SRP40_YEAST - dbPTM
SRP40_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRP40_YEAST
UniProt AC P32583
Protein Name Suppressor protein SRP40
Gene Name SRP40
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 406
Subcellular Localization
Protein Description Not known; weak suppressor of a mutant of the subunit AC40 of DNA dependent RNA polymerase I and III..
Protein Sequence MASKKIKVDEVPKLSVKEKEIEEKSSSSSSSSSSSSSSSSSSSSSSSSSGESSSSSSSSSSSSSSDSSDSSDSESSSSSSSSSSSSSSSSDSESSSESDSSSSGSSSSSSSSSDESSSESESEDETKKRARESDNEDAKETKKAKTEPESSSSSESSSSGSSSSSESESGSESDSDSSSSSSSSSDSESDSESDSQSSSSSSSSDSSSDSDSSSSDSSSDSDSSSSSSSSSSDSDSDSDSSSDSDSSGSSDSSSSSDSSSDESTSSDSSDSDSDSDSGSSSELETKEATADESKAEETPASSNESTPSASSSSSANKLNIPAGTDEIKEGQRKHFSRVDRSKINFEAWELTDNTYKGAAGTWGEKANEKLGRVRGKDFTKNKNKMKRGSYRGGSITLESGSYKFQD
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
13AcetylationIKVDEVPKLSVKEKE
CCCCCCCCCCCCHHH		59.5824489116
133PhosphorylationTKKRARESDNEDAKE
HHHHHHHCCCHHHHH		39.9325521595
141PhosphorylationDNEDAKETKKAKTEP
CCHHHHHHHHHCCCC		36.8219684113
289PhosphorylationELETKEATADESKAE
HHHHHHCCCCHHHHH		35.4117330950
293PhosphorylationKEATADESKAEETPA
HHCCCCHHHHHCCCC		37.4020377248
298PhosphorylationDESKAEETPASSNES
CHHHHHCCCCCCCCC		18.7022369663
301PhosphorylationKAEETPASSNESTPS
HHHCCCCCCCCCCCC		34.5922369663
302PhosphorylationAEETPASSNESTPSA
HHCCCCCCCCCCCCC		46.8822369663
305PhosphorylationTPASSNESTPSASSS
CCCCCCCCCCCCCCC		50.2820377248
306PhosphorylationPASSNESTPSASSSS
CCCCCCCCCCCCCCC		18.3222369663
308PhosphorylationSSNESTPSASSSSSA
CCCCCCCCCCCCCCC		40.6522369663
310PhosphorylationNESTPSASSSSSANK
CCCCCCCCCCCCCCC		34.7822369663
311PhosphorylationESTPSASSSSSANKL
CCCCCCCCCCCCCCC		33.6822369663
312PhosphorylationSTPSASSSSSANKLN
CCCCCCCCCCCCCCC		26.3022369663
313PhosphorylationTPSASSSSSANKLNI
CCCCCCCCCCCCCCC		35.1022369663
314PhosphorylationPSASSSSSANKLNIP
CCCCCCCCCCCCCCC		37.5020377248
317AcetylationSSSSSANKLNIPAGT
CCCCCCCCCCCCCCC		42.5022865919
365AcetylationAAGTWGEKANEKLGR
CCCCHHHHHHHHHHC		53.2025381059
369AcetylationWGEKANEKLGRVRGK
HHHHHHHHHHCCCCC		56.9225381059
389PhosphorylationKNKMKRGSYRGGSIT
CCCCCCCCCCCCCEE		18.7117287358
390PhosphorylationNKMKRGSYRGGSITL
CCCCCCCCCCCCEEE		18.9919823750
394PhosphorylationRGSYRGGSITLESGS
CCCCCCCCEEEECCC		18.4122369663
396PhosphorylationSYRGGSITLESGSYK
CCCCCCEEEECCCEE		26.6022369663
399PhosphorylationGGSITLESGSYKFQD
CCCEEEECCCEECCC		35.8319823750
401PhosphorylationSITLESGSYKFQD--
CEEEECCCEECCC--		34.1319823750
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRP40_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 SRP40_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSM5_YEASTLSM5genetic
12700234
C1TC_YEASTADE3genetic
12700234
GLYC_YEASTSHM2genetic
12700234
FBRL_YEASTNOP1physical
16554755
YRA1_YEASTYRA1physical
16554755
PPN1_YEASTPPN1physical
16554755
PRP43_YEASTPRP43physical
16554755
NOP56_YEASTNOP56physical
16554755
NOP58_YEASTNOP58physical
16554755
SSF1_YEASTSSF1genetic
17314980
REI1_YEASTREI1genetic
17314980
WHI4_YEASTWHI4genetic
17314980
RT107_YEASTRTT107genetic
17314980
CF130_YEASTCAF130genetic
17314980
SDS3_YEASTSDS3genetic
17314980
PRI1_YEASTPRI1genetic
17314980
RPB4_YEASTRPB4genetic
17314980
XRN1_YEASTXRN1genetic
17314980
PFD3_YEASTPAC10genetic
17314980
YC16_YEASTYCR087C-Aphysical
11283351
HMO1_YEASTHMO1physical
11283351
YKC3_YEASTYKL023Wphysical
11283351
DBP2_YEASTDBP2physical
18467557
SLS1_YEASTSLS1genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
IF4F1_YEASTTIF4631genetic
19061648
TMA23_YEASTTMA23genetic
19061648
FKBP_YEASTFPR1genetic
19061648
SSB1_YEASTSSB1physical
19536198
UBP3_YEASTUBP3genetic
19547744
CSG2_YEASTCSG2genetic
20093466
PAT1_YEASTPAT1genetic
20093466
SPR28_YEASTSPR28genetic
20093466
RL29_YEASTRPL29genetic
20093466
PIH1_YEASTPIH1genetic
20093466
SSF1_YEASTSSF1genetic
20093466
OSH3_YEASTOSH3genetic
20093466
NAM8_YEASTNAM8genetic
20093466
RM49_YEASTMRP49genetic
20093466
LDB18_YEASTLDB18genetic
20093466
ERG3_YEASTERG3genetic
20093466
MSC1_YEASTMSC1genetic
20093466
ERG6_YEASTERG6genetic
20093466
PALI_YEASTRIM9genetic
20093466
SAP30_YEASTSAP30genetic
20093466
SCS7_YEASTSCS7genetic
20093466
JNM1_YEASTJNM1genetic
20093466
CYB5_YEASTCYB5genetic
20093466
SWS2_YEASTSWS2genetic
20093466
RCF2_YEASTRCF2genetic
20093466
ATP23_YEASTATP23genetic
20093466
ZEO1_YEASTZEO1genetic
20093466
REXO4_YEASTREX4genetic
20093466
NOP12_YEASTNOP12genetic
20093466
MDM12_YEASTMDM12genetic
20093466
YORA4_YEASTYOR114Wgenetic
20093466
MSS18_YEASTMSS18genetic
20093466
UAP1_YEASTQRI1genetic
27708008
ACT_YEASTACT1genetic
27708008
XPO1_YEASTCRM1genetic
27708008
ABF1_YEASTABF1genetic
27708008
CAP_YEASTSRV2genetic
27708008
SAP30_YEASTSAP30genetic
27708008
LSM7_YEASTLSM7genetic
27708008
MAK16_YEASTMAK16genetic
27708008
CDC10_YEASTCDC10genetic
27708008
APC11_YEASTAPC11genetic
27708008
FBRL_YEASTNOP1genetic
27708008
NSE4_YEASTNSE4genetic
27708008
NHP2_YEASTNHP2genetic
27708008
MAK21_YEASTMAK21genetic
27708008
RS13_YEASTRPS13genetic
27708008
TFC6_YEASTTFC6genetic
27708008
UTP5_YEASTUTP5genetic
27708008
MOB2_YEASTMOB2genetic
27708008
PMM_YEASTSEC53genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PRP43_YEASTPRP43genetic
27708008
COPB2_YEASTSEC27genetic
27708008
BCD1_YEASTBCD1genetic
27708008
RPF1_YEASTRPF1genetic
27708008
MET30_YEASTMET30genetic
27708008
SHQ1_YEASTSHQ1genetic
27708008
CYAA_YEASTCYR1genetic
27708008
EXO70_YEASTEXO70genetic
27708008
NNF1_YEASTNNF1genetic
27708008
NOP56_YEASTNOP56genetic
27708008
DBP9_YEASTDBP9genetic
27708008
RU1C_YEASTYHC1genetic
27708008
ERO1_YEASTERO1genetic
27708008
RNT1_YEASTRNT1genetic
27708008
HAS1_YEASTHAS1genetic
27708008
RLP7_YEASTRLP7genetic
27708008
NOP2_YEASTNOP2genetic
27708008
DPOA_YEASTPOL1genetic
27708008
UTP23_YEASTUTP23genetic
27708008
XRN2_YEASTRAT1genetic
27708008
UFE1_YEASTUFE1genetic
27708008
RPB2_YEASTRPB2genetic
27708008
MED4_YEASTMED4genetic
27708008
NIP7_YEASTNIP7genetic
27708008
ATC3_YEASTDRS2genetic
27708008
CSG2_YEASTCSG2genetic
27708008
REI1_YEASTREI1genetic
27708008
MAF1_YEASTMAF1genetic
27708008
YD124_YEASTYDR124Wgenetic
27708008
NUM1_YEASTNUM1genetic
27708008
SHE9_YEASTSHE9genetic
27708008
AST2_YEASTAST2genetic
27708008
RL29_YEASTRPL29genetic
27708008
PIH1_YEASTPIH1genetic
27708008
SSF1_YEASTSSF1genetic
27708008
OSH3_YEASTOSH3genetic
27708008
NAM8_YEASTNAM8genetic
27708008
PHO86_YEASTPHO86genetic
27708008
BCA2_YEASTBAT2genetic
27708008
COXM1_YEASTCMC1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
RM49_YEASTMRP49genetic
27708008
ERG3_YEASTERG3genetic
27708008
SIC1_YEASTSIC1genetic
27708008
ERG6_YEASTERG6genetic
27708008
RCF1_YEASTRCF1genetic
27708008
PALI_YEASTRIM9genetic
27708008
SCS7_YEASTSCS7genetic
27708008
SWS2_YEASTSWS2genetic
27708008
CYB5_YEASTCYB5genetic
27708008
ATP23_YEASTATP23genetic
27708008
RRP6_YEASTRRP6genetic
27708008
YORA4_YEASTYOR114Wgenetic
27708008
COQ7_YEASTCAT5genetic
27708008
DCI1_YEASTDCI1genetic
27708008
PALA_YEASTRIM20genetic
27708008
YP162_YEASTYPL162Cgenetic
27708008
MSS18_YEASTMSS18genetic
27708008
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRP40_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-394, 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 THR-289; SER-293; SER-301;SER-308 AND SER-313, AND MASS 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-133; SER-389 ANDSER-394, 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 THR-289, AND MASSSPECTROMETRY.

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