TGL5_YEAST - dbPTM
TGL5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGL5_YEAST
UniProt AC Q12043
Protein Name Lipase 5
Gene Name TGL5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 749
Subcellular Localization Lipid droplet. Membrane
Single-pass membrane protein. Lipid particle.
Protein Description Releases specific fatty acids from neutral lipid triacylglycerols (TAG) thereby supplying fatty acids to a general acylation process. May have a specific role in sporulation..
Protein Sequence MSNTLPVTEFLLSKYYELSNTPATDSSSLFKWLYHKTLSRKQLLISDLSSQKKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNSKSPNENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDPHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITARFRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMVGQFHEVLKNPSQLFLLHQTTLGARATWPKISMIQNNCGQEFALDKAITFLKEKIIISSSIKNPLQFYQPRFSEQIKSLSIMDADLPGVDLEESSSNSLSIIKSPNKTAAPGRFPLQPLPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKANSLSFAIGASSLRLKKSPLKVPSRPQFKKRSSYYNQNMSAEMRKNRKKSGTISSYDVQTNSEDFPIPAIENGSFDNTLFNPSRFPMDAMSAATNDNFMNNSDIFQN
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
39PhosphorylationWLYHKTLSRKQLLIS
HHHHHCCCHHHHHHH		42.5417287358
49PhosphorylationQLLISDLSSQKKHAI
HHHHHHHHHCCCCCC		35.4017287358
50PhosphorylationLLISDLSSQKKHAIS
HHHHHHHHCCCCCCC		54.0017287358
270N-linked_GlycosylationKISRFCQNGTWFNNQ
EHHHHHHCCCCCCCC		51.55-
289N-linked_GlycosylationTMLSFLGNLTFREAY
HHHHHHHHCHHHHHH		37.75-
297N-linked_GlycosylationLTFREAYNKTGKILN
CHHHHHHHCCCCEEE		42.32-
304N-linked_GlycosylationNKTGKILNITVSPAS
HCCCCEEEEEECHHH		31.21-
321N-linked_GlycosylationEQPKLLNNLTAPNVL
CCCHHHHCCCCCCHH		38.44-
355PhosphorylationLFEKDPHTGKIKEWG
CCCCCCCCCCCCCCC		45.6327017623
369PhosphorylationGATNLHLSNMKFMDG
CCCEEECCCCEECCC		24.9127017623
474N-linked_GlycosylationFLQQYSGNVTILPDL
HHHHHCCCEEEECCH		23.09-
532PhosphorylationFALDKAITFLKEKII
HHHHHHHHHHHHCEE		27.9821126336
563PhosphorylationSEQIKSLSIMDADLP
HHHHHHHCCCCCCCC		23.9819779198
579PhosphorylationVDLEESSSNSLSIIK
CCCCCCCCCCCEEEE		39.4519779198
587PhosphorylationNSLSIIKSPNKTAAP
CCCEEEECCCCCCCC		24.2421440633
589N-linked_GlycosylationLSIIKSPNKTAAPGR
CEEEECCCCCCCCCC		62.49-
604PhosphorylationFPLQPLPSPSSTFNK
CCCCCCCCCCCCCCH		45.1321082442
606PhosphorylationLQPLPSPSSTFNKRK
CCCCCCCCCCCCHHH		46.4728152593
607PhosphorylationQPLPSPSSTFNKRKM
CCCCCCCCCCCHHHC		40.1621440633
608PhosphorylationPLPSPSSTFNKRKMD
CCCCCCCCCCHHHCC		35.2525371407
618PhosphorylationKRKMDMLSPSPSPST
HHHCCCCCCCCCCCC		19.3919823750
620PhosphorylationKMDMLSPSPSPSTSP
HCCCCCCCCCCCCCC		34.3322890988
622PhosphorylationDMLSPSPSPSTSPQR
CCCCCCCCCCCCCCC		35.5019823750
624PhosphorylationLSPSPSPSTSPQRSK
CCCCCCCCCCCCCCC		45.9422890988
625PhosphorylationSPSPSPSTSPQRSKS
CCCCCCCCCCCCCCC		48.0522890988
626PhosphorylationPSPSPSTSPQRSKSS
CCCCCCCCCCCCCCC		24.3119823750
630PhosphorylationPSTSPQRSKSSFTQQ
CCCCCCCCCCCCCCH		31.4821551504
632PhosphorylationTSPQRSKSSFTQQGT
CCCCCCCCCCCCHHH		31.7528889911
633PhosphorylationSPQRSKSSFTQQGTR
CCCCCCCCCCCHHHH		35.7330377154
645PhosphorylationGTRQKANSLSFAIGA
HHHHHHHHHHHEEEC		30.1928152593
647PhosphorylationRQKANSLSFAIGASS
HHHHHHHHHEEECCC		16.6819779198
660PhosphorylationSSLRLKKSPLKVPSR
CCCCCCCCCCCCCCC		33.6021440633
674PhosphorylationRPQFKKRSSYYNQNM
CCCHHCCHHHHCCCC		31.4130377154
675PhosphorylationPQFKKRSSYYNQNMS
CCHHCCHHHHCCCCC		35.3530377154
676PhosphorylationQFKKRSSYYNQNMSA
CHHCCHHHHCCCCCH		14.0027017623
677PhosphorylationFKKRSSYYNQNMSAE
HHCCHHHHCCCCCHH		16.5427017623
680N-linked_GlycosylationRSSYYNQNMSAEMRK
CHHHHCCCCCHHHHH		23.80-
682PhosphorylationSYYNQNMSAEMRKNR
HHHCCCCCHHHHHCC		28.7327017623
714N-linked_GlycosylationFPIPAIENGSFDNTL
CCCCCCCCCCCCCCC		45.34-
716PhosphorylationIPAIENGSFDNTLFN
CCCCCCCCCCCCCCC		40.8019779198
742N-linked_GlycosylationATNDNFMNNSDIFQN
HCCCCCCCCCHHCCC		40.49-
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 TGL5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGL5_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 TGL5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMH2_YEASTBMH2physical
16554755
GLO2_YEASTGLO2physical
16554755
HXKA_YEASTHXK1physical
16554755
SYEC_YEASTGUS1physical
16554755
ZUO1_YEASTZUO1physical
16554755
SSZ1_YEASTSSZ1physical
16554755
GRP78_YEASTKAR2physical
16554755
HSP77_YEASTSSC1physical
16554755
NAP1_YEASTNAP1physical
16554755
GLYC_YEASTSHM2physical
16554755
EF3A_YEASTYEF3physical
16554755
EIF3C_YEASTNIP1physical
16554755
SSB2_YEASTSSB2physical
16554755
TGL5_YEASTTGL5physical
18467557
ATC3_YEASTDRS2genetic
27708008
CG13_YEASTCLN3genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
SHC1_YEASTSHC1genetic
27708008
SPO74_YEASTSPO74genetic
27708008
XRN1_YEASTXRN1genetic
27708008
HFM1_YEASTHFM1genetic
27708008
RAV1_YEASTRAV1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
PPQ1_YEASTPPQ1genetic
27708008
YP022_YEASTYPR022Cgenetic
27708008
KAR3_YEASTKAR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGL5_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-604; SER-618 ANDSER-622, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49 AND SER-50,AND MASS SPECTROMETRY.

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