SYV_YEAST - dbPTM
SYV_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYV_YEAST
UniProt AC P07806
Protein Name Valine--tRNA ligase, mitochondrial
Gene Name VAS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1104
Subcellular Localization Isoform Cytoplasmic: Cytoplasm.
Isoform Mitochondrial: Mitochondrion.
Protein Description
Protein Sequence MNKWLNTLSKTFTFRLLNCHYRRSLPLCQNFSLKKSLTHNQVRFFKMSDLDNLPPVDPKTGEVIINPLKEDGSPKTPKEIEKEKKKAEKLLKFAAKQAKKNAAATTGASQKKPKKKKEVEPIPEFIDKTVPGEKKILVSLDDPALKAYNPANVESSWYDWWIKTGVFEPEFTADGKVKPEGVFCIPAPPPNVTGALHIGHALTIAIQDSLIRYNRMKGKTVLFLPGFDHAGIATQSVVEKQIWAKDRKTRHDYGREAFVGKVWEWKEEYHSRIKNQIQKLGASYDWSREAFTLSPELTKSVEEAFVRLHDEGVIYRASRLVNWSVKLNTAISNLEVENKDVKSRTLLSVPGYDEKVEFGVLTSFAYPVIGSDEKLIIATTRPETIFGDTAVAVHPDDDRYKHLHGKFIQHPFLPRKIPIITDKEAVDMEFGTGAVKITPAHDQNDYNTGKRHNLEFINILTDDGLLNEECGPEWQGMKRFDARKKVIEQLKEKNLYVGQEDNEMTIPTCSRSGDIIEPLLKPQWWVSQSEMAKDAIKVVRDGQITITPKSSEAEYFHWLGNIQDWCISRQLWWGHRCPVYFINIEGEEHDRIDGDYWVAGRSMEEAEKKAAAKYPNSKFTLEQDEDVLDTWFSSGLWPFSTLGWPEKTKDMETFYPFSMLETGWDILFFWVTRMILLGLKLTGSVPFKEVFCHSLVRDAQGRKMSKSLGNVIDPLDVITGIKLDDLHAKLLQGNLDPREVEKAKIGQKESYPNGIPQCGTDAMRFALCAYTTGGRDINLDILRVEGYRKFCNKIYQATKFALMRLGDDYQPPATEGLSGNESLVEKWILHKLTETSKIVNEALDKRDFLTSTSSIYEFWYLICDVYIENSKYLIQEGSAIEKKSAKDTLYILLDNALKLIHPFMPFISEEMWQRLPKRSTEKAASIVKASYPVYVSEYDDVKSANAYDLVLNITKEARSLLSEYNILKNGKVFVESNHEEYFKTAEDQKDSIVSLIKAIDEVTVVRDASEIPEGCVLQSVNPEVNVHLLVKGHVDIDAEIAKVQKKLEKAKKSKNGIEQTINSKDYETKANTQAKEANKSKLDNTVAEIEGLEATIENLKRLKL
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
38PhosphorylationFSLKKSLTHNQVRFF
CCCCCCCCCCCEEEE		26.3520377248
59UbiquitinationNLPPVDPKTGEVIIN
CCCCCCCCCCCEEEC		65.7717644757
69UbiquitinationEVIINPLKEDGSPKT
CEEECCCCCCCCCCC		55.8217644757
69SuccinylationEVIINPLKEDGSPKT
CEEECCCCCCCCCCC		55.8223954790
73PhosphorylationNPLKEDGSPKTPKEI
CCCCCCCCCCCHHHH		35.2325752575
75UbiquitinationLKEDGSPKTPKEIEK
CCCCCCCCCHHHHHH		78.2317644757
76PhosphorylationKEDGSPKTPKEIEKE
CCCCCCCCHHHHHHH		42.8725752575
105PhosphorylationAKKNAAATTGASQKK
HHHHHHHHCCCCCCC		22.4922369663
106PhosphorylationKKNAAATTGASQKKP
HHHHHHHCCCCCCCC		26.4822369663
109PhosphorylationAAATTGASQKKPKKK
HHHHCCCCCCCCCCC		43.8322369663
128AcetylationPIPEFIDKTVPGEKK
CCHHHHCCCCCCCCE		46.7524489116
219UbiquitinationRYNRMKGKTVLFLPG
HHHCCCCCEEEEECC		29.9117644757
240UbiquitinationATQSVVEKQIWAKDR
CCHHHHHHHHHCCCC		35.1617644757
261AcetylationGREAFVGKVWEWKEE
CCHHHHHHHHHHHHH		38.5824489116
261UbiquitinationGREAFVGKVWEWKEE
CCHHHHHHHHHHHHH		38.5822817900
266AcetylationVGKVWEWKEEYHSRI
HHHHHHHHHHHHHHH		29.2024489116
266UbiquitinationVGKVWEWKEEYHSRI
HHHHHHHHHHHHHHH		29.2022817900
274UbiquitinationEEYHSRIKNQIQKLG
HHHHHHHHHHHHHHC		41.5123749301
279UbiquitinationRIKNQIQKLGASYDW
HHHHHHHHHCCCCCC		50.9823749301
279AcetylationRIKNQIQKLGASYDW
HHHHHHHHHCCCCCC		50.9824489116
294PhosphorylationSREAFTLSPELTKSV
CHHHHCCCHHHHHCH		17.1722369663
298PhosphorylationFTLSPELTKSVEEAF
HCCCHHHHHCHHHHH		21.4422369663
299UbiquitinationTLSPELTKSVEEAFV
CCCHHHHHCHHHHHH		66.1924961812
299AcetylationTLSPELTKSVEEAFV
CCCHHHHHCHHHHHH		66.1924489116
326UbiquitinationRLVNWSVKLNTAISN
HHHCEEHHHCCHHHC		30.4215699485
332PhosphorylationVKLNTAISNLEVENK
HHHCCHHHCCEECCC		32.6628889911
339UbiquitinationSNLEVENKDVKSRTL
HCCEECCCCCCCCEE		50.8519722269
339AcetylationSNLEVENKDVKSRTL
HCCEECCCCCCCCEE		50.8524489116
342UbiquitinationEVENKDVKSRTLLSV
EECCCCCCCCEEEEC		44.3319722269
342AcetylationEVENKDVKSRTLLSV
EECCCCCCCCEEEEC		44.3324489116
362PhosphorylationKVEFGVLTSFAYPVI
CEEEEEEEECCEEEC		21.2819823750
363PhosphorylationVEFGVLTSFAYPVIG
EEEEEEEECCEEECC		12.0619823750
366PhosphorylationGVLTSFAYPVIGSDE
EEEEECCEEECCCCC		8.9519823750
371PhosphorylationFAYPVIGSDEKLIIA
CCEEECCCCCEEEEE		31.3219823750
374UbiquitinationPVIGSDEKLIIATTR
EECCCCCEEEEEECC		50.4017644757
401UbiquitinationHPDDDRYKHLHGKFI
CCCCCCHHHHCCCCC		40.3517644757
423AcetylationKIPIITDKEAVDMEF
CCCCCCCHHHCCCCC		38.6324489116
450UbiquitinationQNDYNTGKRHNLEFI
CCCCCCCCCCCCEEE		48.7423749301
491AcetylationKKVIEQLKEKNLYVG
HHHHHHHHHCCCCCC		67.3522865919
496PhosphorylationQLKEKNLYVGQEDNE
HHHHCCCCCCCCCCC		16.3628889911
706UbiquitinationAQGRKMSKSLGNVID
HHCCHHHHHHCCCCC		46.3224961812
706AcetylationAQGRKMSKSLGNVID
HHCCHHHHHHCCCCC		46.3224489116
707PhosphorylationQGRKMSKSLGNVIDP
HCCHHHHHHCCCCCH		33.9122369663
722UbiquitinationLDVITGIKLDDLHAK
HHHHHCEEHHHHHHH		47.4024961812
722AcetylationLDVITGIKLDDLHAK
HHHHHCEEHHHHHHH		47.4024489116
729AcetylationKLDDLHAKLLQGNLD
EHHHHHHHHHCCCCC		38.6924489116
748AcetylationEKAKIGQKESYPNGI
HHHHCCCCCCCCCCC		43.3324489116
748UbiquitinationEKAKIGQKESYPNGI
HHHHCCCCCCCCCCC		43.3323749301
793AcetylationGYRKFCNKIYQATKF
HHHHHHHHHHHHHHH		43.9322865919
799AcetylationNKIYQATKFALMRLG
HHHHHHHHHHHHHCC		31.4924489116
826UbiquitinationGNESLVEKWILHKLT
CCHHHHHHHHHHHHH		31.8617644757
831AcetylationVEKWILHKLTETSKI
HHHHHHHHHHHHHHH		54.3724489116
837AcetylationHKLTETSKIVNEALD
HHHHHHHHHHHHHHH		59.0824489116
882AcetylationQEGSAIEKKSAKDTL
ECCCCCCCCCHHHHH		46.0124489116
922UbiquitinationLPKRSTEKAASIVKA
CCCCCHHHHHHHHHH		49.7123749301
928UbiquitinationEKAASIVKASYPVYV
HHHHHHHHHCCCEEE		29.9123749301
943PhosphorylationSEYDDVKSANAYDLV
ECCCCCCCCCHHHHH		26.9721440633
959PhosphorylationNITKEARSLLSEYNI
HHHHHHHHHHHHHCC		40.4821440633
968AcetylationLSEYNILKNGKVFVE
HHHHCCHHCCEEEEE		60.9124489116
971AcetylationYNILKNGKVFVESNH
HCCHHCCEEEEECCC		41.7224489116
983UbiquitinationSNHEEYFKTAEDQKD
CCCHHHHCCHHHHHH		46.0215699485
983AcetylationSNHEEYFKTAEDQKD
CCCHHHHCCHHHHHH		46.0224489116
989UbiquitinationFKTAEDQKDSIVSLI
HCCHHHHHHHHHHHH		66.8124961812
997UbiquitinationDSIVSLIKAIDEVTV
HHHHHHHHHHCEEEE		44.5815699485
1003PhosphorylationIKAIDEVTVVRDASE
HHHHCEEEEEECHHH		15.9628889911
1042AcetylationDIDAEIAKVQKKLEK
CCHHHHHHHHHHHHH		51.3524489116
1064SuccinylationIEQTINSKDYETKAN
HHHHHCCHHHHHHHH		60.9023954790
1064UbiquitinationIEQTINSKDYETKAN
HHHHHCCHHHHHHHH		60.9024961812
1064AcetylationIEQTINSKDYETKAN
HHHHHCCHHHHHHHH		60.9024489116
1069AcetylationNSKDYETKANTQAKE
CCHHHHHHHHHHHHH		27.9122865919
1079UbiquitinationTQAKEANKSKLDNTV
HHHHHHHHHHCCHHH		56.8915699485
1081UbiquitinationAKEANKSKLDNTVAE
HHHHHHHHCCHHHHH		62.5615699485
1100UbiquitinationEATIENLKRLKL---
HHHHHHHHHCCC---		68.2315699485
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 SYV_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYV_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 SYV_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UTP8_YEASTUTP8physical
17634288
HSP78_YEASTHSP78physical
19536198
ADH2_YEASTADH2genetic
21623372
HTD2_YEASTHTD2genetic
21623372
ACOX_YEASTPOX1genetic
21623372
THDH_YEASTILV1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
IDHC_YEASTIDP2genetic
21623372
SERA_YEASTSER3genetic
21623372
COQ4_YEASTCOQ4genetic
21623372
PHO84_YEASTPHO84genetic
21623372
BAP2_YEASTBAP2genetic
21623372
COQ3_YEASTCOQ3genetic
21623372
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYV_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-73; SER-294; SER-332;SER-707 AND THR-1003, AND MASS SPECTROMETRY.

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