ASSY_YEAST - dbPTM
ASSY_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASSY_YEAST
UniProt AC P22768
Protein Name Argininosuccinate synthase
Gene Name ARG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 420
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the eighth step in arginine biosynthesis. Also has a catabolic function as the first enzyme of citrulline utilization as nitrogen source via arginine and the reactions involved in the arginase pathway..
Protein Sequence MSKGKVCLAYSGGLDTSVILAWLLDQGYEVVAFMANVGQEEDFDAAKEKALKIGACKFVCVDCREDFVKDILFPAVQVNAVYEDVYLLGTSLARPVIAKAQIDVAKQEGCFAVSHGCTGKGNDQIRFELSFYALKPDVKCITPWRMPEFFERFAGRKDLLDYAAQKGIPVAQTKAKPWSTDENQAHISYEAGILEDPDTTPPKDMWKLIVDPMDAPDQPQDLTIDFERGLPVKLTYTDNKTSKEVSVTKPLDVFLAASNLARANGVGRIDIVEDRYINLKSRGCYEQAPLTVLRKAHVDLEGLTLDKEVRQLRDSFVTPNYSRLIYNGSYFTPECEYIRSMIQPSQNSVNGTVRVRLYKGNVIILGRSTKTEKLYDPTESSMDELTGFLPTDTTGFIAIQAIRIKKYGESKKTKGEELTL
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
57AcetylationALKIGACKFVCVDCR
HHHCCCCEEEEECCC
40.0525381059
106AcetylationKAQIDVAKQEGCFAV
HHHHHHHHHCCCEEE
49.0524489116
135UbiquitinationELSFYALKPDVKCIT
EEEEEEECCCCEEEC
30.8824961812
157SuccinylationFERFAGRKDLLDYAA
HHHHCCCHHHHHHHH
52.3823954790
162PhosphorylationGRKDLLDYAAQKGIP
CCHHHHHHHHHCCCC
12.1028889911
173PhosphorylationKGIPVAQTKAKPWST
CCCCCEECCCCCCCC
24.1922369663
233AcetylationFERGLPVKLTYTDNK
ECCCCEEEEEEECCC
32.9224489116
243AcetylationYTDNKTSKEVSVTKP
EECCCCCCEEEECCC
68.3324489116
246PhosphorylationNKTSKEVSVTKPLDV
CCCCCEEEECCCHHH
25.7622369663
248PhosphorylationTSKEVSVTKPLDVFL
CCCEEEECCCHHHHH
21.3122369663
249AcetylationSKEVSVTKPLDVFLA
CCEEEECCCHHHHHH
41.2324489116
258PhosphorylationLDVFLAASNLARANG
HHHHHHHHHHHHHCC
27.1122369663
280AcetylationEDRYINLKSRGCYEQ
ECCEEECCCCCCCCC
33.3525381059
307UbiquitinationLEGLTLDKEVRQLRD
CCCCCCCHHHHHHHH
62.3124961812
315PhosphorylationEVRQLRDSFVTPNYS
HHHHHHHCCCCCCCC
18.3822369663
318PhosphorylationQLRDSFVTPNYSRLI
HHHHCCCCCCCCEEE
12.1022369663
321PhosphorylationDSFVTPNYSRLIYNG
HCCCCCCCCEEEECC
9.0722369663
322PhosphorylationSFVTPNYSRLIYNGS
CCCCCCCCEEEECCC
27.5322369663
375PhosphorylationSTKTEKLYDPTESSM
CCCCCCCCCCCCCCH
30.8322369663
378PhosphorylationTEKLYDPTESSMDEL
CCCCCCCCCCCHHHH
45.6722369663
380PhosphorylationKLYDPTESSMDELTG
CCCCCCCCCHHHHCC
33.1822369663
381PhosphorylationLYDPTESSMDELTGF
CCCCCCCCHHHHCCC
24.8322369663
386PhosphorylationESSMDELTGFLPTDT
CCCHHHHCCCCCCCC
24.6822369663
391PhosphorylationELTGFLPTDTTGFIA
HHCCCCCCCCCCEEE
48.3922369663
393PhosphorylationTGFLPTDTTGFIAIQ
CCCCCCCCCCEEEEE
31.1522369663
394PhosphorylationGFLPTDTTGFIAIQA
CCCCCCCCCEEEEEE
32.6722369663
413PhosphorylationKYGESKKTKGEELTL
ECCCCCCCCCCCCCC
48.2822369663
419PhosphorylationKTKGEELTL------
CCCCCCCCC------
33.4322369663

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 ASSY_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASSY_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 ASSY_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 ASSY_YEAST

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Related Literatures of Post-Translational Modification

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