TRM2_YEAST - dbPTM
TRM2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM2_YEAST
UniProt AC P33753
Protein Name tRNA (uracil(54)-C(5))-methyltransferase
Gene Name TRM2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 639
Subcellular Localization
Protein Description Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation..
Protein Sequence MYEQFEFSFFFFENSDNKVKYKAHLISSIKRWSIITCMRCFWTVQKSIFKARFFACRNFVKKHNYKLISTMTGSTEMVPPTMKHTVDNKRLSSPLTDSGNRRTKKPKLRKYKAKKVETTSPMGVLEFEVNDLLKSQNLSREQVLNDVTSILNDKSSTDGPIVLQYHREVKNVKVLEITSNGNGLALIDNPVETEKKQVVIIPFGLPGDVVNIKVFKTHPYYVESDLLDVVEKSPMRRDDLIRDKYFGKSSGSQLEFLTYDDQLELKRKTIMNAYKFFAPRLVAEKLLPPFDTTVASPLQFGYRTKITPHFDMPKRKQKELSVRPPLGFGQKGRPQWRKDTLDIGGHGSILDIDECVLATEVLNKGLTNERRKFEQEFKNYKKGATILLRENTTILDPSKPTLEQLTEEASRDENGDISYVEVEDKKNNVRLAKTCVTNPRQIVTEYVDGYTFNFSAGEFFQNNNSILPIVTKYVRDNLQAPAKGDDNKTKFLVDAYCGSGLFSICSSKGVDKVIGVEISADSVSFAEKNAKANGVENCRFIVGKAEKLFESIDTPSENTSVILDPPRKGCDELFLKQLAAYNPAKIIYISCNVHSQARDVEYFLKETENGSAHQIESIRGFDFFPQTHHVESVCIMKRI
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
69PhosphorylationKHNYKLISTMTGSTE
HCCCEEEEECCCCCC		23.6730377154
72PhosphorylationYKLISTMTGSTEMVP
CEEEEECCCCCCCCC		28.2430377154
74PhosphorylationLISTMTGSTEMVPPT
EEEECCCCCCCCCCC		16.4230377154
75PhosphorylationISTMTGSTEMVPPTM
EEECCCCCCCCCCCC		29.4630377154
81PhosphorylationSTEMVPPTMKHTVDN
CCCCCCCCCCCCCCC		32.5527017623
89AcetylationMKHTVDNKRLSSPLT
CCCCCCCCCCCCCCC		50.6925381059
92PhosphorylationTVDNKRLSSPLTDSG
CCCCCCCCCCCCCCC		33.6622369663
93PhosphorylationVDNKRLSSPLTDSGN
CCCCCCCCCCCCCCC		28.6422369663
96PhosphorylationKRLSSPLTDSGNRRT
CCCCCCCCCCCCCCC		31.3522369663
98PhosphorylationLSSPLTDSGNRRTKK
CCCCCCCCCCCCCCC		32.5020377248
103PhosphorylationTDSGNRRTKKPKLRK
CCCCCCCCCCCCHHH		39.9319823750
418PhosphorylationRDENGDISYVEVEDK
CCCCCCCCEEEEECC		28.0627017623
419PhosphorylationDENGDISYVEVEDKK
CCCCCCCEEEEECCC		10.8527017623
434PhosphorylationNNVRLAKTCVTNPRQ
CCEEEEEECCCCHHH		13.4528889911
531UbiquitinationSFAEKNAKANGVENC
CHHHHHHHHCCCCCC		52.3423749301
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 TRM2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM2_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 TRM2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXO1_YEASTEXO1genetic
17534700
KU80_YEASTYKU80genetic
17534700
RAD52_YEASTRAD52genetic
9871117
UBI4P_YEASTUBI4genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
SRP40_YEASTSRP40genetic
19061648
RRP6_YEASTRRP6genetic
19061648
PFD5_YEASTGIM5genetic
19061648
TMA23_YEASTTMA23genetic
19061648
CAK1_YEASTCAK1genetic
19061648
PRP11_YEASTPRP11genetic
19061648
ARC1_YEASTARC1genetic
19061648
SAP30_YEASTSAP30genetic
19061648
SSB1_YEASTSSB1physical
19536198
CSG2_YEASTCSG2genetic
20093466
TAN1_YEASTTAN1genetic
20093466
CGR1_YEASTCGR1genetic
20093466
ATE1_YEASTATE1genetic
20093466
ENO1_YEASTENO1genetic
20093466
KAPA_YEASTTPK1genetic
20093466
YL352_YEASTYLR352Wgenetic
20093466
BUD8_YEASTBUD8genetic
20093466
VAC14_YEASTVAC14genetic
20093466
RS7B_YEASTRPS7Bgenetic
20093466
KTR1_YEASTKTR1genetic
20093466
JID1_YEASTJID1genetic
20093466
EXO1_YEASTEXO1genetic
17205207
CND2_YEASTBRN1genetic
27708008
RPN12_YEASTRPN12genetic
27708008
SWC4_YEASTSWC4genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
RPN6_YEASTRPN6genetic
27708008
NOP14_YEASTNOP14genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CAB5_YEASTCAB5genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
ACT_YEASTACT1genetic
27708008
SAD1_YEASTSAD1genetic
27708008
STT3_YEASTSTT3genetic
27708008
GPI10_YEASTGPI10genetic
27708008
SDO1_YEASTSDO1genetic
27708008
MCM5_YEASTMCM5genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
LCB1_YEASTLCB1genetic
27708008
DBP6_YEASTDBP6genetic
27708008
NUF2_YEASTNUF2genetic
27708008
TYSY_YEASTCDC21genetic
27708008
DYR_YEASTDFR1genetic
27708008
SEC63_YEASTSEC63genetic
27708008
PSA7_YEASTPRE10genetic
27708008
GPI2_YEASTGPI2genetic
27708008
DIM1_YEASTDIM1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
UBX3_YEASTUBX3genetic
27708008
MAF1_YEASTMAF1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
SND1_YEASTYDR186Cgenetic
27708008
HIM1_YEASTHIM1genetic
27708008
MCM21_YEASTMCM21genetic
27708008
TAN1_YEASTTAN1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
UBR1_YEASTUBR1genetic
27708008
SLH1_YEASTSLH1genetic
27708008
ICE2_YEASTICE2genetic
27708008
ASF1_YEASTASF1genetic
27708008
BUD8_YEASTBUD8genetic
27708008
VAC14_YEASTVAC14genetic
27708008
RS7B_YEASTRPS7Bgenetic
27708008
ATP23_YEASTATP23genetic
27708008
MED1_YEASTMED1genetic
27708008
ARX1_YEASTARX1genetic
29674565
SWC5_YEASTSWC5genetic
29674565
DBF2_YEASTDBF2genetic
29674565
TAF11_YEASTTAF11genetic
29674565
TRS23_YEASTTRS23genetic
29674565
PRP21_YEASTPRP21genetic
29674565
GGPPS_YEASTBTS1genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRM2_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, AND MASSSPECTROMETRY.
"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-93 AND THR-96, AND MASSSPECTROMETRY.
"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-93, AND MASSSPECTROMETRY.
"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-92 AND SER-93, AND MASSSPECTROMETRY.

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