IML2_YEAST - dbPTM
IML2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IML2_YEAST
UniProt AC P47031
Protein Name Inclusion body clearance protein IML2 {ECO:0000305|PubMed:26004510}
Gene Name IML2 {ECO:0000303|PubMed:10628851}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 731
Subcellular Localization Cytoplasm . Nucleus . Localized exclusively in cytoplasmic inclusion bodies under protein folding stress conditions.
Protein Description Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing..
Protein Sequence MFRVFGSFGSKGNQSSGEEQSTKTKQVLKQANDFEIALKAMDFVLDDRTDEGLNLLKKAEMETGSDQTILTLARGVIEFLQATLSFETEEMKRAAITLGKAEQMSWKSKQNAEKTNFRSSSIYPPGTVYAVTYTESCLLHALLMLFSESMMEAAKALLKLRRAYTMLQDIMVTVKKAERSKNSSSPSPSEKSQESCGSFVSAETTFISVDIPYKLSSEDKSNPLLLEFAEKIYTMRMGRLSGAHIGNTPSFHRLRDDLGLQTTPSQASDRHSVSDDFDLEQATIDEFIHSGANLCYGILQVVLSLLPPAIGAVLSIVGFKGSREEGLRLVWKATKERNVHGCIGLLGLMFYYDGPFQFTDADFDIPPNDNGSRALNKSRTNDSSLLPGYMDSATLLHPGKILEDALLKARALFPNSALWLLNEAKMLAGKGRLRDSLALMDSIDVNSIRMRQVKSLMVFERAILLVNLHEYNRAADDLISLLDISDWSHALYTYFAGCCYLENWRMTQLGLLNDGKEQFYKERARELIFDAPSLLGKKTFKSKNLPLDRFMLRKVQQFNNMQKKLNLQEPLDSIATSPVHELAYFYNGYNRMTENDLILTKKMLTEYHNPAIDSEDPDQELIRNLLLSLTLRRLGDAERGLALLDDIVLPKIFYIQNGKVKYFKKTEDPWAYPAALYERALFCWKLGGMESLNECREWLLRAQNYAADYELSTRIGMKIKAALDRVENALA
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
7Phosphorylation-MFRVFGSFGSKGNQ
-CCEEECCCCCCCCC		18.2522369663
10PhosphorylationRVFGSFGSKGNQSSG
EEECCCCCCCCCCCC		35.0722369663
11UbiquitinationVFGSFGSKGNQSSGE
EECCCCCCCCCCCCC		63.3623749301
23UbiquitinationSGEEQSTKTKQVLKQ
CCCCCHHHHHHHHHH		60.0017644757
29UbiquitinationTKTKQVLKQANDFEI
HHHHHHHHHHCCHHH		48.8115699485
39UbiquitinationNDFEIALKAMDFVLD
CCHHHHHHHHHHHHC		32.4217644757
57UbiquitinationDEGLNLLKKAEMETG
HHHHHHHHHHHCCCC		53.7717644757
58UbiquitinationEGLNLLKKAEMETGS
HHHHHHHHHHCCCCC		49.9317644757
92UbiquitinationSFETEEMKRAAITLG
CCCCHHHHHHHHHHH		42.0117644757
100UbiquitinationRAAITLGKAEQMSWK
HHHHHHHHHHHCCHH		52.4417644757
107UbiquitinationKAEQMSWKSKQNAEK
HHHHCCHHHHHCHHH		40.2317644757
127PhosphorylationSSIYPPGTVYAVTYT
CCCCCCCCEEEEEEC		19.0028747907
129PhosphorylationIYPPGTVYAVTYTES
CCCCCCEEEEEECHH		8.6628747907
132PhosphorylationPGTVYAVTYTESCLL
CCCEEEEEECHHHHH		19.2928747907
133PhosphorylationGTVYAVTYTESCLLH
CCEEEEEECHHHHHH		11.2528747907
134PhosphorylationTVYAVTYTESCLLHA
CEEEEEECHHHHHHH		16.4428747907
136PhosphorylationYAVTYTESCLLHALL
EEEEECHHHHHHHHH		11.4128747907
180PhosphorylationTVKKAERSKNSSSPS
HHHHHHHCCCCCCCC		27.9128889911
183PhosphorylationKAERSKNSSSPSPSE
HHHHCCCCCCCCCCH		35.6127717283
184PhosphorylationAERSKNSSSPSPSEK
HHHCCCCCCCCCCHH		56.5128889911
185PhosphorylationERSKNSSSPSPSEKS
HHCCCCCCCCCCHHH		29.2627214570
187PhosphorylationSKNSSSPSPSEKSQE
CCCCCCCCCCHHHHH		42.9028889911
189PhosphorylationNSSSPSPSEKSQESC
CCCCCCCCHHHHHHH		63.0927717283
216PhosphorylationVDIPYKLSSEDKSNP
EECCCCCCCCCCCCH		27.7729136822
217PhosphorylationDIPYKLSSEDKSNPL
ECCCCCCCCCCCCHH		61.3229136822
220UbiquitinationYKLSSEDKSNPLLLE
CCCCCCCCCCHHHHH		48.3523749301
220AcetylationYKLSSEDKSNPLLLE
CCCCCCCCCCHHHHH		48.3524489116
221PhosphorylationKLSSEDKSNPLLLEF
CCCCCCCCCHHHHHH		56.8729136822
241PhosphorylationTMRMGRLSGAHIGNT
HHHHHCCCCCCCCCC		32.3529688323
248PhosphorylationSGAHIGNTPSFHRLR
CCCCCCCCCCHHHCH		18.3329688323
250PhosphorylationAHIGNTPSFHRLRDD
CCCCCCCCHHHCHHC		31.4827214570
262PhosphorylationRDDLGLQTTPSQASD
HHCCCCCCCCCCCCC		45.8026447709
263PhosphorylationDDLGLQTTPSQASDR
HCCCCCCCCCCCCCC		14.1622369663
265PhosphorylationLGLQTTPSQASDRHS
CCCCCCCCCCCCCCC		35.9622369663
268PhosphorylationQTTPSQASDRHSVSD
CCCCCCCCCCCCCCC		27.7822369663
378PhosphorylationGSRALNKSRTNDSSL
CCCCCCCCCCCCCCC		43.1722369663
380PhosphorylationRALNKSRTNDSSLLP
CCCCCCCCCCCCCCC		50.9325521595
383PhosphorylationNKSRTNDSSLLPGYM
CCCCCCCCCCCCCCC		25.5922369663
384PhosphorylationKSRTNDSSLLPGYMD
CCCCCCCCCCCCCCC		36.4722369663
389PhosphorylationDSSLLPGYMDSATLL
CCCCCCCCCCCCEEC		8.8722369663
392PhosphorylationLLPGYMDSATLLHPG
CCCCCCCCCEECCCC		13.4622369663
394PhosphorylationPGYMDSATLLHPGKI
CCCCCCCEECCCCHH		33.5319795423
400UbiquitinationATLLHPGKILEDALL
CEECCCCHHHHHHHH		48.8717644757
408UbiquitinationILEDALLKARALFPN
HHHHHHHHHHHHCCH		36.3524961812
425UbiquitinationLWLLNEAKMLAGKGR
HHHHHHHHHHCCCCC		28.4117644757
507PhosphorylationYLENWRMTQLGLLND
HHHCCCEEEECCCCC		16.4519779198
516UbiquitinationLGLLNDGKEQFYKER
ECCCCCCHHHHHHHH		51.7323749301
521UbiquitinationDGKEQFYKERARELI
CCHHHHHHHHHHHHH		41.8517644757
537UbiquitinationDAPSLLGKKTFKSKN
CCHHHHCCCCHHCCC		48.9217644757
538UbiquitinationAPSLLGKKTFKSKNL
CHHHHCCCCHHCCCC		58.3517644757
554UbiquitinationLDRFMLRKVQQFNNM
HHHHHHHHHHHHHHH		40.2017644757
563UbiquitinationQQFNNMQKKLNLQEP
HHHHHHHHHCCCCCC		48.7517644757
564UbiquitinationQFNNMQKKLNLQEPL
HHHHHHHHCCCCCCH		26.2217644757
601UbiquitinationENDLILTKKMLTEYH
HHCHHHHHHHHHHCC		32.5117644757
602UbiquitinationNDLILTKKMLTEYHN
HCHHHHHHHHHHCCC		33.6317644757
630PhosphorylationRNLLLSLTLRRLGDA
HHHHHHHHHHHHCCH		18.1628889911
651UbiquitinationLDDIVLPKIFYIQNG
HHCCHHCEEEEEECC		41.0917644757
664UbiquitinationNGKVKYFKKTEDPWA
CCEEEEEECCCCCCC		56.5517644757
665UbiquitinationGKVKYFKKTEDPWAY
CEEEEEECCCCCCCC		47.4417644757
685UbiquitinationERALFCWKLGGMESL
HHHHHHHHHCCCCHH		38.1315699485
720UbiquitinationTRIGMKIKAALDRVE
HHHHHHHHHHHHHHH		23.3017644757
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 IML2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IML2_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 IML2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALO_YEASTALO1physical
18467557
PET10_YEASTPET10physical
26004510
ACT_YEASTACT1genetic
27708008
SEC17_YEASTSEC17genetic
27708008
CALM_YEASTCMD1genetic
27708008
MAK5_YEASTMAK5genetic
27708008
TRS20_YEASTTRS20genetic
27708008
DPOD_YEASTPOL3genetic
27708008
SPC19_YEASTSPC19genetic
27708008
COG3_YEASTCOG3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
CDC20_YEASTCDC20genetic
27708008
PRP43_YEASTPRP43genetic
27708008
DAM1_YEASTDAM1genetic
27708008
FDFT_YEASTERG9genetic
27708008
ATC7_YEASTNEO1genetic
27708008
ESS1_YEASTESS1genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
BET3_YEASTBET3genetic
27708008
SEC22_YEASTSEC22genetic
27708008
SEN1_YEASTSEN1genetic
27708008
ORC1_YEASTORC1genetic
27708008
BET5_YEASTBET5genetic
27708008
HMCS_YEASTERG13genetic
27708008
LCB1_YEASTLCB1genetic
27708008
MVD1_YEASTMVD1genetic
27708008
MED4_YEASTMED4genetic
27708008
SEC63_YEASTSEC63genetic
27708008
THIL_YEASTERG10genetic
27708008
NAB3_YEASTNAB3genetic
27708008
DIM1_YEASTDIM1genetic
27708008
SRP54_YEASTSRP54genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IML2_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-7; SER-221; THR-263;SER-378; THR-380; SER-383 AND SER-384, 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 THR-380 AND SER-383, ANDMASS 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-265; SER-268 ANDSER-383, 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-383, AND MASSSPECTROMETRY.

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