TBA1A_HUMAN - dbPTM
TBA1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA1A_HUMAN
UniProt AC Q71U36
Protein Name Tubulin alpha-1A chain
Gene Name TUBA1A
Organism Homo sapiens (Human).
Sequence Length 451
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 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--MRECISIHVGQAG
--CCCEEEEEECCHH
20.50-
16PhosphorylationVGQAGVQIGNACWEL
ECCHHEEECHHHHHC
4.2232142685
24PhosphorylationGNACWELYCLEHGIQ
CHHHHHCHHHHCCCC
5.40-
25NeddylationNACWELYCLEHGIQP
HHHHHCHHHHCCCCC
5.8632015554
25UbiquitinationNACWELYCLEHGIQP
HHHHHCHHHHCCCCC
5.8632142685
38PhosphorylationQPDGQMPSDKTIGGG
CCCCCCCCCCCCCCC
46.5326074081
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
40MethylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
40UbiquitinationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8225463755
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7419664994
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.8529255136
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0225159151
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0023927012
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6821890473
60SumoylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6819811145
60MethylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60NeddylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6832015554
60SumoylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6821906983
61MethylationSETGAGKHVPRAVFV
CCCCCCCCCCEEEEE
33.62-
61UbiquitinationSETGAGKHVPRAVFV
CCCCCCCCCCEEEEE
33.6227667366
64MethylationGAGKHVPRAVFVDLE
CCCCCCCEEEEECCC
42.15-
73PhosphorylationVFVDLEPTVIDEVRT
EEECCCCEEEHHCCC
22.2530108239
77UbiquitinationLEPTVIDEVRTGTYR
CCCEEEHHCCCCCCH
23.8321963094
80PhosphorylationTVIDEVRTGTYRQLF
EEEHHCCCCCCHHCC
38.7728857561
82PhosphorylationIDEVRTGTYRQLFHP
EHHCCCCCCHHCCCH
18.2128857561
83NitrationDEVRTGTYRQLFHPE
HHCCCCCCHHCCCHH
9.56-
83PhosphorylationDEVRTGTYRQLFHPE
HHCCCCCCHHCCCHH
9.5628857561
89UbiquitinationTYRQLFHPEQLITGK
CCHHCCCHHHHCCCC
24.5625015289
94PhosphorylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH
51.2828152594
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7121890473
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7130582623
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7121906983
103NitrationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.48-
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.4827155012
108NitrationNNYARGHYTIGKEII
HHCCCCCCCCCHHHH
11.68-
108PhosphorylationNNYARGHYTIGKEII
HHCCCCCCCCCHHHH
11.6825884760
109PhosphorylationNYARGHYTIGKEIID
HCCCCCCCCCHHHHH
19.9928796482
112UbiquitinationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.7221890473
112SumoylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.72-
112AcetylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.7218528869
112SumoylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.72-
112UbiquitinationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.7221906983
123PhosphorylationDLVLDRIRKLADQCT
HHHHHHHHHHHHHCC
28.9132142685
124AcetylationLVLDRIRKLADQCTG
HHHHHHHHHHHHCCC
45.7315611751
124UbiquitinationLVLDRIRKLADQCTG
HHHHHHHHHHHHCCC
45.7321906983
128AcetylationRIRKLADQCTGLQGF
HHHHHHHHCCCCCCE
22.5119608861
128UbiquitinationRIRKLADQCTGLQGF
HHHHHHHHCCCCCCE
22.5127667366
129UbiquitinationIRKLADQCTGLQGFL
HHHHHHHCCCCCCEE
3.1627667366
131UbiquitinationKLADQCTGLQGFLVF
HHHHHCCCCCCEEEE
24.5122817900
151PhosphorylationGTGSGFTSLLMERLS
CCCCCHHHHHHHHHC
19.76-
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.1128355574
161NitrationMERLSVDYGKKSKLE
HHHHCCCCCCCCCEE
28.79-
161PhosphorylationMERLSVDYGKKSKLE
HHHHCCCCCCCCCEE
28.7923911959
163UbiquitinationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8721890473
163AcetylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8719608861
163MethylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8719608861
163UbiquitinationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8727667366
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.7521890473
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.7521906983
165PhosphorylationSVDYGKKSKLEFSIY
CCCCCCCCCEEEEEE
46.0622817900
166UbiquitinationVDYGKKSKLEFSIYP
CCCCCCCCEEEEEEE
62.0022817900
170PhosphorylationKKSKLEFSIYPAPQV
CCCCEEEEEEECCCC
16.3123663014
172PhosphorylationSKLEFSIYPAPQVST
CCEEEEEEECCCCCE
7.6723663014
178PhosphorylationIYPAPQVSTAVVEPY
EEECCCCCEEEEECC
12.8523663014
179PhosphorylationYPAPQVSTAVVEPYN
EECCCCCEEEEECCC
25.3123663014
185PhosphorylationSTAVVEPYNSILTTH
CEEEEECCCCCCCCC
14.1823663014
187PhosphorylationAVVEPYNSILTTHTT
EEEECCCCCCCCCCC
17.0923663014
190PhosphorylationEPYNSILTTHTTLEH
ECCCCCCCCCCCCCC
18.1823663014
191PhosphorylationPYNSILTTHTTLEHS
CCCCCCCCCCCCCCC
17.4923663014
193PhosphorylationNSILTTHTTLEHSDC
CCCCCCCCCCCCCCE
30.8623663014
194PhosphorylationSILTTHTTLEHSDCA
CCCCCCCCCCCCCEE
23.6523663014
198PhosphorylationTHTTLEHSDCAFMVD
CCCCCCCCCEEEEEC
25.6326356563
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.3025884760
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCCCCHHHH
49.5528796482
224NitrationLDIERPTYTNLNRLI
CCCCCCCCCCHHHHH
9.05-
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCCCCHHHHH
9.0519605366
225PhosphorylationDIERPTYTNLNRLIG
CCCCCCCCCHHHHHH
35.3928555341
236PhosphorylationRLIGQIVSSITASLR
HHHHHHHHHHHHHCC
20.0427732954
237PhosphorylationLIGQIVSSITASLRF
HHHHHHHHHHHHCCC
17.0527732954
239PhosphorylationGQIVSSITASLRFDG
HHHHHHHHHHCCCCC
16.4927732954
241PhosphorylationIVSSITASLRFDGAL
HHHHHHHHCCCCCCC
16.07-
245UbiquitinationITASLRFDGALNVDL
HHHHCCCCCCCCCCC
34.7121963094
253PhosphorylationGALNVDLTEFQTNLV
CCCCCCCCEEECCCC
30.2321712546
257PhosphorylationVDLTEFQTNLVPYPR
CCCCEEECCCCCCCC
35.5221712546
262NitrationFQTNLVPYPRIHFPL
EECCCCCCCCCCCCC
9.54-
262PhosphorylationFQTNLVPYPRIHFPL
EECCCCCCCCCCCCC
9.5422817901
269NeddylationYPRIHFPLATYAPVI
CCCCCCCCCCCCCCC
5.6332015554
269UbiquitinationYPRIHFPLATYAPVI
CCCCCCCCCCCCCCC
5.6321963094
271PhosphorylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0921945579
272NitrationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.87-
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.8721945579
276UbiquitinationLATYAPVISAEKAYH
CCCCCCCCCHHHHHH
2.9221963094
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5221945579
280UbiquitinationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.7021906983
282Nitrated tyrosineVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
282NitrationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
282NitrationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
282PhosphorylationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.5625159151
287PhosphorylationKAYHEQLSVAEITNA
HHHHHHCCHHHHHHH
20.9822322096
291AcetylationEQLSVAEITNACFEP
HHCCHHHHHHHHCCC
2.3119608861
291UbiquitinationEQLSVAEITNACFEP
HHCCHHHHHHHHCCC
2.3127667366
292PhosphorylationQLSVAEITNACFEPA
HCCHHHHHHHHCCCH
14.3130576142
295GlutathionylationVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.2722555962
301NeddylationACFEPANQMVKCDPR
HHCCCHHHCCCCCCC
39.9032015554
301UbiquitinationACFEPANQMVKCDPR
HHCCCHHHCCCCCCC
39.9021963094
303UbiquitinationFEPANQMVKCDPRHG
CCCHHHCCCCCCCCC
3.9321963094
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8121890473
304NeddylationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8132015554
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8121963094
311UbiquitinationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.2321890473
311AcetylationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.2322632513
311UbiquitinationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.2321906983
312PhosphorylationCDPRHGKYMACCLLY
CCCCCCCEEEEHHHC
8.4428152594
314PhosphorylationPRHGKYMACCLLYRG
CCCCCEEEEHHHCCC
4.2732142685
315GlutathionylationRHGKYMACCLLYRGD
CCCCEEEEHHHCCCC
0.6722555962
317UbiquitinationGKYMACCLLYRGDVV
CCEEEEHHHCCCCCC
4.7821963094
319PhosphorylationYMACCLLYRGDVVPK
EEEEHHHCCCCCCCC
10.2923917254
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.8021890473
326SumoylationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.80-
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.8022632523
326SumoylationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.8019608861
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCCHHHHH
63.8027667366
334PhosphorylationDVNAAIATIKTKRTI
CCHHHHHHCCCCCEE
19.5223401153
335NeddylationVNAAIATIKTKRTIQ
CHHHHHHCCCCCEEE
3.8432015554
335UbiquitinationVNAAIATIKTKRTIQ
CHHHHHHCCCCCEEE
3.8427667366
336SumoylationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.57-
336AcetylationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.5714497329
336NeddylationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.5732015554
336SumoylationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.57-
336UbiquitinationNAAIATIKTKRTIQF
HHHHHHCCCCCEEEE
43.5721906983
337PhosphorylationAAIATIKTKRTIQFV
HHHHHCCCCCEEEEE
23.1630266825
338MethylationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.4114505105
338UbiquitinationAIATIKTKRTIQFVD
HHHHCCCCCEEEEEE
42.4121963094
340PhosphorylationATIKTKRTIQFVDWC
HHCCCCCEEEEEEEC
22.2328857561
347GlutathionylationTIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5522555962
347S-palmitoylationTIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5529575903
349PhosphorylationQFVDWCPTGFKVGIN
EEEEECCCCEEEEEE
52.7121712546
352AcetylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.6813670219
352SumoylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.6821963094
357NitrationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.07-
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.0727273156
359UbiquitinationKVGINYQPPTVVPGG
EEEEECCCCEECCCC
19.0332142685
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH
40.6028152594
366AcetylationPPTVVPGGDLAKVQR
CCEECCCCCHHHHHH
22.2319608861
366UbiquitinationPPTVVPGGDLAKVQR
CCEECCCCCHHHHHH
22.2321963094
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3121890473
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370AcetylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3122632503
370NeddylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3132015554
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3121906983
376GlutathionylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9022555962
379PhosphorylationQRAVCMLSNTTAIAE
HHHHHHHCCHHHHHH
12.7819664995
381PhosphorylationAVCMLSNTTAIAEAW
HHHHHCCHHHHHHHH
17.7730108239
382PhosphorylationVCMLSNTTAIAEAWA
HHHHCCHHHHHHHHH
21.9530108239
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9921890473
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9914496259
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9921906983
395UbiquitinationWARLDHKFDLMYAKR
HHHCCCCCCHHHEEE
8.6021963094
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.1028674151
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1113670207
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1119608861
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1121963094
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC
5.4528796482
419PhosphorylationGMEEGEFSEAREDMA
CCCCCCHHHHHHHHH
26.5028270605
430UbiquitinationEDMAALEKDYEEVGV
HHHHHHHHCHHHHCC
67.4721906983
432PhosphorylationMAALEKDYEEVGVDS
HHHHHHCHHHHCCCC
25.6728796482
439PhosphorylationYEEVGVDSVEGEGEE
HHHHCCCCCCCCCCC
21.4720201521
4455-glutamyl polyglutamateDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
445Formation of an isopeptide bondDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
451NitrationGEEEGEEY-------
CCCCCCCC-------
21.39-
451NitrationGEEEGEEY-------
CCCCCCCC-------
21.3910339593
451PhosphorylationGEEEGEEY-------
CCCCCCCC-------
21.3928674151

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
165SPhosphorylationKinasePKCAP17252
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
40KAcetylation

24906155
40KMethylation

24906155

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 TBA1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIS1_HUMANPAFAH1B1physical
9384577
MYC_HUMANMYCphysical
20691906
VAV_HUMANVAV1physical
8530437
ZAP70_HUMANZAP70physical
8530437
ACTN1_HUMANACTN1physical
18341635
DAG1_HUMANDAG1physical
18341635
MTAP2_HUMANMAP2physical
18341635
ITB1_HUMANITGB1physical
18341635
PDC6I_HUMANPDCD6IPphysical
12771190
CBL_HUMANCBLphysical
15878338
IFNE_HUMANIFNEphysical
22565157
TAU_HUMANMAPTphysical
22565157
SQSTM_HUMANSQSTM1physical
22565157
UBC_HUMANUBCphysical
22565157
CYLD_HUMANCYLDphysical
18222923
HDAC6_HUMANHDAC6physical
19961433
TBB2A_HUMANTUBB2Aphysical
22939629
TBA1B_HUMANTUBA1Bphysical
22939629
TBB5_HUMANTUBBphysical
22939629
TBB4B_HUMANTUBB4Bphysical
22939629
TBB6_HUMANTUBB6physical
22939629
TBB3_HUMANTUBB3physical
22939629
TBA4A_HUMANTUBA4Aphysical
22939629
VATB2_HUMANATP6V1B2physical
22939629
MARE1_HUMANMAPRE1physical
16455083
CLIP1_HUMANCLIP1physical
16455083
G3P_HUMANGAPDHphysical
22863883
METK2_HUMANMAT2Aphysical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
TBA4A_HUMANTUBA4Aphysical
22863883
TBB6_HUMANTUBB6physical
22863883
TBB5_HUMANTUBBphysical
22863883
ATX3_HUMANATXN3physical
24685680
TBB5_HUMANTUBBphysical
24688049
F110C_HUMANFAM110Cphysical
19698782
TBB4B_HUMANTUBB4Bphysical
26344197
S10A9_HUMANS100A9physical
15331440
S10A8_HUMANS100A8physical
15331440
T11L2_HUMANTCP11L2physical
28514442
TTC5_HUMANTTC5physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TBB3_HUMANTUBB3physical
28514442
TUSC3_HUMANTUSC3genetic
27453043
CDC73_HUMANCDC73genetic
27453043
ATAD5_HUMANATAD5genetic
27453043
CHK1_HUMANCHEK1genetic
27453043
L2GL1_HUMANLLGL1genetic
27453043
ING4_HUMANING4genetic
27453043
ING5_HUMANING5genetic
27453043
WRN_HUMANWRNgenetic
27453043
BLM_HUMANBLMgenetic
27453043
XRCC3_HUMANXRCC3genetic
27453043
RB_HUMANRB1genetic
27453043
1433Z_HUMANYWHAZgenetic
27453043
WEE1_HUMANWEE1genetic
27453043
RL11_HUMANRPL11genetic
27453043
TITIN_HUMANTTNgenetic
27453043
PHB2_HUMANPHB2genetic
27453043
CC14A_HUMANCDC14Agenetic
27453043
MTOR_HUMANMTORgenetic
27453043
CHK2_HUMANCHEK2genetic
27453043

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611603Lissencephaly 3 (LIS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00518Albendazole
DB00643Mebendazole
DB00570Vinblastine
Regulatory Network of TBA1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.
"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-48 AND SER-439, AND MASSSPECTROMETRY.
"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-439, AND MASSSPECTROMETRY.
"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-439, AND MASSSPECTROMETRY.

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