dbPTM

TBB5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TBB5_HUMAN
UniProt AC	P07437
Protein Name	Tubulin beta chain
Gene Name	TUBB
Organism	Homo sapiens (Human).
Sequence Length	444
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	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MREIVHIQA ------CCEEEEEEC	42.20	-
12	S-nitrosocysteine	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	-
12	Glutathionylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	22555962
12	S-nitrosylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	19483679
19	"N6,N6-dimethyllysine"	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	-
19	Acetylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	25953088
19	Methylation	CGNQIGAKFWEVISD CCCCHHHHHHEHHHC	45.88	-
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	28464451
33	Phosphorylation	DEHGIDPTGTYHGDS CCCCCCCCCCCCCCC	38.11	24043423
35	Phosphorylation	HGIDPTGTYHGDSDL CCCCCCCCCCCCCCC	18.15	25159151
36	Phosphorylation	GIDPTGTYHGDSDLQ CCCCCCCCCCCCCCE	12.73	19605366
40	Phosphorylation	TGTYHGDSDLQLDRI CCCCCCCCCCEEEEE	44.83	25159151
46	Methylation	DSDLQLDRISVYYNE CCCCEEEEEEEEEEC	31.51	30761469
48	Phosphorylation	DLQLDRISVYYNEAT CCEEEEEEEEEECCC	12.64	19664994
50	Phosphorylation	QLDRISVYYNEATGG EEEEEEEEEECCCCC	8.19	19605366
51	Phosphorylation	LDRISVYYNEATGGK EEEEEEEEECCCCCC	12.36	27273156
55	Phosphorylation	SVYYNEATGGKYVPR EEEEECCCCCCCCCE	40.04	23401153
56	Phosphorylation	VYYNEATGGKYVPRA EEEECCCCCCCCCEE	37.33	15592455
58	Methylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	129815
58	Acetylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	19608861
58	Succinylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
58	Ubiquitination	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
58	Malonylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	26320211
58	Succinylation	YNEATGGKYVPRAIL EECCCCCCCCCEEEE	44.40	-
59	Phosphorylation	NEATGGKYVPRAILV ECCCCCCCCCEEEEE	20.97	27174698
60	Phosphorylation	EATGGKYVPRAILVD CCCCCCCCCEEEEEE	2.70	-
66	Methylation	YVPRAILVDLEPGTM CCCEEEEEECCCCCC	6.88	-
68	Phosphorylation	PRAILVDLEPGTMDS CEEEEEECCCCCCCC	7.16	-
70	Phosphorylation	AILVDLEPGTMDSVR EEEEECCCCCCCCCC	51.34	-
71	Phosphorylation	ILVDLEPGTMDSVRS EEEECCCCCCCCCCC	25.05	-
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	30266825
73	Sulfoxidation	VDLEPGTMDSVRSGP EECCCCCCCCCCCCC	4.48	21406390
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	30266825
78	Phosphorylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	21082442
78	Methylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	-
78	Sumoylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	-
78	Ubiquitination	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	-
78	Acetylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	-
78	O-linked_Glycosylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	31373491
92	Phosphorylation	FRPDNFVFGQSGAGN CCCCCEEECCCCCCC	6.88	-
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	28674151
98	Phosphorylation	VFGQSGAGNNWAKGH EECCCCCCCCCCCCC	31.37	-
103	Acetylation	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	134097
103	Ubiquitination	GAGNNWAKGHYTEGA CCCCCCCCCCCCCHH	37.52	21906983
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	SVLDVVRKEAESCDC HHHHHHHHHHHHCCC	50.06	-
123	Sumoylation	VLDVVRKEAESCDCL HHHHHHHHHHHCCCC	47.29	-
123	Ubiquitination	VLDVVRKEAESCDCL HHHHHHHHHHHCCCC	47.29	-
126	Phosphorylation	VVRKEAESCDCLQGF HHHHHHHHCCCCCEE	23.46	30576142
127	Phosphorylation	VRKEAESCDCLQGFQ HHHHHHHCCCCCEEE	3.01	-
129	Glutathionylation	KEAESCDCLQGFQLT HHHHHCCCCCEEEEE	3.42	22555962
135	Phosphorylation	DCLQGFQLTHSLGGG CCCCEEEEEEECCCC	4.31	-
136	Phosphorylation	CLQGFQLTHSLGGGT CCCEEEEEEECCCCC	9.91	25159151
138	Phosphorylation	QGFQLTHSLGGGTGS CEEEEEEECCCCCCC	24.39	30576142
142	Ubiquitination	LTHSLGGGTGSGMGT EEEECCCCCCCCHHH	25.71	-
143	Phosphorylation	THSLGGGTGSGMGTL EEECCCCCCCCHHHH	31.30	30278072
145	Phosphorylation	SLGGGTGSGMGTLLI ECCCCCCCCHHHHHH	25.99	30576142
146	Phosphorylation	LGGGTGSGMGTLLIS CCCCCCCCHHHHHHH	21.64	-
149	Phosphorylation	GTGSGMGTLLISKIR CCCCCHHHHHHHHHH	14.97	30576142
153	Phosphorylation	GMGTLLISKIREEYP CHHHHHHHHHHHHCC	23.23	21406692
154	Ubiquitination	MGTLLISKIREEYPD HHHHHHHHHHHHCCC	38.50	-
156	Phosphorylation	TLLISKIREEYPDRI HHHHHHHHHHCCCCC	34.14	-
159	Phosphorylation	ISKIREEYPDRIMNT HHHHHHHCCCCCCCC	12.99	28152594
162	Methylation	IREEYPDRIMNTFSV HHHHCCCCCCCCEEC	26.08	-
163	Phosphorylation	REEYPDRIMNTFSVV HHHCCCCCCCCEECC	3.04	-
164	Sulfoxidation	EEYPDRIMNTFSVVP HHCCCCCCCCEECCC	3.94	28183972
166	Phosphorylation	YPDRIMNTFSVVPSP CCCCCCCCEECCCCC	10.41	23911959
168	Phosphorylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	23911959
168	O-linked_Glycosylation	DRIMNTFSVVPSPKV CCCCCCEECCCCCCC	21.84	31373491
172	Phosphorylation	NTFSVVPSPKVSDTV CCEECCCCCCCCCCE	26.24	25159151
173	Phosphorylation	TFSVVPSPKVSDTVV CEECCCCCCCCCCEE	34.69	-
174	Ubiquitination	FSVVPSPKVSDTVVE EECCCCCCCCCCEEE	59.72	-
176	Phosphorylation	VVPSPKVSDTVVEPY CCCCCCCCCCEEECC	33.42	26074081
179	Phosphorylation	SPKVSDTVVEPYNAT CCCCCCCEEECCCCE	5.72	-
182	Methylation	VSDTVVEPYNATLSV CCCCEEECCCCEEEH	18.97	-
183	Phosphorylation	SDTVVEPYNATLSVH CCCEEECCCCEEEHH	12.15	25884760
186	Phosphorylation	VVEPYNATLSVHQLV EEECCCCEEEHHHHH	18.87	-
188	Phosphorylation	EPYNATLSVHQLVEN ECCCCEEEHHHHHCC	17.13	-
192	Phosphorylation	ATLSVHQLVENTDET CEEEHHHHHCCCCCE	2.93	16371510
196	Phosphorylation	VHQLVENTDETYCID HHHHHCCCCCEEEEC	23.00	-
199	Phosphorylation	LVENTDETYCIDNEA HHCCCCCEEEECHHH	26.88	-
200	Phosphorylation	VENTDETYCIDNEAL HCCCCCEEEECHHHH	5.83	-
203	Phosphorylation	TDETYCIDNEALYDI CCCEEEECHHHHHHH	43.27	-
208	Phosphorylation	CIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	25884760
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	21906983
216	Phosphorylation	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	-
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
228	Phosphorylation	TYGDLNHLVSATMSG CCCCHHHHHHHHHCC	2.95	-
230	Phosphorylation	GDLNHLVSATMSGVT CCHHHHHHHHHCCCH	25.12	28152594
232	Phosphorylation	LNHLVSATMSGVTTC HHHHHHHHHCCCHHH	12.36	28152594
234	Phosphorylation	HLVSATMSGVTTCLR HHHHHHHCCCHHHHH	26.25	28152594
236	Ubiquitination	VSATMSGVTTCLRFP HHHHHCCCHHHHHCC	2.92	-
237	Phosphorylation	SATMSGVTTCLRFPG HHHHCCCHHHHHCCC	18.47	28450419
238	Phosphorylation	ATMSGVTTCLRFPGQ HHHCCCHHHHHCCCC	13.72	28450419
239	S-nitrosocysteine	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	-
239	Phosphorylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	-
239	Glutathionylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	22555962
239	S-nitrosylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	19483679
241	Phosphorylation	SGVTTCLRFPGQLNA CCCHHHHHCCCCCCH	37.55	-
242	Phosphorylation	GVTTCLRFPGQLNAD CCHHHHHCCCCCCHH	5.27	-
252	Sumoylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	20639865
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	-
254	Phosphorylation	NADLRKLAVNMVPFP CHHHHHHHHHCCCCC	8.15	-
257	Sulfoxidation	LRKLAVNMVPFPRLH HHHHHHHCCCCCCCC	3.05	28183972
267	Sulfoxidation	FPRLHFFMPGFAPLT CCCCCEECCCCCCCC	2.87	28183972
272	Sumoylation	FFMPGFAPLTSRGSQ EECCCCCCCCCCCCH	33.63	-
272	Ubiquitination	FFMPGFAPLTSRGSQ EECCCCCCCCCCCCH	33.63	-
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHE	18.47	22617229
274	O-linked_Glycosylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHE	18.47	31373491
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHEE	42.18	22617229
276	Methylation	GFAPLTSRGSQQYRA CCCCCCCCCCHHEEE	43.47	-
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHEEEEE	17.01	22617229
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHEEEEEHHH	7.10	23403867
285	Phosphorylation	SQQYRALTVPELTQQ CHHEEEEEHHHHHHH	32.79	27499020
290	Phosphorylation	ALTVPELTQQVFDAK EEEHHHHHHHHHHHH	18.46	30576142
294	Phosphorylation	PELTQQVFDAKNMMA HHHHHHHHHHHHHHH	7.03	-
295	Phosphorylation	ELTQQVFDAKNMMAA HHHHHHHHHHHHHHH	58.75	-
296	Methylation	LTQQVFDAKNMMAAC HHHHHHHHHHHHHHC	8.15	-
297	Ubiquitination	TQQVFDAKNMMAACD HHHHHHHHHHHHHCC	47.42	21906983
297	Acetylation	TQQVFDAKNMMAACD HHHHHHHHHHHHHCC	47.42	26051181
298	Phosphorylation	QQVFDAKNMMAACDP HHHHHHHHHHHHCCC	27.47	-
303	Glutathionylation	AKNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	22555962
303	S-nitrosylation	AKNMMAACDPRHGRY HHHHHHHCCCCCCCE	5.55	25040305
305	Phosphorylation	NMMAACDPRHGRYLT HHHHHCCCCCCCEEH	30.01	-
310	Phosphorylation	CDPRHGRYLTVAAVF CCCCCCCEEHHHHHH	16.00	28152594
312	Phosphorylation	PRHGRYLTVAAVFRG CCCCCEEHHHHHHCC	10.12	27273156
317	Ubiquitination	YLTVAAVFRGRMSMK EEHHHHHHCCCCCHH	6.17	-
318	Methylation	LTVAAVFRGRMSMKE EHHHHHHCCCCCHHH	25.80	-
321	Sulfoxidation	AAVFRGRMSMKEVDE HHHHCCCCCHHHHHH	5.23	28183972
322	Phosphorylation	AVFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	21712546
323	Sulfoxidation	VFRGRMSMKEVDEQM HHCCCCCHHHHHHHH	2.91	28183972
324	Acetylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	25953088
324	Sumoylation	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	-
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	18781797
330	Phosphorylation	MKEVDEQMLNVQNKN HHHHHHHHHHCCCCC	2.50	-
330	Sulfoxidation	MKEVDEQMLNVQNKN HHHHHHHHHHCCCCC	2.50	21406390
332	Phosphorylation	EVDEQMLNVQNKNSS HHHHHHHHCCCCCCC	28.17	-
336	Acetylation	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	25953088
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	21890473
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	22617229
338	Methylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	-
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	25159151
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	25159151
342	Phosphorylation	NKNSSYFVEWIPNNV CCCCCHHEEECCCCC	4.53	-
344	Sumoylation	NSSYFVEWIPNNVKT CCCHHEEECCCCCCE	13.16	-
344	Ubiquitination	NSSYFVEWIPNNVKT CCCHHEEECCCCCCE	13.16	-
344	Acetylation	NSSYFVEWIPNNVKT CCCHHEEECCCCCCE	13.16	-
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	21906983
351	Phosphorylation	WIPNNVKTAVCDIPP ECCCCCCEEECCCCC	21.75	-
354	Glutathionylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	22555962
354	S-palmitoylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	29575903
356	Ubiquitination	VKTAVCDIPPRGLKM CCEEECCCCCCCCEE	4.24	-
356	Acetylation	VKTAVCDIPPRGLKM CCEEECCCCCCCCEE	4.24	-
358	Phosphorylation	TAVCDIPPRGLKMAV EEECCCCCCCCEEEE	43.22	-
359	Phosphorylation	AVCDIPPRGLKMAVT EECCCCCCCCEEEEE	58.69	-
360	Phosphorylation	VCDIPPRGLKMAVTF ECCCCCCCCEEEEEE	35.11	-
362	Ubiquitination	DIPPRGLKMAVTFIG CCCCCCCEEEEEECC	27.86	21906983
363	Sulfoxidation	IPPRGLKMAVTFIGN CCCCCCEEEEEECCC	4.33	28465586
366	Phosphorylation	RGLKMAVTFIGNSTA CCCEEEEEECCCCHH	10.45	-
370	Sumoylation	MAVTFIGNSTAIQEL EEEEECCCCHHHHHH	31.22	-
370	Ubiquitination	MAVTFIGNSTAIQEL EEEEECCCCHHHHHH	31.22	-
371	Phosphorylation	AVTFIGNSTAIQELF EEEECCCCHHHHHHH	17.63	29802988
372	Phosphorylation	VTFIGNSTAIQELFK EEECCCCHHHHHHHH	31.60	21712546
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	25953088
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	20972266
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
382	Ubiquitination	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	-
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	21712546
388	Sulfoxidation	ISEQFTAMFRRKAFL HHHHHHHHHHHHHHH	2.14	28183972
391	Phosphorylation	QFTAMFRRKAFLHWY HHHHHHHHHHHHHHH	24.32	-
392	Ubiquitination	FTAMFRRKAFLHWYT HHHHHHHHHHHHHHC	38.95	-
399	Phosphorylation	KAFLHWYTGEGMDEM HHHHHHHCCCCCCHH	24.46	24275569
399	Ubiquitination	KAFLHWYTGEGMDEM HHHHHHHCCCCCCHH	24.46	-
402	Phosphorylation	LHWYTGEGMDEMEFT HHHHCCCCCCHHCCC	30.13	-
406	Phosphorylation	TGEGMDEMEFTEAES CCCCCCHHCCCHHHH	4.46	-
409	Phosphorylation	GMDEMEFTEAESNMN CCCHHCCCHHHHHHH	22.45	12631274
419	Phosphorylation	ESNMNDLVSEYQQYQ HHHHHHHHHHHHHHH	4.57	-
420	Phosphorylation	SNMNDLVSEYQQYQD HHHHHHHHHHHHHHH	37.57	12631274
422	Phosphorylation	MNDLVSEYQQYQDAT HHHHHHHHHHHHHCC	8.07	22817900
425	Phosphorylation	LVSEYQQYQDATAEE HHHHHHHHHHCCHHH	7.88	22817900
429	Phosphorylation	YQQYQDATAEEEEDF HHHHHHCCHHHHHHH	42.78	19007248
438	5-glutamyl polyglutamate	EEEEDFGEEAEEEA- HHHHHHHHHHHHHC-	54.77	-
438	Formation of an isopeptide bond	EEEEDFGEEAEEEA- HHHHHHHHHHHHHC-	54.77	-

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
166	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS
172	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:12716939

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 TBB5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYC_HUMAN	MYC	physical	20691906
KAT2A_HUMAN	KAT2A	physical	20691906
PDC6I_HUMAN	PDCD6IP	physical	12771190
CNN1_HUMAN	CNN1	physical	10220577
LRRK2_HUMAN	LRRK2	physical	19545277
KSYK_HUMAN	SYK	physical	9880513
VAV_HUMAN	VAV1	physical	9880513
HDAC6_HUMAN	HDAC6	physical	19961433
A4_HUMAN	APP	physical	21832049
U520_HUMAN	SNRNP200	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
XPO1_HUMAN	XPO1	physical	22939629
TCPB_HUMAN	CCT2	physical	23190606
MARE1_HUMAN	MAPRE1	physical	16455083
CLIP1_HUMAN	CLIP1	physical	16455083
HD_HUMAN	HTT	physical	11870213
G3P_HUMAN	GAPDH	physical	22863883
MAT2B_HUMAN	MAT2B	physical	22863883
TBA4A_HUMAN	TUBA4A	physical	22863883
TBB2A_HUMAN	TUBB2A	physical	22863883
TBB4B_HUMAN	TUBB4B	physical	22863883
TRXR1_HUMAN	TXNRD1	physical	22863883
ATX3_HUMAN	ATXN3	physical	24685680
PHB2_HUMAN	PHB2	physical	26344197
LNX2_HUMAN	LNX2	physical	21516116
CNDH2_HUMAN	NCAPH2	physical	21516116
S10A9_HUMAN	S100A9	physical	15331440
S10A8_HUMAN	S100A8	physical	15331440
ARL2_HUMAN	ARL2	physical	28514442
TBCD_HUMAN	TBCD	physical	28514442
TTC5_HUMAN	TTC5	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
PLD2_HUMAN	PLD2	physical	28514442
T11L1_HUMAN	TCP11L1	physical	28514442
EPHA4_HUMAN	EPHA4	physical	28514442
BCD1_HUMAN	ZNHIT6	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
MCM8_HUMAN	MCM8	physical	28514442
TBB4A_HUMAN	TUBB4A	physical	28514442
RL23_HUMAN	RPL23	physical	28514442
ALR_HUMAN	GFER	physical	28514442
DAAM1_HUMAN	DAAM1	physical	28514442
PEX14_HUMAN	PEX14	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
RTEL1_HUMAN	RTEL1	physical	28514442
EMAL4_HUMAN	EML4	physical	28514442
KC1G3_HUMAN	CSNK1G3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615771	Cortical dysplasia, complex, with other brain malformations 6 (CDCBM6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01394	Colchicine
DB01179	Podofilox
DB00570	Vinblastine
DB00541	Vincristine
DB00361	Vinorelbine

Regulatory Network of TBB5_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
"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 SER-48; THR-55 AND THR-429,AND MASS SPECTROMETRY.	19007248 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, AND MASSSPECTROMETRY.	19534553 [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-36, AND MASSSPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-324, AND MASSSPECTROMETRY.	18781797 [Abstract]

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