dbPTM

TBB2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB2A_HUMAN
UniProt AC	Q13885
Protein Name	Tubulin beta-2A chain
Gene Name	TUBB2A
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 (By similarity)..
Protein Sequence	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA

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
18	Ubiquitination	QCGNQIGAKFWEVIS CCCCCHHHHHHEHHH	12.90	22817900
19	"N6,N6-dimethyllysine"	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	-
19	Acetylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	25953088
19	Ubiquitination	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	16196087
19	Methylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	-
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	20068231
33	Phosphorylation	DEHGIDPTGSYHGDS CCCCCCCCCCCCCCC	34.70	24076635
35	Phosphorylation	HGIDPTGSYHGDSDL CCCCCCCCCCCCCCC	19.21	24076635
36	Phosphorylation	GIDPTGSYHGDSDLQ CCCCCCCCCCCCCCE	15.92	22817900
37	Ubiquitination	IDPTGSYHGDSDLQL CCCCCCCCCCCCCEE	34.97	29967540
40	Phosphorylation	TGSYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	23532336
50	Phosphorylation	QLERINVYYNEAAGN EEEEEEEEEEHHCCC	8.97	23917254
51	Phosphorylation	LERINVYYNEAAGNK EEEEEEEEEHHCCCC	11.40	27642862
58	Acetylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	26051181
58	Succinylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	-
58	Ubiquitination	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	23000965
58	Succinylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	21890473
59	Phosphorylation	NEAAGNKYVPRAILV EHHCCCCCCCEEEEE	21.49	29438985
69	Ubiquitination	RAILVDLEPGTMDSV EEEEEECCCCCCCCC	36.90	29967540
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	30266825
73	Sulfoxidation	VDLEPGTMDSVRSGP EECCCCCCCCCCCCC	4.48	28183972
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	10930119
103	Ubiquitination	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	21906983
103	Sumoylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	-
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	25884760
106	Nitration	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	-
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	25884760
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	22617229
122	Ubiquitination	SVLDVVRKESESCDC HHHHHHHHHCCCCCC	54.72	29967540
126	Phosphorylation	VVRKESESCDCLQGF HHHHHCCCCCCCCCE	25.24	-
129	Glutathionylation	KESESCDCLQGFQLT HHCCCCCCCCCEEEE	3.42	22555962
131	Ubiquitination	SESCDCLQGFQLTHS CCCCCCCCCEEEEEE	57.92	21963094
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	29967540
159	Phosphorylation	ISKIREEYPDRIMNT HHHHHHHCCCCCCHH	12.99	28152594
162	Methylation	IREEYPDRIMNTFSV HHHHCCCCCCHHEEC	26.08	-
166	Phosphorylation	YPDRIMNTFSVMPSP CCCCCCHHEECCCCC	10.41	29978859
167	Ubiquitination	PDRIMNTFSVMPSPK CCCCCHHEECCCCCC	4.38	23000965
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
183	Nitration	SDTVVEPYNATLSVH CCCEEECCCCEEEHH	12.15	-
193	Phosphorylation	TLSVHQLVENTDETY EEEHHHHHCCCCCCE	4.25	32645325
200	Nitration	VENTDETYSIDNEAL HCCCCCCEEECHHHH	11.11	-
208	Phosphorylation	SIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	25884760
212	Ubiquitination	EALYDICFRTLKLTT HHHHHHHHHEECCCC	7.36	22817900
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
239	Ubiquitination	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	23000965
239	Glutathionylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	22555962
251	Ubiquitination	GQLNADLRKLAVNMV CCCCHHHHHHHHHCC	32.27	32142685
251	Neddylation	GQLNADLRKLAVNMV CCCCHHHHHHHHHCC	32.27	32015554
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	21906983
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
265	Ubiquitination	VPFPRLHFFMPGFAP CCCCCCCEECCCCCC	7.12	21963094
265	Neddylation	VPFPRLHFFMPGFAP CCCCCCCEECCCCCC	7.12	32015554
267	Sulfoxidation	FPRLHFFMPGFAPLT CCCCCEECCCCCCCC	2.87	28183972
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	22617229
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHH	42.18	22617229
276	Methylation	GFAPLTSRGSQQYRA CCCCCCCCCCHHHHE	43.47	-
277	Ubiquitination	FAPLTSRGSQQYRAL CCCCCCCCCHHHHEE	29.58	22817900
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	-
293	Sulfoxidation	VPELTQQMFDSKNMM HHHHHHHHHCCCCCH	2.64	30846556
294	Ubiquitination	PELTQQMFDSKNMMA HHHHHHHHCCCCCHH	9.25	23000965
297	Ubiquitination	TQQMFDSKNMMAACD HHHHHCCCCCHHHCC	51.19	22817900
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	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	72597355
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	21906983
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
330	Sulfoxidation	MKEVDEQMLNVQNKN HHHHHHHHHHCCCCC	2.50	28183972
336	Acetylation	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	7890913
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	21906983
336	Neddylation	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	32015554
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	21906983
350	Sumoylation	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
350	Neddylation	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	32015554
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	21906983
363	Sulfoxidation	IPPRGLKMSATFIGN CCCCCCCEEEEECCC	3.86	28183972
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	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	7354903
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	23000965
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 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 TBB2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RIC8A_HUMAN	RIC8A	physical	16169070
SCG1_HUMAN	CHGB	physical	16169070
HMMR_HUMAN	HMMR	physical	10547355
TBB4B_HUMAN	TUBB4B	physical	22939629
TBB5_HUMAN	TUBB	physical	22939629
MIPT3_HUMAN	TRAF3IP1	physical	20391533
PCBP1_HUMAN	PCBP1	physical	22863883
PFKAM_HUMAN	PFKM	physical	22863883
TBA1C_HUMAN	TUBA1C	physical	22863883
TBA4A_HUMAN	TUBA4A	physical	22863883
EFTU_HUMAN	TUFM	physical	22863883
EMAL4_HUMAN	EML4	physical	26186194
TBCD_HUMAN	TBCD	physical	26186194
TCPW_HUMAN	CCT6B	physical	26186194
OZF_HUMAN	ZNF146	physical	26186194
TCPB_HUMAN	CCT2	physical	26186194
TTC5_HUMAN	TTC5	physical	26186194
EMAL2_HUMAN	EML2	physical	26186194
EMAL1_HUMAN	EML1	physical	26186194
ARL2_HUMAN	ARL2	physical	26186194
ALR_HUMAN	GFER	physical	26186194
EMAL2_HUMAN	EML2	physical	28514442
ARL2_HUMAN	ARL2	physical	28514442
TBCD_HUMAN	TBCD	physical	28514442
EMAL4_HUMAN	EML4	physical	28514442
TTC5_HUMAN	TTC5	physical	28514442
TBB5_HUMAN	TUBB	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442
TCPZ_HUMAN	CCT6A	physical	28514442
ALR_HUMAN	GFER	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615763	Cortical dysplasia, complex, with other brain malformations 5 (CDCBM5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TBB2A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-95, AND MASSSPECTROMETRY.	19690332 [Abstract]

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