dbPTM

TBB5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB5_MOUSE
UniProt AC	P99024
Protein Name	Tubulin beta-5 chain
Gene Name	Tubb5
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	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosocysteine	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	-
12	S-nitrosylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	24926564
33	Phosphorylation	DEHGIDPTGTYHGDS CCCCCCCCCCCCCCC	38.11	21149613
35	Phosphorylation	HGIDPTGTYHGDSDL CCCCCCCCCCCCCCC	18.15	21149613
36	Phosphorylation	GIDPTGTYHGDSDLQ CCCCCCCCCCCCCCE	12.73	21149613
40	Phosphorylation	TGTYHGDSDLQLDRI CCCCCCCCCCEEEEE	44.83	21149613
46	Methylation	DSDLQLDRISVYYNE CCCCEEEEEEEEEEC	31.51	30761471
48	Phosphorylation	DLQLDRISVYYNEAT CCEEEEEEEEEECCC	12.64	28066266
50	Phosphorylation	QLDRISVYYNEATGG EEEEEEEEEECCCCC	8.19	22817900
51	Phosphorylation	LDRISVYYNEATGGK EEEEEEEEECCCCCC	12.36	21454597
55	Phosphorylation	SVYYNEATGGKYVPR EEEEECCCCCCCCCE	40.04	25521595
58	Succinylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	23806337
58	Acetylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	23806337
58	Succinylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
58	Ubiquitination	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
59	Phosphorylation	NEATGGKYVPRAILV ECCCCCCCCCEEEEE	20.97	29514104
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
122	Ubiquitination	SVLDVVRKEAESCDC 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	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	-
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
239	S-nitrosylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	20925432
239	S-nitrosocysteine	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	27667366
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	15614737
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHE	18.47	21082442
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHEE	42.18	25177544
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHEEEEE	17.01	26239621
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHEEEEEHHH	7.10	23984901
285	Phosphorylation	SQQYRALTVPELTQQ CHHEEEEEHHHHHHH	32.79	27600695
290	Phosphorylation	ALTVPELTQQVFDAK EEEHHHHHHHHHHHH	18.46	27600695
297	Acetylation	TQQVFDAKNMMAACD HHHHHHHHHHHHHCC	47.42	23806337
297	Succinylation	TQQVFDAKNMMAACD HHHHHHHHHHHHHCC	47.42	23806337
297	Ubiquitination	TQQVFDAKNMMAACD HHHHHHHHHHHHHCC	47.42	-
303	S-nitrosylation	AKNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	24926564
303	Glutathionylation	AKNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	24333276
312	Phosphorylation	PRHGRYLTVAAVFRG CCCCCEEHHHHHHCC	10.12	22006019
318	Methylation	LTVAAVFRGRMSMKE EHHHHHHCCCCCHHH	25.80	-
322	Phosphorylation	AVFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	26370283
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	27667366
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	24926564
366	Phosphorylation	RGLKMAVTFIGNSTA CCCEEEEEECCCCHH	10.45	22817900
371	Phosphorylation	AVTFIGNSTAIQELF EEEECCCCHHHHHHH	17.63	26643407
372	Phosphorylation	VTFIGNSTAIQELFK EEECCCCHHHHHHHH	31.60	26643407
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	129813
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	23684622
438	Formation of an isopeptide bond	EEEEDFGEEAEEEA- HHHHHHHHHHHHHC-	54.77	-
438	5-glutamyl polyglutamate	EEEEDFGEEAEEEA- HHHHHHHHHHHHHC-	54.77	-

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	P06493	PSP
172	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
172	S	Phosphorylation		16371510
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 TBB5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TSP1_HUMAN	THBS1	physical	20360068
TBCD_HUMAN	TBCD	physical	20360068
T11L1_HUMAN	TCP11L1	physical	20360068
DNJA1_HUMAN	DNAJA1	physical	20360068
ARL2_HUMAN	ARL2	physical	20360068
AIFM1_HUMAN	AIFM1	physical	20360068
CDN2A_HUMAN	CDKN2A	physical	20360068
ARF_HUMAN	CDKN2A	physical	20360068
DNJA4_HUMAN	DNAJA4	physical	20360068
DNJA2_HUMAN	DNAJA2	physical	20360068
PNKD_HUMAN	PNKD	physical	20360068

Drug and Disease Associations

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

Regulatory Network of TBB5_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASSSPECTROMETRY.	15648052 [Abstract]
"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-340, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, AND MASSSPECTROMETRY.	17947660 [Abstract]

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