ARG56_YEAST - dbPTM
ARG56_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARG56_YEAST
UniProt AC Q01217
Protein Name Protein ARG5,6, mitochondrial
Gene Name ARG5,6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 863
Subcellular Localization Mitochondrion.
Protein Description
Protein Sequence MPSASLLVSTKRLNASKFQKFVSSLNKSTIAGFASVPLRAPPSVAFTRKKVGYSKRYVSSTNGFSATRSTVIQLLNNISTKREVEQYLKYFTSVSQQQFAVIKVGGAIISDNLHELASCLAFLYHVGLYPIVLHGTGPQVNGRLEAQGIEPDYIDGIRITDEHTMAVVRKCFLEQNLKLVTALEQLGVRARPITSGVFTADYLDKDKYKLVGNIKSVTKEPIEASIKAGALPILTSLAETASGQMLNVNADVAAGELARVFEPLKIVYLNEKGGIINGSTGEKISMINLDEEYDDLMKQSWVKYGTKLKIREIKELLDYLPRSSSVAIINVQDLQKELFTDSGAGTMIRRGYKLVKRSSIGEFPSADALRKALQRDAGISSGKESVASYLRYLENSDFVSYADEPLEAVAIVKKDTNVPTLDKFVCSDAAWLNNVTDNVFNVLRRDFPALQWVVSENDANIAWHFDKSQGSYLKGGKVLFWYGIDDINTISELVENFVKSCDTASTLNSSASSGVFANKKSARSYSTRSTPRPEGVNTNPGRVALIGARGYTGKNLVSLINGHPYLEVAHVSSRELKGQKLQDYTKSEIIYESLQIQDIRKLEEQNAVDFWVMALPNKVCEPFVETIQSVHGKSKIIDLSADHRFVSESDWAYGLPELNDRAKIANAAKIANPGCYATGSQLTISPLTKYINGLPTVFGVSGYSGAGTKPSPKNDPKFLNNNLIPYALSDHIHEREISARIGHNVAFMPHVGQWFQGISLTVSIPIKKGSLSIDEIRKLYRNFYEDEKLVHVIDDIPLVKDIEGTHGVVIGGFKLNDAEDRVVVCATIDNLLKGAATQCLQNINLAMGYGEYAGIPENKIIGV
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
3Phosphorylation-----MPSASLLVST
-----CCCHHHEEEC
29.2319823750
5Phosphorylation---MPSASLLVSTKR
---CCCHHHEEECCC
26.9419823750
9PhosphorylationPSASLLVSTKRLNAS
CCHHHEEECCCCCHH
28.3419823750
10PhosphorylationSASLLVSTKRLNASK
CHHHEEECCCCCHHH
16.8319823750
16PhosphorylationSTKRLNASKFQKFVS
ECCCCCHHHHHHHHH
32.6919823750
23PhosphorylationSKFQKFVSSLNKSTI
HHHHHHHHHCCCCCC
32.0426447709
24PhosphorylationKFQKFVSSLNKSTIA
HHHHHHHHCCCCCCC
30.5726447709
28PhosphorylationFVSSLNKSTIAGFAS
HHHHCCCCCCCEEEC
24.7926447709
29PhosphorylationVSSLNKSTIAGFASV
HHHCCCCCCCEEECC
19.2226447709
35PhosphorylationSTIAGFASVPLRAPP
CCCCEEECCCCCCCC
23.2326447709
205AcetylationFTADYLDKDKYKLVG
EEHHHCCCCCCEEEE
54.2324489116
265AcetylationARVFEPLKIVYLNEK
HHHCCCEEEEEECCC
40.6224489116
272SuccinylationKIVYLNEKGGIINGS
EEEEECCCCCEECCC
62.4523954790
272AcetylationKIVYLNEKGGIINGS
EEEEECCCCCEECCC
62.4524489116
303AcetylationLMKQSWVKYGTKLKI
HHHHHHHHHCCHHCH
31.5322865919
314AcetylationKLKIREIKELLDYLP
HHCHHHHHHHHHHCC
37.2424489116
358PhosphorylationGYKLVKRSSIGEFPS
CEEEEEHHCCCCCCC
22.1629136822
359PhosphorylationYKLVKRSSIGEFPSA
EEEEEHHCCCCCCCH
38.3517330950
365PhosphorylationSSIGEFPSADALRKA
HCCCCCCCHHHHHHH
44.0719823750
554AcetylationGARGYTGKNLVSLIN
ECCCCCCCCHHHHHC
39.0324489116
709AcetylationGYSGAGTKPSPKNDP
CCCCCCCCCCCCCCH
42.4524489116
711PhosphorylationSGAGTKPSPKNDPKF
CCCCCCCCCCCCHHH
50.4927017623
717AcetylationPSPKNDPKFLNNNLI
CCCCCCHHHHCCCCH
66.4024489116
814AcetylationGVVIGGFKLNDAEDR
EEEECEEECCCCCCC
50.0524489116

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 ARG56_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARG56_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 ARG56_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSM12_YEASTLSM12physical
16554755
CAN1_YEASTCAN1genetic
16941010
GAP1_YEASTGAP1genetic
16941010
GAP1_YEASTGAP1genetic
21526172

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARG56_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-358 AND SER-359, ANDMASS 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-359, 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-359, AND MASSSPECTROMETRY.

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