dbPTM

TBB4B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB4B_HUMAN
UniProt AC	P68371
Protein Name	Tubulin beta-4B chain
Gene Name	TUBB4B
Organism	Homo sapiens (Human).
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
2	Methylation	------MREIVHLQA ------CCEEEEECC	42.20	-
19	Acetylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	7681317
19	Methylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	7681317
19	Ubiquitination	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	16196087
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	20068231
33	Phosphorylation	DEHGIDPTGTYHGDS CCCCCCCCCCCCCCC	38.11	28796482
35	Phosphorylation	HGIDPTGTYHGDSDL CCCCCCCCCCCCCCC	18.15	28796482
36	Nitration	GIDPTGTYHGDSDLQ CCCCCCCCCCCCCCE	12.73	-
36	Phosphorylation	GIDPTGTYHGDSDLQ CCCCCCCCCCCCCCE	12.73	28796482
40	Phosphorylation	TGTYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	28796482
50	Phosphorylation	QLERINVYYNEATGG EEEEEEEEEECCCCC	8.97	25159151
51	Phosphorylation	LERINVYYNEATGGK EEEEEEEEECCCCCC	11.40	27273156
55	Phosphorylation	NVYYNEATGGKYVPR EEEEECCCCCCCCCE	40.04	25159151
58	Sumoylation	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	-
58	Acetylation	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	19608861
58	Succinylation	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	23954790
58	Sumoylation	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	19608861
58	Ubiquitination	YNEATGGKYVPRAVL EECCCCCCCCCEEEE	44.40	27667366
59	Phosphorylation	NEATGGKYVPRAVLV ECCCCCCCCCEEEEE	20.97	28152594
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	20873877
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	21712546
78	Phosphorylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	21082442
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	28674151
103	Acetylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	70535
103	Sumoylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	-
103	Ubiquitination	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	21906983
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	25884760
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	25884760
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	22617229
122	Ubiquitination	SVLDVVRKEAESCDC HHHHHHHHHHHHCCC	50.06	29967540
126	Phosphorylation	VVRKEAESCDCLQGF HHHHHHHHCCCCCEE	23.46	30576142
136	Phosphorylation	CLQGFQLTHSLGGGT CCCEEEEEEECCCCC	9.91	25159151
138	Phosphorylation	QGFQLTHSLGGGTGS CEEEEEEECCCCCCC	24.39	30576142
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	30278072
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	30576142
149	Phosphorylation	GTGSGMGTLLISKIR CCCCCHHHHHHHHHH	14.97	30576142
153	Phosphorylation	GMGTLLISKIREEYP CHHHHHHHHHHHHCC	23.23	21406692
154	Ubiquitination	MGTLLISKIREEYPD HHHHHHHHHHHHCCC	38.50	16196087
159	Phosphorylation	ISKIREEYPDRIMNT HHHHHHHCCCCCCCC	12.99	28152594
162	Methylation	IREEYPDRIMNTFSV HHHHCCCCCCCCEEC	26.08	-
164	Sulfoxidation	EEYPDRIMNTFSVVP HHCCCCCCCCEECCC	3.94	28183972
166	Phosphorylation	YPDRIMNTFSVVPSP CCCCCCCCEECCCCC	10.41	23911959
168	O-linked_Glycosylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	26165356
168	Phosphorylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	23911959
172	O-linked_Glycosylation	NTFSVVPSPKVSDTV CCEECCCCCCCCCCE	26.24	26165356
172	Phosphorylation	NTFSVVPSPKVSDTV CCEECCCCCCCCCCE	26.24	25159151
174	Ubiquitination	FSVVPSPKVSDTVVE EECCCCCCCCCCEEE	59.72	16196087
176	Phosphorylation	VVPSPKVSDTVVEPY 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 HHHHHEECCCCCCCC	43.08	21963094
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCCCH	29.19	28152594
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCCCHH	24.86	28152594
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCCCHHHH	37.74	21082442
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCCCHHHHH	15.17	21082442
230	Phosphorylation	GDLNHLVSATMSGVT CCHHHHHHHHHCCCH	25.12	28152594
232	Phosphorylation	LNHLVSATMSGVTTC HHHHHHHHHCCCHHH	12.36	28152594
234	Phosphorylation	HLVSATMSGVTTCLR HHHHHHHCCCHHHHH	26.25	28152594
237	Phosphorylation	SATMSGVTTCLRFPG HHHHCCCHHHHHCCC	18.47	28450419
238	Phosphorylation	ATMSGVTTCLRFPGQ HHHCCCHHHHHCCCC	13.72	28450419
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	27667366
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	O-linked_Glycosylation	SQQYRALTVPELTQQ CHHHEEEEHHHHHHH	32.79	26165356
285	Phosphorylation	SQQYRALTVPELTQQ CHHHEEEEHHHHHHH	32.79	28857561
290	O-linked_Glycosylation	ALTVPELTQQMFDAK EEEHHHHHHHHHCCC	18.32	26165356
290	Phosphorylation	ALTVPELTQQMFDAK EEEHHHHHHHHHCCC	18.32	16565220
297	Acetylation	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	70539
297	Ubiquitination	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	21963094
310	Phosphorylation	CDPRHGRYLTVAAVF CCCCCCCEEHHHHHH	16.00	28152594
312	Phosphorylation	PRHGRYLTVAAVFRG CCCCCEEHHHHHHCC	10.12	27273156
318	Methylation	LTVAAVFRGRMSMKE EHHHHHHCCCCCHHH	25.80	-
322	Phosphorylation	AVFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	21712546
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	72597343
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	21906983
330	Sulfoxidation	MKEVDEQMLNVQNKN HHHHHHHHHHCCCCC	2.50	28183972
336	Acetylation	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	185081
336	Neddylation	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	32015554
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	32142685
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	22617229
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	25159151
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	25159151
350	Neddylation	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	32015554
350	Sumoylation	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	21963094
351	Phosphorylation	WIPNNVKTAVCDIPP ECCCCCCEEECCCCC	21.75	-
354	S-nitrosylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	22126794
354	S-palmitoylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	29575903
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEECC	33.36	21906983
363	Sulfoxidation	IPPRGLKMSATFIGN CCCCCCCEEEEECCC	3.86	28183972
364	Phosphorylation	PPRGLKMSATFIGNS CCCCCCEEEEECCCH	23.67	28857561
366	O-linked_Glycosylation	RGLKMSATFIGNSTA CCCCEEEEECCCHHH	14.42	26165356
366	Phosphorylation	RGLKMSATFIGNSTA CCCCEEEEECCCHHH	14.42	28857561
371	Phosphorylation	SATFIGNSTAIQELF EEEECCCHHHHHHHH	17.63	23186163
372	Phosphorylation	ATFIGNSTAIQELFK EEECCCHHHHHHHHH	31.60	23186163
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	25038526
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	23000965
382	O-linked_Glycosylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	26165356
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	21712546
388	Sulfoxidation	ISEQFTAMFRRKAFL HHHHHHHHHHHHHHH	2.14	28183972
392	Ubiquitination	FTAMFRRKAFLHWYT HHHHHHHHHHHHHHC	38.95	-
399	Phosphorylation	KAFLHWYTGEGMDEM HHHHHHHCCCCCCHH	24.46	24275569
409	Phosphorylation	GMDEMEFTEAESNMN CCCHHCCCHHHHHHH	22.45	12631274
420	Phosphorylation	SNMNDLVSEYQQYQD HHHHHHHHHHHHHHC	37.57	12631274
422	Phosphorylation	MNDLVSEYQQYQDAT HHHHHHHHHHHHCCH	8.07	22817900
425	Phosphorylation	LVSEYQQYQDATAEE HHHHHHHHHCCHHHH	7.88	-
438	5-glutamyl polyglutamate	EEEGEFEEEAEEEVA HHHCCCHHHHHHHHC	68.76	-
438	Formation of an isopeptide bond	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	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 TBB4B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ODO2_HUMAN	DLST	physical	16169070
PSME1_HUMAN	PSME1	physical	16169070
TBB5_HUMAN	TUBB	physical	22939629
XPO1_HUMAN	XPO1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
ISOC1_HUMAN	ISOC1	physical	22863883
MCTS1_HUMAN	MCTS1	physical	22863883
PCP_HUMAN	PRCP	physical	22863883
RAB1A_HUMAN	RAB1A	physical	22863883
TBA4A_HUMAN	TUBA4A	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
1433B_HUMAN	YWHAB	physical	22863883
PHB2_HUMAN	PHB2	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197

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
DB00518	Albendazole
DB00643	Mebendazole

Regulatory Network of TBB4B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-322, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND MASSSPECTROMETRY.	19007248 [Abstract]

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