ARGJ_YEAST - dbPTM
ARGJ_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARGJ_YEAST
UniProt AC Q04728
Protein Name Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03124}
Gene Name ARG7 {ECO:0000255|HAMAP-Rule:MF_03124}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 441
Subcellular Localization Mitochondrion matrix .
Protein Description Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate..
Protein Sequence MRISSTLLQRSKQLIDKYALYVPKTGSFPKGFEVGYTASGVKKNGSLDLGVILNTNKSRPSTAAAVFTTNKFKAAPVLTSKKVLETARGKNINAIVVNSGCANSVTGDLGMKDAQVMIDLVNDKIGQKNSTLVMSTGVIGQRLQMDKISTGINKIFGEEKFGSDFNSWLNVAKSICTTDTFPKLVTSRFKLPSGTEYTLTGMAKGAGMICPNMATLLGFIVTDLPIESKALQKMLTFATTRSFNCISVDGDMSTNDTICMLANGAIDTKEINEDSKDFEQVKLQVTEFAQRLAQLVVRDGEGSTKFVTVNVKNALHFEDAKIIAESISNSMLVKTALYGQDANWGRILCAIGYAKLNDLKSLDVNKINVSFIATDNSEPRELKLVANGVPQLEIDETRASEILALNDLEVSVDLGTGDQAAQFWTCDLSHEYVTINGDYRS
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
24AcetylationKYALYVPKTGSFPKG
HEEEEECCCCCCCCC
56.3124489116
46PhosphorylationSGVKKNGSLDLGVIL
CCCCCCCEEEEEEEE
28.2722369663
55PhosphorylationDLGVILNTNKSRPST
EEEEEEECCCCCCCC
40.3522369663
58PhosphorylationVILNTNKSRPSTAAA
EEEECCCCCCCCEEE
52.0422369663
61PhosphorylationNTNKSRPSTAAAVFT
ECCCCCCCCEEEEEE
29.5722369663
62PhosphorylationTNKSRPSTAAAVFTT
CCCCCCCCEEEEEEC
24.0122369663
68PhosphorylationSTAAAVFTTNKFKAA
CCEEEEEECCCCCCC
23.9022369663
69PhosphorylationTAAAVFTTNKFKAAP
CEEEEEECCCCCCCC
25.5822369663
90AcetylationVLETARGKNINAIVV
HHHHHCCCCCEEEEE
49.4524489116
124AcetylationMIDLVNDKIGQKNST
HHHHHCCCCCCCCCE
43.4624489116
147AcetylationGQRLQMDKISTGINK
HHHHCHHHHCCCHHH
32.9624489116
154AcetylationKISTGINKIFGEEKF
HHCCCHHHHHCCCHH
37.1824489116
190AcetylationKLVTSRFKLPSGTEY
HHHEECCCCCCCCEE
59.3822865919
233AcetylationIESKALQKMLTFATT
CCCHHHHHHHHHHHC
36.4124489116
236PhosphorylationKALQKMLTFATTRSF
HHHHHHHHHHHCCCC
14.0227017623
253PhosphorylationISVDGDMSTNDTICM
EEEECCCCCCCEEEH
28.8827017623
257PhosphorylationGDMSTNDTICMLANG
CCCCCCCEEEHHCCC
20.3927017623
268PhosphorylationLANGAIDTKEINEDS
HCCCCCCHHHCCCCC
25.1827017623
275PhosphorylationTKEINEDSKDFEQVK
HHHCCCCCCCHHHHH
28.1327017623
276AcetylationKEINEDSKDFEQVKL
HHCCCCCCCHHHHHH
77.9424489116
276SuccinylationKEINEDSKDFEQVKL
HHCCCCCCCHHHHHH
77.9423954790
282AcetylationSKDFEQVKLQVTEFA
CCCHHHHHHHHHHHH
32.6624489116
355AcetylationLCAIGYAKLNDLKSL
HHHHHCHHHHCCCCC
39.0624489116
360AcetylationYAKLNDLKSLDVNKI
CHHHHCCCCCCCCEE
52.4124489116
360SuccinylationYAKLNDLKSLDVNKI
CHHHHCCCCCCCCEE
52.4123954790

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 ARGJ_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARGJ_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 ARGJ_YEAST !!

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

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARGJ_YEAST

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Related Literatures of Post-Translational Modification

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