dbPTM

TBB4A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB4A_MOUSE
UniProt AC	Q9D6F9
Protein Name	Tubulin beta-4A chain
Gene Name	Tubb4a
Organism	Mus musculus (Mouse).
Sequence Length	444
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	MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEGEFEEEAEEEVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosocysteine	VHLQAGQCGNQIGAK EEECCCCCCCCHHHH	5.60	-
12	S-nitrosylation	VHLQAGQCGNQIGAK EEECCCCCCCCHHHH	5.60	24895380
33	Phosphorylation	DEHGIDPTGTYHGDS CCCCCCCCCCCCCCC	38.11	22807455
36	Phosphorylation	GIDPTGTYHGDSDLQ CCCCCCCCCCCCCCE	12.73	22817900
40	Phosphorylation	TGTYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	19060867
50	Phosphorylation	QLERINVYYNEATGG EEEEEEEEEECCCCC	8.97	-
51	Phosphorylation	LERINVYYNEATGGN EEEEEEEEECCCCCC	11.40	29899451
55	Phosphorylation	NVYYNEATGGNYVPR EEEEECCCCCCCCCE	39.17	25521595
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	22817900
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	28638064
78	Phosphorylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	22817900
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	26745281
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	-
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	-
122	Ubiquitination	AVLDVVRKEAESCDC HHHHHHHHHHHHCCC	50.06	-
126	Phosphorylation	VVRKEAESCDCLQGF HHHHHHHHCCCCCEE	23.46	26745281
136	Phosphorylation	CLQGFQLTHSLGGGT CCCEEEEEEECCCCC	9.91	29899451
138	Phosphorylation	QGFQLTHSLGGGTGS CEEEEEEECCCCCCC	24.39	26745281
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	29899451
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	24759943
149	Phosphorylation	GTGSGMGTLLISKIR CCCCCHHHHHHHHHH	14.97	26745281
154	Ubiquitination	MGTLLISKIREEFPD HHHHHHHHHHHHCCC	38.50	-
166	Phosphorylation	FPDRIMNTFSVVPSP CCCHHHHCCCCCCCC	10.41	28638064
168	Phosphorylation	DRIMNTFSVVPSPKV CHHHHCCCCCCCCCC	21.84	26643407
172	Phosphorylation	NTFSVVPSPKVSDTV HCCCCCCCCCCCCCE	26.24	23684622
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	18563927
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	-
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCCCH	29.19	19060867
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCCCHH	24.86	22817900
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCCCHHHH	37.74	19060867
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCCCHHHHH	15.17	-
234	Phosphorylation	HLVSATMSGVTTCLR HHHHHHHCCCHHHHH	26.25	22006019
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	27667366
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	15614909
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	21082442
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHE	42.18	25177544
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHHEEEE	17.01	26239621
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHHEEEEHHH	7.10	23984901
285	Phosphorylation	SQQYRALTVPELTQQ CHHHEEEEHHHHHHH	32.79	-
297	Ubiquitination	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	-
303	S-nitrosocysteine	AKNMMAACDPRHGRY CCHHHHHCCCCCCCE	5.55	-
312	Phosphorylation	PRHGRYLTVAAVFRG CCCCCEEHHHHHHCC	10.12	22006019
322	Phosphorylation	AVFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	-
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	22790023
335	Phosphorylation	EQMLSVQSKNSSYFV HHHHHHHHCCCCCEE	31.48	22817900
336	Ubiquitination	QMLSVQSKNSSYFVE HHHHHHHCCCCCEEE	43.70	-
338	Phosphorylation	LSVQSKNSSYFVEWI HHHHHCCCCCEEEEC	30.10	26745281
339	Phosphorylation	SVQSKNSSYFVEWIP HHHHCCCCCEEEECC	31.80	26745281
340	Phosphorylation	VQSKNSSYFVEWIPN HHHCCCCCEEEECCC	16.09	25521595
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
354	S-nitrosylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCH	3.49	22588120
366	Phosphorylation	RGLKMAATFIGNSTA CCHHHHHHHHCCHHH	13.27	-
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	134119
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	22790023
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	23684622
436	Formation of an isopeptide bond	TAEEGEFEEEAEEEV CHHCCCCHHHHHHHH	51.10	-
436	5-glutamyl polyglutamate	TAEEGEFEEEAEEEV CHHCCCCHHHHHHHH	51.10	-

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	P11440	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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TBB4A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
LRRK2_MOUSE	Lrrk2	physical	19545277

Drug and Disease Associations

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

Regulatory Network of TBB4A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASSSPECTROMETRY.	18034455 [Abstract]

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