PUS9_YEAST - dbPTM
PUS9_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUS9_YEAST
UniProt AC Q12069
Protein Name tRNA pseudouridine(32) synthase, mitochondrial
Gene Name PUS9
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 462
Subcellular Localization Mitochondrion .
Protein Description Responsible for synthesis of pseudouridine from uracil-32 in mitochondrial transfer RNAs..
Protein Sequence MQRNNRLRNLFTVPVIMARQLKRNALSAGLAFAGNATSNEFDEHLQNEVEREREIQKKKKIKRTQSKKSPDLINKSTFQSRTIGSKKEKHRQLDPEYEIVIDGPLRKIKPYHFTYRTFCKERWRDKKLVDVFISEFRDRESEYYKRTIENGDVHINDETADLSTVIRNGDLITHQVHRHEPPVTSRPIKVIFEDDNIMVIDKPSGIPVHPTGRYRFNTITKMLQNNLGFVVNPCNRLDRLTSGLMFLAKTPKGADNIGDQLKAREVTKEYVAKVVGEFPETEVIVEKPLKLIEPRLALNAVCQMDEKGAKHAKTVFNRISYDGKTSIVKCKPLTGRSHQIRVHLQYLGHPIANDPIYSNDEVWGNNLGKGGQADFDIVITKLDEIGKRKPAKSWFHSNGGYGEVLRQEKCSICESDLYTDPGPNDLDLWLHAYLYESTETEEGTEKKKWCYKTEYPEWALRR
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
68AcetylationIKRTQSKKSPDLINK
HCCCCCCCCCCCCCH
72.9025381059
69PhosphorylationKRTQSKKSPDLINKS
CCCCCCCCCCCCCHH
27.6417563356

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 PUS9_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUS9_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 PUS9_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS4_YEASTRPT2physical
16554755
RPN10_YEASTRPN10physical
16554755
MGR1_YEASTMGR1genetic
20093466
RIM1_YEASTRIM1genetic
20093466
ATG15_YEASTATG15genetic
20093466
TMS1_YEASTTMS1genetic
20093466
YD124_YEASTYDR124Wgenetic
20093466
EMI1_YEASTEMI1genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
ASK10_YEASTASK10genetic
20093466
NPR3_YEASTNPR3genetic
20093466
OPI1_YEASTOPI1genetic
20093466
PTK2_YEASTPTK2genetic
20093466
RL22A_YEASTRPL22Agenetic
20093466
LIPB_YEASTLIP2genetic
20093466
ATP10_YEASTATP10genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
ATP23_YEASTATP23genetic
20093466
NIP80_YEASTNIP100genetic
20093466

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUS9_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-69, 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-69, AND MASSSPECTROMETRY.

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