YL149_YEAST - dbPTM
YL149_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YL149_YEAST
UniProt AC Q99296
Protein Name Uncharacterized protein YLR149C
Gene Name YLR149C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 730
Subcellular Localization
Protein Description
Protein Sequence MTIDGTGQSKEALQDERLNTGSDKVYQNYMMPALELYDAKVSINHWQLRDCIKPGSMNQSKLYYIYDHSIRVLDTDSSVLRSPVRRHNSIQPSNSGKNSTEKTSTKGSRTTGSYISKNLHVPSEKLVEFNFKPRCFTELNGLTVCGGLIGSDDKGFPSNWNRLAQDANISLPPPSQPINISKNISFPINSHYSNPNIWKGIVEFYNQETDTMMTFTLGQFINNCVTLYDRASMQFDLFACNNDGHLYQCDVSNRDVTLVKRYADLKFPLNNASLSHDGQTMVVSGDSNKFAVYNQNELTNQFSLHYDNHPSWGSSVNRVRRIPRFALPDESEYIENIYEAPNSDHGFYNSFSENDLQFATVFQNGTCAIYDIRNMATPMAEISSTRPHSHNGAFRVCRFSYGLDDLLFISEHQGRVHVVDTRNYVNHQVIVIPDKVNMEYINERKHNTNHNFTTNNNNENESNDSKNELQGADYRSLSRRRFSLPSMPNVTTEPWITMAQRIPKKYLEPQILPFPKVMDKISNESVLFSTKGSSSSDVAHPYKRRCSFRVRRVSTSAPTADYSNNNVNASLGTPAADSIATSSSNSAPQNLIDPLILSHQQASNDVFEDDEYYEAYNDVHSTYRVSSDYHGVSARAFESFLRPPSTPDLPSDDDNFAANSRNNRGTSNFLRRPVITTQESNEFSEENNISGIDWVEDRNGSSLIIGTDYGIMRWNINSWARRSFSSYDLC
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
77PhosphorylationIRVLDTDSSVLRSPV
EEEECCCCCHHCCCC
25.1621440633
78PhosphorylationRVLDTDSSVLRSPVR
EEECCCCCHHCCCCC
28.1619779198
82PhosphorylationTDSSVLRSPVRRHNS
CCCCHHCCCCCCCCC
24.4817330950
89PhosphorylationSPVRRHNSIQPSNSG
CCCCCCCCCCCCCCC
19.2421082442
483PhosphorylationSLSRRRFSLPSMPNV
HHHCCCCCCCCCCCC
37.2422369663
486PhosphorylationRRRFSLPSMPNVTTE
CCCCCCCCCCCCCCC
52.7622369663
491PhosphorylationLPSMPNVTTEPWITM
CCCCCCCCCCCCCHH
31.8922369663
492PhosphorylationPSMPNVTTEPWITMA
CCCCCCCCCCCCHHH
35.4522369663
497PhosphorylationVTTEPWITMAQRIPK
CCCCCCCHHHHHCCH
11.5522369663
522PhosphorylationPKVMDKISNESVLFS
CHHHHCCCCCEEEEE
40.0430377154
525PhosphorylationMDKISNESVLFSTKG
HHCCCCCEEEEECCC
28.5028889911
533PhosphorylationVLFSTKGSSSSDVAH
EEEECCCCCCCCCCC
28.7122369663
534PhosphorylationLFSTKGSSSSDVAHP
EEECCCCCCCCCCCC
42.4022369663
535PhosphorylationFSTKGSSSSDVAHPY
EECCCCCCCCCCCCC
32.0522369663
536PhosphorylationSTKGSSSSDVAHPYK
ECCCCCCCCCCCCCC
37.7422369663
639PhosphorylationVSARAFESFLRPPST
CCHHHHHHHCCCCCC
24.1122369663
645PhosphorylationESFLRPPSTPDLPSD
HHHCCCCCCCCCCCC
56.0822369663
646PhosphorylationSFLRPPSTPDLPSDD
HHCCCCCCCCCCCCC
26.9622369663
651PhosphorylationPSTPDLPSDDDNFAA
CCCCCCCCCCCCCCC
62.0522369663
660PhosphorylationDDNFAANSRNNRGTS
CCCCCCCCCCCCCCC
31.4922369663
723PhosphorylationINSWARRSFSSYDLC
HHHHHHHHCCCCCCC
24.7523749301
726PhosphorylationWARRSFSSYDLC---
HHHHHCCCCCCC---
22.2130377154

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 YL149_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YL149_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 YL149_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGF29_YEASTSGF29genetic
27708008
NAA38_YEASTMAK31genetic
27708008
FUB1_YEASTFUB1genetic
27708008
PDP2_YEASTPTC6genetic
27708008
AHC2_YEASTAHC2genetic
27708008
RTK1_YEASTRTK1genetic
27708008
UGX2_YEASTUGX2genetic
27708008
VPS41_YEASTVPS41genetic
27708008
RM01_YEASTMRPL1genetic
27708008
PEF1_YEASTPEF1genetic
27708008
ETR1_YEASTETR1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
SDS24_YEASTSDS24genetic
27708008
SWC5_YEASTSWC5genetic
27708008
VHC1_YEASTVHC1genetic
27708008
DPB3_YEASTDPB3genetic
27708008
YCE2_YEASTYCL042Wgenetic
27708008
RIM1_YEASTRIM1genetic
27708008
ELO2_YEASTELO2genetic
27708008
THRC_YEASTTHR4genetic
27708008
CYPR_YEASTCPR4genetic
27708008
YCZ0_YEASTYCR100Cgenetic
27708008
YCZ2_YEASTYCR102Cgenetic
27708008
PEX19_YEASTPEX19genetic
27708008
VAM6_YEASTVAM6genetic
27708008
CYK3_YEASTCYK3genetic
27708008
YD129_YEASTYDL129Wgenetic
27708008
YD144_YEASTYDL144Cgenetic
27708008
UGA3_YEASTUGA3genetic
27708008
YD180_YEASTYDL180Wgenetic
27708008
UPS3_YEASTUPS3genetic
27708008
SGPL_YEASTDPL1genetic
27708008
BCS1_YEASTBCS1genetic
27708008
SAC7_YEASTSAC7genetic
27708008
UBP3_YEASTUBP3genetic
27708008
ODPA_YEASTPDA1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
ASF1_YEASTASF1genetic
27708008
MMS22_YEASTMMS22genetic
27708008
SRC1_YEASTSRC1genetic
27708008
SDHF2_YEASTSDH5genetic
27708008
NACB1_YEASTEGD1genetic
27708008
PPQ1_YEASTPPQ1genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
DOM34_YEASTDOM34genetic
29158977

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YL149_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-82; SER-89; SER-525;SER-651 AND SER-723, 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-89; SER-645; THR-646 ANDSER-651, 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-82, AND MASSSPECTROMETRY.

TOP