dbPTM

TBA1B_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBA1B_RAT
UniProt AC	Q6P9V9
Protein Name	Tubulin alpha-1B chain
Gene Name	Tuba1b
Organism	Rattus norvegicus (Rat).
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	MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
40	Methylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	-
40	Acetylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	13667011
41	Phosphorylation	GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC	29.82	27097102
48	Phosphorylation	TIGGGDDSFNTFFSE CCCCCCCCHHHCCCC	25.74	27097102
51	Phosphorylation	GGDDSFNTFFSETGA CCCCCHHHCCCCCCC	24.85	27097102
54	Phosphorylation	DSFNTFFSETGAGKH CCHHHCCCCCCCCCC	30.02	23984901
56	Phosphorylation	FNTFFSETGAGKHVP HHHCCCCCCCCCCCC	31.00	23984901
60	Ubiquitination	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	-
60	Acetylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	20679115
80	Phosphorylation	TVIDEVRTGTYRQLF EEEHHCCCCCCHHCC	38.77	23984901
82	Phosphorylation	IDEVRTGTYRQLFHP EHHCCCCCCHHCCCH	18.21	23984901
83	Phosphorylation	DEVRTGTYRQLFHPE HHCCCCCCHHCCCHH	9.56	23984901
96	Ubiquitination	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	-
96	Acetylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	30596257
103	Phosphorylation	KEDAANNYARGHYTI CHHHHHHCCCCCCCC	9.48	27097102
108	Phosphorylation	NNYARGHYTIGKEII HHCCCCCCCCCHHHH	11.68	27097102
109	Phosphorylation	NYARGHYTIGKEIID HCCCCCCCCCHHHHH	19.99	27097102
140	Phosphorylation	QGFLVFHSFGGGTGS CCEEEEEECCCCCCC	17.70	30240740
158	Phosphorylation	SLLMERLSVDYGKKS HHHHHHHCCCCCCCC	21.11	30240740
163	Ubiquitination	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	-
163	Acetylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	13667049
164	Ubiquitination	LSVDYGKKSKLEFSI HCCCCCCCCCEEEEE	48.75	-
210	Phosphorylation	MVDNEAIYDICRRNL EECHHHHHHHHHCCC	13.30	-
223	Phosphorylation	NLDIERPTYTNLNRL CCCCCCCCHHCHHHH	49.55	27097102
224	Phosphorylation	LDIERPTYTNLNRLI CCCCCCCHHCHHHHH	9.05	27097102
225	Phosphorylation	DIERPTYTNLNRLIS CCCCCCHHCHHHHHH	35.39	27097102
232	Phosphorylation	TNLNRLISQIVSSIT HCHHHHHHHHHHHHH	20.60	28689409
237	Phosphorylation	LISQIVSSITASLRF HHHHHHHHHHHHCCC	17.05	23984901
271	Phosphorylation	RIHFPLATYAPVISA CCCCCCCCCCCCCCH	28.09	30240740
272	Phosphorylation	IHFPLATYAPVISAE CCCCCCCCCCCCCHH	11.87	-
277	Phosphorylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	23984901
282	Nitrated tyrosine	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	-
282	Phosphorylation	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	23984901
282	Nitration	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	-
287	Phosphorylation	KAYHEQLSVAEITNA HHHHHHCCHHHHHHH	20.98	23984901
292	Phosphorylation	QLSVAEITNACFEPA HCCHHHHHHHHCCCH	14.31	23984901
295	S-nitrosylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	16418269
295	S-nitrosocysteine	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	-
304	Ubiquitination	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	-
311	Ubiquitination	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	-
312	Phosphorylation	CDPRHGKYMACCLLY CCCCCCCEEEEHHHC	8.44	-
319	Phosphorylation	YMACCLLYRGDVVPK EEEEHHHCCCCCCCC	10.29	-
326	Ubiquitination	YRGDVVPKDVNAAIA CCCCCCCCCHHHHHH	63.80	-
326	Acetylation	YRGDVVPKDVNAAIA CCCCCCCCCHHHHHH	63.80	22632545
334	Phosphorylation	DVNAAIATIKTKRSI CHHHHHHHCCCCCEE	19.52	27097102
336	Acetylation	NAAIATIKTKRSIQF HHHHHHCCCCCEEEE	43.57	13667055
336	Ubiquitination	NAAIATIKTKRSIQF HHHHHHCCCCCEEEE	43.57	-
337	Phosphorylation	AAIATIKTKRSIQFV HHHHHCCCCCEEEEE	28.04	23984901
338	Ubiquitination	AIATIKTKRSIQFVD HHHHCCCCCEEEEEE	38.86	-
339	Methylation	IATIKTKRSIQFVDW HHHCCCCCEEEEEEE	44.20	-
340	Phosphorylation	ATIKTKRSIQFVDWC HHCCCCCEEEEEEEC	23.46	30411139
347	S-nitrosylation	SIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	16418269
347	S-nitrosocysteine	SIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	-
352	Ubiquitination	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
357	Phosphorylation	GFKVGINYQPPTVVP CEEEEEECCCCEECC	22.07	23984901
361	Phosphorylation	GINYQPPTVVPGGDL EEECCCCEECCCCCH	40.60	23984901
370	Acetylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	22632537
370	Ubiquitination	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	-
376	S-nitrosocysteine	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	-
376	S-nitrosylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	16418269
394	Ubiquitination	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	-
394	Acetylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	13667109
399	Phosphorylation	DHKFDLMYAKRAFVH CCCCCHHHEEEHHHH	19.10	-
401	Ubiquitination	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	-
401	Acetylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	13667117
408	Phosphorylation	KRAFVHWYVGEGMEE EEHHHHHHCCCCCCC	5.45	25403869
432	Phosphorylation	MAALEKDYEEVGVDS HHHHHHCHHHHCCCC	25.67	28689409
439	Phosphorylation	YEEVGVDSVEGEGEE HHHHCCCCCCCCCCC	21.47	29779826
445	5-glutamyl polyglutamate	DSVEGEGEEEGEEY- CCCCCCCCCCCCCC-	48.88	-
445	Formation of an isopeptide bond	DSVEGEGEEEGEEY- CCCCCCCCCCCCCC-	48.88	-
451	Nitration	GEEEGEEY------- 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 TBA1B_RAT !!

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 TBA1B_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TBA1B_RAT !!

Drug and Disease Associations

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

Regulatory Network of TBA1B_RAT

Related Literatures of Post-Translational Modification

S-nitrosylation
Reference	PubMed
"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures."; Hao G., Derakhshan B., Shi L., Campagne F., Gross S.S.; Proc. Natl. Acad. Sci. U.S.A. 103:1012-1017(2006). Cited for: S-NITROSYLATION [LARGE SCALE ANALYSIS] AT CYS-295 AND CYS-376, ANDMASS SPECTROMETRY.	16418269 [Abstract]

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