TRM82_YEAST - dbPTM
TRM82_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRM82_YEAST
UniProt AC Q03774
Protein Name tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82 {ECO:0000255|HAMAP-Rule:MF_03056}
Gene Name TRM82 {ECO:0000255|HAMAP-Rule:MF_03056}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 444
Subcellular Localization Nucleus .
Protein Description Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit..
Protein Sequence MSVIHPLQNLLTSRDGSLVFAIIKNCILSFKYQSPNHWEFAGKWSDDFDKIQESRNTTAKEQQGQSSENENENKKLKSNKGDSIKRTAAKVPSPGLGAPPIYSYIRNLRLTSDESRLIACADSDKSLLVFDVDKTSKNVLKLRKRFCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFTQEPILGHVSMLTDVHLIKDSDGHQFIITSDRDEHIKISHYPQCFIVDKWLFGHKHFVSSICCGKDYLLLSAGGDDKIFAWDWKTGKNLSTFDYNSLIKPYLNDQHLAPPRFQNENNDIIEFAVSKIIKSKNLPFVAFFVEATKCIIILEMSEKQKGDLALKQIITFPYNVISLSAHNDEFQVTLDNKESSGVQKNFAKFIEYNLNENSFVVNNEKSNEFDSAIIQSVQGDSNLVTKKEEIYPLYNVSSLRKHGEHYS
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
31UbiquitinationKNCILSFKYQSPNHW
HHHEEEEEECCCCCC
38.7223749301
50AcetylationKWSDDFDKIQESRNT
ECCCCHHHHHHHHHC
46.4024489116
66PhosphorylationAKEQQGQSSENENEN
HHHHHCCCCCCHHHH
46.5828889911
67PhosphorylationKEQQGQSSENENENK
HHHHCCCCCCHHHHH
36.2317563356
85AcetylationSNKGDSIKRTAAKVP
CCCCCHHHHHHCCCC
47.8825381059
87PhosphorylationKGDSIKRTAAKVPSP
CCCHHHHHHCCCCCC
26.4322369663
90AcetylationSIKRTAAKVPSPGLG
HHHHHHCCCCCCCCC
52.8224489116
93PhosphorylationRTAAKVPSPGLGAPP
HHHCCCCCCCCCCCC
34.2922369663
287PhosphorylationYNSLIKPYLNDQHLA
HHHCCHHHCCCCCCC
17.0922369663
385UbiquitinationGVQKNFAKFIEYNLN
CHHHHHHHHHHEECC
42.6123749301

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 TRM82_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRM82_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 TRM82_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXKA_YEASTHXK1physical
16554755
DUS1_YEASTDUS1genetic
16387656
DUS2_YEASTSMM1genetic
16387656
MOD5_YEASTMOD5genetic
18314501
PUS1_YEASTPUS1genetic
18314501
XPOT_YEASTLOS1genetic
18314501
TRM10_YEASTTRM10genetic
18314501
PT309_YEASTPET309genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
STP1_YEASTSTP1genetic
19061648
PUS7_YEASTPUS7genetic
19061648
PFD5_YEASTGIM5genetic
19061648
PUS1_YEASTPUS1genetic
19061648
LRP1_YEASTLRP1genetic
19061648
PFD5_YEASTGIM5genetic
19547744
IST2_YEASTIST2genetic
20093466
MAF1_YEASTMAF1genetic
20093466
UBP3_YEASTUBP3genetic
20093466
PUS3_YEASTDEG1genetic
20093466
FEN1_YEASTRAD27genetic
20093466
PNT1_YEASTPNT1genetic
20093466
PUS1_YEASTPUS1genetic
20093466
CUR1_YEASTCUR1genetic
20093466
DUS4_YEASTDUS4genetic
16387656
TRM10_YEASTTRM10genetic
16387656
NCL1_YEASTNCL1genetic
16387656
PUS7_YEASTPUS7genetic
16387656
DUS3_YEASTDUS3genetic
16387656
CSN12_YEASTYJR084Wgenetic
27708008
RTG3_YEASTRTG3genetic
27708008
MTU1_YEASTSLM3genetic
27708008
HTD2_YEASTHTD2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRM82_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-67 AND SER-93, AND MASSSPECTROMETRY.

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