TBA1_YEAST - dbPTM
TBA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBA1_YEAST
UniProt AC P09733
Protein Name Tubulin alpha-1 chain
Gene Name TUB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 447
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 MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRNGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVLDRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSAEYGKKSKLEFAVYPAPQVSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKSKAFHESNSVSEITNACFEPGNQMVKCDPRDGKYMATCLLYRGDVVTRDVQRAVEQVKNKKTVQLVDWCPTGFKIGICYEPPTATPNSQLATVDRAVCMLSNTTSIAEAWKRIDRKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALERDYIEVGADSYAEEEEF
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
44UbiquitinationEDGLSKPKGGEEGFS
CCCCCCCCCCCCCCH		81.1217644757
51PhosphorylationKGGEEGFSTFFHETG
CCCCCCCHHCCCCCC		34.8521440633
61AcetylationFHETGYGKFVPRAIY
CCCCCCCCEECEEEE		34.4024489116
61UbiquitinationFHETGYGKFVPRAIY
CCCCCCCCEECEEEE		34.4017644757
85AcetylationEVRNGPYKDLFHPEQ
CHHCCCCCCCCCHHH		51.6024489116
85UbiquitinationEVRNGPYKDLFHPEQ
CHHCCCCCCCCCHHH		51.6017644757
97AcetylationPEQLISGKEDAANNY
HHHHHCCCHHHHHHC		45.7024489116
97UbiquitinationPEQLISGKEDAANNY
HHHHHCCCHHHHHHC		45.7017644757
272PhosphorylationRIHFPLVSYSPVLSK
CCCCCCEECCCCCCH		27.8122369663
273PhosphorylationIHFPLVSYSPVLSKS
CCCCCEECCCCCCHH		14.9822369663
274PhosphorylationHFPLVSYSPVLSKSK
CCCCEECCCCCCHHH		10.8822369663
278PhosphorylationVSYSPVLSKSKAFHE
EECCCCCCHHHCCCC		34.8122369663
279UbiquitinationSYSPVLSKSKAFHES
ECCCCCCHHHCCCCC		52.3817644757
279AcetylationSYSPVLSKSKAFHES
ECCCCCCHHHCCCCC		52.3824489116
290PhosphorylationFHESNSVSEITNACF
CCCCCCHHHHHHHHC		24.0919779198
305UbiquitinationEPGNQMVKCDPRDGK
CCCCCEEEECCCCCC		27.8123749301
312AcetylationKCDPRDGKYMATCLL
EECCCCCCEEEEEEE		35.8224489116
340UbiquitinationVEQVKNKKTVQLVDW
HHHHCCCCCEEEEEE		64.4217644757
353UbiquitinationDWCPTGFKIGICYEP
EECCCCCEEEEEECC		41.1717644757
377S-palmitoylationATVDRAVCMLSNTTS
CHHCHHHHHHCCCHH		1.9011553707
390UbiquitinationTSIAEAWKRIDRKFD
HHHHHHHHHHHHHHH		46.6617644757
440PhosphorylationYIEVGADSYAEEEEF
CEECCCCCCCCCCCC		26.2128889911
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 TBA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBA1_YEAST !!
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 TBA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAC2_YEASTPAC2physical
9885248
TBB_YEASTTUB2physical
9398684
PAC2_YEASTPAC2genetic
9725898
TBCA_YEASTRBL2genetic
10978276
BUB1_YEASTBUB1genetic
12136005
BUB1_YEASTBUB1genetic
7622604
BUB3_YEASTBUB3genetic
12136005
BUB3_YEASTBUB3genetic
7622604
MPS1_YEASTMPS1genetic
12136005
TBCA_YEASTRBL2genetic
9725898
TBA3_YEASTTUB3genetic
7622604
TBA3_YEASTTUB3genetic
10793159
TBCB_YEASTALF1genetic
9885248
TBA3_YEASTTUB3genetic
3294100
RCC1_YEASTSRM1genetic
8070652
TBB_YEASTTUB2genetic
3066684
PAC2_YEASTPAC2genetic
9215891
CIN4_YEASTCIN4genetic
9215891
CIN1_YEASTCIN1genetic
9215891
TBCC_YEASTCIN2genetic
9215891
ARP9_YEASTARP9genetic
15525520
TBCA_YEASTRBL2genetic
15525520
RSC1_YEASTRSC1genetic
15525520
RSC4_YEASTRSC4genetic
15525520
RSC6_YEASTRSC6genetic
15525520
RSC8_YEASTRSC8genetic
15525520
RSC9_YEASTRSC9genetic
15525520
STH1_YEASTSTH1genetic
15525520
TBA3_YEASTTUB3genetic
15525520
MHP1_YEASTMHP1genetic
9855114
ATS1_YEASTATS1genetic
8070652
TBB_YEASTTUB2physical
17634282
STU2_YEASTSTU2physical
17634282
LIS1_YEASTPAC1physical
17634282
BIM1_YEASTBIM1genetic
18411245
MDY2_YEASTMDY2physical
20722039
MCM22_YEASTMCM22genetic
20608984
SUM1_YEASTSUM1genetic
20608984
SUM1_YEASTSUM1genetic
22285862
TBB_YEASTTUB2physical
9725898
TBG_YEASTTUB4physical
22472440
SPC97_YEASTSPC97physical
22472440
SPC98_YEASTSPC98physical
22472440
SPC72_YEASTSPC72physical
22472440
SP110_YEASTSPC110physical
22472440
STU2_YEASTSTU2physical
22904013
MCM16_YEASTMCM16genetic
23480593
MCM22_YEASTMCM22genetic
23480593
CHL4_YEASTCHL4genetic
23480593
IML3_YEASTIML3genetic
23480593
MCM21_YEASTMCM21genetic
23480593
CTF19_YEASTCTF19genetic
23480593
LPX1_YEASTLPX1physical
23518202
TBB_YEASTTUB2physical
24099757
PAC2_YEASTPAC2physical
20204449
TBB_YEASTTUB2physical
21888381
KIP3_YEASTKIP3physical
22431622
ERF3_YEASTSUP35physical
24981173
PUB1_YEASTPUB1physical
24981173
IF4E_YEASTCDC33physical
24981173
RL28_YEASTRPL28physical
24981173
CND2_YEASTBRN1physical
25135640
SMC2_YEASTSMC2physical
25135640
SMC4_YEASTSMC4physical
25135640
CND3_YEASTYCG1physical
25135640
CND1_YEASTYCS4physical
25135640
SMC5_YEASTSMC5physical
25135640
TBB_YEASTTUB2physical
25097237
STU2_YEASTSTU2physical
25097237
RHO1_YEASTRHO1genetic
27466378
TBB_YEASTTUB2physical
28652389
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBA1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASSSPECTROMETRY.

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