dbPTM

TBB2B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB2B_MOUSE
UniProt AC	Q9CWF2
Protein Name	Tubulin beta-2B chain
Gene Name	Tubb2b
Organism	Mus musculus (Mouse).
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. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration..
Protein Sequence	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	24895380
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	26370283
33	Phosphorylation	DEHGIDPTGSYHGDS CCCCCCCCCCCCCCC	34.70	29899451
35	Phosphorylation	HGIDPTGSYHGDSDL CCCCCCCCCCCCCCC	19.21	19060867
36	Phosphorylation	GIDPTGSYHGDSDLQ CCCCCCCCCCCCCCE	15.92	22817900
40	Phosphorylation	TGSYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	21183079
46	Methylation	DSDLQLERINVYYNE CCCCEEEEEEEEEEC	34.08	26542125
50	Phosphorylation	QLERINVYYNEATGN EEEEEEEEEECCCCC	8.97	25177544
51	Phosphorylation	LERINVYYNEATGNK EEEEEEEEECCCCCC	11.40	29899451
55	Phosphorylation	NVYYNEATGNKYVPR EEEEECCCCCCCCCE	34.80	25521595
58	Succinylation	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	-
58	Acetylation	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	22826441
58	Succinylation	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	-
58	Ubiquitination	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	-
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	20415495
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	22817900
78	Phosphorylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	22817900
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	26745281
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	12692561
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	12692561
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	27600695
124	Phosphorylation	LDVVRKESESCDCLQ HHHHHHHCCCCCCCC	37.53	20139300
126	Phosphorylation	VVRKESESCDCLQGF HHHHHCCCCCCCCCE	25.24	22817900
166	Phosphorylation	YPDRIMNTFSVMPSP CCCCCCHHEECCCCC	10.41	-
168	Phosphorylation	DRIMNTFSVMPSPKV CCCCHHEECCCCCCC	18.57	-
172	Phosphorylation	NTFSVMPSPKVSDTV HHEECCCCCCCCCCE	21.18	19737024
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	18563927
211	Glutathionylation	NEALYDICFRTLKLT HHHHHHHHHHEECCC	1.40	24333276
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	-
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	15614893
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	21082442
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHH	42.18	25177544
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHHHEEE	17.01	26239621
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHHHEEEHHH	7.10	23984901
285	Phosphorylation	SQQYRALTVPELTQQ CHHHHEEEHHHHHHH	32.79	-
290	Phosphorylation	ALTVPELTQQMFDSK EEEHHHHHHHHHCCC	18.32	-
296	Phosphorylation	LTQQMFDSKNMMAAC HHHHHHCCCCCHHHC	18.05	20139300
297	Ubiquitination	TQQMFDSKNMMAACD HHHHHCCCCCHHHCC	51.19	-
312	Phosphorylation	PRHGRYLTVAAIFRG CCCCCCHHHHHHHCC	10.12	22817900
318	Methylation	LTVAAIFRGRMSMKE HHHHHHHCCCCCHHH	26.20	-
322	Phosphorylation	AIFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	26370283
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	-
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	26745281
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	25521595
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	25521595
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
354	S-nitrosylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	24895380
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEECC	33.36	-
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	156607
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	-
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	23684622
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	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 TBB2B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CG025_HUMAN	C7orf25	physical	16169070

Drug and Disease Associations

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

Regulatory Network of TBB2B_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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