YKR18_YEAST - dbPTM
YKR18_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YKR18_YEAST
UniProt AC P36114
Protein Name IML2-like protein YKR018C
Gene Name YKR018C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 725
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MFKVFGFGAKEEIPELSQEEKTKAILKQAHDFEQALRAMDYVLDDNADEGLALLDESDAKEASDQTINALARGVIEFLEATLGFEAEEMKKASATLAKAEALSLKSRERAQKIGLKSSSLYPPGTVYAVTYTESCLLHALLMIFSESMMEAAKAILKLRKSYYMLQEILETIKAANKAKKLKITSGSEDKESTPATFITGGDAFNSVDIPYELTPEEQKDKDLLQFAEQIHSMRTERLSGAHIGNSPAINRLRGELGLQAMEDLPEEEITDHKVLSDDIDLSQATIDEFVHSGVNLCFGILQVVISLLPPAIGAVLSVVGFRGSREEGLRLVWKATKQRNVHGCIGLLALMFYYDGPFQFTDDDFDIPAAVKDSSNSEDSEDEEMDGPTLLHPGKILEDALLQSRALFPNSALWLLNEARMLSGKGRLEEAVALMDSIDVSKIRMRQVKSLMIFDRAITLIHLHQYDRAAEDILSLLDISDWSHAFYTYFAGCCYLENWRMCEMGLMKSDKKDEYQKKAEELIFTSVNLLGKKTFKSKNLPLDRFILRKVEQFKAKKEELGVENPLDGIATSPVHEIAYFYNGYNRMSEEHLELTKKMLTEYRNPAIEALDSDQELIKDLLVSLTLRRLGHIQEGCDILDEKVLPKFFSIQNGKVKYIKKTEDPWAYPTALYERALFTWKLEGMDGLPESKEWLLRAQGYADDYELSTRVGMKIKAAIDRVDHSL
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
3Acetylation-----MFKVFGFGAK
-----CCCEECCCCC		35.0424489116
3Ubiquitination-----MFKVFGFGAK
-----CCCEECCCCC		35.0424961812
10AcetylationKVFGFGAKEEIPELS
CEECCCCCHHCCCCC		57.1524489116
10UbiquitinationKVFGFGAKEEIPELS
CEECCCCCHHCCCCC		57.1523749301
103PhosphorylationLAKAEALSLKSRERA
HHHHHHHHHHHHHHH		40.5819795423
112AcetylationKSRERAQKIGLKSSS
HHHHHHHHHCCCCCC		37.4425381059
184PhosphorylationKAKKLKITSGSEDKE
HHHCCCCCCCCCCCC		26.0030377154
185PhosphorylationAKKLKITSGSEDKES
HHCCCCCCCCCCCCC		43.7428889911
187PhosphorylationKLKITSGSEDKESTP
CCCCCCCCCCCCCCC		42.2521440633
190UbiquitinationITSGSEDKESTPATF
CCCCCCCCCCCCCEE		49.8924961812
192PhosphorylationSGSEDKESTPATFIT
CCCCCCCCCCCEEEE		45.4922369663
193PhosphorylationGSEDKESTPATFITG
CCCCCCCCCCEEEEC		20.3120377248
196PhosphorylationDKESTPATFITGGDA
CCCCCCCEEEECCCC		19.4420377248
199PhosphorylationSTPATFITGGDAFNS
CCCCEEEECCCCCCC		30.8122369663
206PhosphorylationTGGDAFNSVDIPYEL
ECCCCCCCCCCCCCC		18.0822369663
211PhosphorylationFNSVDIPYELTPEEQ
CCCCCCCCCCCHHHH		24.7329136822
219UbiquitinationELTPEEQKDKDLLQF
CCCHHHHHCHHHHHH		70.7624961812
221UbiquitinationTPEEQKDKDLLQFAE
CHHHHHCHHHHHHHH		58.2624961812
239PhosphorylationSMRTERLSGAHIGNS
HHCHHHCCCCCCCCC		39.9129136822
246PhosphorylationSGAHIGNSPAINRLR
CCCCCCCCHHHHHHH		15.5322369663
374PhosphorylationIPAAVKDSSNSEDSE
CCCHHCCCCCCCCCC		26.2122890988
375PhosphorylationPAAVKDSSNSEDSED
CCHHCCCCCCCCCCC		55.2822369663
377PhosphorylationAVKDSSNSEDSEDEE
HHCCCCCCCCCCCCC		44.7422369663
380PhosphorylationDSSNSEDSEDEEMDG
CCCCCCCCCCCCCCC		42.7822369663
389PhosphorylationDEEMDGPTLLHPGKI
CCCCCCCCCCCCCHH		47.7022890988
425UbiquitinationEARMLSGKGRLEEAV
HHHHHCCCCCHHHHH		37.1719722269
508UbiquitinationMCEMGLMKSDKKDEY
CHHHCCCCCCCHHHH		61.6223749301
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 YKR18_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YKR18_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 YKR18_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECM33_YEASTECM33genetic
20093466
UBC4_YEASTUBC4genetic
20093466
TPS1_YEASTTPS1genetic
20093466
CCZ1_YEASTCCZ1genetic
20093466
SGF29_YEASTSGF29genetic
20093466
RV161_YEASTRVS161genetic
20093466
FUB1_YEASTFUB1genetic
20093466
MTU1_YEASTSLM3genetic
20093466
YD042_YEASTYDR042Cgenetic
20093466
VMS1_YEASTVMS1genetic
20093466
MNN10_YEASTMNN10genetic
20093466
GNTK_YEASTYDR248Cgenetic
20093466
IPK1_YEASTIPK1genetic
20093466
LSM6_YEASTLSM6genetic
20093466
EF2_YEASTEFT2genetic
20093466
RS17B_YEASTRPS17Bgenetic
20093466
SDC1_YEASTSDC1genetic
20093466
SAK1_YEASTSAK1genetic
20093466
PEA2_YEASTPEA2genetic
20093466
ODPA_YEASTPDA1genetic
20093466
YFF2_YEASTYFL052Wgenetic
20093466
IES1_YEASTIES1genetic
20093466
RTG2_YEASTRTG2genetic
20093466
RTF1_YEASTRTF1genetic
20093466
AAKG_YEASTSNF4genetic
20093466
MPC1_YEASTMPC1genetic
20093466
PALF_YEASTRIM8genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
PACC_YEASTRIM101genetic
20093466
MED20_YEASTSRB2genetic
20093466
PTPA1_YEASTRRD1genetic
20093466
RPI1_YEASTRPI1genetic
20093466
FIS1_YEASTFIS1genetic
20093466
GSH1_YEASTGSH1genetic
20093466
IML2_YEASTIML2genetic
20093466
CYP7_YEASTCPR7genetic
20093466
DOA1_YEASTDOA1genetic
20093466
DNM1_YEASTDNM1genetic
20093466
RS3A1_YEASTRPS1Agenetic
20093466
RIM13_YEASTRIM13genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
SCS7_YEASTSCS7genetic
20093466
TOP1_YEASTTOP1genetic
20093466
SGT2_YEASTSGT2genetic
20093466
VHS3_YEASTVHS3genetic
20093466
SUR1_YEASTSUR1genetic
20093466
LCL1_YEASTLCL1genetic
20093466
CSR2_YEASTCSR2genetic
20093466
CGS5_YEASTCLB5genetic
20093466
YKR18_YEASTYKR018Cphysical
22940862
IES1_YEASTIES1genetic
27708008
RCY1_YEASTRCY1genetic
27708008
TIR4_YEASTTIR4genetic
27708008
VPS17_YEASTVPS17genetic
27708008
PMA2_YEASTPMA2genetic
27708008
DEP1_YEASTDEP1genetic
27708008
YBF9_YEASTYBL059Wgenetic
27708008
CSG2_YEASTCSG2genetic
27708008
ECM33_YEASTECM33genetic
27708008
UBC4_YEASTUBC4genetic
27708008
TPS1_YEASTTPS1genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
SEC66_YEASTSEC66genetic
27708008
SGF29_YEASTSGF29genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RV161_YEASTRVS161genetic
27708008
FUB1_YEASTFUB1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
VAM6_YEASTVAM6genetic
27708008
OST4_YEASTOST4genetic
27708008
AAD4_YEASTAAD4genetic
27708008
YD042_YEASTYDR042Cgenetic
27708008
VMS1_YEASTVMS1genetic
27708008
RM01_YEASTMRPL1genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
IPK1_YEASTIPK1genetic
27708008
EF2_YEASTEFT2genetic
27708008
RS17B_YEASTRPS17Bgenetic
27708008
PFA5_YEASTPFA5genetic
27708008
SDC1_YEASTSDC1genetic
27708008
SNF1_YEASTSNF1genetic
27708008
SAK1_YEASTSAK1genetic
27708008
ODPA_YEASTPDA1genetic
27708008
RIM15_YEASTRIM15genetic
27708008
FAR7_YEASTFAR7genetic
27708008
SGF73_YEASTSGF73genetic
27708008
MPC1_YEASTMPC1genetic
27708008
MDM34_YEASTMDM34genetic
27708008
RTF1_YEASTRTF1genetic
27708008
RTG2_YEASTRTG2genetic
27708008
RPI1_YEASTRPI1genetic
27708008
PTPA1_YEASTRRD1genetic
27708008
ASF1_YEASTASF1genetic
27708008
CYP7_YEASTCPR7genetic
27708008
YJ24_YEASTKCH1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
STE24_YEASTSTE24genetic
27708008
ILM1_YEASTILM1genetic
27708008
DOA1_YEASTDOA1genetic
27708008
DNM1_YEASTDNM1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
ARV1_YEASTARV1genetic
27708008
ATP10_YEASTATP10genetic
27708008
RS3A1_YEASTRPS1Agenetic
27708008
MSC1_YEASTMSC1genetic
27708008
FAR3_YEASTFAR3genetic
27708008
MGR3_YEASTMGR3genetic
27708008
RIM13_YEASTRIM13genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
ELP6_YEASTELP6genetic
27708008
FAR11_YEASTFAR11genetic
27708008
VPS27_YEASTVPS27genetic
27708008
RCF2_YEASTRCF2genetic
27708008
HUB1_YEASTHUB1genetic
27708008
SGT2_YEASTSGT2genetic
27708008
WHI2_YEASTWHI2genetic
27708008
VHS3_YEASTVHS3genetic
27708008
COQ7_YEASTCAT5genetic
27708008
LCB4_YEASTLCB4genetic
27708008
PALA_YEASTRIM20genetic
27708008
PDE2_YEASTPDE2genetic
27708008
MRX11_YEASTYPL041Cgenetic
27708008
LGE1_YEASTLGE1genetic
27708008
LCL1_YEASTLCL1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
FMP30_YEASTFMP30genetic
27708008
YME1_YEASTYME1genetic
27708008
CSR2_YEASTCSR2genetic
27708008
MSS18_YEASTMSS18genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YKR18_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-192; THR-193; THR-196;SER-246; SER-375; SER-377; SER-380 AND THR-389, 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-380, 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-380, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-380, ANDMASS SPECTROMETRY.

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