NSG2_YEAST - dbPTM
NSG2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSG2_YEAST
UniProt AC P53898
Protein Name Protein NSG2
Gene Name NSG2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 299
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-dependent degradation. Binds directly to the sterol-sensing domain (SSD)-containing transmembrane region of HMG2, promoting its folding to protect it from degradation..
Protein Sequence MANRGEPDPKKSTESICSLTKPQLYSLYDDDVVRSEDNEIYEELKRSVSIDSTKYSRDQTIDSTFYLAHKVGGSLPRNTVSSNNLERILSASSIHENFPSRTRQTRQNILHYLQAVLILSLSGFAYHELSRNLHDNHLLHPDFASRPLLLGVKLCNWLSNGVLPNWLGYGVEGLLFGSVVPILDNIFQTEVVKSSVHHDSLTSVIRSINAMLGVTFGIRKIQWNSSLQAAGAWGLLNIILWLFFDGSISMLMSCICIGVGCCISCYKDIIDGSQFLYFMDFYFLGSLMFGKLGRYLYSH
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
12PhosphorylationGEPDPKKSTESICSL
CCCCCCCCHHHHHHC		43.4617330950
13PhosphorylationEPDPKKSTESICSLT
CCCCCCCHHHHHHCC		42.5017330950
15PhosphorylationDPKKSTESICSLTKP
CCCCCHHHHHHCCCH		29.0517330950
18PhosphorylationKSTESICSLTKPQLY
CCHHHHHHCCCHHHH		37.0917330950
20PhosphorylationTESICSLTKPQLYSL
HHHHHHCCCHHHHHC		25.1217330950
25PhosphorylationSLTKPQLYSLYDDDV
HCCCHHHHHCCCCCC		7.4419795423
26PhosphorylationLTKPQLYSLYDDDVV
CCCHHHHHCCCCCCC		29.1019795423
28PhosphorylationKPQLYSLYDDDVVRS
CHHHHHCCCCCCCCC		16.0419779198
35PhosphorylationYDDDVVRSEDNEIYE
CCCCCCCCCCHHHHH		37.3821440633
41PhosphorylationRSEDNEIYEELKRSV
CCCCHHHHHHHHHHC		9.3629688323
45AcetylationNEIYEELKRSVSIDS
HHHHHHHHHHCCCCC		46.0024489116
47PhosphorylationIYEELKRSVSIDSTK
HHHHHHHHCCCCCCC		20.7322890988
49PhosphorylationEELKRSVSIDSTKYS
HHHHHHCCCCCCCCC		23.1725521595
52PhosphorylationKRSVSIDSTKYSRDQ
HHHCCCCCCCCCCCC		25.7325521595
53PhosphorylationRSVSIDSTKYSRDQT
HHCCCCCCCCCCCCC		30.1919823750
55PhosphorylationVSIDSTKYSRDQTID
CCCCCCCCCCCCCCC		14.7129136822
56PhosphorylationSIDSTKYSRDQTIDS
CCCCCCCCCCCCCCH		30.8229136822
60PhosphorylationTKYSRDQTIDSTFYL
CCCCCCCCCCHHHHH		30.9228889911
63PhosphorylationSRDQTIDSTFYLAHK
CCCCCCCHHHHHHHH		19.3023749301
64PhosphorylationRDQTIDSTFYLAHKV
CCCCCCHHHHHHHHH		16.7324961812
66PhosphorylationQTIDSTFYLAHKVGG
CCCCHHHHHHHHHCC		11.7629688323
70AcetylationSTFYLAHKVGGSLPR
HHHHHHHHHCCCCCC		36.6524489116
70UbiquitinationSTFYLAHKVGGSLPR
HHHHHHHHHCCCCCC		36.6524961812
74PhosphorylationLAHKVGGSLPRNTVS
HHHHHCCCCCCCCCC		29.3125752575
79PhosphorylationGGSLPRNTVSSNNLE
CCCCCCCCCCCCHHH		24.0422890988
81PhosphorylationSLPRNTVSSNNLERI
CCCCCCCCCCHHHHH		25.8822369663
82PhosphorylationLPRNTVSSNNLERIL
CCCCCCCCCHHHHHH		25.9622890988
90PhosphorylationNNLERILSASSIHEN
CHHHHHHHHHHHHHC		24.5922369663
92PhosphorylationLERILSASSIHENFP
HHHHHHHHHHHHCCC		26.8422369663
93PhosphorylationERILSASSIHENFPS
HHHHHHHHHHHCCCC		27.9022369663
100PhosphorylationSIHENFPSRTRQTRQ
HHHHCCCCCCHHHHH		41.9922890988
195PhosphorylationQTEVVKSSVHHDSLT
CCCHHHHHCCHHHHH		21.5427017623
200PhosphorylationKSSVHHDSLTSVIRS
HHHCCHHHHHHHHHH		29.2327017623
215PhosphorylationINAMLGVTFGIRKIQ
HHHHHCCCCCEEEEE		17.8528889911
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 NSG2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSG2_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 NSG2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UPPS_YEASTNUS1genetic
16269340
PGA14_YEASTYNL190Wgenetic
16269340
YNT4_YEASTYNL194Cgenetic
16269340
ALG9_YEASTALG9genetic
16269340
ARF1_YEASTARF1genetic
16269340
ARV1_YEASTARV1genetic
16269340
AGP2_YEASTAGP2genetic
20093466
MTU1_YEASTSLM3genetic
20093466
PP2C2_YEASTPTC2genetic
20093466
MUP1_YEASTMUP1genetic
20093466
UPPS_YEASTNUS1genetic
21987634
DOP1_YEASTDOP1genetic
21987634
MS116_YEASTMSS116genetic
21987634
GEP4_YEASTGEP4genetic
21987634
PGA14_YEASTYNL190Wgenetic
21987634
ALG9_YEASTALG9genetic
21987634
SQS1_YEASTSQS1genetic
21987634
URE2_YEASTURE2genetic
21987634
G6PD_YEASTZWF1genetic
21987634
IDH2_YEASTIDH2physical
22940862
ATC4_YEASTDNF2genetic
23891562
BCS1_YEASTBCS1genetic
27708008
AGP2_YEASTAGP2genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
TPS2_YEASTTPS2genetic
27708008
MUP1_YEASTMUP1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
DAL81_YEASTDAL81genetic
27708008
LST4_YEASTLST4genetic
27708008
YM79_YEASTYMR244Wgenetic
27708008
PMA2_YEASTPMA2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSG2_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-12; SER-15; SER-18;SER-49; SER-52; THR-53; SER-81; SER-82; SER-90 AND SER-93, AND MASSSPECTROMETRY.
"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-90; SER-92 AND SER-93,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 SER-90, AND MASSSPECTROMETRY.
"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-49 AND THR-53, AND MASSSPECTROMETRY.
"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 SER-49; SER-52; SER-90 ANDSER-93, AND MASS SPECTROMETRY.

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