dbPTM

TBA1C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBA1C_HUMAN
UniProt AC	Q9BQE3
Protein Name	Tubulin alpha-1C chain
Gene Name	TUBA1C
Organism	Homo sapiens (Human).
Sequence Length	449
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	MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSADGEDEGEEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	O-linked_Glycosylation	--MRECISIHVGQAG --CCCEEEEEECCHH	20.50	28510447
6	Phosphorylation	--MRECISIHVGQAG --CCCEEEEEECCHH	20.50	-
24	Phosphorylation	GNACWELYCLEHGIQ CHHHHHCHHHHCCCC	5.40	-
38	O-linked_Glycosylation	QPDGQMPSDKTIGGG CCCCCCCCCCCCCCC	46.53	28510447
38	Phosphorylation	QPDGQMPSDKTIGGG CCCCCCCCCCCCCCC	46.53	26074081
40	Acetylation	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	24906155
40	Ubiquitination	DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC	46.51	24906155
41	O-linked_Glycosylation	GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC	29.82	28510447
41	Phosphorylation	GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC	29.82	25463755
48	Phosphorylation	TIGGGDDSFNTFFSE CCCCCCCCHHHCCCC	25.74	19664994
51	Phosphorylation	GGDDSFNTFFSETGA CCCCCHHHCCCCCCC	24.85	29255136
54	Phosphorylation	DSFNTFFSETGAGKH CCHHHCCCCCCCCCC	30.02	25159151
56	O-linked_Glycosylation	FNTFFSETGAGKHVP HHHCCCCCCCCCCCC	31.00	28510447
56	Phosphorylation	FNTFFSETGAGKHVP HHHCCCCCCCCCCCC	31.00	23927012
60	Sumoylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	-
60	Acetylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	19811241
60	Sumoylation	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	19608861
60	Ubiquitination	FSETGAGKHVPRAVF CCCCCCCCCCCEEEE	40.68	20639865
73	Phosphorylation	VFVDLEPTVIDEVRT EEECCCCEEEHHCCC	22.25	30108239
80	O-linked_Glycosylation	TVIDEVRTGTYRQLF EEEHHCCCCCCHHCC	38.77	28510447
80	Phosphorylation	TVIDEVRTGTYRQLF EEEHHCCCCCCHHCC	38.77	28857561
82	Phosphorylation	IDEVRTGTYRQLFHP EHHCCCCCCHHCCCH	18.21	28857561
83	Phosphorylation	DEVRTGTYRQLFHPE HHCCCCCCHHCCCHH	9.56	28857561
94	O-linked_Glycosylation	FHPEQLITGKEDAAN CCHHHHCCCCHHHHH	51.28	28510447
94	Phosphorylation	FHPEQLITGKEDAAN CCHHHHCCCCHHHHH	51.28	28152594
96	Sumoylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	-
96	Acetylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	30584151
96	Sumoylation	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	-
96	Ubiquitination	PEQLITGKEDAANNY HHHHCCCCHHHHHHC	43.71	20639865
103	Phosphorylation	KEDAANNYARGHYTI CHHHHHHCCCCCCCC	9.48	27155012
108	Phosphorylation	NNYARGHYTIGKEII HHCCCCCCCCCHHHH	11.68	25884760
109	O-linked_Glycosylation	NYARGHYTIGKEIID HCCCCCCCCCHHHHH	19.99	28510447
109	Phosphorylation	NYARGHYTIGKEIID HCCCCCCCCCHHHHH	19.99	28796482
112	Sumoylation	RGHYTIGKEIIDLVL CCCCCCCHHHHHHHH	41.72	-
112	Acetylation	RGHYTIGKEIIDLVL CCCCCCCHHHHHHHH	41.72	19608861
112	Sumoylation	RGHYTIGKEIIDLVL CCCCCCCHHHHHHHH	41.72	19608861
112	Ubiquitination	RGHYTIGKEIIDLVL CCCCCCCHHHHHHHH	41.72	19608861
124	Acetylation	LVLDRIRKLADQCTG HHHHHHHHHHHHCCC	45.73	156239
124	Ubiquitination	LVLDRIRKLADQCTG HHHHHHHHHHHHCCC	45.73	21906983
145	O-linked_Glycosylation	FHSFGGGTGSGFTSL EEECCCCCCCCHHHH	31.30	28510447
147	O-linked_Glycosylation	SFGGGTGSGFTSLLM ECCCCCCCCHHHHHH	30.48	28510447
151	Phosphorylation	GTGSGFTSLLMERLS CCCCCHHHHHHHHHC	19.76	-
158	Phosphorylation	SLLMERLSVDYGKKS HHHHHHHCCCCCCCC	21.11	28355574
161	Phosphorylation	MERLSVDYGKKSKLE HHHHCCCCCCCCCEE	28.79	23911959
163	Acetylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	129755
163	Methylation	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	129755
163	Ubiquitination	RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE	47.87	21890473
164	Ubiquitination	LSVDYGKKSKLEFSI HCCCCCCCCCEEEEE	48.75	21906983
165	Phosphorylation	SVDYGKKSKLEFSIY CCCCCCCCCEEEEEE	46.06	22817900
166	Ubiquitination	VDYGKKSKLEFSIYP CCCCCCCCEEEEEEE	62.00	-
170	Phosphorylation	KKSKLEFSIYPAPQV CCCCEEEEEEECCCC	16.31	23663014
172	Phosphorylation	SKLEFSIYPAPQVST CCEEEEEEECCCCCE	7.67	23663014
178	Phosphorylation	IYPAPQVSTAVVEPY EEECCCCCEEEEECC	12.85	23663014
179	Phosphorylation	YPAPQVSTAVVEPYN EECCCCCEEEEECCC	25.31	23663014
185	Phosphorylation	STAVVEPYNSILTTH CEEEEECCCCCCCCC	14.18	23663014
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
210	Phosphorylation	MVDNEAIYDICRRNL EECHHHHHHHHHCCC	13.30	25884760
223	Phosphorylation	NLDIERPTYTNLNRL CCCCCCCCHHCHHHH	49.55	28796482
224	Phosphorylation	LDIERPTYTNLNRLI CCCCCCCHHCHHHHH	9.05	19605366
225	O-linked_Glycosylation	DIERPTYTNLNRLIS CCCCCCHHCHHHHHH	35.39	28510447
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
253	Phosphorylation	GALNVDLTEFQTNLV CCCCCCCCEEECCCC	30.23	21712546
257	O-linked_Glycosylation	VDLTEFQTNLVPYPR CCCCEEECCCCCCCC	35.52	28510447
257	Phosphorylation	VDLTEFQTNLVPYPR CCCCEEECCCCCCCC	35.52	21712546
262	Phosphorylation	FQTNLVPYPRIHFPL EECCCCCCCCCCCCC	9.54	22817901
271	O-linked_Glycosylation	RIHFPLATYAPVISA CCCCCCCCCCCCCCH	28.09	28510447
271	Phosphorylation	RIHFPLATYAPVISA CCCCCCCCCCCCCCH	28.09	21945579
272	Phosphorylation	IHFPLATYAPVISAE CCCCCCCCCCCCCHH	11.87	21945579
277	O-linked_Glycosylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	28510447
277	Phosphorylation	ATYAPVISAEKAYHE CCCCCCCCHHHHHHH	30.52	21945579
280	Acetylation	APVISAEKAYHEQLT CCCCCHHHHHHHCCC	54.70	88231
280	Ubiquitination	APVISAEKAYHEQLT CCCCCHHHHHHHCCC	54.70	-
282	Nitrated tyrosine	VISAEKAYHEQLTVA CCCHHHHHHHCCCHH	19.56	-
282	Nitration	VISAEKAYHEQLTVA CCCHHHHHHHCCCHH	19.56	-
282	Phosphorylation	VISAEKAYHEQLTVA CCCHHHHHHHCCCHH	19.56	22817900
287	Phosphorylation	KAYHEQLTVAEITNA HHHHHCCCHHHHHHH	19.84	-
292	Phosphorylation	QLTVAEITNACFEPA CCCHHHHHHHHCCCH	14.31	26126808
295	Glutathionylation	VAEITNACFEPANQM HHHHHHHHCCCHHHC	4.27	22555962
302	Sulfoxidation	CFEPANQMVKCDPRH HCCCHHHCCCCCCCC	2.89	30846556
304	Ubiquitination	EPANQMVKCDPRHGK CCHHHCCCCCCCCCC	27.81	21906983
311	Acetylation	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	129747
311	Ubiquitination	KCDPRHGKYMACCLL CCCCCCCCEEEEHHH	26.23	21890473
312	Phosphorylation	CDPRHGKYMACCLLY CCCCCCCEEEEHHHC	8.44	28152594
315	Glutathionylation	RHGKYMACCLLYRGD CCCCEEEEHHHCCCC	0.67	22555962
319	Phosphorylation	YMACCLLYRGDVVPK EEEEHHHCCCCCCCC	10.29	23917254
326	Sumoylation	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	-
326	Acetylation	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	22632557
326	Sumoylation	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	-
326	Ubiquitination	YRGDVVPKDVNAAIA CCCCCCCCCCHHHHH	63.80	21906983
334	O-linked_Glycosylation	DVNAAIATIKTKRTI CCHHHHHHCCCCCEE	19.52	28510447
334	Phosphorylation	DVNAAIATIKTKRTI CCHHHHHHCCCCCEE	19.52	23401153
336	Sumoylation	NAAIATIKTKRTIQF HHHHHHCCCCCEEEE	43.57	-
336	Acetylation	NAAIATIKTKRTIQF HHHHHHCCCCCEEEE	43.57	134093
336	Sumoylation	NAAIATIKTKRTIQF HHHHHHCCCCCEEEE	43.57	-
336	Ubiquitination	NAAIATIKTKRTIQF HHHHHHCCCCCEEEE	43.57	20639865
337	Phosphorylation	AAIATIKTKRTIQFV HHHHHCCCCCEEEEE	23.16	30266825
338	Methylation	AIATIKTKRTIQFVD HHHHCCCCCEEEEEE	42.41	184699
338	Ubiquitination	AIATIKTKRTIQFVD HHHHCCCCCEEEEEE	42.41	21906983
340	O-linked_Glycosylation	ATIKTKRTIQFVDWC HHCCCCCEEEEEEEC	22.23	28510447
340	Phosphorylation	ATIKTKRTIQFVDWC HHCCCCCEEEEEEEC	22.23	28857561
347	Glutathionylation	TIQFVDWCPTGFKVG EEEEEEECCCCEEEE	1.55	22555962
349	Phosphorylation	QFVDWCPTGFKVGIN EEEEECCCCEEEEEE	52.71	21712546
352	Acetylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	129743
352	Sumoylation	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
352	Ubiquitination	DWCPTGFKVGINYQP EECCCCEEEEEECCC	40.68	-
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	184703
370	Sumoylation	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	-
370	Ubiquitination	VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH	46.31	21906983
376	Glutathionylation	AKVQRAVCMLSNTTA HHHHHHHHHHCCCHH	1.90	22555962
377	Sulfoxidation	KVQRAVCMLSNTTAV HHHHHHHHHCCCHHH	3.55	28465586
379	Phosphorylation	QRAVCMLSNTTAVAE HHHHHHHCCCHHHHH	12.78	21712546
381	O-linked_Glycosylation	AVCMLSNTTAVAEAW HHHHHCCCHHHHHHH	16.86	28510447
382	O-linked_Glycosylation	VCMLSNTTAVAEAWA HHHHCCCHHHHHHHH	24.32	28510447
394	Sumoylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	-
394	Acetylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	134089
394	Sumoylation	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	-
394	Ubiquitination	AWARLDHKFDLMYAK HHHHCCCCCCHHHEE	39.99	21890473
399	Phosphorylation	DHKFDLMYAKRAFVH CCCCCHHHEEEHHHH	19.10	28674151
401	Sumoylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	-
401	Acetylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	129751
401	Sumoylation	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	-
401	Ubiquitination	KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH	27.11	21890473
408	Phosphorylation	KRAFVHWYVGEGMEE EEHHHHHHCCCCCCC	5.45	28796482
419	O-linked_Glycosylation	GMEEGEFSEAREDMA CCCCCCHHHHHHHHH	26.50	28510447
419	Phosphorylation	GMEEGEFSEAREDMA CCCCCCHHHHHHHHH	26.50	28270605
425	Sulfoxidation	FSEAREDMAALEKDY HHHHHHHHHHHHHHH	1.69	30846556
430	Ubiquitination	EDMAALEKDYEEVGA HHHHHHHHHHHHHCC	67.47	21906983
432	Phosphorylation	MAALEKDYEEVGADS HHHHHHHHHHHCCCC	25.67	28176443
439	Phosphorylation	YEEVGADSADGEDEG HHHHCCCCCCCCCCC	27.94	25159151
449	Nitration	GEDEGEEY------- CCCCCCCC-------	21.39	-
449	Phosphorylation	GEDEGEEY------- CCCCCCCC-------	21.39	28176443

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
158	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
165	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

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 TBA1C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBB6_HUMAN	TUBB6	physical	22939629
TBB3_HUMAN	TUBB3	physical	22939629
TBA4A_HUMAN	TUBA4A	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
G3P_HUMAN	GAPDH	physical	22863883
TBA4A_HUMAN	TUBA4A	physical	22863883
TBB4B_HUMAN	TUBB4B	physical	22863883
TBB5_HUMAN	TUBB	physical	22863883
RM02_HUMAN	MRPL2	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
AL3A2_HUMAN	ALDH3A2	physical	26496610
ADT2_HUMAN	SLC25A5	physical	26496610
AT1A1_HUMAN	ATP1A1	physical	26496610
AT2A2_HUMAN	ATP2A2	physical	26496610
AT2B1_HUMAN	ATP2B1	physical	26496610
ATPA_HUMAN	ATP5A1	physical	26496610
ATPB_HUMAN	ATP5B	physical	26496610
AUP1_HUMAN	AUP1	physical	26496610
BASI_HUMAN	BSG	physical	26496610
PYR1_HUMAN	CAD	physical	26496610
TCPZ_HUMAN	CCT6A	physical	26496610
CPSM_HUMAN	CPS1	physical	26496610
EF1A1_HUMAN	EEF1A1	physical	26496610
GCDH_HUMAN	GCDH	physical	26496610
DNJA1_HUMAN	DNAJA1	physical	26496610
HSPB1_HUMAN	HSPB1	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
CH60_HUMAN	HSPD1	physical	26496610
PDE3A_HUMAN	PDE3A	physical	26496610
MPCP_HUMAN	SLC25A3	physical	26496610
PRS8_HUMAN	PSMC5	physical	26496610
RCN1_HUMAN	RCN1	physical	26496610
RCN2_HUMAN	RCN2	physical	26496610
RNF5_HUMAN	RNF5	physical	26496610
RPN1_HUMAN	RPN1	physical	26496610
AAAT_HUMAN	SLC1A5	physical	26496610
SSRD_HUMAN	SSR4	physical	26496610
TCPA_HUMAN	TCP1	physical	26496610
TCPG_HUMAN	CCT3	physical	26496610
FXR1_HUMAN	FXR1	physical	26496610
LAT1_HUMAN	SLC7A5	physical	26496610
ATPK_HUMAN	ATP5J2	physical	26496610
LGAT1_HUMAN	LPGAT1	physical	26496610
KIF14_HUMAN	KIF14	physical	26496610
TXND9_HUMAN	TXNDC9	physical	26496610
DNJA2_HUMAN	DNAJA2	physical	26496610
TBA1B_HUMAN	TUBA1B	physical	26496610
TBB3_HUMAN	TUBB3	physical	26496610
TBB4B_HUMAN	TUBB4B	physical	26496610
HAX1_HUMAN	HAX1	physical	26496610
TCPH_HUMAN	CCT7	physical	26496610
TCPD_HUMAN	CCT4	physical	26496610
TCPB_HUMAN	CCT2	physical	26496610
ATP5L_HUMAN	ATP5L	physical	26496610
TCPQ_HUMAN	CCT8	physical	26496610
AFG32_HUMAN	AFG3L2	physical	26496610
SC61B_HUMAN	SEC61B	physical	26496610
STIP1_HUMAN	STIP1	physical	26496610
GCN1_HUMAN	GCN1L1	physical	26496610
TCPE_HUMAN	CCT5	physical	26496610
TRI32_HUMAN	TRIM32	physical	26496610
FAF2_HUMAN	FAF2	physical	26496610
EMAL2_HUMAN	EML2	physical	26496610
ATX10_HUMAN	ATXN10	physical	26496610
SERA_HUMAN	PHGDH	physical	26496610
PTHB1_HUMAN	BBS9	physical	26496610
PKN3_HUMAN	PKN3	physical	26496610
ZC21A_HUMAN	ZC2HC1A	physical	26496610
ATD3A_HUMAN	ATAD3A	physical	26496610
MA7D1_HUMAN	MAP7D1	physical	26496610
ZNFX1_HUMAN	ZNFX1	physical	26496610
ESYT2_HUMAN	ESYT2	physical	26496610
SRPRB_HUMAN	SRPRB	physical	26496610
AHNK_HUMAN	AHNAK	physical	26496610
YIPF5_HUMAN	YIPF5	physical	26496610
TBB6_HUMAN	TUBB6	physical	26496610
USMG5_HUMAN	USMG5	physical	26496610
TM209_HUMAN	TMEM209	physical	26496610
NEK9_HUMAN	NEK9	physical	26496610
RRFM_HUMAN	MRRF	physical	26496610
TIM50_HUMAN	TIMM50	physical	26496610
PGAM5_HUMAN	PGAM5	physical	26496610
TBB5_HUMAN	TUBB	physical	26496610
T11L2_HUMAN	TCP11L2	physical	26496610
T11L2_HUMAN	TCP11L2	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
TTC5_HUMAN	TTC5	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TBA1C_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-112, AND MASS SPECTROMETRY.	19608861 [Abstract]
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 TYR-432 AND SER-439, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-439, 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-439, AND MASSSPECTROMETRY.	18691976 [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-41; SER-48; THR-51;THR-334 AND SER-439, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-439, AND MASSSPECTROMETRY.	17081983 [Abstract]
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