dbPTM

TBB6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB6_HUMAN
UniProt AC	Q9BUF5
Protein Name	Tubulin beta-6 chain
Gene Name	TUBB6
Organism	Homo sapiens (Human).
Sequence Length	446
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	MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQYQDATANDGEEAFEDEEEEIDG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Phosphorylation	GIDPAGGYVGDSALQ CCCCCCCCCCCCHHE	10.59	18452278
40	Phosphorylation	AGGYVGDSALQLERI CCCCCCCCHHEEEEE	25.58	18452278
50	Phosphorylation	QLERINVYYNESSSQ EEEEEEEEECCCCCC	8.97	28152594
51	Phosphorylation	LERINVYYNESSSQK EEEEEEEECCCCCCC	14.26	25348954
54	Phosphorylation	INVYYNESSSQKYVP EEEEECCCCCCCCCC	31.48	28152594
55	Phosphorylation	NVYYNESSSQKYVPR EEEECCCCCCCCCCC	30.52	28152594
56	Phosphorylation	VYYNESSSQKYVPRA EEECCCCCCCCCCCE	39.71	17525332
58	Ubiquitination	YNESSSQKYVPRAAL ECCCCCCCCCCCEEE	50.60	21890473
58	Acetylation	YNESSSQKYVPRAAL ECCCCCCCCCCCEEE	50.60	26051181
59	Phosphorylation	NESSSQKYVPRAALV CCCCCCCCCCCEEEE	14.19	30174305
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	24275569
73	Sulfoxidation	VDLEPGTMDSVRSGP EECCCCCCCCCCCCC	4.48	30846556
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	28857561
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	20873877
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	20873877
136	Phosphorylation	CLQGFQLTHSLGGGT CCCCEEEEECCCCCC	9.91	-
138	Phosphorylation	QGFQLTHSLGGGTGS CCEEEEECCCCCCCC	24.39	25627689
143	Phosphorylation	THSLGGGTGSGMGTL EECCCCCCCCCHHHH	31.30	-
145	Phosphorylation	SLGGGTGSGMGTLLI CCCCCCCCCHHHHHH	25.99	-
147	Sulfoxidation	GGGTGSGMGTLLISK CCCCCCCHHHHHHHH	3.87	30846556
149	Phosphorylation	GTGSGMGTLLISKIR CCCCCHHHHHHHHHH	14.97	-
153	Phosphorylation	GMGTLLISKIREEFP CHHHHHHHHHHHHCC	23.23	-
154	Ubiquitination	MGTLLISKIREEFPD HHHHHHHHHHHHCCC	38.50	-
166	Phosphorylation	FPDRIMNTFSVMPSP CCCHHHHHCCCCCCC	10.41	20068231
168	Phosphorylation	DRIMNTFSVMPSPKV CHHHHHCCCCCCCCC	18.57	20068231
172	Phosphorylation	NTFSVMPSPKVSDTV HHCCCCCCCCCCCCE	21.18	29978859
176	Phosphorylation	VMPSPKVSDTVVEPY CCCCCCCCCCEEECC	33.42	26074081
183	Phosphorylation	SDTVVEPYNATLSVH CCCEEECCCCEEEHH	12.15	25884760
196	Phosphorylation	VHQLVENTDETYCID HHHHHCCCCCEEEEC	23.00	-
199	Phosphorylation	LVENTDETYCIDNEA HHCCCCCEEEECHHH	26.88	-
200	Phosphorylation	VENTDETYCIDNEAL HCCCCCEEEECHHHH	5.83	-
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	25884760
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCH	43.08	-
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCHHH	29.19	-
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCHHHH	24.86	25921289
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCHHHHHH	37.74	22817900
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCHHHHHHH	15.17	25884760
230	Phosphorylation	GDLNHLVSATMSGVT HHHHHHHHHHHCCCC	25.12	18691976
232	Phosphorylation	LNHLVSATMSGVTTS HHHHHHHHHCCCCCC	12.36	21406692
233	Sulfoxidation	NHLVSATMSGVTTSL HHHHHHHHCCCCCCC	3.08	30846556
234	Phosphorylation	HLVSATMSGVTTSLR HHHHHHHCCCCCCCC	26.25	21406692
237	Phosphorylation	SATMSGVTTSLRFPG HHHHCCCCCCCCCCC	17.75	21406692
238	Phosphorylation	ATMSGVTTSLRFPGQ HHHCCCCCCCCCCCC	24.29	21406692
239	Phosphorylation	TMSGVTTSLRFPGQL HHCCCCCCCCCCCCC	14.26	21406692
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	20639865
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
267	Sulfoxidation	FPRLHFFMPGFAPLT CCCCCEECCCCCCCC	2.87	28183972
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	22617229
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHE	42.18	22617229
276	Methylation	GFAPLTSRGSQQYRA CCCCCCCCCCHHHEE	43.47	-
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHHEEEE	17.01	22617229
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHHEEEEHHH	7.10	23403867
285	Phosphorylation	SQQYRALTVPELTQQ CHHHEEEEHHHHHHH	32.79	29978859
290	Phosphorylation	ALTVPELTQQMFDAR EEEHHHHHHHHHHHH	18.32	29978859
293	Sulfoxidation	VPELTQQMFDARNMM HHHHHHHHHHHHHHH	2.06	30846556
297	Ubiquitination	TQQMFDARNMMAACD HHHHHHHHHHHHHCC	33.16	21890473
303	S-palmitoylation	ARNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	29575903
310	Phosphorylation	CDPRHGRYLTVATVF CCCCCCCEEEEEEEE	16.00	28152594
312	Phosphorylation	PRHGRYLTVATVFRG CCCCCEEEEEEEEEC	10.12	28152594
315	Phosphorylation	GRYLTVATVFRGPMS CCEEEEEEEEECCCC	18.81	24076635
321	Sulfoxidation	ATVFRGPMSMKEVDE EEEEECCCCHHHHHH	7.33	30846556
322	Phosphorylation	TVFRGPMSMKEVDEQ EEEECCCCHHHHHHH	29.81	24719451
323	Sulfoxidation	VFRGPMSMKEVDEQM EEECCCCHHHHHHHH	3.31	30846556
324	Ubiquitination	FRGPMSMKEVDEQML EECCCCHHHHHHHHH	47.48	21890473
330	Sulfoxidation	MKEVDEQMLAIQSKN HHHHHHHHHHHHCCC	2.28	30846556
335	Phosphorylation	EQMLAIQSKNSSYFV HHHHHHHCCCCCCEE	27.91	23911959
336	Ubiquitination	QMLAIQSKNSSYFVE HHHHHHCCCCCCEEE	44.46	21890473
338	Phosphorylation	LAIQSKNSSYFVEWI HHHHCCCCCCEEEEC	30.10	22617229
339	Phosphorylation	AIQSKNSSYFVEWIP HHHCCCCCCEEEECC	31.80	25159151
340	Phosphorylation	IQSKNSSYFVEWIPN HHCCCCCCEEEECCC	16.09	25159151
350	Ubiquitination	EWIPNNVKVAVCDIP EECCCCEEEEEECCC	26.97	21890473
362	Ubiquitination	DIPPRGLKMASTFIG CCCCCCHHHHHHHHC	34.93	2190698
363	Sulfoxidation	IPPRGLKMASTFIGN CCCCCHHHHHHHHCC	4.24	21406390
365	Phosphorylation	PRGLKMASTFIGNST CCCHHHHHHHHCCCH	21.98	28857561
366	Phosphorylation	RGLKMASTFIGNSTA CCHHHHHHHHCCCHH	15.10	28857561
371	Phosphorylation	ASTFIGNSTAIQELF HHHHHCCCHHHHHHH	17.63	21712546
372	Phosphorylation	STFIGNSTAIQELFK HHHHCCCHHHHHHHH	31.60	21712546
379	Ubiquitination	TAIQELFKRISEQFS HHHHHHHHHHHHHHH	62.54	-
379	Acetylation	TAIQELFKRISEQFS HHHHHHHHHHHHHHH	62.54	25038526
388	Sulfoxidation	ISEQFSAMFRRKAFL HHHHHHHHHHHHHHH	2.32	30846556
409	Phosphorylation	GMDEMEFTEAESNMN CCCHHCCCHHHHHHH	22.45	12631274
420	Phosphorylation	SNMNDLVSEYQQYQD HHHHHHHHHHHHHHH	37.57	12631274
422	Phosphorylation	MNDLVSEYQQYQDAT HHHHHHHHHHHHHHC	8.07	-
438	Formation of an isopeptide bond	NDGEEAFEDEEEEID CCCHHHHHHHHHHCC	72.12	-
438	5-glutamyl polyglutamate	NDGEEAFEDEEEEID CCCHHHHHHHHHHCC	72.12	-

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	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 TBB6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCBP1_HUMAN	PCBP1	physical	22863883
TBA4A_HUMAN	TUBA4A	physical	22863883
TBB4B_HUMAN	TUBB4B	physical	22863883

Drug and Disease Associations

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

Regulatory Network of TBB6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY.	17525332 [Abstract]

show