dbPTM

TBB2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB2B_HUMAN
UniProt AC	Q9BVA1
Protein Name	Tubulin beta-2B chain
Gene Name	TUBB2B
Organism	Homo sapiens (Human).
Sequence Length	445
Subcellular Localization	Cytoplasm, cytoskeleton .
Protein Description	Tubulin is the major constituent of microtubules. [PubMed: 23001566]
Protein Sequence	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MREIVHIQA ------CCEEEEEEC	42.20	-
12	Glutathionylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	22555962
12	S-palmitoylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	26865113
19	"N6,N6-dimethyllysine"	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	-
19	Acetylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	7670147
19	Methylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	-
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	21406692
33	Phosphorylation	DEHGIDPTGSYHGDS CCCCCCCCCCCCCCC	34.70	21406692
35	Phosphorylation	HGIDPTGSYHGDSDL CCCCCCCCCCCCCCC	19.21	21406692
36	Phosphorylation	GIDPTGSYHGDSDLQ CCCCCCCCCCCCCCE	15.92	21406692
40	Phosphorylation	TGSYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	23532336
50	Phosphorylation	QLERINVYYNEATGN EEEEEEEEEECCCCC	8.97	25884760
51	Phosphorylation	LERINVYYNEATGNK EEEEEEEEECCCCCC	11.40	21406692
55	Phosphorylation	NVYYNEATGNKYVPR EEEEECCCCCCCCCE	34.80	26670566
58	Ubiquitination	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	21890473
58	Acetylation	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	25038526
58	Succinylation	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	-
58	Succinylation	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	21890473
58	Ubiquitination	YNEATGNKYVPRAIL EECCCCCCCCCEEEE	49.31	21890473
59	Phosphorylation	NEATGNKYVPRAILV ECCCCCCCCCEEEEE	21.49	29438985
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	30266825
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	30266825
78	Phosphorylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	21082442
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	28674151
103	Acetylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	155739
103	Sumoylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	-
103	Ubiquitination	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	21906983
106	Nitration	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	-
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	25884760
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	25884760
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	22617229
122	Ubiquitination	SVLDVVRKESESCDC HHHHHHHHHCCCCCC	54.72	-
126	Phosphorylation	VVRKESESCDCLQGF HHHHHCCCCCCCCCE	25.24	-
129	Glutathionylation	KESESCDCLQGFQLT HHCCCCCCCCCEEEE	3.42	22555962
136	Phosphorylation	CLQGFQLTHSLGGGT CCCCEEEEEECCCCC	9.91	27251275
138	Phosphorylation	QGFQLTHSLGGGTGS CCEEEEEECCCCCCC	24.39	27251275
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	27251275
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	27251275
149	Phosphorylation	GTGSGMGTLLISKIR CCCCCHHHHHHHHHH	14.97	24173317
153	Phosphorylation	GMGTLLISKIREEYP CHHHHHHHHHHHHCC	23.23	-
154	Ubiquitination	MGTLLISKIREEYPD HHHHHHHHHHHHCCC	38.50	-
159	Phosphorylation	ISKIREEYPDRIMNT HHHHHHHCCCCCCHH	12.99	28152594
162	Methylation	IREEYPDRIMNTFSV HHHHCCCCCCHHEEC	26.08	-
166	Phosphorylation	YPDRIMNTFSVMPSP CCCCCCHHEECCCCC	10.41	29978859
168	Phosphorylation	DRIMNTFSVMPSPKV CCCCHHEECCCCCCC	18.57	20068231
172	Phosphorylation	NTFSVMPSPKVSDTV HHEECCCCCCCCCCE	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 HHHHHEECCCCCCCC	43.08	21890473
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	21890473
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
239	Glutathionylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	22555962
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	21890473
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	21890473
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	22617229
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHH	42.18	22617229
276	Methylation	GFAPLTSRGSQQYRA CCCCCCCCCCHHHHE	43.47	-
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHHHEEE	17.01	22617229
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHHHEEEHHH	7.10	23403867
285	Phosphorylation	SQQYRALTVPELTQQ CHHHHEEEHHHHHHH	32.79	23186163
290	Phosphorylation	ALTVPELTQQMFDSK EEEHHHHHHHHHCCC	18.32	-
297	Ubiquitination	TQQMFDSKNMMAACD HHHHHCCCCCHHHCC	51.19	21890473
297	Ubiquitination	TQQMFDSKNMMAACD HHHHHCCCCCHHHCC	51.19	21890473
303	Glutathionylation	SKNMMAACDPRHGRY CCCCHHHCCCCCCCC	5.55	22555962
310	Phosphorylation	CDPRHGRYLTVAAIF CCCCCCCCHHHHHHH	16.00	23917254
312	Phosphorylation	PRHGRYLTVAAIFRG CCCCCCHHHHHHHCC	10.12	24076635
318	Methylation	LTVAAIFRGRMSMKE HHHHHHHCCCCCHHH	26.20	-
322	Phosphorylation	AIFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	21712546
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	21890473
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	72597337
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	21890473
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	21890473
336	Acetylation	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	185085
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	21890473
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	22617229
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	25159151
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	25159151
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	21890473
350	Sumoylation	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	21890473
351	Phosphorylation	WIPNNVKTAVCDIPP ECCCCCCEEECCCCC	21.75	-
354	Glutathionylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	22555962
354	S-palmitoylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	29575903
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEECC	33.36	21890473
364	Phosphorylation	PPRGLKMSATFIGNS CCCCCCEEEEECCCH	23.67	28857561
366	Phosphorylation	RGLKMSATFIGNSTA CCCCEEEEECCCHHH	14.42	28857561
371	Phosphorylation	SATFIGNSTAIQELF EEEECCCHHHHHHHH	17.63	23186163
372	Phosphorylation	ATFIGNSTAIQELFK EEECCCHHHHHHHHH	31.60	23186163
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	21890473
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	156605
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	21890473
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	21712546
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 HHHHHHHHHHHHCCC	8.07	-
438	5-glutamyl polyglutamate	DEQGEFEEEEGEDEA HCCCCCCHHCCCCCC	67.67	-
438	Formation of an isopeptide bond	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	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 TBB2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC6_HUMAN	HDAC6	physical	12606581
TBB3_HUMAN	TUBB3	physical	26186194
TBB8_HUMAN	TUBB8	physical	26186194
TBB1_HUMAN	TUBB1	physical	26186194
TCPH_HUMAN	CCT7	physical	26186194
TBCD_HUMAN	TBCD	physical	26186194
TCPG_HUMAN	CCT3	physical	26186194
TCPW_HUMAN	CCT6B	physical	26186194
TCPZ_HUMAN	CCT6A	physical	26186194
OZF_HUMAN	ZNF146	physical	26186194
SEN2_HUMAN	TSEN2	physical	26186194
TCPB_HUMAN	CCT2	physical	26186194
EPHA4_HUMAN	EPHA4	physical	26186194
TTC5_HUMAN	TTC5	physical	26186194
EMAL4_HUMAN	EML4	physical	26186194
EMAL1_HUMAN	EML1	physical	26186194
EMAL2_HUMAN	EML2	physical	26186194
T11L1_HUMAN	TCP11L1	physical	26186194
ARL2_HUMAN	ARL2	physical	26186194
C42S2_HUMAN	CDC42SE2	physical	26186194
CAYP1_HUMAN	CAPS	physical	26186194
RS4X_HUMAN	RPS4X	physical	26344197
TBA1C_HUMAN	TUBA1C	physical	26344197
TBA3E_HUMAN	TUBA3E	physical	26344197
ARL2_HUMAN	ARL2	physical	28514442
EMAL2_HUMAN	EML2	physical	28514442
CAYP1_HUMAN	CAPS	physical	28514442
TBB1_HUMAN	TUBB1	physical	28514442
TBCD_HUMAN	TBCD	physical	28514442
EMAL6_HUMAN	EML6	physical	28514442
TTC5_HUMAN	TTC5	physical	28514442
EPHA4_HUMAN	EPHA4	physical	28514442
T11L1_HUMAN	TCP11L1	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
EMAL4_HUMAN	EML4	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442
TCPZ_HUMAN	CCT6A	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610031	Polymicrogyria, symmetric or asymmetric (PMGYSA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TBB2B_HUMAN

Related Literatures of Post-Translational Modification

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