SER33_YEAST - dbPTM
SER33_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SER33_YEAST
UniProt AC P40510
Protein Name D-3-phosphoglycerate dehydrogenase 2
Gene Name SER33
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 469
Subcellular Localization
Protein Description Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate..
Protein Sequence MSYSAADNLQDSFQRAMNFSGSPGAVSTSPTQSFMNTLPRRVSITKQPKALKPFSTGDMNILLLENVNATAIKIFKDQGYQVEFHKSSLPEDELIEKIKDVHAIGIRSKTRLTEKILQHARNLVCIGCFCIGTNQVDLKYAASKGIAVFNSPFSNSRSVAELVIGEIISLARQLGDRSIELHTGTWNKVAARCWEVRGKTLGIIGYGHIGSQLSVLAEAMGLHVLYYDIVTIMALGTARQVSTLDELLNKSDFVTLHVPATPETEKMLSAPQFAAMKDGAYVINASRGTVVDIPSLIQAVKANKIAGAALDVYPHEPAKNGEGSFNDELNSWTSELVSLPNIILTPHIGGSTEEAQSSIGIEVATALSKYINEGNSVGSVNFPEVSLKSLDYDQENTVRVLYIHRNVPGVLKTVNDILSDHNIEKQFSDSHGEIAYLMADISSVNQSEIKDIYEKLNQTSAKVSIRLLY
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
2Phosphorylation------MSYSAADNL
------CCCCHHHHH		28.0022369663
2Acetylation------MSYSAADNL
------CCCCHHHHH		28.0022814378
3Phosphorylation-----MSYSAADNLQ
-----CCCCHHHHHH		10.8829136822
4Phosphorylation----MSYSAADNLQD
----CCCCHHHHHHH		15.0722369663
12PhosphorylationAADNLQDSFQRAMNF
HHHHHHHHHHHHHCC		15.4329136822
17OxidationQDSFQRAMNFSGSPG
HHHHHHHHCCCCCCC		5.9215665377
20PhosphorylationFQRAMNFSGSPGAVS
HHHHHCCCCCCCCCC		33.1022369663
22PhosphorylationRAMNFSGSPGAVSTS
HHHCCCCCCCCCCCC		20.9722369663
27PhosphorylationSGSPGAVSTSPTQSF
CCCCCCCCCCCCHHH		23.7222890988
28PhosphorylationGSPGAVSTSPTQSFM
CCCCCCCCCCCHHHH		31.9322369663
29PhosphorylationSPGAVSTSPTQSFMN
CCCCCCCCCCHHHHH		20.6022369663
31PhosphorylationGAVSTSPTQSFMNTL
CCCCCCCCHHHHHCC		36.2922369663
33PhosphorylationVSTSPTQSFMNTLPR
CCCCCCHHHHHCCCC		29.0122890988
35OxidationTSPTQSFMNTLPRRV
CCCCHHHHHCCCCCE		4.5415665377
37PhosphorylationPTQSFMNTLPRRVSI
CCHHHHHCCCCCEEC		26.7622890988
43PhosphorylationNTLPRRVSITKQPKA
HCCCCCEECCCCCCC		23.8022369663
45PhosphorylationLPRRVSITKQPKALK
CCCCEECCCCCCCCC		19.0022369663
86AcetylationGYQVEFHKSSLPEDE
CCEEEEEHHCCCHHH		47.2424489116
97AcetylationPEDELIEKIKDVHAI
CHHHHHHHHHHHHHC		48.3224489116
115AcetylationSKTRLTEKILQHARN
CCCCCHHHHHHHHHH		43.4022865919
188UbiquitinationLHTGTWNKVAARCWE
EECCCHHHHHHHHHE		25.4717644757
242PhosphorylationLGTARQVSTLDELLN
HCCHHCCCCHHHHHC		18.2128889911
243PhosphorylationGTARQVSTLDELLNK
CCHHCCCCHHHHHCC		39.1030377154
250UbiquitinationTLDELLNKSDFVTLH
CHHHHHCCCCCEEEE		51.9124961812
261PhosphorylationVTLHVPATPETEKML
EEEECCCCHHHHHHH		18.6522369663
264PhosphorylationHVPATPETEKMLSAP
ECCCCHHHHHHHCCH		41.9522369663
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 SER33_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SER33_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 SER33_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SERA_YEASTSER3physical
10688190
SER33_YEASTSER33physical
10688190
SER33_YEASTSER33physical
11283351
SERA_YEASTSER3physical
18719252
SER33_YEASTSER33physical
18719252
SERA_YEASTSER3genetic
18408719
RQC2_YEASTTAE2genetic
20691087
SERA_YEASTSER3physical
20826334
GGPPS_YEASTBTS1genetic
21623372
FCY22_YEASTFCY22genetic
18192430
TPO2_YEASTTPO2genetic
18192430
ATP11_YEASTATP11genetic
18192430
RXT2_YEASTRXT2genetic
18192430
CGR1_YEASTCGR1genetic
18192430
PP11_YEASTSIT4genetic
18192430
PP4R2_YEASTPSY4genetic
18192430
TAF12_YEASTTAF12genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
GPI8_YEASTGPI8genetic
27708008
RSP5_YEASTRSP5genetic
27708008
ACT_YEASTACT1genetic
27708008
NUP57_YEASTNUP57genetic
27708008
COFI_YEASTCOF1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
UTP15_YEASTUTP15genetic
27708008
CAP_YEASTSRV2genetic
27708008
GLYC_YEASTSHM2physical
26527276
SET1_YEASTSET1physical
26527276
KPYK1_YEASTCDC19physical
26527276
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SER33_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-22; THR-28; SER-29 ANDTHR-31, 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-22, AND MASSSPECTROMETRY.

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