AB140_YEAST - dbPTM
AB140_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB140_YEAST
UniProt AC Q08641
Protein Name tRNA(Thr) (cytosine(32)-N(3))-methyltransferase
Gene Name ABP140
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 628
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasmic and cortical cytoskeleton.
Protein Description S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser). Binds F-actin and shows weak F-actin cross-linking activity..
Protein Sequence MGVADLIKKFESISKEEGDATVDTNSSSKPLKSNDETKELHQQESTAVPQEVDVNEEFENEPETINSSRTAEKPLETNLPKPETNEEDEEEGSMSENKIYSKGENADINVNDFQEYKEMENTGAEVLASSVEESDAIQEGVAEETEGIATPKQKENEKNDESEEESANNASEPAEEYSQSEEDADIEQSNGKETENAENASQQANDGSTSTTTSKNKKKKNKKKNKKKRNGNVNTNANVDDSTKTGENDDTTGDTTSSTTSAIQEVNDLEVVDDSCLGIDQQHNREHLKALTQDVKEETLENIAHEGRGDNTGDQNAVEKSDFEKSDTEGSRIGRDLPFEFGKRNLTEESDVWDHNAWDNVEWGEEQVQQAEEKIKEQFKHPVPEFDKKLYNENPARYWDIFYKNNKENFFKDRKWLQIEFPILYASTRKDAEPVTIFEIGCGAGNTFFPILKDNENENLRIIAADFAPRAVELVKNSEQFNPKYGHATVWDLANPDGNLPDGVEPHSVDIAVMIFVFSALAPNQWDQAMDNLHKILKPGGKIIFRDYGAYDLTQVRFKKNRILEENFYVRGDGTRVYFFSEEKLREIFTKKYFLENKIGTDRRLLVNRKRQLKMYRCWVQAVFDVPQ
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
8AcetylationMGVADLIKKFESISK
CCHHHHHHHHHHCCH		59.7225381059
9AcetylationGVADLIKKFESISKE
CHHHHHHHHHHCCHH		47.5825381059
12PhosphorylationDLIKKFESISKEEGD
HHHHHHHHCCHHHCC		34.9824961812
14PhosphorylationIKKFESISKEEGDAT
HHHHHHCCHHHCCCE		43.2124961812
15AcetylationKKFESISKEEGDATV
HHHHHCCHHHCCCEE		59.1024489116
21PhosphorylationSKEEGDATVDTNSSS
CHHHCCCEECCCCCC		24.5322369663
24PhosphorylationEGDATVDTNSSSKPL
HCCCEECCCCCCCCC		32.4422369663
26PhosphorylationDATVDTNSSSKPLKS
CCEECCCCCCCCCCC		37.7722369663
27PhosphorylationATVDTNSSSKPLKSN
CEECCCCCCCCCCCC		44.4422369663
28PhosphorylationTVDTNSSSKPLKSND
EECCCCCCCCCCCCH		37.8122369663
37PhosphorylationPLKSNDETKELHQQE
CCCCCHHHHHHHHHH		32.4627017623
38AcetylationLKSNDETKELHQQES
CCCCHHHHHHHHHHH		57.1224489116
64PhosphorylationEFENEPETINSSRTA
HHCCCCCCCCCCCCC		35.8522369663
67PhosphorylationNEPETINSSRTAEKP
CCCCCCCCCCCCCCC		19.8322369663
68PhosphorylationEPETINSSRTAEKPL
CCCCCCCCCCCCCCC		29.2128132839
70PhosphorylationETINSSRTAEKPLET
CCCCCCCCCCCCCCC		40.9122369663
73AcetylationNSSRTAEKPLETNLP
CCCCCCCCCCCCCCC		53.0624489116
77PhosphorylationTAEKPLETNLPKPET
CCCCCCCCCCCCCCC		50.1422369663
84PhosphorylationTNLPKPETNEEDEEE
CCCCCCCCCHHHCCC		57.3622369663
93PhosphorylationEEDEEEGSMSENKIY
HHHCCCCCCCCCCCC		23.5522369663
95PhosphorylationDEEEGSMSENKIYSK
HCCCCCCCCCCCCCC		39.4522369663
100PhosphorylationSMSENKIYSKGENAD
CCCCCCCCCCCCCCC		13.1229136822
102UbiquitinationSENKIYSKGENADIN
CCCCCCCCCCCCCCC		53.9623749301
122PhosphorylationEYKEMENTGAEVLAS
HHHHHHHCCHHHHHH		25.1821551504
129PhosphorylationTGAEVLASSVEESDA
CCHHHHHHHHCHHHH		30.6521551504
150PhosphorylationEETEGIATPKQKENE
HHCCCCCCCCHHCCC		29.1527214570
162PhosphorylationENEKNDESEEESANN
CCCCCCCCHHHHHHC		53.8520377248
166PhosphorylationNDESEEESANNASEP
CCCCHHHHHHCCCCC		39.3119795423
171PhosphorylationEESANNASEPAEEYS
HHHHHCCCCCHHHHH		46.3519795423
177PhosphorylationASEPAEEYSQSEEDA
CCCCHHHHHCCHHHH		11.9619795423
178PhosphorylationSEPAEEYSQSEEDAD
CCCHHHHHCCHHHHH		30.4320377248
180PhosphorylationPAEEYSQSEEDADIE
CHHHHHCCHHHHHHH		36.6920377248
189PhosphorylationEDADIEQSNGKETEN
HHHHHHHHCCCCCCC		34.4619795423
194PhosphorylationEQSNGKETENAENAS
HHHCCCCCCCHHHHH		37.7222369663
201PhosphorylationTENAENASQQANDGS
CCCHHHHHHHCCCCC		34.1122369663
208PhosphorylationSQQANDGSTSTTTSK
HHHCCCCCCCCCCCC		23.2722369663
209PhosphorylationQQANDGSTSTTTSKN
HHCCCCCCCCCCCCH		35.3122369663
210PhosphorylationQANDGSTSTTTSKNK
HCCCCCCCCCCCCHH		26.0022369663
211PhosphorylationANDGSTSTTTSKNKK
CCCCCCCCCCCCHHH		33.8922369663
212PhosphorylationNDGSTSTTTSKNKKK
CCCCCCCCCCCHHHH		28.9222369663
213PhosphorylationDGSTSTTTSKNKKKK
CCCCCCCCCCHHHHC		37.4822369663
214PhosphorylationGSTSTTTSKNKKKKN
CCCCCCCCCHHHHCC		31.9422369663
245PhosphorylationNVDDSTKTGENDDTT
CCCCCCCCCCCCCCC		50.2219779198
251PhosphorylationKTGENDDTTGDTTSS
CCCCCCCCCCCCCCC		35.2319779198
256PhosphorylationDDTTGDTTSSTTSAI
CCCCCCCCCCCCHHH		25.9719779198
261PhosphorylationDTTSSTTSAIQEVND
CCCCCCCHHHHHCCC		24.3819779198
296AcetylationKALTQDVKEETLENI
HHHHHHHHHHHHHHH		59.1124489116
312PhosphorylationHEGRGDNTGDQNAVE
HCCCCCCCCCCCCCC		47.0419684113
320AcetylationGDQNAVEKSDFEKSD
CCCCCCCHHHHCCCC		49.0424489116
321PhosphorylationDQNAVEKSDFEKSDT
CCCCCCHHHHCCCCC		33.7417330950
325UbiquitinationVEKSDFEKSDTEGSR
CCHHHHCCCCCCCCC		54.3324961812
326PhosphorylationEKSDFEKSDTEGSRI
CHHHHCCCCCCCCCC		42.4325521595
328PhosphorylationSDFEKSDTEGSRIGR
HHHCCCCCCCCCCCC		49.7019823750
331PhosphorylationEKSDTEGSRIGRDLP
CCCCCCCCCCCCCCC		17.9422890988
343AcetylationDLPFEFGKRNLTEES
CCCCCCCCCCCCCCC		43.3524489116
343UbiquitinationDLPFEFGKRNLTEES
CCCCCCCCCCCCCCC		43.3524961812
347PhosphorylationEFGKRNLTEESDVWD
CCCCCCCCCCCCCCC		41.0528889911
350PhosphorylationKRNLTEESDVWDHNA
CCCCCCCCCCCCCCC		31.0920377248
404AcetylationRYWDIFYKNNKENFF
HHHHHEEECCCHHCC		43.2124489116
476AcetylationPRAVELVKNSEQFNP
HHHHHHHHCHHHCCC		68.3424489116
476UbiquitinationPRAVELVKNSEQFNP
HHHHHHHHCHHHCCC		68.3423749301
584AcetylationVYFFSEEKLREIFTK
EEEECHHHHHHHHHH		49.1124489116
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 AB140_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AB140_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 AB140_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AB140_YEASTABP140physical
21518805
TRM1_YEASTTRM1genetic
21518804
ACT_YEASTACT1physical
21792172
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AB140_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; THR-150; SER-321 ANDSER-326, AND MASS SPECTROMETRY.
"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-321 AND SER-326, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; THR-328 ANDSER-331, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-321 AND SER-326,AND MASS SPECTROMETRY.

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