dbPTM

TBA4A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBA4A_HUMAN
UniProt AC	P68366
Protein Name	Tubulin alpha-4A chain
Gene Name	TUBA4A
Organism	Homo sapiens (Human).
Sequence Length	448
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	MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MRECISVHVGQAG --CCCEEEEEEHHHH	20.16	15345747
10	Ubiquitination	ECISVHVGQAGVQMG CEEEEEEHHHHHHHC	9.20	27667366
11	Ubiquitination	CISVHVGQAGVQMGN EEEEEEHHHHHHHCH	33.58	27667366
13	Ubiquitination	SVHVGQAGVQMGNAC EEEEHHHHHHHCHHH	11.42	22817900
24	Phosphorylation	GNACWELYCLEHGIQ CHHHHHHHHHHCCCC	5.40	-
25	Acetylation	NACWELYCLEHGIQP HHHHHHHHHHCCCCC	5.86	8294455
38	Phosphorylation	QPDGQMPSDKTIGGG CCCCCCCCCCCCCCC	46.53	24275569
40	Acetylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	24906155
41	Phosphorylation	GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC	29.82	21712546
45	Ubiquitination	SDKTIGGGDDSFTTF CCCCCCCCCCCCEEE	30.27	22817900
48	Phosphorylation	TIGGGDDSFTTFFCE CCCCCCCCCEEEEEE	29.27	28731282
50	Phosphorylation	GGGDDSFTTFFCETG CCCCCCCEEEEEECC	27.01	21712546
51	Phosphorylation	GGDDSFTTFFCETGA CCCCCCEEEEEECCC	16.83	28102081
54	S-nitrosocysteine	DSFTTFFCETGAGKH CCCEEEEEECCCCCC	3.90	-
54	Glutathionylation	DSFTTFFCETGAGKH CCCEEEEEECCCCCC	3.90	22555962
54	S-nitrosylation	DSFTTFFCETGAGKH CCCEEEEEECCCCCC	3.90	20140087
54	S-palmitoylation	DSFTTFFCETGAGKH CCCEEEEEECCCCCC	3.90	29575903
56	Phosphorylation	FTTFFCETGAGKHVP CEEEEEECCCCCCCC	33.25	24732914
60	Acetylation	FCETGAGKHVPRAVF EEECCCCCCCCCEEE	40.68	26051181
60	Ubiquitination	FCETGAGKHVPRAVF EEECCCCCCCCCEEE	40.68	22817900
73	Phosphorylation	VFVDLEPTVIDEIRN EEECCCCCHHHHHHC	22.25	-
81	Acetylation	VIDEIRNGPYRQLFH HHHHHHCCCCHHHCC	15.69	-
81	Ubiquitination	VIDEIRNGPYRQLFH HHHHHHCCCCHHHCC	15.69	21890473
81	Ubiquitination	VIDEIRNGPYRQLFH HHHHHHCCCCHHHCC	15.69	32142685
83	Nitrated tyrosine	DEIRNGPYRQLFHPE HHHHCCCCHHHCCHH	16.64	-
83	Nitration	DEIRNGPYRQLFHPE HHHHCCCCHHHCCHH	16.64	-
94	Phosphorylation	FHPEQLITGKEDAAN CCHHHHCCCCHHHHH	51.28	28152594
96	Sumoylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	-
96	Acetylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	30584145
96	Sumoylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	-
96	Ubiquitination	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	27667366
97	Ubiquitination	EQLITGKEDAANNYA HHHCCCCHHHHHHCC	54.98	-
97	Ubiquitination	EQLITGKEDAANNYA HHHCCCCHHHHHHCC	54.98	21963094
103	Phosphorylation	KEDAANNYARGHYTI CHHHHHHCCCCCCCC	9.48	27155012
108	Phosphorylation	NNYARGHYTIGKEII HHCCCCCCCCCHHHH	11.68	25884760
109	Phosphorylation	NYARGHYTIGKEIID HCCCCCCCCCHHHHH	19.99	28796482
112	Sumoylation	RGHYTIGKEIIDPVL CCCCCCCHHHHHHHH	41.72	-
112	Acetylation	RGHYTIGKEIIDPVL CCCCCCCHHHHHHHH	41.72	26051181
112	Sumoylation	RGHYTIGKEIIDPVL CCCCCCCHHHHHHHH	41.72	-
112	Ubiquitination	RGHYTIGKEIIDPVL CCCCCCCHHHHHHHH	41.72	21906983
124	"N6,N6-dimethyllysine"	PVLDRIRKLSDQCTG HHHHHHHHHHHHCCC	50.39	-
124	Methylation	PVLDRIRKLSDQCTG HHHHHHHHHHHHCCC	50.39	-
124	Ubiquitination	PVLDRIRKLSDQCTG HHHHHHHHHHHHCCC	50.39	-
127	Ubiquitination	DRIRKLSDQCTGLQG HHHHHHHHHCCCCCE	58.99	21963094
143	Phosphorylation	LVFHSFGGGTGSGFT EEEEECCCCCCCCHH	28.60	32142685
148	Acetylation	FGGGTGSGFTSLLME CCCCCCCCHHHHHHH	31.06	-
148	Ubiquitination	FGGGTGSGFTSLLME CCCCCCCCHHHHHHH	31.06	21890473
148	Acetylation	FGGGTGSGFTSLLME CCCCCCCCHHHHHHH	31.06	19608861
148	Ubiquitination	FGGGTGSGFTSLLME CCCCCCCCHHHHHHH	31.06	27667366
149	Ubiquitination	GGGTGSGFTSLLMER CCCCCCCHHHHHHHH	4.49	21890473
149	Ubiquitination	GGGTGSGFTSLLMER CCCCCCCHHHHHHHH	4.49	27667366
151	Phosphorylation	GTGSGFTSLLMERLS CCCCCHHHHHHHHHC	19.76	-
151	Ubiquitination	GTGSGFTSLLMERLS CCCCCHHHHHHHHHC	19.76	21963094
158	Phosphorylation	SLLMERLSVDYGKKS HHHHHHHCCCCCCCC	21.11	28355574
158	Ubiquitination	SLLMERLSVDYGKKS HHHHHHHCCCCCCCC	21.11	21963094
161	Nitration	MERLSVDYGKKSKLE HHHHCCCCCCCCCEE	28.79	-
161	Phosphorylation	MERLSVDYGKKSKLE HHHHCCCCCCCCCEE	28.79	23911959
163	Acetylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	129735
163	Methylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	129735
163	Ubiquitination	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	27667366
164	Ubiquitination	LSVDYGKKSKLEFSI HCCCCCCCCCEEEEE	48.75	21906983
165	Phosphorylation	SVDYGKKSKLEFSIY CCCCCCCCCEEEEEE	46.06	22817900
166	Ubiquitination	VDYGKKSKLEFSIYP CCCCCCCCEEEEEEE	62.00	22817900
170	Phosphorylation	KKSKLEFSIYPAPQV CCCCEEEEEEECCCC	16.31	23663014
172	Phosphorylation	SKLEFSIYPAPQVST CCEEEEEEECCCCCE	7.67	23663014
173	Ubiquitination	KLEFSIYPAPQVSTA CEEEEEEECCCCCEE	35.48	23000965
178	Phosphorylation	IYPAPQVSTAVVEPY EEECCCCCEEEEECC	12.85	23663014
179	Phosphorylation	YPAPQVSTAVVEPYN EECCCCCEEEEECCC	25.31	23663014
183	Ubiquitination	QVSTAVVEPYNSILT CCCEEEEECCCCCCC	35.15	21963094
185	Phosphorylation	STAVVEPYNSILTTH CEEEEECCCCCCCCC	14.18	23663014
185	Ubiquitination	STAVVEPYNSILTTH CEEEEECCCCCCCCC	14.18	22817900
187	Phosphorylation	AVVEPYNSILTTHTT EEEECCCCCCCCCCC	17.09	23663014
190	Phosphorylation	EPYNSILTTHTTLEH ECCCCCCCCCCCCCC	18.18	23663014
191	Phosphorylation	PYNSILTTHTTLEHS CCCCCCCCCCCCCCC	17.49	23663014
193	Phosphorylation	NSILTTHTTLEHSDC CCCCCCCCCCCCCCE	30.86	23663014
194	Phosphorylation	SILTTHTTLEHSDCA CCCCCCCCCCCCCEE	23.65	23663014
198	Phosphorylation	THTTLEHSDCAFMVD CCCCCCCCCEEEEEC	25.63	26356563
199	Ubiquitination	HTTLEHSDCAFMVDN CCCCCCCCEEEEECH	29.67	21963094
210	Phosphorylation	MVDNEAIYDICRRNL EECHHHHHHHHHCCC	13.30	25884760
217	Ubiquitination	YDICRRNLDIERPTY HHHHHCCCCCCCCCH	7.14	27667366
223	Phosphorylation	NLDIERPTYTNLNRL CCCCCCCCHHCHHHH	49.55	28796482
224	Phosphorylation	LDIERPTYTNLNRLI CCCCCCCHHCHHHHH	9.05	19605366
225	Phosphorylation	DIERPTYTNLNRLIS CCCCCCHHCHHHHHH	35.39	28555341
232	Phosphorylation	TNLNRLISQIVSSIT HCHHHHHHHHHHHHH	20.60	21712546
236	Phosphorylation	RLISQIVSSITASLR HHHHHHHHHHHHHCC	20.04	23403867
237	Phosphorylation	LISQIVSSITASLRF HHHHHHHHHHHHCCC	17.05	23403867
239	Phosphorylation	SQIVSSITASLRFDG HHHHHHHHHHCCCCC	16.49	23403867
241	Phosphorylation	IVSSITASLRFDGAL HHHHHHHHCCCCCCC	16.07	23403867
241	Ubiquitination	IVSSITASLRFDGAL HHHHHHHHCCCCCCC	16.07	27667366
248	Ubiquitination	SLRFDGALNVDLTEF HCCCCCCCCCCCCEE	8.63	21963094
253	Phosphorylation	GALNVDLTEFQTNLV CCCCCCCCEEECCCC	30.23	21712546
257	Phosphorylation	VDLTEFQTNLVPYPR CCCCEEECCCCCCCC	35.52	21712546
262	Phosphorylation	FQTNLVPYPRIHFPL EECCCCCCCCCCCCC	9.54	22817901
265	Ubiquitination	NLVPYPRIHFPLATY CCCCCCCCCCCCCCC	3.20	-
265	Ubiquitination	NLVPYPRIHFPLATY CCCCCCCCCCCCCCC	3.20	21963094
271	Phosphorylation	RIHFPLATYAPVISA CCCCCCCCCCCCCCH	28.09	21945579
272	Phosphorylation	IHFPLATYAPVISAE CCCCCCCCCCCCCHH	11.87	21945579
277	Phosphorylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	21945579
277	Ubiquitination	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	22817900
280	Acetylation	APVISAEKAYHEQLS CCCCCHHHHHHHHCC	54.70	88225
280	Ubiquitination	APVISAEKAYHEQLS CCCCCHHHHHHHHCC	54.70	21906983
282	Phosphorylation	VISAEKAYHEQLSVA CCCHHHHHHHHCCHH	19.56	25159151
287	Phosphorylation	KAYHEQLSVAEITNA HHHHHHCCHHHHHHH	20.98	22322096
289	Ubiquitination	YHEQLSVAEITNACF HHHHCCHHHHHHHHC	10.09	21890473
289	Neddylation	YHEQLSVAEITNACF HHHHCCHHHHHHHHC	10.09	32015554
289	Ubiquitination	YHEQLSVAEITNACF HHHHCCHHHHHHHHC	10.09	21963094
292	Phosphorylation	QLSVAEITNACFEPA HCCHHHHHHHHCCCH	14.31	30576142
295	S-nitrosocysteine	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	-
295	Glutathionylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	22555962
295	S-nitrosylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	20140087
296	Acetylation	AEITNACFEPANQMV HHHHHHHCCCHHHCC	13.48	-
296	Ubiquitination	AEITNACFEPANQMV HHHHHHHCCCHHHCC	13.48	21890473
296	Acetylation	AEITNACFEPANQMV HHHHHHHCCCHHHCC	13.48	19608861
296	Ubiquitination	AEITNACFEPANQMV HHHHHHHCCCHHHCC	13.48	21963094
304	Neddylation	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	32015554
304	Ubiquitination	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	21963094
311	Ubiquitination	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	21890473
311	Acetylation	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	19608861
311	Ubiquitination	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	23000965
312	Phosphorylation	CDPRHGKYMACCLLY CCCCCCCEEEEHHHC	8.44	28152594
315	Glutathionylation	RHGKYMACCLLYRGD CCCCEEEEHHHCCCC	0.67	22555962
319	Phosphorylation	YMACCLLYRGDVVPK EEEEHHHCCCCCCCC	10.29	23917254
321	Ubiquitination	ACCLLYRGDVVPKDV EEHHHCCCCCCCCCH	20.64	-
321	Ubiquitination	ACCLLYRGDVVPKDV EEHHHCCCCCCCCCH	20.64	32142685
323	Ubiquitination	CLLYRGDVVPKDVNA HHHCCCCCCCCCHHH	9.88	22817900
325	Phosphorylation	LYRGDVVPKDVNAAI HCCCCCCCCCHHHHH	27.29	32142685
326	Ubiquitination	YRGDVVPKDVNAAIA CCCCCCCCCHHHHHH	63.80	23000965
334	Phosphorylation	DVNAAIAAIKTKRSI CHHHHHHHHHCCCCE	9.56	32142685
336	Sumoylation	NAAIAAIKTKRSIQF HHHHHHHHCCCCEEE	43.18	-
336	Acetylation	NAAIAAIKTKRSIQF HHHHHHHHCCCCEEE	43.18	26051181
336	Sumoylation	NAAIAAIKTKRSIQF HHHHHHHHCCCCEEE	43.18	-
336	Ubiquitination	NAAIAAIKTKRSIQF HHHHHHHHCCCCEEE	43.18	21906983
337	Ubiquitination	AAIAAIKTKRSIQFV HHHHHHHCCCCEEEE	26.10	-
337	Neddylation	AAIAAIKTKRSIQFV HHHHHHHCCCCEEEE	26.10	32015554
337	Phosphorylation	AAIAAIKTKRSIQFV HHHHHHHCCCCEEEE	26.10	28464451
337	Ubiquitination	AAIAAIKTKRSIQFV HHHHHHHCCCCEEEE	26.10	21963094
338	Ubiquitination	AIAAIKTKRSIQFVD HHHHHHCCCCEEEEE	38.86	22817900
339	Methylation	IAAIKTKRSIQFVDW HHHHHCCCCEEEEEE	44.20	-
340	Phosphorylation	AAIKTKRSIQFVDWC HHHHCCCCEEEEEEC	23.46	26846344
347	S-nitrosocysteine	SIQFVDWCPTGFKVG CEEEEEECCCCEEEE	1.55	-
347	Glutathionylation	SIQFVDWCPTGFKVG CEEEEEECCCCEEEE	1.55	22555962
347	S-nitrosylation	SIQFVDWCPTGFKVG CEEEEEECCCCEEEE	1.55	20140087
347	S-palmitoylation	SIQFVDWCPTGFKVG CEEEEEECCCCEEEE	1.55	29575903
349	Phosphorylation	QFVDWCPTGFKVGIN EEEEECCCCEEEEEE	52.71	30266825
352	Acetylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	129723
352	Neddylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	32015554
352	Sumoylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
352	Ubiquitination	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	21906983
355	Acetylation	PTGFKVGINYQPPTV CCCEEEEEECCCCEE	4.93	-
355	Ubiquitination	PTGFKVGINYQPPTV CCCEEEEEECCCCEE	4.93	21890473
355	Acetylation	PTGFKVGINYQPPTV CCCEEEEEECCCCEE	4.93	19608861
355	Neddylation	PTGFKVGINYQPPTV CCCEEEEEECCCCEE	4.93	32015554
355	Ubiquitination	PTGFKVGINYQPPTV CCCEEEEEECCCCEE	4.93	27667366
357	Nitration	GFKVGINYQPPTVVP CEEEEEECCCCEECC	22.07	-
357	Phosphorylation	GFKVGINYQPPTVVP CEEEEEECCCCEECC	22.07	27273156
361	Phosphorylation	GINYQPPTVVPGGDL EEECCCCEECCCCCH	40.60	28152594
370	Sumoylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	-
370	Acetylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	19608861
370	Neddylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	32015554
370	Sumoylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	19608861
370	Ubiquitination	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	27667366
376	S-nitrosocysteine	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	-
376	Glutathionylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	22555962
376	S-nitrosylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH	1.90	20140087
379	Ubiquitination	QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH	12.78	21890473
379	Acetylation	QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH	12.78	19608861
379	Phosphorylation	QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH	12.78	19664995
379	Ubiquitination	QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH	12.78	32142685
381	Phosphorylation	AVCMLSNTTAIAEAW HHHHHCCHHHHHHHH	17.77	30108239
382	Phosphorylation	VCMLSNTTAIAEAWA HHHHCCHHHHHHHHH	21.95	30108239
386	Ubiquitination	SNTTAIAEAWARLDH CCHHHHHHHHHHCCC	38.33	-
386	Acetylation	SNTTAIAEAWARLDH CCHHHHHHHHHHCCC	38.33	19608861
386	Ubiquitination	SNTTAIAEAWARLDH CCHHHHHHHHHHCCC	38.33	21963094
394	Sumoylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	-
394	Acetylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	19608861
394	Sumoylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	19608861
394	Ubiquitination	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	32142685
399	Phosphorylation	DHKFDLMYAKRAFVH CCCCCHHHEEEHHHH	19.10	28674151
401	Sumoylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	-
401	Acetylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	129731
401	Sumoylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	19608861
401	Ubiquitination	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	21963094
408	Phosphorylation	KRAFVHWYVGEGMEE EEHHHHHHCCCCCCC	5.45	28796482
413	Sulfoxidation	HWYVGEGMEEGEFSE HHHCCCCCCCCCHHH	3.54	28183972
415	Ubiquitination	YVGEGMEEGEFSEAR HCCCCCCCCCHHHHH	55.95	-
415	Ubiquitination	YVGEGMEEGEFSEAR HCCCCCCCCCHHHHH	55.95	22817900
419	Phosphorylation	GMEEGEFSEAREDMA CCCCCCHHHHHHHHH	26.50	28270605
430	Ubiquitination	EDMAALEKDYEEVGI HHHHHHHHCHHHHCC	67.47	22817900
432	Phosphorylation	MAALEKDYEEVGIDS HHHHHHCHHHHCCCC	25.67	20044836
439	O-linked_Glycosylation	YEEVGIDSYEDEDEG HHHHCCCCCCCCCCC	28.62	29351928
439	Phosphorylation	YEEVGIDSYEDEDEG HHHHCCCCCCCCCCC	28.62	22817900
440	Phosphorylation	EEVGIDSYEDEDEGE HHHCCCCCCCCCCCC	24.53	22817900

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
Oops, there are no upstream regulatory protein records of TBA4A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
40	K	Acetylation	24906155
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen.
40	K	Methylation	24906155
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

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 TBA4A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBB5_HUMAN	TUBB	physical	22939629
TBB2A_HUMAN	TUBB2A	physical	22939629
TBB3_HUMAN	TUBB3	physical	22939629
TBB4B_HUMAN	TUBB4B	physical	22939629
PRPS1_HUMAN	PRPS1	physical	22863883
RS27A_HUMAN	RPS27A	physical	22863883
TRXR1_HUMAN	TXNRD1	physical	22863883
MGRN1_HUMAN	MGRN1	physical	24556679
TAU_HUMAN	MAPT	physical	24251416
PYR1_HUMAN	CAD	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
PSMD1_HUMAN	PSMD1	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
TBB2A_HUMAN	TUBB2A	physical	26344197
TBB2B_HUMAN	TUBB2B	physical	26344197
TBB3_HUMAN	TUBB3	physical	26344197
T11L2_HUMAN	TCP11L2	physical	28514442
DLGP5_HUMAN	DLGAP5	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442
DAAM1_HUMAN	DAAM1	physical	28514442
TKT_HUMAN	TKT	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616208	Amyotrophic lateral sclerosis 22, with or without frontotemporal dementia (ALS22)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB06772	Cabazitaxel
DB01179	Podofilox
DB00541	Vincristine

Regulatory Network of TBA4A_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-163 AND LYS-311, AND MASSSPECTROMETRY.	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-48 AND SER-340, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-340, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND TYR-440, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-272, AND MASSSPECTROMETRY.	15592455 [Abstract]

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