ELO2_YEAST - dbPTM
ELO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELO2_YEAST
UniProt AC P25358
Protein Name Elongation of fatty acids protein 2 {ECO:0000303|PubMed:9211877}
Gene Name ELO2 {ECO:0000303|PubMed:9211877}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 347
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Component of a microsomal membrane-bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase II, which elongates 16-18 carbon fatty acyl-CoAs such as palmitoyl-CoA and stearoyl-CoA to 20-22-carbon fatty acids by incorporation of malonyl-CoA. [PubMed: 9211877]
Protein Sequence MNSLVTQYAAPLFERYPQLHDYLPTLERPFFNISLWEHFDDVVTRVTNGRFVPSEFQFIAGELPLSTLPPVLYAITAYYVIIFGGRFLLSKSKPFKLNGLFQLHNLVLTSLSLTLLLLMVEQLVPIIVQHGLYFAICNIGAWTQPLVTLYYMNYIVKFIEFIDTFFLVLKHKKLTFLHTYHHGATALLCYTQLMGTTSISWVPISLNLGVHVVMYWYYFLAARGIRVWWKEWVTRFQIIQFVLDIGFIYFAVYQKAVHLYFPILPHCGDCVGSTTATFAGCAIISSYLVLFISFYINVYKRKGTKTSRVVKRAHGGVAAKVNEYVNVDLKNVPTPSPSPKPQHRRKR
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
32N-linked_GlycosylationTLERPFFNISLWEHF
CCCCCCEEEEHHHHH		24.26-
330AcetylationEYVNVDLKNVPTPSP
EECCCCCCCCCCCCC		51.9724489116
334PhosphorylationVDLKNVPTPSPSPKP
CCCCCCCCCCCCCCC		31.9222369663
336PhosphorylationLKNVPTPSPSPKPQH
CCCCCCCCCCCCCCC		40.2522369663
338PhosphorylationNVPTPSPSPKPQHRR
CCCCCCCCCCCCCCC		50.3122369663
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 ELO2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELO2_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 ELO2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TECR_YEASTTSC13physical
11113186
ELO3_YEASTELO3genetic
9211877
SSO2_YEASTSSO2genetic
16269340
ERG4_YEASTERG4genetic
16269340
HACD_YEASTPHS1genetic
16269340
PGA3_YEASTPGA3genetic
16269340
TRS85_YEASTTRS85genetic
16269340
MGA2_YEASTMGA2genetic
16269340
TRS20_YEASTTRS20genetic
16269340
GUP1_YEASTGUP1genetic
16269340
RIC1_YEASTRIC1genetic
16269340
GET2_YEASTGET2genetic
16269340
RGP1_YEASTRGP1genetic
16269340
TECR_YEASTTSC13genetic
11113186
COS8_YEASTCOS8genetic
21187432
GUP1_YEASTGUP1genetic
20526336
RV161_YEASTRVS161genetic
20526336
RV167_YEASTRVS167genetic
20526336
RIC1_YEASTRIC1genetic
20526336
TPM1_YEASTTPM1genetic
20526336
GSF2_YEASTGSF2genetic
20526336
TSC10_YEASTTSC10genetic
20526336
DS1P1_YEASTLCB3genetic
20526336
SEM1_YEASTSEM1genetic
20526336
FABD_YEASTMCT1genetic
21623372
FUMH_YEASTFUM1genetic
21623372
LEU9_YEASTLEU9genetic
21623372
ATPF_YEASTATP4genetic
21623372
ETR1_YEASTETR1genetic
21623372
ACON_YEASTACO1genetic
21623372
METK1_YEASTSAM1genetic
21623372
SKN1_YEASTSKN1genetic
21623372
ISN1_YEASTISN1genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
FADH_YEASTSFA1genetic
21623372
HFA1_YEASTHFA1genetic
21623372
TRX2_YEASTTRX2genetic
21623372
PPB_YEASTPHO8genetic
21623372
ACBP_YEASTACB1genetic
21623372
GLG2_YEASTGLG2genetic
21623372
SGPL_YEASTDPL1genetic
21623372
ACON2_YEASTACO2genetic
21623372
RPE_YEASTRPE1genetic
21623372
TKT1_YEASTTKL1genetic
21623372
SUMT_YEASTMET1genetic
21623372
FABG_YEASTOAR1genetic
21623372
CSG2_YEASTCSG2genetic
21623372
TPS1_YEASTTPS1genetic
21623372
ERG2_YEASTERG2genetic
21623372
HXKB_YEASTHXK2genetic
21623372
ALN_YEASTDAL1genetic
21623372
SERC_YEASTSER1genetic
21623372
GPP2_YEASTGPP2genetic
21623372
ELO3_YEASTELO3genetic
21623372
SUR1_YEASTSUR1genetic
21623372
COQ4_YEASTCOQ4genetic
21623372
PHO84_YEASTPHO84genetic
21623372
DDP1_YEASTDDP1genetic
21623372
FCY21_YEASTFCY21genetic
21623372
AYR1_YEASTAYR1genetic
21623372
HUT1_YEASTHUT1genetic
21623372
EPT1_YEASTEPT1genetic
21623372
CBS_YEASTCYS4genetic
21623372
SYSM_YEASTDIA4genetic
21623372
ACS1_YEASTACS1genetic
21623372
CYS3_YEASTCYS3genetic
21623372
HNT2_YEASTHNT2genetic
21623372
NDH2_YEASTNDE2genetic
21623372
ATPO_YEASTATP5genetic
21623372
DHSD_YEASTSDH4genetic
21623372
CISY1_YEASTCIT1genetic
21623372
OPT1_YEASTOPT1genetic
21623372
PPT2_YEASTPPT2genetic
21623372
NDH1_YEASTNDE1genetic
21623372
DCAM_YEASTSPE2genetic
21623372
MHT1_YEASTMHT1genetic
21623372
ADH3_YEASTADH3genetic
21623372
HSP71_YEASTSSA1physical
22940862
DED1_YEASTDED1physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP72_YEASTSSA2physical
22940862
KPYK1_YEASTCDC19physical
22940862
ELO3_YEASTELO3genetic
24239358
ORM2_YEASTORM2genetic
24239358
LCB4_YEASTLCB4genetic
24239358
ATG1_YEASTATG1genetic
24239358
ATG7_YEASTATG7genetic
24239358
ELO3_YEASTELO3genetic
25519905
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELO2_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 THR-334; SER-336 ANDSER-338, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 ANDSER-338, 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 THR-334; SER-336 ANDSER-338, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 ANDSER-338, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 ANDSER-338, AND MASS SPECTROMETRY.

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