YG5B_YEAST - dbPTM
YG5B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YG5B_YEAST
UniProt AC P53316
Protein Name Uncharacterized RNA-binding protein YGR250C
Gene Name YGR250C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 781
Subcellular Localization
Protein Description
Protein Sequence MNIAEEPSDEVISSGPEDTDICSQQTSASAEAGDQSIKIERKTSTGLQLEQLANTNLLTIRIKWQLQEEEDDHCNSRITDQIMDTIQHYKGISVNNSDTETYEFLPDTRRLQVLEQNKDIYLYEHGSQEYEKSYKDNEEEDDWRYDTVLQAQFKYPKSLENACTDISELLKSEPIGQHIDKWSIGVNKHALTYPGNIFVGGIAKSLSIGELSFLFSKYGPILSMKLIYDKTKGEPNGYGFISYPLGSQASLCIKELNGRTVNGSTLFINYHVERKERERIHWDHVKENNNDDNFRCLFIGNLPYHNPEKVETLITPKEVIEVIKKELSKKFPDFDIISYYFPKRSNTRSSSSVSFNEEGSVESNKSSNNTNGNAQDEDMLKGYGFIKLINHEQALAAIETFNGFMWHGNRLVVNKAVQHKVYNNHNSHDRHPSISNHNDMEVLEFANNPMYDYNNYTYDRYYFNNNKNGNSNDTSNVRYFDSVRSTPVAEKMDLFYPQRESFSEGRGQRVPRFMGNKFDMYQYPSTSYSLPIPMSNQQESNLYVKHIPLSWTDEDLYDFYKSFGEIISVKVITVGGSKNKYRQQSNDSSSDNDLPVGSSRGYGFVSFESPLDAAKAILNTDGYQVSKDQVLSVSFAQKRGNLSSSDDDDQSQTDNSSKFQNFQPHNDYHKAYPTKYNKKFINALMTQNQSQQQVSRENYFIPLQYPNTNTKPVNSYNLISANQNNANWMMPMFPSFGFIPQVPPVPYIIPPQNPAANHIPIMANGSNEEEEFSSGDYSMDY
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
27PhosphorylationDICSQQTSASAEAGD
CCCCCCCCCCHHHCC		18.8528889911
29PhosphorylationCSQQTSASAEAGDQS
CCCCCCCCHHHCCCE		26.8027214570
43PhosphorylationSIKIERKTSTGLQLE
EEEEEEECCCCCCHH		37.4322369663
44PhosphorylationIKIERKTSTGLQLEQ
EEEEEECCCCCCHHH		24.4222369663
45PhosphorylationKIERKTSTGLQLEQL
EEEEECCCCCCHHHH		47.3322369663
55PhosphorylationQLEQLANTNLLTIRI
CHHHHHHCCEEEEEE		22.9522369663
59PhosphorylationLANTNLLTIRIKWQL
HHHCCEEEEEEEEEC		16.0422369663
218PhosphorylationLSFLFSKYGPILSMK
HHHHHHCHHCEEEEE		27.2522369663
223PhosphorylationSKYGPILSMKLIYDK
HCHHCEEEEEEEEEC		18.0022369663
238PhosphorylationTKGEPNGYGFISYPL
CCCCCCCCCEECEEC		18.5927017623
250PhosphorylationYPLGSQASLCIKELN
EECCCCEEEEEHHHC		19.0127017623
345PhosphorylationSYYFPKRSNTRSSSS
EEECCCCCCCCCCCC		48.9924961812
347PhosphorylationYFPKRSNTRSSSSVS
ECCCCCCCCCCCCEE		32.9224961812
349PhosphorylationPKRSNTRSSSSVSFN
CCCCCCCCCCCEEEC		32.3128889911
350PhosphorylationKRSNTRSSSSVSFNE
CCCCCCCCCCEEECC		24.2824961812
351PhosphorylationRSNTRSSSSVSFNEE
CCCCCCCCCEEECCC		35.6927214570
352PhosphorylationSNTRSSSSVSFNEEG
CCCCCCCCEEECCCC		24.5925752575
354PhosphorylationTRSSSSVSFNEEGSV
CCCCCCEEECCCCCE		25.0528889911
360PhosphorylationVSFNEEGSVESNKSS
EEECCCCCEECCCCC		26.4527017623
366PhosphorylationGSVESNKSSNNTNGN
CCEECCCCCCCCCCC		42.4222369663
367PhosphorylationSVESNKSSNNTNGNA
CEECCCCCCCCCCCC		35.3922369663
370PhosphorylationSNKSSNNTNGNAQDE
CCCCCCCCCCCCCCH		49.0722369663
433PhosphorylationNSHDRHPSISNHNDM
CCCCCCCCCCCCCCH		32.3028889911
435PhosphorylationHDRHPSISNHNDMEV
CCCCCCCCCCCCHHH		36.0528889911
461PhosphorylationNNYTYDRYYFNNNKN
CCCCEEEEEECCCCC		14.9829734811
474PhosphorylationKNGNSNDTSNVRYFD
CCCCCCCCCCCCCCC		26.8424961812
475PhosphorylationNGNSNDTSNVRYFDS
CCCCCCCCCCCCCCC		35.8724961812
479PhosphorylationNDTSNVRYFDSVRST
CCCCCCCCCCCCCCC		13.8822369663
482PhosphorylationSNVRYFDSVRSTPVA
CCCCCCCCCCCCCHH		14.9922369663
485PhosphorylationRYFDSVRSTPVAEKM
CCCCCCCCCCHHHHC		34.6022369663
486PhosphorylationYFDSVRSTPVAEKMD
CCCCCCCCCHHHHCC		15.9522369663
496PhosphorylationAEKMDLFYPQRESFS
HHHCCCCCCCCHHCC		13.0222369663
501PhosphorylationLFYPQRESFSEGRGQ
CCCCCCHHCCCCCCC		35.9422369663
503PhosphorylationYPQRESFSEGRGQRV
CCCCHHCCCCCCCCC		48.7122369663
552PhosphorylationKHIPLSWTDEDLYDF
EECCCCCCCHHHHHH		26.5721440633
573PhosphorylationIISVKVITVGGSKNK
EEEEEEEEECCCCHH		18.9828889911
577PhosphorylationKVITVGGSKNKYRQQ
EEEEECCCCHHCCCC		27.4221440633
581PhosphorylationVGGSKNKYRQQSNDS
ECCCCHHCCCCCCCC		24.0521440633
585PhosphorylationKNKYRQQSNDSSSDN
CHHCCCCCCCCCCCC		33.9822369663
588PhosphorylationYRQQSNDSSSDNDLP
CCCCCCCCCCCCCCC		35.6722369663
589PhosphorylationRQQSNDSSSDNDLPV
CCCCCCCCCCCCCCC		44.5722369663
590PhosphorylationQQSNDSSSDNDLPVG
CCCCCCCCCCCCCCC		44.3722369663
598PhosphorylationDNDLPVGSSRGYGFV
CCCCCCCCCCCCCEE		19.6622369663
599PhosphorylationNDLPVGSSRGYGFVS
CCCCCCCCCCCCEEE		24.6422369663
602PhosphorylationPVGSSRGYGFVSFES
CCCCCCCCCEEEECC		13.2821440633
609PhosphorylationYGFVSFESPLDAAKA
CCEEEECCHHHHHHH		28.8427214570
643PhosphorylationAQKRGNLSSSDDDDQ
EHHHCCCCCCCCCCC		31.6229136822
644PhosphorylationQKRGNLSSSDDDDQS
HHHCCCCCCCCCCCC		40.7429136822
645PhosphorylationKRGNLSSSDDDDQSQ
HHCCCCCCCCCCCCC		41.5029136822
651PhosphorylationSSDDDDQSQTDNSSK
CCCCCCCCCCCCCHH		41.8825521595
653PhosphorylationDDDDQSQTDNSSKFQ
CCCCCCCCCCCHHHC		42.2525521595
656PhosphorylationDQSQTDNSSKFQNFQ
CCCCCCCCHHHCCCC		37.4029136822
657PhosphorylationQSQTDNSSKFQNFQP
CCCCCCCHHHCCCCC		43.6821440633
690PhosphorylationALMTQNQSQQQVSRE
HHHCCCHHHHCHHHH		37.1927214570
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 YG5B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YG5B_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 YG5B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGN1_YEASTSGN1physical
10688190
H2A2_YEASTHTA2physical
16554755
ATPG_YEASTATP3physical
16554755
NOP14_YEASTNOP14physical
16554755
HMO1_YEASTHMO1physical
16554755
RV167_YEASTRVS167physical
16554755
LEUC_YEASTLEU1physical
16554755
YOR1_YEASTYOR1physical
16554755
SGN1_YEASTSGN1physical
16554755
TCPQ_YEASTCCT8physical
16554755
G3P1_YEASTTDH1physical
16554755
OTC_YEASTARG3physical
16554755
U5072_YEASTYML002Wphysical
16554755
GAL80_YEASTGAL80physical
16554755
SEC65_YEASTSEC65physical
16554755
SRP72_YEASTSRP72physical
16554755
PABP_YEASTPAB1physical
16429126
IMDH4_YEASTIMD4physical
16429126
SGN1_YEASTSGN1physical
18467557
PPID_YEASTCPR6physical
18467557
TAD2_YEASTTAD2genetic
19061648
NMD5_YEASTNMD5genetic
19061648
KA120_YEASTKAP120genetic
19061648
PAT1_YEASTPAT1genetic
19061648
EF1A_YEASTTEF2genetic
19061648
XRN1_YEASTXRN1genetic
19061648
TFS2_YEASTDST1genetic
19061648
LSM1_YEASTLSM1genetic
19061648
UAF30_YEASTUAF30genetic
19061648
BRR1_YEASTBRR1genetic
19061648
NCBP2_YEASTCBC2physical
18719252
SGF29_YEASTSGF29genetic
27708008
RTG3_YEASTRTG3genetic
27708008
AGP1_YEASTAGP1genetic
27708008
STE50_YEASTSTE50genetic
27708008
RV161_YEASTRVS161genetic
27708008
RIM1_YEASTRIM1genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
PUS9_YEASTPUS9genetic
27708008
UBP1_YEASTUBP1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
NU133_YEASTNUP133genetic
27708008
ERG6_YEASTERG6genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YG5B_YEAST

loading...

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-27; SER-29; SER-44;THR-45; SER-352; SER-485; THR-486; SER-501 AND SER-651, 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-44 AND SER-501, 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-482; SER-485; THR-486AND SER-501, AND MASS 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-44, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory