dbPTM

TBB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB3_HUMAN
UniProt AC	Q13509
Protein Name	Tubulin beta-3 chain
Gene Name	TUBB3
Organism	Homo sapiens (Human).
Sequence Length	450
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. TUBB3 plays a critical role in proper axon guidance and mantainance..
Protein Sequence	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEAQGPK

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-nitrosylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	22178444
19	"N6,N6-dimethyllysine"	CGNQIGAKFWEVISD CCCCHHHHHHHHHHC	45.88	-
19	Acetylation	CGNQIGAKFWEVISD CCCCHHHHHHHHHHC	45.88	7670013
19	Methylation	CGNQIGAKFWEVISD CCCCHHHHHHHHHHC	45.88	-
25	Phosphorylation	AKFWEVISDEHGIDP HHHHHHHHCCCCCCC	41.96	20068231
31	Ubiquitination	ISDEHGIDPSGNYVG HHCCCCCCCCCCCCC	35.59	-
36	Phosphorylation	GIDPSGNYVGDSDLQ CCCCCCCCCCCCCCE	14.88	27642862
48	Phosphorylation	DLQLERISVYYNEAS CCEEEEEEEEECCCC	15.41	28152594
50	Phosphorylation	QLERISVYYNEASSH EEEEEEEEECCCCCC	8.19	28152594
51	Phosphorylation	LERISVYYNEASSHK EEEEEEEECCCCCCC	12.36	28152594
55	Phosphorylation	SVYYNEASSHKYVPR EEEECCCCCCCCCCE	27.14	28152594
56	Phosphorylation	VYYNEASSHKYVPRA EEECCCCCCCCCCEE	30.92	28152594
58	Acetylation	YNEASSHKYVPRAIL ECCCCCCCCCCEEEE	50.30	23236377
58	Ubiquitination	YNEASSHKYVPRAIL ECCCCCCCCCCEEEE	50.30	19608861
58	Malonylation	YNEASSHKYVPRAIL ECCCCCCCCCCEEEE	50.30	26320211
59	Phosphorylation	NEASSHKYVPRAILV CCCCCCCCCCEEEEE	15.40	29438985
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCHHHHCC	28.64	30266825
73	Sulfoxidation	VDLEPGTMDSVRSGA EECCCCCCHHHHCCC	4.48	30846556
75	Phosphorylation	LEPGTMDSVRSGAFG CCCCCCHHHHCCCCC	14.49	30266825
95	Phosphorylation	DNFIFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	21601212
103	Ubiquitination	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
129	Glutathionylation	KECENCDCLQGFQLT HHCCCCCCCCCEEEE	3.13	22555962
136	Phosphorylation	CLQGFQLTHSLGGGT CCCCEEEEEECCCCC	9.91	-
138	Phosphorylation	QGFQLTHSLGGGTGS CCEEEEEECCCCCCC	24.39	25627689
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	-
144	Ubiquitination	HSLGGGTGSGMGTLL EECCCCCCCCHHHHH	26.02	21890473
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	-
149	Phosphorylation	GTGSGMGTLLISKVR CCCCCHHHHHHHHHH	14.97	17855441
156	Methylation	TLLISKVREEYPDRI HHHHHHHHHHCCCCC	34.46	18967103
162	Methylation	VREEYPDRIMNTFSV HHHHCCCCCCCCEEC	26.08	-
164	Sulfoxidation	EEYPDRIMNTFSVVP HHCCCCCCCCEECCC	3.94	30846556
166	Phosphorylation	YPDRIMNTFSVVPSP CCCCCCCCEECCCCC	10.41	23911959
168	Phosphorylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	23911959
172	Phosphorylation	NTFSVVPSPKVSDTV CCEECCCCCCCCCCE	26.24	25159151
176	Phosphorylation	VVPSPKVSDTVVEPY CCCCCCCCCCEECCC	33.42	26074081
180	Ubiquitination	PKVSDTVVEPYNATL CCCCCCEECCCCCEE	7.14	21890473
196	Phosphorylation	IHQLVENTDETYCID HHHHHCCCCCEEEEC	23.00	-
199	Phosphorylation	LVENTDETYCIDNEA HHCCCCCEEEECHHH	26.88	-
200	Phosphorylation	VENTDETYCIDNEAL HCCCCCEEEECHHHH	5.83	-
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHHC	15.43	25884760
216	Ubiquitination	DICFRTLKLATPTYG HHHHHHCCCCCCCCH	35.15	21906983
219	Phosphorylation	FRTLKLATPTYGDLN HHHCCCCCCCCHHHH	26.97	24076635
221	Phosphorylation	TLKLATPTYGDLNHL HCCCCCCCCHHHHHH	35.46	17929957
225	Ubiquitination	ATPTYGDLNHLVSAT CCCCCHHHHHHHHHH	3.65	21890473
230	Phosphorylation	GDLNHLVSATMSGVT HHHHHHHHHHHCCCC	25.12	18691976
233	Sulfoxidation	NHLVSATMSGVTTSL HHHHHHHHCCCCCCC	3.08	30846556
237	Phosphorylation	SATMSGVTTSLRFPG HHHHCCCCCCCCCCC	17.75	19060867
239	Phosphorylation	TMSGVTTSLRFPGQL HHCCCCCCCCCCCCC	14.26	19060867
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	20639865
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	21890473
257	Sulfoxidation	LRKLAVNMVPFPRLH HHHHHHHCCCCCCCC	3.05	30846556
264	Ubiquitination	MVPFPRLHFFMPGFA CCCCCCCCCCCCCCC	18.38	21890473
267	Sulfoxidation	FPRLHFFMPGFAPLT CCCCCCCCCCCCCCC	2.87	30846556
274	Phosphorylation	MPGFAPLTARGSQQY CCCCCCCCCCCCHHH	17.16	24719451
278	Phosphorylation	APLTARGSQQYRALT CCCCCCCCHHHEEEE	14.46	21406692
278	Ubiquitination	APLTARGSQQYRALT CCCCCCCCHHHEEEE	14.46	21890473
285	Phosphorylation	SQQYRALTVPELTQQ CHHHEEEEHHHHHHH	32.79	28857561
290	Phosphorylation	ALTVPELTQQMFDAK EEEHHHHHHHHHCCC	18.32	16565220
290	Ubiquitination	ALTVPELTQQMFDAK EEEHHHHHHHHHCCC	18.32	21890473
293	Sulfoxidation	VPELTQQMFDAKNMM HHHHHHHHHCCCHHH	2.06	30846556
297	Acetylation	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	134105
297	Ubiquitination	TQQMFDAKNMMAACD HHHHHCCCHHHHHCC	47.42	21890473
303	Glutathionylation	AKNMMAACDPRHGRY CCHHHHHCCCCCCCE	5.55	22555962
307	Ubiquitination	MAACDPRHGRYLTVA HHHCCCCCCCEEEHE	30.39	21890473
310	Phosphorylation	CDPRHGRYLTVATVF CCCCCCCEEEHEEEE	16.00	28152594
312	Phosphorylation	PRHGRYLTVATVFRG CCCCCEEEHEEEEEC	10.12	28152594
315	Phosphorylation	GRYLTVATVFRGRMS CCEEEHEEEEECCCC	18.81	20068231
322	Phosphorylation	TVFRGRMSMKEVDEQ EEEECCCCHHHHHHH	25.91	20068231
324	Ubiquitination	FRGRMSMKEVDEQML EECCCCHHHHHHHHH	47.48	21890473
330	Sulfoxidation	MKEVDEQMLAIQSKN HHHHHHHHHHHHHCC	2.28	30846556
335	Phosphorylation	EQMLAIQSKNSSYFV HHHHHHHHCCCCCEE	27.91	29978859
336	Ubiquitination	QMLAIQSKNSSYFVE HHHHHHHCCCCCEEE	44.46	21890473
338	Phosphorylation	LAIQSKNSSYFVEWI HHHHHCCCCCEEEEC	30.10	22617229
339	Phosphorylation	AIQSKNSSYFVEWIP HHHHCCCCCEEEECC	31.80	25159151
340	Phosphorylation	IQSKNSSYFVEWIPN HHHCCCCCEEEECCC	16.09	25159151
350	Ubiquitination	EWIPNNVKVAVCDIP EECCCCEEEEEECCC	26.97	21890473
362	Ubiquitination	DIPPRGLKMSSTFIG CCCCCCCCCCCCCCC	39.29	21906983
363	Sulfoxidation	IPPRGLKMSSTFIGN CCCCCCCCCCCCCCC	4.62	21406390
364	Phosphorylation	PPRGLKMSSTFIGNS CCCCCCCCCCCCCCH	25.33	28857561
365	Phosphorylation	PRGLKMSSTFIGNST CCCCCCCCCCCCCHH	24.68	21712546
366	Phosphorylation	RGLKMSSTFIGNSTA CCCCCCCCCCCCHHH	16.38	28857561
371	Phosphorylation	SSTFIGNSTAIQELF CCCCCCCHHHHHHHH	17.63	22210691
372	Phosphorylation	STFIGNSTAIQELFK CCCCCCHHHHHHHHH	31.60	22210691
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	25038526
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	21906983
380	Dimethylation	AIQELFKRISEQFTA HHHHHHHHHHHHHHH	30.26	-
380	Methylation	AIQELFKRISEQFTA HHHHHHHHHHHHHHH	30.26	115390523
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	21712546
388	Sulfoxidation	ISEQFTAMFRRKAFL HHHHHHHHHHHHHHH	2.14	30846556
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	22817900
425	Phosphorylation	LVSEYQQYQDATAEE HHHHHHHHHCCCHHH	7.88	-
437	Phosphorylation	AEEEGEMYEDDEEES HHHHCCCCCCHHHHH	16.35	8619990
438	5-glutamyl polyglutamate	EEEGEMYEDDEEESE HHHCCCCCCHHHHHH	58.64	-
438	Formation of an isopeptide bond	EEEGEMYEDDEEESE HHHCCCCCCHHHHHH	58.64	-
444	Phosphorylation	YEDDEEESEAQGPK- CCCHHHHHHHCCCC-	41.32	8619990

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
409	T	Phosphorylation	Kinase	ADRBK1	P25098	GPS
420	S	Phosphorylation	Kinase	ADRBK1	P25098	GPS
444	S	Phosphorylation	Kinase	ADRBK1	P25098	GPS
444	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

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 TBB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPTSA_HUMAN	SPTSSA	physical	16169070
INSM1_HUMAN	INSM1	physical	16169070
SE1L3_HUMAN	SEL1L3	physical	16169070
LAP4A_HUMAN	LAPTM4A	physical	16169070
RM28_HUMAN	MRPL28	physical	16169070
PHIP_HUMAN	PHIP	physical	16169070
ROBO1_HUMAN	ROBO1	physical	16169070
ARHG7_HUMAN	ARHGEF7	physical	16169070
GBRAP_HUMAN	GABARAP	physical	16169070
RIPL2_HUMAN	RILPL2	physical	16169070
DX39B_HUMAN	DDX39B	physical	16169070
HEXDC_HUMAN	HEXDC	physical	16169070
KHDR1_HUMAN	KHDRBS1	physical	16169070
TRFE_HUMAN	TF	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
THIC_HUMAN	ACAT2	physical	22863883
CAZA1_HUMAN	CAPZA1	physical	22863883
CAPZB_HUMAN	CAPZB	physical	22863883
MOES_HUMAN	MSN	physical	22863883
STK26_HUMAN	STK26	physical	22863883
PAPS1_HUMAN	PAPSS1	physical	22863883
TAU_HUMAN	MAPT	physical	24251416
MTCL1_HUMAN	MTCL1	physical	23902687
PIWL1_HUMAN	PIWIL1	physical	26317901
TBA1B_HUMAN	TUBA1B	physical	26317901
STMN1_HUMAN	STMN1	physical	26317901
DLGP5_HUMAN	DLGAP5	physical	28514442
EMAL6_HUMAN	EML6	physical	28514442
TBB1_HUMAN	TUBB1	physical	28514442
EMAL2_HUMAN	EML2	physical	28514442
EMAL1_HUMAN	EML1	physical	28514442
TTC5_HUMAN	TTC5	physical	28514442
EMAL4_HUMAN	EML4	physical	28514442
AIFM1_HUMAN	AIFM1	physical	28514442
CENPJ_HUMAN	CENPJ	physical	28514442
T11L1_HUMAN	TCP11L1	physical	28514442
TOIP2_HUMAN	TOR1AIP2	physical	28514442
IFG15_HUMAN	TOR1AIP2	physical	28514442
EF1D_HUMAN	EEF1D	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600638	Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A)
614039	Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB04845	Ixabepilone

Regulatory Network of TBB3_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
"Microtubule regulation in mitosis: tubulin phosphorylation by thecyclin-dependent kinase Cdk1."; Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I.,Juillan-Binard C., Lantez V., Job D.; Mol. Biol. Cell 17:1041-1050(2006). Cited for: PHOSPHORYLATION AT SER-172 BY CDK1, AND MUTAGENESIS OF SER-172.	16371510 [Abstract]

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