dbPTM

TBA1C_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBA1C_MOUSE
UniProt AC	P68373
Protein Name	Tubulin alpha-1C chain
Gene Name	Tuba1c
Organism	Mus musculus (Mouse).
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	MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSAEGDDEGEEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MRECISIHVGQAG --CCCEEEEEECCHH	20.50	15345747
40	Acetylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	155547
40	Ubiquitination	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	-
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	-
60	Acetylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	19850441
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	-
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	156241
158	Phosphorylation	SLLMERLSVDYGKKS HHHHHHHCCCCCCCC	21.11	27180971
161	Phosphorylation	MERLSVDYGKKSKLE HHHHCCCCCCCCCEE	28.79	29472430
163	Ubiquitination	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	-
163	Acetylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	129757
164	Ubiquitination	LSVDYGKKSKLEFSI HCCCCCCCCCEEEEE	48.75	-
165	Phosphorylation	SVDYGKKSKLEFSIY CCCCCCCCCEEEEEE	46.06	-
166	Ubiquitination	VDYGKKSKLEFSIYP CCCCCCCCEEEEEEE	62.00	-
210	Phosphorylation	MVDNEAIYDICRRNL EECHHHHHHHHHCCC	13.30	22817900
223	Phosphorylation	NLDIERPTYTNLNRL CCCCCCCCHHCHHHH	49.55	22817900
224	Phosphorylation	LDIERPTYTNLNRLI CCCCCCCHHCHHHHH	9.05	22817900
225	Phosphorylation	DIERPTYTNLNRLIS CCCCCCHHCHHHHHH	35.39	22817900
232	Phosphorylation	TNLNRLISQIVSSIT HCHHHHHHHHHHHHH	20.60	26824392
236	Phosphorylation	RLISQIVSSITASLR HHHHHHHHHHHHHCC	20.04	23984901
237	Phosphorylation	LISQIVSSITASLRF HHHHHHHHHHHHCCC	17.05	23984901
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	30813341
282	Nitrated tyrosine	VISAEKAYHEQLTVA CCCHHHHHHHCCCHH	19.56	-
282	Nitration	VISAEKAYHEQLTVA CCCHHHHHHHCCCHH	19.56	16800626
282	Nitration	VISAEKAYHEQLTVA CCCHHHHHHHCCCHH	19.56	16800626
295	S-palmitoylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	28526873
295	Glutathionylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	24333276
304	Ubiquitination	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	-
305	Glutathionylation	PANQMVKCDPRHGKY CHHHCCCCCCCCCCE	6.23	24333276
311	Ubiquitination	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	-
315	S-palmitoylation	RHGKYMACCLLYRGD CCCCEEEEHHHCCCC	0.67	28526873
316	S-palmitoylation	HGKYMACCLLYRGDV CCCEEEEHHHCCCCC	1.81	28526873
316	S-nitrosylation	HGKYMACCLLYRGDV CCCEEEEHHHCCCCC	1.81	24926564
319	Phosphorylation	YMACCLLYRGDVVPK EEEEHHHCCCCCCCC	10.29	22817900
326	Ubiquitination	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	-
326	Acetylation	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	-
334	Phosphorylation	DVNAAIATIKTKRTI CCHHHHHHCCCCCEE	19.52	26824392
336	Ubiquitination	NAAIATIKTKRTIQF HHHHHHCCCCCEEEE	43.57	-
337	Phosphorylation	AAIATIKTKRTIQFV HHHHHCCCCCEEEEE	23.16	27600695
338	Ubiquitination	AIATIKTKRTIQFVD HHHHCCCCCEEEEEE	42.41	-
340	Phosphorylation	ATIKTKRTIQFVDWC HHCCCCCEEEEEEEC	22.23	22817900
347	S-nitrosocysteine	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	-
347	S-palmitoylation	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	28526873
347	S-nitrosylation	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	22588120
352	Ubiquitination	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
352	Acetylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	129745
357	Phosphorylation	GFKVGINYQPPTVVP CEEEEEECCCCEECC	22.07	25521595
361	Phosphorylation	GINYQPPTVVPGGDL EEECCCCEECCCCCH	40.60	25159016
370	Ubiquitination	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	-
376	S-palmitoylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	28526873
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	-
399	Phosphorylation	DHKFDLMYAKRAFVH CCCCCHHHEEEHHHH	19.10	26745281
401	Acetylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	129753
401	Ubiquitination	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	-
408	Phosphorylation	KRAFVHWYVGEGMEE EEHHHHHHCCCCCCC	5.45	25777480
419	Phosphorylation	GMEEGEFSEAREDMA CCCCCCHHHHHHHHH	26.50	22817900
432	Phosphorylation	MAALEKDYEEVGADS HHHHHHHHHHHCCCC	25.67	25619855
439	Phosphorylation	YEEVGADSAEGDDEG HHHHCCCCCCCCCCC	27.90	25521595
449	Phosphorylation	GDDEGEEY------- CCCCCCCC-------	21.39	25619855
449	Nitration	GDDEGEEY------- 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 TBA1C_MOUSE !!

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 TBA1C_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TBA1C_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of TBA1C_MOUSE

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-282, AND MASS SPECTROMETRY.	16800626 [Abstract]

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