ARE2_YEAST - dbPTM
ARE2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARE2_YEAST
UniProt AC P53629
Protein Name Sterol O-acyltransferase 2
Gene Name ARE2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 642
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Ensures probably most of the acyltransferase activity. Suppression of ARE2 reduces sterol ester levels to 25% of the normal value..
Protein Sequence MDKKKDLLENEQFLRIQKLNAADAGKRQSITVDDEGELYGLDTSGNSPANEHTATTITQNHSVVASNGDVAFIPGTATEGNTEIVTEEVIETDDNMFKTHVKTLSSKEKARYRQGSSNFISYFDDMSFEHRPSILDGSVNEPFKTKFVGPTLEKEIRRREKELMAMRKNLHHRKSSPDAVDSVGKNDGAAPTTVPTAATSETVVTVETTIISSNFSGLYVAFWMAIAFGAVKALIDYYYQHNGSFKDSEILKFMTTNLFTVASVDLLMYLSTYFVVGIQYLCKWGVLKWGTTGWIFTSIYEFLFVIFYMYLTENILKLHWLSKIFLFLHSLVLLMKMHSFAFYNGYLWGIKEELQFSKSALAKYKDSINDPKVIGALEKSCEFCSFELSSQSLSDQTQKFPNNISAKSFFWFTMFPTLIYQIEYPRTKEIRWSYVLEKICAIFGTIFLMMIDAQILMYPVAMRALAVRNSEWTGILDRLLKWVGLLVDIVPGFIVMYILDFYLIWDAILNCVAELTRFGDRYFYGDWWNCVSWADFSRIWNIPVHKFLLRHVYHSSMSSFKLNKSQATLMTFFLSSVVHELAMYVIFKKLRFYLFFFQMLQMPLVALTNTKFMRNRTIIGNVIFWLGICMGPSVMCTLYLTF
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
18AcetylationEQFLRIQKLNAADAG
HHHHHHHHHCHHHCC		41.1422865919
29PhosphorylationADAGKRQSITVDDEG
HHCCCCCCEEECCCC		25.0228889911
47PhosphorylationGLDTSGNSPANEHTA
EECCCCCCCCCCCCC		28.9928889911
92PhosphorylationVTEEVIETDDNMFKT
EEEEEEECCCCCCHH		37.2127214570
116PhosphorylationKARYRQGSSNFISYF
HHHHHCCCCCHHHHC		17.4824961812
117PhosphorylationARYRQGSSNFISYFD
HHHHCCCCCHHHHCC		42.4524961812
127PhosphorylationISYFDDMSFEHRPSI
HHHCCCCCCCCCCCC		34.1824961812
133PhosphorylationMSFEHRPSILDGSVN
CCCCCCCCCCCCCCC		35.4224961812
175PhosphorylationKNLHHRKSSPDAVDS
HCCCCCCCCHHHHHH		47.2422369663
176PhosphorylationNLHHRKSSPDAVDSV
CCCCCCCCHHHHHHC		29.8125521595
182PhosphorylationSSPDAVDSVGKNDGA
CCHHHHHHCCCCCCC		26.6022890988
339PhosphorylationVLLMKMHSFAFYNGY
HHHHHHHHHHHHCCC		18.1230377154
343PhosphorylationKMHSFAFYNGYLWGI
HHHHHHHHCCCCCCH		12.3030377154
346PhosphorylationSFAFYNGYLWGIKEE
HHHHHCCCCCCHHHH		8.8130377154
357PhosphorylationIKEELQFSKSALAKY
HHHHHHCCHHHHHHH		16.8530377154
565PhosphorylationSSFKLNKSQATLMTF
HCCCCCHHHHHHHHH		24.7927017623
568PhosphorylationKLNKSQATLMTFFLS
CCCHHHHHHHHHHHH		14.9327017623
584PhosphorylationVVHELAMYVIFKKLR
HHHHHHHHHHHHHHH		5.7027017623
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 ARE2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARE2_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 ARE2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2C1_YEASTPTC1physical
11805837
ARV1_YEASTARV1genetic
11063737
PDAT_YEASTLRO1genetic
11741946
ARE1_YEASTARE1genetic
11741946
DGAT2_YEASTDGA1genetic
11741946
UBX2_YEASTUBX2genetic
16269340
YNE6_YEASTYNL046Wgenetic
16269340
BFR1_YEASTBFR1genetic
16269340
GET2_YEASTGET2genetic
16269340
YMD8_YEASTYMD8genetic
16269340
SCS7_YEASTSCS7genetic
16269340
DGAT2_YEASTDGA1genetic
19608739
PDAT_YEASTLRO1genetic
19608739
DGAT2_YEASTDGA1genetic
19690167
PDAT_YEASTLRO1genetic
19690167
UBX2_YEASTUBX2genetic
19690167
HPH2_YEASTFRT2genetic
20093466
YAJ9_YEASTYAR029Wgenetic
20093466
RDH54_YEASTRDH54genetic
20093466
AMN1_YEASTAMN1genetic
20093466
PEX32_YEASTPEX32genetic
20093466
DCC1_YEASTDCC1genetic
20093466
RBSK_YEASTRBK1genetic
20093466
ARE1_YEASTARE1genetic
20093466
BUD31_YEASTBUD31genetic
20093466
PMT5_YEASTPMT5genetic
20093466
HSP78_YEASTHSP78genetic
20093466
RAD51_YEASTRAD51genetic
20093466
KA122_YEASTKAP122genetic
20093466
ICE2_YEASTICE2genetic
20093466
BAR1_YEASTBAR1genetic
20093466
SDHX_YEASTYJL045Wgenetic
20093466
RS30A_YEASTRPS30Agenetic
20093466
RS30B_YEASTRPS30Agenetic
20093466
MOT3_YEASTMOT3genetic
20093466
MCA1_YEASTMCA1genetic
20093466
LIS1_YEASTPAC1genetic
20093466
PDE2_YEASTPDE2genetic
20093466
MTHR1_YEASTMET12genetic
20093466
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
STE24_YEASTSTE24physical
16093310
SCS7_YEASTSCS7genetic
20526336
ARK1_YEASTARK1genetic
20526336
RIC1_YEASTRIC1genetic
20526336
PAH1_YEASTPAH1genetic
21422231
PHSG_YEASTGPH1genetic
21623372
DGAT2_YEASTDGA1genetic
21693588
PDAT_YEASTLRO1genetic
21693588
CSG2_YEASTCSG2genetic
21987634
RGP1_YEASTRGP1genetic
21987634
DOP1_YEASTDOP1genetic
21987634
IPK1_YEASTIPK1genetic
21987634
GLN3_YEASTGLN3genetic
21987634
VPS1_YEASTVPS1genetic
21987634
LAS1_YEASTLAS1genetic
21987634
ERG3_YEASTERG3genetic
21987634
YPT6_YEASTYPT6genetic
21987634
CYK2_YEASTHOF1genetic
21987634
ERG2_YEASTERG2genetic
21987634
KIME_YEASTERG12genetic
21987634
SCS7_YEASTSCS7genetic
21987634
VDAC1_YEASTPOR1genetic
21987634
BLH1_YEASTLAP3genetic
21987634
YME1_YEASTYME1genetic
21987634
PDAT_YEASTLRO1genetic
22738231
DGAT2_YEASTDGA1genetic
22738231
DOA10_YEASTSSM4genetic
23898401
UBC7_YEASTUBC7genetic
23898401
ARE2_YEASTARE2physical
26220175
COS8_YEASTCOS8physical
26220175
COS12_YEASTCOS12physical
26220175
GLT1_YEASTGLT1physical
26220175
MFB1_YEASTMFB1physical
26220175
NUP84_YEASTNUP84physical
26220175
PDR11_YEASTPDR11physical
26220175
SIP18_YEASTSIP18physical
26220175
YJ66_YEASTYJR096Wphysical
26220175
SLU7_YEASTSLU7physical
26220175
MTF1_YEASTMTF1physical
26220175
ATP8_YEASTATP8physical
26220175
ALG5_YEASTALG5physical
26220175
RDH54_YEASTRDH54genetic
27708008
RBSK_YEASTRBK1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PMT5_YEASTPMT5genetic
27708008
VMS1_YEASTVMS1genetic
27708008
IPT1_YEASTIPT1genetic
27708008
SPS2_YEASTSPS2genetic
27708008
KA122_YEASTKAP122genetic
27708008
SPO11_YEASTSPO11genetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
VPS51_YEASTVPS51genetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
MOT3_YEASTMOT3genetic
27708008
RIM11_YEASTRIM11genetic
27708008
LIS1_YEASTPAC1genetic
27708008
MED1_YEASTMED1genetic
27708008
DGAT2_YEASTDGA1genetic
26432634
PDAT_YEASTLRO1genetic
26432634
PCY1_YEASTPCT1genetic
26269581
DGK1_YEASTDGK1genetic
26269581
DGAT2_YEASTDGA1genetic
27170177
PDAT_YEASTLRO1genetic
27170177
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARE2_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-29; SER-47; SER-175 ANDSER-176, 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 SER-175 AND SER-176, ANDMASS 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-175, AND MASSSPECTROMETRY.
"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 SER-175, AND MASSSPECTROMETRY.

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