20.98	25521595
292	Phosphorylation	QLSVAEITNACFEPA HCCHHHHHHHHCCCH	14.31	23984901
295	Glutathionylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	24333276
295	S-nitrosocysteine	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	-
295	S-nitrosylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	24895380
304	Ubiquitination	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	22790023
305	Glutathionylation	PANQMVKCDPRHGKY CHHHCCCCCCCCCCE	6.23	24333276
311	Ubiquitination	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	-
316	Glutathionylation	HGKYMACCLLYRGDV CCCEEEEHHHCCCCC	1.81	24333276
319	Phosphorylation	YMACCLLYRGDVVPK EEEEHHHCCCCCCCC	10.29	22817900
326	Malonylation	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	26073543
326	Ubiquitination	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	27667366
334	Phosphorylation	DVNAAIATIKTKRTI CCHHHHHHCCCCCEE	19.52	26824392
336	Ubiquitination	NAAIATIKTKRTIQF HHHHHHCCCCCEEEE	43.57	22790023
337	Phosphorylation	AAIATIKTKRTIQFV HHHHHCCCCCEEEEE	23.16	27600695
338	Ubiquitination	AIATIKTKRTIQFVD HHHHCCCCCEEEEEE	42.41	22790023
340	Phosphorylation	ATIKTKRTIQFVDWC HHCCCCCEEEEEEEC	22.23	22817900
347	S-nitrosylation	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	24895380
347	S-nitrosocysteine	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	-
347	Glutathionylation	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	24333276
352	Acetylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	129725
352	Ubiquitination	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
357	Phosphorylation	GFKVGINYQPPTVVP CEEEEEECCCCEECC	22.07	25521595
361	Phosphorylation	GINYQPPTVVPGGDL EEECCCCEECCCCCH	40.60	25159016
370	Ubiquitination	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	22790023
376	S-nitrosocysteine	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	-
376	S-nitrosylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	24895380
376	Glutathionylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	24333276
379	Phosphorylation	QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH	12.78	22817900
381	Phosphorylation	AVCMLSNTTAIAEAW HHHHHCCHHHHHHHH	17.77	23984901
382	Phosphorylation	VCMLSNTTAIAEAWA HHHHCCHHHHHHHHH	21.95	23984901
394	Ubiquitination	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	22790023
399	Phosphorylation	DHKFDLMYAKRAFVH CCCCCHHHEEEHHHH	19.10	26745281
401	Acetylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	129733
401	Ubiquitination	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	22790023
408	Phosphorylation	KRAFVHWYVGEGMEE EEHHHHHHCCCCCCC	5.45	25777480
419	Phosphorylation	GMEEGEFSEAREDMA CCCCCCHHHHHHHHH	26.50	22817900
432	Phosphorylation	MAALEKDYEEVGVDS HHHHHHCHHHHCCCC	25.67	25619855
439	Phosphorylation	YEEVGVDSVEGEGEE HHHHCCCCCCCCCCC	21.47	25521595
445	5-glutamyl polyglutamate	DSVEGEGEEEGEEY- CCCCCCCCCCCCCC-	48.88	-
445	Formation of an isopeptide bond	DSVEGEGEEEGEEY- CCCCCCCCCCCCCC-	48.88	1967194
451	Nitration	GEEEGEEY------- CCCCCCCC-------	21.39	-
451	Phosphorylation	GEEEGEEY------- CCCCCCCC-------	21.39	25619855

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
432	Y	Phosphorylation	Kinase	SYK	P48025	GPS
432	Y	Phosphorylation	Kinase	SYK	Q99MN1	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
40	K	Acetylation	-
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen.
40	K	Methylation	-
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 TBA1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS105_MOUSE	Hsph1	physical	12749852
TCPH_MOUSE	Cct7	physical	11532003
TCPD_MOUSE	Cct4	physical	11532003
SYUA_HUMAN	SNCA	physical	11698390
TAU_HUMAN	MAPT	physical	11698390
SYUB_HUMAN	SNCB	physical	11698390

Drug and Disease Associations

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

Regulatory Network of TBA1A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.	15345747 [Abstract]

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