dbPTM

TBB4B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB4B_MOUSE
UniProt AC	P68372
Protein Name	Tubulin beta-4B chain
Gene Name	Tubb4b
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..
Protein Sequence	MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFEEEAEEEVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosylation	VHLQAGQCGNQIGAK EEECCCCCCCCHHHH	5.60	22588120
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	LERINVYYNEATGGK EEEEEEEEECCCCCC	11.40	22817900
55	Phosphorylation	NVYYNEATGGKYVPR EEEEECCCCCCCCCE	40.04	25521595
58	Acetylation	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	23806337
58	Malonylation	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	26320211
58	Ubiquitination	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	27667366
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
103	Methylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	12692561
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	12692561
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	12692561
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	27600695
122	Ubiquitination	SVLDVVRKEAESCDC HHHHHHHHHHHHCCC	50.06	22790023
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	MGTLLISKIREEYPD HHHHHHHHHHHHCCC	38.50	-
162	Dimethylation	IREEYPDRIMNTFSV HHHHCCCCCCCCEEC	26.08	-
166	Phosphorylation	YPDRIMNTFSVVPSP CCCCCCCCEECCCCC	10.41	28638064
168	Phosphorylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	26643407
172	Phosphorylation	NTFSVVPSPKVSDTV CCEECCCCCCCCCCE	26.24	26824392
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	18563927
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	22790023
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	Succinylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	23806337
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	27667366
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	23806337
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	22790023
312	Phosphorylation	PRHGRYLTVAAVFRG CCCCCEEHHHHHHCC	10.12	22006019
322	Phosphorylation	AVFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	26370283
324	Succinylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	23806337
324	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	23806337
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	27667366
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	22790023
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	22324799
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	22588120
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEECC	33.36	22790023
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	22790023
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	129741
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	23684622
438	Formation of an isopeptide bond	EEEGEFEEEAEEEVA HHHCCCHHHHHHHHC	68.76	-
438	5-glutamyl polyglutamate	EEEGEFEEEAEEEVA HHHCCCHHHHHHHHC	68.76	-

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 TBB4B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBCD_HUMAN	TBCD	physical	20360068
PFD1_HUMAN	PFDN1	physical	20360068
SERA_HUMAN	PHGDH	physical	20360068
FBLN1_HUMAN	FBLN1	physical	20360068
PFD3_HUMAN	VBP1	physical	20360068
DNJA1_HUMAN	DNAJA1	physical	20360068
CY1_HUMAN	CYC1	physical	20360068
MIA40_HUMAN	CHCHD4	physical	20360068
PFD2_HUMAN	PFDN2	physical	20360068
VDAC3_HUMAN	VDAC3	physical	20360068
DNJA2_HUMAN	DNAJA2	physical	20360068
PFD6_HUMAN	PFDN6	physical	20360068
BASI_HUMAN	BSG	physical	20360068
ICAM1_HUMAN	ICAM1	physical	20360068
MGST3_HUMAN	MGST3	physical	20360068
RRAS2_HUMAN	RRAS2	physical	20360068
MA7D1_HUMAN	MAP7D1	physical	20360068
PFD5_HUMAN	PFDN5	physical	20360068
AIFM1_HUMAN	AIFM1	physical	20360068
ARL2_HUMAN	ARL2	physical	20360068
TIM50_HUMAN	TIMM50	physical	20360068
MAIP1_HUMAN	C2orf47	physical	20360068

Drug and Disease Associations

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

Regulatory Network of TBB4B_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-51, AND MASSSPECTROMETRY.	18034455 [Abstract]

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