TBA1B_HUMAN - dbPTM
TBA1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA1B_HUMAN
UniProt AC P68363
Protein Name Tubulin alpha-1B chain
Gene Name TUBA1B
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 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
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-
6O-linked_Glycosylation--MRECISIHVGQAG
--CCCEEEEEECCHH
20.5031373491
24PhosphorylationGNACWELYCLEHGIQ
CHHHHHCHHHHCCCC
5.40-
38PhosphorylationQPDGQMPSDKTIGGG
CCCCCCCCCCCCCCC
46.5326074081
40AcetylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
40UbiquitinationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
40MethylationDGQMPSDKTIGGGDD
CCCCCCCCCCCCCCC
46.5124906155
41PhosphorylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8225463755
41O-linked_GlycosylationGQMPSDKTIGGGDDS
CCCCCCCCCCCCCCC
29.8231373491
48PhosphorylationTIGGGDDSFNTFFSE
CCCCCCCCHHHCCCC
25.7419664994
51PhosphorylationGGDDSFNTFFSETGA
CCCCCHHHCCCCCCC
24.8529255136
54PhosphorylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0225159151
54O-linked_GlycosylationDSFNTFFSETGAGKH
CCHHHCCCCCCCCCC
30.0231373491
56PhosphorylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0023927012
56O-linked_GlycosylationFNTFFSETGAGKHVP
HHHCCCCCCCCCCCC
31.0031373491
60AcetylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6823954790
60SumoylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6827667366
60SumoylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60NeddylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6832015554
602-HydroxyisobutyrylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.68-
60MethylationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6812692561
60UbiquitinationFSETGAGKHVPRAVF
CCCCCCCCCCCEEEE
40.6821890473
73PhosphorylationVFVDLEPTVIDEVRT
EEECCCCEEEHHCCC
22.2530108239
73O-linked_GlycosylationVFVDLEPTVIDEVRT
EEECCCCEEEHHCCC
22.2531373491
80PhosphorylationTVIDEVRTGTYRQLF
EEEHHCCCCCCHHCC
38.7728857561
80O-linked_GlycosylationTVIDEVRTGTYRQLF
EEEHHCCCCCCHHCC
38.7731373491
82PhosphorylationIDEVRTGTYRQLFHP
EHHCCCCCCHHCCCH
18.2128857561
83PhosphorylationDEVRTGTYRQLFHPE
HHCCCCCCHHCCCHH
9.5628857561
94PhosphorylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH
51.2828152594
94O-linked_GlycosylationFHPEQLITGKEDAAN
CCHHHHCCCCHHHHH
51.2831373491
96AcetylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7123749302
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7121906983
96SumoylationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.71-
96UbiquitinationPEQLITGKEDAANNY
HHHHCCCCHHHHHHC
43.7121890473
103PhosphorylationKEDAANNYARGHYTI
CHHHHHHCCCCCCCC
9.4827155012
108PhosphorylationNNYARGHYTIGKEII
HHCCCCCCCCCHHHH
11.6825884760
109PhosphorylationNYARGHYTIGKEIID
HCCCCCCCCCHHHHH
19.9928796482
109O-linked_GlycosylationNYARGHYTIGKEIID
HCCCCCCCCCHHHHH
19.9931373491
112AcetylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.7223954790
112SumoylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.72-
112UbiquitinationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.7221963094
112SumoylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.72-
1122-HydroxyisobutyrylationRGHYTIGKEIIDLVL
CCCCCCCHHHHHHHH
41.72-
124AcetylationLVLDRIRKLADQCTG
HHHHHHHHHHHHCCC
45.7321466224
124UbiquitinationLVLDRIRKLADQCTG
HHHHHHHHHHHHCCC
45.7321906983
145O-linked_GlycosylationFHSFGGGTGSGFTSL
EEECCCCCCCCHHHH
31.3031373491
147O-linked_GlycosylationSFGGGTGSGFTSLLM
ECCCCCCCCHHHHHH
30.4831373491
151PhosphorylationGTGSGFTSLLMERLS
CCCCCHHHHHHHHHC
19.76-
154SulfoxidationSGFTSLLMERLSVDY
CCHHHHHHHHHCCCC
3.2330846556
158PhosphorylationSLLMERLSVDYGKKS
HHHHHHHCCCCCCCC
21.1128355574
161PhosphorylationMERLSVDYGKKSKLE
HHHHCCCCCCCCCEE
28.7923911959
161NitrationMERLSVDYGKKSKLE
HHHHCCCCCCCCCEE
28.79-
163MethylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.87129187
163AcetylationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8723749302
163UbiquitinationRLSVDYGKKSKLEFS
HHCCCCCCCCCEEEE
47.8727667366
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.7521906983
164UbiquitinationLSVDYGKKSKLEFSI
HCCCCCCCCCEEEEE
48.7521890473
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
188UbiquitinationVVEPYNSILTTHTTL
EEECCCCCCCCCCCC
3.3621890473
190PhosphorylationEPYNSILTTHTTLEH
ECCCCCCCCCCCCCC
18.1823663014
191PhosphorylationPYNSILTTHTTLEHS
CCCCCCCCCCCCCCC
17.4923663014
193PhosphorylationNSILTTHTTLEHSDC
CCCCCCCCCCCCCCE
30.8623663014
194PhosphorylationSILTTHTTLEHSDCA
CCCCCCCCCCCCCEE
23.6523663014
195UbiquitinationILTTHTTLEHSDCAF
CCCCCCCCCCCCEEE
6.1521890473
198PhosphorylationTHTTLEHSDCAFMVD
CCCCCCCCCEEEEEC
25.6326356563
210PhosphorylationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.3025884760
210UbiquitinationMVDNEAIYDICRRNL
EECHHHHHHHHHCCC
13.3021890473
220UbiquitinationCRRNLDIERPTYTNL
HHCCCCCCCCCHHCH
52.8821890473
222UbiquitinationRNLDIERPTYTNLNR
CCCCCCCCCHHCHHH
19.5721890473
223PhosphorylationNLDIERPTYTNLNRL
CCCCCCCCHHCHHHH
49.5528796482
224PhosphorylationLDIERPTYTNLNRLI
CCCCCCCHHCHHHHH
9.0519605366
225PhosphorylationDIERPTYTNLNRLIS
CCCCCCHHCHHHHHH
35.3928555341
225O-linked_GlycosylationDIERPTYTNLNRLIS
CCCCCCHHCHHHHHH
35.3931373491
232PhosphorylationTNLNRLISQIVSSIT
HCHHHHHHHHHHHHH
20.6021712546
236PhosphorylationRLISQIVSSITASLR
HHHHHHHHHHHHHCC
20.0423403867
236UbiquitinationRLISQIVSSITASLR
HHHHHHHHHHHHHCC
20.0421890473
237PhosphorylationLISQIVSSITASLRF
HHHHHHHHHHHHCCC
17.0523403867
239PhosphorylationSQIVSSITASLRFDG
HHHHHHHHHHCCCCC
16.4923403867
241PhosphorylationIVSSITASLRFDGAL
HHHHHHHHCCCCCCC
16.0723403867
253PhosphorylationGALNVDLTEFQTNLV
CCCCCCCCEEECCCC
30.2321712546
254UbiquitinationALNVDLTEFQTNLVP
CCCCCCCEEECCCCC
42.9521890473
257PhosphorylationVDLTEFQTNLVPYPR
CCCCEEECCCCCCCC
35.5221712546
257O-linked_GlycosylationVDLTEFQTNLVPYPR
CCCCEEECCCCCCCC
35.5231373491
262PhosphorylationFQTNLVPYPRIHFPL
EECCCCCCCCCCCCC
9.5422817901
271PhosphorylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0921945579
271O-linked_GlycosylationRIHFPLATYAPVISA
CCCCCCCCCCCCCCH
28.0931373491
272PhosphorylationIHFPLATYAPVISAE
CCCCCCCCCCCCCHH
11.8721945579
277PhosphorylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5221945579
277O-linked_GlycosylationATYAPVISAEKAYHE
CCCCCCCCHHHHHHH
30.5231373491
278UbiquitinationTYAPVISAEKAYHEQ
CCCCCCCHHHHHHHH
15.9321890473
280AcetylationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.7088221
280UbiquitinationAPVISAEKAYHEQLS
CCCCCHHHHHHHHCC
54.7021906983
282Nitrated tyrosineVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
282PhosphorylationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.5625159151
282NitrationVISAEKAYHEQLSVA
CCCHHHHHHHHCCHH
19.56-
285UbiquitinationAEKAYHEQLSVAEIT
HHHHHHHHCCHHHHH
26.2321890473
287PhosphorylationKAYHEQLSVAEITNA
HHHHHHCCHHHHHHH
20.9822322096
292PhosphorylationQLSVAEITNACFEPA
HCCHHHHHHHHCCCH
14.3130576142
295GlutathionylationVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.2722555962
295S-nitrosylationVAEITNACFEPANQM
HHHHHHHHCCCHHHC
4.2725040305
302SulfoxidationCFEPANQMVKCDPRH
HCCCHHHCCCCCCCC
2.8930846556
304UbiquitinationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8121963094
304NeddylationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8132015554
3042-HydroxyisobutyrylationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.81-
304AcetylationEPANQMVKCDPRHGK
CCHHHCCCCCCCCCC
27.8126051181
311AcetylationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.2323954790
311UbiquitinationKCDPRHGKYMACCLL
CCCCCCCCEEEEHHH
26.2321906983
312PhosphorylationCDPRHGKYMACCLLY
CCCCCCCEEEEHHHC
8.4428152594
314UbiquitinationPRHGKYMACCLLYRG
CCCCCEEEEHHHCCC
4.2721890473
315GlutathionylationRHGKYMACCLLYRGD
CCCCEEEEHHHCCCC
0.6722555962
316S-nitrosylationHGKYMACCLLYRGDV
CCCEEEEHHHCCCCC
1.8125040305
319PhosphorylationYMACCLLYRGDVVPK
EEEEHHHCCCCCCCC
10.2923917254
326AcetylationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.8021466224
326SumoylationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.80-
326UbiquitinationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.8027667366
326SumoylationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.80-
3262-HydroxyisobutyrylationYRGDVVPKDVNAAIA
CCCCCCCCCHHHHHH
63.80-
334PhosphorylationDVNAAIATIKTKRSI
CHHHHHHHCCCCCEE
19.5223401153
334O-linked_GlycosylationDVNAAIATIKTKRSI
CHHHHHHHCCCCCEE
19.5231373491
336AcetylationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.5726051181
336SumoylationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.57-
336UbiquitinationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.5721906983
336SumoylationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.57-
336NeddylationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.5732015554
3362-HydroxyisobutyrylationNAAIATIKTKRSIQF
HHHHHHCCCCCEEEE
43.57-
337PhosphorylationAAIATIKTKRSIQFV
HHHHHCCCCCEEEEE
28.0430266825
338MethylationAIATIKTKRSIQFVD
HHHHCCCCCEEEEEE
38.86184615
338UbiquitinationAIATIKTKRSIQFVD
HHHHCCCCCEEEEEE
38.8621987572
339MethylationIATIKTKRSIQFVDW
HHHCCCCCEEEEEEE
44.20-
340PhosphorylationATIKTKRSIQFVDWC
HHCCCCCEEEEEEEC
23.4626846344
340O-linked_GlycosylationATIKTKRSIQFVDWC
HHCCCCCEEEEEEEC
23.4631373491
347GlutathionylationSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5522555962
347S-nitrosylationSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5525040305
347S-palmitoylationSIQFVDWCPTGFKVG
EEEEEEECCCCEEEE
1.5529575903
349PhosphorylationQFVDWCPTGFKVGIN
EEEEECCCCEEEEEE
52.7130266825
352AcetylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.6826051181
352UbiquitinationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.6821906983
352SumoylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.68-
352NeddylationDWCPTGFKVGINYQP
EECCCCEEEEEECCC
40.6832015554
357PhosphorylationGFKVGINYQPPTVVP
CEEEEEECCCCEECC
22.0727273156
361PhosphorylationGINYQPPTVVPGGDL
EEECCCCEECCCCCH
40.6028152594
370AcetylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3123749302
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370UbiquitinationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3127667366
370SumoylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
370NeddylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.3132015554
3702-HydroxyisobutyrylationVPGGDLAKVQRAVCM
CCCCCHHHHHHHHHH
46.31-
376GlutathionylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9022555962
376S-nitrosylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9025040305
376S-palmitoylationAKVQRAVCMLSNTTA
HHHHHHHHHHCCHHH
1.9026865113
377SulfoxidationKVQRAVCMLSNTTAI
HHHHHHHHHCCHHHH
3.5530846556
379PhosphorylationQRAVCMLSNTTAIAE
HHHHHHHCCHHHHHH
12.7819664995
381O-linked_GlycosylationAVCMLSNTTAIAEAW
HHHHHCCHHHHHHHH
17.7731373491
381PhosphorylationAVCMLSNTTAIAEAW
HHHHHCCHHHHHHHH
17.7730108239
382O-linked_GlycosylationVCMLSNTTAIAEAWA
HHHHCCHHHHHHHHH
21.9531373491
382PhosphorylationVCMLSNTTAIAEAWA
HHHHCCHHHHHHHHH
21.9530108239
394MethylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394AcetylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9923954790
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
394UbiquitinationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.9932142685
394SumoylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
3942-HydroxyisobutyrylationAWARLDHKFDLMYAK
HHHHCCCCCCHHHEE
39.99-
399PhosphorylationDHKFDLMYAKRAFVH
CCCCCHHHEEEHHHH
19.1028674151
401AcetylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1127178108
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
401UbiquitinationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.1121963094
401SumoylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
4012-HydroxyisobutyrylationKFDLMYAKRAFVHWY
CCCHHHEEEHHHHHH
27.11-
408PhosphorylationKRAFVHWYVGEGMEE
EEHHHHHHCCCCCCC
5.4528796482
413SulfoxidationHWYVGEGMEEGEFSE
HHHCCCCCCCCCHHH
3.5430846556
419PhosphorylationGMEEGEFSEAREDMA
CCCCCCHHHHHHHHH
26.5028270605
419O-linked_GlycosylationGMEEGEFSEAREDMA
CCCCCCHHHHHHHHH
26.5031373491
425SulfoxidationFSEAREDMAALEKDY
HHHHHHHHHHHHHCH
1.6930846556
430UbiquitinationEDMAALEKDYEEVGV
HHHHHHHHCHHHHCC
67.4721906983
430AcetylationEDMAALEKDYEEVGV
HHHHHHHHCHHHHCC
67.4726051181
432PhosphorylationMAALEKDYEEVGVDS
HHHHHHCHHHHCCCC
25.6728796482
439PhosphorylationYEEVGVDSVEGEGEE
HHHHCCCCCCCCCCC
21.4720201521
4455-glutamyl polyglutamateDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
445Formation of an isopeptide bondDSVEGEGEEEGEEY-
CCCCCCCCCCCCCC-
48.88-
451PhosphorylationGEEEGEEY-------
CCCCCCCC-------
21.3928674151
451NitrationGEEEGEEY-------
CCCCCCCC-------
21.3910339593

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
253TPhosphorylationKinasePKCBP68403
PSP
334TPhosphorylationKinaseMAP3K7O43318
GPS
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:18195004

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 TBA1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD3Z_HUMANCD247physical
15084271
ZAP70_HUMANZAP70physical
15084271
TM1L1_HUMANTOM1L1physical
21900206
SYUA_HUMANSNCAphysical
11698390
SYUA_HUMANSNCAphysical
16216085
SC6A3_HUMANSLC6A3physical
16216085
TBB1_HUMANTUBB1physical
16216085
TBA1C_HUMANTUBA1Cphysical
22939629
TBB2A_HUMANTUBB2Aphysical
22939629
TCPZ_HUMANCCT6Aphysical
22939629
TBB4B_HUMANTUBB4Bphysical
22939629
TBB6_HUMANTUBB6physical
22939629
TBB3_HUMANTUBB3physical
22939629
TBB2B_HUMANTUBB2Bphysical
22939629
TBB5_HUMANTUBBphysical
22939629
U520_HUMANSNRNP200physical
22939629
U2AF1_HUMANU2AF1physical
22939629
VDAC1_HUMANVDAC1physical
12087096
HDAC6_HUMANHDAC6physical
23798680
ATRAP_HUMANAGTRAPphysical
25416956
MTCL1_HUMANMTCL1physical
23902687
RANB9_HUMANRANBP9physical
25659156
PIWL1_HUMANPIWIL1physical
26317901
TBB3_HUMANTUBB3physical
26317901
STMN1_HUMANSTMN1physical
26317901
T11L2_HUMANTCP11L2physical
28514442
TXND9_HUMANTXNDC9physical
28514442
DLGP5_HUMANDLGAP5physical
28514442
TBA1C_HUMANTUBA1Cphysical
28514442
TBA1A_HUMANTUBA1Aphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPH_HUMANCCT7physical
28514442
TCPD_HUMANCCT4physical
28514442
MICU1_HUMANMICU1physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPA_HUMANTCP1physical
28514442
TCPG_HUMANCCT3physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-340; TYR-432; SER-439AND TYR-451, AND MASS SPECTROMETRY.
"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-232 AND SER-340, ANDMASS SPECTROMETRY.
"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-334 ANDSER-439, AND MASS SPECTROMETRY.
"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.
Ubiquitylation
ReferencePubMed
"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-326 AND LYS-370, AND MASSSPECTROMETRY.

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