SYSC_YEAST - dbPTM
SYSC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYSC_YEAST
UniProt AC P07284
Protein Name Serine--tRNA ligase, cytoplasmic
Gene Name SES1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 462
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)..
Protein Sequence MLDINQFIEDKGGNPELIRQSQKARNASVEIVDEIISDYKDWVKTRFELDELNKKFNKLQKDIGLKFKNKEDASGLLAEKEKLTQQKKELTEKEQQEDKDLKKKVFQVGNIVHPSVVVSNDEENNELVRTWKPEDLEAVGPIASVTGKPASLSHHEILLRLDGYDPDRGVKICGHRGYFFRNYGVFLNQALINYGLQFLAAKGYIPLQAPVMMNKELMSKTAQLSEFDEELYKVIDGEDEKYLIATSEQPISAYHSGEWFEKPQEQLPIHYVGYSSCFRREAGSHGKDAWGVFRVHAFEKIEQFVITEPEKSWEEFEKMISYSEEFYKSLKLPYRIVGIVSGELNNAAAKKYDLEAWFPYQKEYKELVSCSNCTDYQSRNLEIRCGIKKMGDREKKYVHCLNSTLAATQRALCCILENYQTEDGLVVPEVLRKYIPGEPEFLPFVNELPKNSTSSKDKKKKN
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
28PhosphorylationSQKARNASVEIVDEI
HHHHHHCCHHHHHHH		24.6724961812
54AcetylationFELDELNKKFNKLQK
HHHHHHHHHHHHHHH		71.9524489116
61AcetylationKKFNKLQKDIGLKFK
HHHHHHHHHHCCCCC		62.8524489116
66AcetylationLQKDIGLKFKNKEDA
HHHHHCCCCCCHHHH		49.4324489116
68AcetylationKDIGLKFKNKEDASG
HHHCCCCCCHHHHHH		66.5724489116
70UbiquitinationIGLKFKNKEDASGLL
HCCCCCCHHHHHHHH		58.5223749301
70SuccinylationIGLKFKNKEDASGLL
HCCCCCCHHHHHHHH		58.5223954790
80AcetylationASGLLAEKEKLTQQK
HHHHHHHHHHHHHHH		55.3224489116
80SuccinylationASGLLAEKEKLTQQK
HHHHHHHHHHHHHHH		55.3223954790
82AcetylationGLLAEKEKLTQQKKE
HHHHHHHHHHHHHHH		68.8324489116
872-HydroxyisobutyrylationKEKLTQQKKELTEKE
HHHHHHHHHHHHHHH		38.10-
93SuccinylationQKKELTEKEQQEDKD
HHHHHHHHHHHHCHH		56.4323954790
99AcetylationEKEQQEDKDLKKKVF
HHHHHHCHHHHHHHE		65.2924489116
119PhosphorylationVHPSVVVSNDEENNE
CCCEEEEECCCCCCE		27.2728889911
132AcetylationNELVRTWKPEDLEAV
CEEEEECCHHHHHCC		37.6124489116
148UbiquitinationPIASVTGKPASLSHH
CEEECCCCCCCCCCC		28.2223749301
171AcetylationYDPDRGVKICGHRGY
CCCCCCCEECCCCCC		34.7924489116
215UbiquitinationQAPVMMNKELMSKTA
CCCCCCCHHHHHCCC		34.0424961812
215AcetylationQAPVMMNKELMSKTA
CCCCCCCHHHHHCCC		34.0424489116
220UbiquitinationMNKELMSKTAQLSEF
CCHHHHHCCCCHHHC		33.6423749301
220AcetylationMNKELMSKTAQLSEF
CCHHHHHCCCCHHHC		33.6422865919
225PhosphorylationMSKTAQLSEFDEELY
HHCCCCHHHCCHHHH		24.9222369663
287AcetylationREAGSHGKDAWGVFR
CCCCCCCCCCCCEEE		38.5624489116
300AcetylationFRVHAFEKIEQFVIT
EEEEECHHEEEEEEC		45.1224489116
300UbiquitinationFRVHAFEKIEQFVIT
EEEEECHHEEEEEEC		45.1224961812
311AcetylationFVITEPEKSWEEFEK
EEECCCCCCHHHHHH		72.1424489116
328AcetylationSYSEEFYKSLKLPYR
CCCHHHHHHCCCCHH		55.4224489116
350UbiquitinationELNNAAAKKYDLEAW
CCCCHHHHHCCHHHH		47.3322817900
3502-HydroxyisobutyrylationELNNAAAKKYDLEAW
CCCCHHHHHCCHHHH		47.33-
350SuccinylationELNNAAAKKYDLEAW
CCCCHHHHHCCHHHH		47.3323954790
351UbiquitinationLNNAAAKKYDLEAWF
CCCHHHHHCCHHHHC		38.9923749301
351AcetylationLNNAAAKKYDLEAWF
CCCHHHHHCCHHHHC		38.9924489116
362UbiquitinationEAWFPYQKEYKELVS
HHHCCCCHHHHHHHC		58.1122817900
362AcetylationEAWFPYQKEYKELVS
HHHCCCCHHHHHHHC		58.1124489116
365UbiquitinationFPYQKEYKELVSCSN
CCCCHHHHHHHCCCC		45.7423749301
365AcetylationFPYQKEYKELVSCSN
CCCCHHHHHHHCCCC		45.7424489116
396AcetylationKMGDREKKYVHCLNS
ECCCCHHHHHHHHHH		47.9925381059
450AcetylationPFVNELPKNSTSSKD
HHHCCCCCCCCCCCH		75.9424489116
453PhosphorylationNELPKNSTSSKDKKK
CCCCCCCCCCCHHCC		46.5428889911
454PhosphorylationELPKNSTSSKDKKKK
CCCCCCCCCCHHCCC		34.9028889911
455PhosphorylationLPKNSTSSKDKKKKN
CCCCCCCCCHHCCCC		44.9928889911
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 SYSC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYSC_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 SYSC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEX21_YEASTPEX21physical
12204379
PEX21_YEASTPEX21physical
17451428
PEX21_YEASTPEX21physical
18067851
VPS41_YEASTVPS41genetic
20526336
VPS16_YEASTVPS16genetic
20526336
YD012_YEASTYDL012Cgenetic
20526336
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYSC_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-119, AND MASSSPECTROMETRY.

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