SLG1_YEAST - dbPTM
SLG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLG1_YEAST
UniProt AC P54867
Protein Name Protein SLG1
Gene Name SLG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 378
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Plays a role during G1 to regulate entering or exiting the cell cycle. Involved in stress responses. Has a role in cell wall integrity signaling. Activates ROM1 or ROM2 catalyzed guanine nucleotide exchange toward RHO1. Important regulator of the actin cytoskeleton rearrangements in conditions of cell wall expansion and membrane stretching. Specifically required for the actin reorganization induced by hypo-osmotic shock. Multicopy suppressor of 1,3-beta-glucan synthase (GS). Activates GS upstream of RHO1. Acts positively on the PKC1-MAPK pathway. Activates transiently SLT2 during alkaline stress, which leads to an increase in the expression of several specific genes..
Protein Sequence MRPNKTSLLLALLSILSQANAYEYVNCFSSLPSDFSKADSYNWQSSSHCNSECSAKGASYFALYNHSECYCGDTNPSGSESTSSSCNTYCFGYSSEMCGGEDAYSVYQLDSDTNSNSISSSDSSTESTSASSSTTSSTTSSTTSTTSSTTSSTTSSMASSSTVQNSPESTQAAASISTSQSSSTVTSESSLTSDTLATSSTSSQSQDATSIIYSTTFHTEGGSTIFVTNTITASAQNSGSATGTAGSDSTSGSKTHKKKANVGAIVGGVVGGVVGAVAIALCILLIVRHINMKREQDRMEKEYQEAIKPVEYPDKLYASSFSSNHGPSSGSFEEEHTKGQTDINPFDDSRRISNGTFINGGPGGKNNVLTVVNPDEAD
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
65N-linked_GlycosylationASYFALYNHSECYCG
CCEEEEECCCEEEEC		32.81-
315UbiquitinationKPVEYPDKLYASSFS
CCCCCCCHHEEECCC		38.6023749301
317PhosphorylationVEYPDKLYASSFSSN
CCCCCHHEEECCCCC		15.3522890988
319PhosphorylationYPDKLYASSFSSNHG
CCCHHEEECCCCCCC		20.5422369663
320PhosphorylationPDKLYASSFSSNHGP
CCHHEEECCCCCCCC		22.4522369663
322PhosphorylationKLYASSFSSNHGPSS
HHEEECCCCCCCCCC		31.9822369663
323PhosphorylationLYASSFSSNHGPSSG
HEEECCCCCCCCCCC		30.7322369663
328PhosphorylationFSSNHGPSSGSFEEE
CCCCCCCCCCCCCCC		52.5022890988
329PhosphorylationSSNHGPSSGSFEEEH
CCCCCCCCCCCCCCC		41.4022369663
331PhosphorylationNHGPSSGSFEEEHTK
CCCCCCCCCCCCCCC		31.2822369663
337PhosphorylationGSFEEEHTKGQTDIN
CCCCCCCCCCCCCCC		39.9022890988
338UbiquitinationSFEEEHTKGQTDINP
CCCCCCCCCCCCCCC		51.4323749301
341PhosphorylationEEHTKGQTDINPFDD
CCCCCCCCCCCCCCC		47.7320377248
349PhosphorylationDINPFDDSRRISNGT
CCCCCCCCCCCCCCC		25.8825521595
353PhosphorylationFDDSRRISNGTFING
CCCCCCCCCCCEECC		27.6522369663
356PhosphorylationSRRISNGTFINGGPG
CCCCCCCCEECCCCC		26.1222369663
365UbiquitinationINGGPGGKNNVLTVV
ECCCCCCCCCEEEEE		51.7923749301
370PhosphorylationGGKNNVLTVVNPDEA
CCCCCEEEEECCCCC		20.3723749301
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 SLG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLG1_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 SLG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROM2_YEASTROM2physical
11113201
MID2_YEASTMID2genetic
10330137
SLT2_YEASTSLT2genetic
9613583
KPC1_YEASTPKC1genetic
12715156
KPC1_YEASTPKC1genetic
9613583
KPC1_YEASTPKC1genetic
9391108
KPC1_YEASTPKC1genetic
9305635
RHO1_YEASTRHO1genetic
9391108
RHO3_YEASTRHO3genetic
9391108
ROM2_YEASTROM2genetic
9613583
STE20_YEASTSTE20genetic
9613583
WSC2_YEASTWSC2genetic
9391108
WSC3_YEASTWSC3genetic
9391108
STH1_YEASTSTH1genetic
12072455
MID2_YEASTMID2genetic
12015967
STT4_YEASTSTT4genetic
12015967
LRG1_YEASTLRG1genetic
11713681
INP51_YEASTINP51genetic
15265867
MID2_YEASTMID2genetic
15470108
BCK1_YEASTBCK1genetic
9613583
RHO3_YEASTRHO3genetic
16514150
RHO4_YEASTRHO4genetic
16514150
MPT5_YEASTMPT5genetic
17172436
MID2_YEASTMID2genetic
17827039
ACK1_YEASTACK1genetic
18806213
MID2_YEASTMID2genetic
15484288
SLT2_YEASTSLT2genetic
20526336
YOL19_YEASTYOL019Wgenetic
20526336
SUR7_YEASTSUR7genetic
20526336
WSC2_YEASTWSC2genetic
20526336
CARP_YEASTPEP4genetic
21708947
KPC1_YEASTPKC1genetic
11554924
RAS2_YEASTRAS2genetic
11589572
WSC4_YEASTWSC4genetic
11589572
BCK1_YEASTBCK1genetic
22747505
SYUA_HUMANSNCAgenetic
22988096
TOS1_YEASTTOS1genetic
23891562
GPI17_YEASTGPI17genetic
23891562
SMI1_YEASTSMI1genetic
23891562
ATC1_YEASTPMR1genetic
23891562
GUP1_YEASTGUP1genetic
23891562
GAS1_YEASTGAS1genetic
23891562
PMT2_YEASTPMT2genetic
23891562
PMT1_YEASTPMT1genetic
23891562
ECM33_YEASTECM33genetic
23891562
KRE1_YEASTKRE1genetic
23891562
CHS5_YEASTCHS5genetic
23891562
CANB_YEASTCNB1genetic
23891562
AYR1_YEASTAYR1genetic
23891562
SPT23_YEASTSPT23genetic
23891562
KIME_YEASTERG12genetic
23891562
SIM1_YEASTSIM1genetic
23891562
GAS3_YEASTGAS3genetic
23891562
MTL1_YEASTMTL1genetic
24260614
FPS1_YEASTFPS1genetic
27607883
ATC3_YEASTDRS2genetic
27708008
BUD14_YEASTBUD14genetic
27708008
AP2A_YEASTAPL3genetic
27708008
DSF2_YEASTDSF2genetic
27708008
RV161_YEASTRVS161genetic
27708008
PER1_YEASTPER1genetic
27708008
ATC4_YEASTDNF2genetic
27708008
SGPL_YEASTDPL1genetic
27708008
SUR2_YEASTSUR2genetic
27708008
SUM1_YEASTSUM1genetic
27708008
RV167_YEASTRVS167genetic
27708008
SNF1_YEASTSNF1genetic
27708008
ERV14_YEASTERV14genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
OSH3_YEASTOSH3genetic
27708008
AP2S_YEASTAPS2genetic
27708008
SPA2_YEASTSPA2genetic
27708008
BUD6_YEASTBUD6genetic
27708008
ERG6_YEASTERG6genetic
27708008
MSG5_YEASTMSG5genetic
27708008
ARL3_YEASTARL3genetic
27708008
PMT2_YEASTPMT2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
RGD1_YEASTRGD1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
PMT1_YEASTPMT1genetic
27708008
ACK1_YEASTACK1genetic
27708008
OST4_YEASTOST4genetic
27708008
YD239_YEASTYDR239Cgenetic
27708008
PAL1_YEASTPAL1genetic
27708008
SXM1_YEASTSXM1genetic
27708008
PP2C2_YEASTPTC2genetic
27708008
PAN2_YEASTPAN2genetic
27708008
PSA3_YEASTPRE9genetic
27708008
FYV8_YEASTFYV8genetic
27708008
ELP2_YEASTELP2genetic
27708008
CCH1_YEASTCCH1genetic
27708008
ERV29_YEASTERV29genetic
27708008
SLT2_YEASTSLT2genetic
27708008
SKN7_YEASTSKN7genetic
27708008
CSK21_YEASTCKA1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
MDM35_YEASTMDM35genetic
27708008
EF1G2_YEASTTEF4genetic
27708008
KTI12_YEASTKTI12genetic
27708008
CANB_YEASTCNB1genetic
27708008
DPH2_YEASTDPH2genetic
27708008
MMP1_YEASTMMP1genetic
27708008
NYV1_YEASTNYV1genetic
27708008
DPH5_YEASTDPH5genetic
27708008
MMR1_YEASTMMR1genetic
27708008
ARV1_YEASTARV1genetic
27708008
MID2_YEASTMID2genetic
27708008
YL346_YEASTYLR346Cgenetic
27708008
ROM2_YEASTROM2genetic
27708008
VID22_YEASTVID22genetic
27708008
ELP1_YEASTIKI3genetic
27708008
VIP1_YEASTVIP1genetic
27708008
ECM7_YEASTECM7genetic
27708008
TMA23_YEASTTMA23genetic
27708008
SCW10_YEASTSCW10genetic
27708008
ELP6_YEASTELP6genetic
27708008
YND5_YEASTYNL035Cgenetic
27708008
YNF8_YEASTYNL058Cgenetic
27708008
MLF3_YEASTMLF3genetic
27708008
PMS1_YEASTPMS1genetic
27708008
YNJ5_YEASTYNL095Cgenetic
27708008
OCA1_YEASTOCA1genetic
27708008
CTU2_YEASTNCS2genetic
27708008
BSC6_YEASTBSC6genetic
27708008
MKK2_YEASTMKK2genetic
27708008
RLF2_YEASTRLF2genetic
27708008
YME1_YEASTYME1genetic
27708008
TIP41_YEASTTIP41genetic
27708008
ROX1_YEASTROX1genetic
27708008
UBA3_YEASTUBA3genetic
27708008
OPY2_YEASTOPY2genetic
27708008
YP078_YEASTYPR078Cgenetic
27708008
CTF4_YEASTCTF4genetic
27708008
OPT2_YEASTOPT2genetic
27708008
ARR3_YEASTARR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLG1_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-331; SER-353 ANDTHR-356, 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-353 AND THR-356, ANDMASS 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 SER-353 AND THR-356, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASSSPECTROMETRY.

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