TBAL3_HUMAN - dbPTM
TBAL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBAL3_HUMAN
UniProt AC A6NHL2
Protein Name Tubulin alpha chain-like 3
Gene Name TUBAL3
Organism Homo sapiens (Human).
Sequence Length 446
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 (By similarity)..
Protein Sequence MRECLSIHIGQAGIQIGDACWELYCLEHGIQPNGVVLDTQQDQLENAKMEHTNASFDTFFCETRAGKHVPRALFVDLEPTVIDGIRTGQHRSLFHPEQLLSGKEDAANNYARGRYSVGSEVIDLVLERTRKLAEQCGGLQGFLIFRSFGGGTGSGFTSLLMERLTGEYSRKTKLEFSVYPAPRISTAVVEPYNSVLTTHSTTEHTDCTFMVDNEAVYDICHRKLGVECPSHASINRLVVQVVSSITASLRFEGPLNVDLIEFQTNLVPYPRIHFPMTAFAPIVSADKAYHEQFSVSDITTACFESSNQLVKCDPRLGKYMACCLLYRGDVVPKEVNAAIAATKSRHSVQFVDWCPTGFKVGINNRPPTVMPGGDLAKVHRSICMLSNTTAIVEAWARLDHKFDLMYAKRAFLHWYLREGMEEAEFLEAREDLAALERDYEEVAQSF
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
92PhosphorylationIRTGQHRSLFHPEQL
CCCCCCHHCCCHHHH		33.0120068231
101PhosphorylationFHPEQLLSGKEDAAN
CCHHHHHCCCHHHHH		57.3120068231
103MethylationPEQLLSGKEDAANNY
HHHHHCCCHHHHHHH		49.39-
103SumoylationPEQLLSGKEDAANNY
HHHHHCCCHHHHHHH		49.39-
110PhosphorylationKEDAANNYARGRYSV
CHHHHHHHHCCCCCC		9.4828152594
115PhosphorylationNNYARGRYSVGSEVI
HHHHCCCCCCHHHHH		15.55-
161SulfoxidationSGFTSLLMERLTGEY
CHHHHHHHHHHHCCC		3.2321406390
172PhosphorylationTGEYSRKTKLEFSVY
HCCCCCCCEEEEEEE		39.49-
192PhosphorylationSTAVVEPYNSVLTTH
EEEEEECCCCEEECC		13.4322468782
197PhosphorylationEPYNSVLTTHSTTEH
ECCCCEEECCCCCCC		21.9522468782
208PhosphorylationTTEHTDCTFMVDNEA
CCCCCCCEEEECCHH		19.9922468782
243PhosphorylationRLVVQVVSSITASLR
HHHHHHHHHHHHEEC		19.7121406692
244PhosphorylationLVVQVVSSITASLRF
HHHHHHHHHHHEECC		16.6121406692
246PhosphorylationVQVVSSITASLRFEG
HHHHHHHHHEECCCC		16.4921406692
248PhosphorylationVVSSITASLRFEGPL
HHHHHHHEECCCCCC		16.0721406692
269PhosphorylationFQTNLVPYPRIHFPM
EECCCCCCCCCCCCC		9.5422817900
278UbiquitinationRIHFPMTAFAPIVSA
CCCCCCCEECCCCCC		7.7323503661
278 (in isoform 2)Ubiquitination-7.73-
316PhosphorylationLVKCDPRLGKYMACC
EEECCHHHHHHCHHH		9.3832142685
318AcetylationKCDPRLGKYMACCLL
ECCHHHHHHCHHHHH		36.1226051181
318UbiquitinationKCDPRLGKYMACCLL
ECCHHHHHHCHHHHH		36.1223503661
319PhosphorylationCDPRLGKYMACCLLY
CCHHHHHHCHHHHHC		6.5328152594
320SulfoxidationDPRLGKYMACCLLYR
CHHHHHHCHHHHHCC		2.3430846556
326PhosphorylationYMACCLLYRGDVVPK
HCHHHHHCCCCCCCH		10.2922817900
342PhosphorylationVNAAIAATKSRHSVQ
HHHHHHHCCCCCEEE		22.1117924679
356PhosphorylationQFVDWCPTGFKVGIN
EEEEECCCCCEEECC		52.7132142685
361 (in isoform 2)Ubiquitination-19.9321890473
361UbiquitinationCPTGFKVGINNRPPT
CCCCCEEECCCCCCC		19.9332142685
368 (in isoform 2)Ubiquitination-31.9221890473
368UbiquitinationGINNRPPTVMPGGDL
ECCCCCCCCCCCCHH		31.9221963094
401SumoylationAWARLDHKFDLMYAK
HHHHCCCHHHHHHHH		39.99-
401UbiquitinationAWARLDHKFDLMYAK
HHHHCCCHHHHHHHH		39.9932142685
401 (in isoform 1)Ubiquitination-39.9921890473
401SumoylationAWARLDHKFDLMYAK
HHHHCCCHHHHHHHH		39.99-
401AcetylationAWARLDHKFDLMYAK
HHHHCCCHHHHHHHH		39.99155461
405SulfoxidationLDHKFDLMYAKRAFL
CCCHHHHHHHHHHHH		3.0921406390
406PhosphorylationDHKFDLMYAKRAFLH
CCHHHHHHHHHHHHH		19.1028674151
408SumoylationKFDLMYAKRAFLHWY
HHHHHHHHHHHHHHH		27.11-
408UbiquitinationKFDLMYAKRAFLHWY
HHHHHHHHHHHHHHH		27.1121906983
408SumoylationKFDLMYAKRAFLHWY
HHHHHHHHHHHHHHH		27.11-
408AcetylationKFDLMYAKRAFLHWY
HHHHHHHHHHHHHHH		27.1119608861
408 (in isoform 1)Ubiquitination-27.1121890473
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 TBAL3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBAL3_HUMAN !!
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 TBAL3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPH_HUMANCCT7physical
26186194
TCPG_HUMANCCT3physical
26186194
TCPW_HUMANCCT6Bphysical
26186194
TCPZ_HUMANCCT6Aphysical
26186194
TCPA_HUMANTCP1physical
26186194
TCPB_HUMANCCT2physical
26186194
RIC8B_HUMANRIC8Bphysical
26186194
TCPB_HUMANCCT2physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPH_HUMANCCT7physical
28514442
TCPZ_HUMANCCT6Aphysical
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 TBAL3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-401 AND LYS-408, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-342, AND MASSSPECTROMETRY.

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