TBB2A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TBB2A_RAT
• UniProt AC: P85108
• Protein Name: Tubulin beta-2A chain
• Gene Name: Tubb2a {ECO:0000250|UniProtKB:Q7TMM9}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 445
• 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: MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA

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
36	Phosphorylation	GIDPTGSYHGDSDLQ CCCCCCCCCCCCCCE	15.92	-
40	Phosphorylation	TGSYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	-
46	Methylation	DSDLQLERINVYYNE CCCCEEEEEEEEEEH	34.08	26494319
50	Phosphorylation	QLERINVYYNEAAGN EEEEEEEEEEHHCCC	8.97	-
51	Phosphorylation	LERINVYYNEAAGNK EEEEEEEEEHHCCCC	11.40	-
58	Acetylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	22902405
58	Ubiquitination	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	-
58	Succinylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	-
58	Succinylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	-
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	23984901
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	27097102
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	23984901
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	-
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	23984901
136	Phosphorylation	CLQGFQLTHSLGGGT CCCCEEEEEECCCCC	9.91	30240740
138	Phosphorylation	QGFQLTHSLGGGTGS CCEEEEEECCCCCCC	24.39	30240740
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	23984901
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	30240740
172	Phosphorylation	NTFSVMPSPKVSDTV HHEECCCCCCCCCCE	21.18	-
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	-
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCCCH	29.19	16641100
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCCCHH	24.86	30240740
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCCCHHHH	37.74	16641100
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCCCHHHHH	15.17	16641100
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	25403869
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHH	42.18	22108457
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHHHEEE	17.01	23984901
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHHHEEEHHH	7.10	23984901
285	Phosphorylation	SQQYRALTVPELTQQ CHHHHEEEHHHHHHH	32.79	22817900
290	Phosphorylation	ALTVPELTQQMFDSK EEEHHHHHHHHHCCC	18.32	-
318	Methylation	LTVAAIFRGRMSMKE HHHHHHHCCCCCHHH	26.20	-
322	Phosphorylation	AIFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	23984901
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	72597353
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	-
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	27097102
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	23984901
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	27097102
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEECC	33.36	-
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	13579721
409	Phosphorylation	GMDEMEFTEAESNMN CCCHHCCCHHHHHHH	22.45	12631274
420	Phosphorylation	SNMNDLVSEYQQYQD HHHHHHHHHHHHHHC	37.57	12631274
438	Formation of an isopeptide bond	DEQGEFEEEEGEDEA HCCCCCCHHCCCCCC	67.67	-
438	5-glutamyl polyglutamate	DEQGEFEEEEGEDEA HCCCCCCHHCCCCCC	67.67	-

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
172	S	Phosphorylation	Kinase	CDK1	P39951	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
172	S	Phosphorylation	Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TBB2A_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of TBB2A_RAT !!

Drug and Disease Associations

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