CUE5_YEAST - dbPTM
CUE5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CUE5_YEAST
UniProt AC Q08412
Protein Name Ubiquitin-binding protein CUE5
Gene Name CUE5 {ECO:0000312|SGD:S000005568}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 411
Subcellular Localization Cytoplasm . Localizes to cytoplasm in a punctate pattern.
Protein Description Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 adapter and thus mediating autophagic clearance of ubiquitin conjugates under starvation conditions. The CUE5-dependent selective autophagy pathway plays an important role in clearance of cytotoxic protein aggregates. Not required for cytoplasmic to vacuole pathway (cvt), mitophagy, pexophagy, or ribophagy..
Protein Sequence MEEKEGIKDSSLLEKSNVPESINEDISKTTDVDLNSDGKKDNDTSAKDGTPKVEEKVNKSSGIDEDEVVTPAEDAKEEEEEHPPLPARRKSEEEPSKENPILQELKDAFPNLEEKYIKAVIIASQGVLSPAFNALLFLSDPESGKDIELPTQPVRKNPEAPARRRQTQLEQDELLARQLDEQFNSSHSRRRNRDRATRSMHEQRRRRHNPNEREQHHEDSEEEDSWSQFVEKDLPELTDRAGRSLQDTANKVSNWISDAYRRNFASGNEQNDNQHGHQDQQEWEPEIVDLSQGGKNSRPQQPERRRFNSFGVQVGDDSLESHGITLHNEDGFEDDEDVPPQLPTRTKSGESTGKVVAETTYIDTPDTETKKKWQPLPPEPLDTTPTKVNAVSRNKKNPDEDEFLINSDDEM
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
4Ubiquitination----MEEKEGIKDSS
----CCCCCCCCCCH		48.1922106047
8UbiquitinationMEEKEGIKDSSLLEK
CCCCCCCCCCHHHHH		63.5123749301
10PhosphorylationEKEGIKDSSLLEKSN
CCCCCCCCHHHHHCC		20.2022369663
11PhosphorylationKEGIKDSSLLEKSNV
CCCCCCCHHHHHCCC		47.2922369663
15UbiquitinationKDSSLLEKSNVPESI
CCCHHHHHCCCCHHH		47.5023749301
15AcetylationKDSSLLEKSNVPESI
CCCHHHHHCCCCHHH		47.5024489116
16PhosphorylationDSSLLEKSNVPESIN
CCHHHHHCCCCHHHC		33.4122890988
21PhosphorylationEKSNVPESINEDISK
HHCCCCHHHCCCHHH		25.3322369663
27PhosphorylationESINEDISKTTDVDL
HHHCCCHHHCCCCCC		35.9522890988
28AcetylationSINEDISKTTDVDLN
HHCCCHHHCCCCCCC		56.6424489116
28UbiquitinationSINEDISKTTDVDLN
HHCCCHHHCCCCCCC		56.6423749301
29PhosphorylationINEDISKTTDVDLNS
HCCCHHHCCCCCCCC		22.8029136822
30PhosphorylationNEDISKTTDVDLNSD
CCCHHHCCCCCCCCC		37.4529136822
36PhosphorylationTTDVDLNSDGKKDND
CCCCCCCCCCCCCCC		55.8522369663
39UbiquitinationVDLNSDGKKDNDTSA
CCCCCCCCCCCCCCC		63.0423749301
44PhosphorylationDGKKDNDTSAKDGTP
CCCCCCCCCCCCCCC		36.5228889911
45PhosphorylationGKKDNDTSAKDGTPK
CCCCCCCCCCCCCCC		35.8626447709
47UbiquitinationKDNDTSAKDGTPKVE
CCCCCCCCCCCCCHH		57.3623749301
50PhosphorylationDTSAKDGTPKVEEKV
CCCCCCCCCCHHHHH		30.0321551504
52UbiquitinationSAKDGTPKVEEKVNK
CCCCCCCCHHHHHHH		63.2224961812
56UbiquitinationGTPKVEEKVNKSSGI
CCCCHHHHHHHCCCC		37.2923749301
59UbiquitinationKVEEKVNKSSGIDED
CHHHHHHHCCCCCHH		49.3224961812
60PhosphorylationVEEKVNKSSGIDEDE
HHHHHHHCCCCCHHH		28.7022369663
61PhosphorylationEEKVNKSSGIDEDEV
HHHHHHCCCCCHHHC		41.1822369663
70PhosphorylationIDEDEVVTPAEDAKE
CCHHHCCCCHHHHHH		23.2022369663
76UbiquitinationVTPAEDAKEEEEEHP
CCCHHHHHHHHHHCC		77.3523749301
90UbiquitinationPPLPARRKSEEEPSK
CCCCCCCCCCCCCCC		57.5824961812
91PhosphorylationPLPARRKSEEEPSKE
CCCCCCCCCCCCCCC		48.7222369663
96PhosphorylationRKSEEEPSKENPILQ
CCCCCCCCCCCHHHH		56.7519795423
97UbiquitinationKSEEEPSKENPILQE
CCCCCCCCCCHHHHH		72.6923749301
156UbiquitinationLPTQPVRKNPEAPAR
CCCCCCCCCCCCCHH		76.6723749301
167PhosphorylationAPARRRQTQLEQDEL
CCHHHHHHHHHHHHH		33.0517330950
185PhosphorylationQLDEQFNSSHSRRRN
HHHHHHHHHHHHHHH		30.6222369663
186PhosphorylationLDEQFNSSHSRRRNR
HHHHHHHHHHHHHHH		26.9622369663
188PhosphorylationEQFNSSHSRRRNRDR
HHHHHHHHHHHHHHH		29.4522369663
220PhosphorylationREQHHEDSEEEDSWS
HHHCCCCCCCHHHHH		43.8722369663
225PhosphorylationEDSEEEDSWSQFVEK
CCCCCHHHHHHHHHH		31.7222890988
227PhosphorylationSEEEDSWSQFVEKDL
CCCHHHHHHHHHHHH		20.0722890988
232UbiquitinationSWSQFVEKDLPELTD
HHHHHHHHHHHHHHH		60.3023749301
238PhosphorylationEKDLPELTDRAGRSL
HHHHHHHHHHHCHHH		23.0628889911
244PhosphorylationLTDRAGRSLQDTANK
HHHHHCHHHHHHHHH		29.4824909858
251UbiquitinationSLQDTANKVSNWISD
HHHHHHHHHHHHHHH		44.5723749301
266PhosphorylationAYRRNFASGNEQNDN
HHHHHCCCCCCCCCC		37.7025704821
295UbiquitinationVDLSQGGKNSRPQQP
EEHHHCCCCCCCCCC		59.5822817900
309PhosphorylationPERRRFNSFGVQVGD
CCHHCCCCCCCEECC		22.2123749301
318PhosphorylationGVQVGDDSLESHGIT
CCEECCCCHHHCCEE		38.4823749301
321PhosphorylationVGDDSLESHGITLHN
ECCCCHHHCCEEEEC		32.1021440633
325PhosphorylationSLESHGITLHNEDGF
CHHHCCEEEECCCCC		26.9328889911
346PhosphorylationPPQLPTRTKSGESTG
CCCCCCCCCCCCCCC		31.8522369663
348PhosphorylationQLPTRTKSGESTGKV
CCCCCCCCCCCCCCE		47.3722369663
351PhosphorylationTRTKSGESTGKVVAE
CCCCCCCCCCCEEEE		46.0822369663
352PhosphorylationRTKSGESTGKVVAET
CCCCCCCCCCEEEEE		36.4022369663
354UbiquitinationKSGESTGKVVAETTY
CCCCCCCCEEEEEEE		33.3623749301
359PhosphorylationTGKVVAETTYIDTPD
CCCEEEEEEEECCCC		18.3722890988
360PhosphorylationGKVVAETTYIDTPDT
CCEEEEEEEECCCCC		15.2422890988
361PhosphorylationKVVAETTYIDTPDTE
CEEEEEEEECCCCCC		12.2922890988
364PhosphorylationAETTYIDTPDTETKK
EEEEEECCCCCCCCC		17.3222369663
367PhosphorylationTYIDTPDTETKKKWQ
EEECCCCCCCCCCCC		46.9222369663
369PhosphorylationIDTPDTETKKKWQPL
ECCCCCCCCCCCCCC		50.7022369663
370UbiquitinationDTPDTETKKKWQPLP
CCCCCCCCCCCCCCC		46.2323749301
371UbiquitinationTPDTETKKKWQPLPP
CCCCCCCCCCCCCCC		67.6622817900
372UbiquitinationPDTETKKKWQPLPPE
CCCCCCCCCCCCCCC		53.2523749301
383PhosphorylationLPPEPLDTTPTKVNA
CCCCCCCCCCCHHHH		42.2125521595
384PhosphorylationPPEPLDTTPTKVNAV
CCCCCCCCCCHHHHC		28.7325521595
386PhosphorylationEPLDTTPTKVNAVSR
CCCCCCCCHHHHCCC		45.6022369663
387UbiquitinationPLDTTPTKVNAVSRN
CCCCCCCHHHHCCCC		34.3923749301
392PhosphorylationPTKVNAVSRNKKNPD
CCHHHHCCCCCCCCC		27.9429136822
395UbiquitinationVNAVSRNKKNPDEDE
HHHCCCCCCCCCHHC		53.4723749301
396UbiquitinationNAVSRNKKNPDEDEF
HHCCCCCCCCCHHCC		76.8023749301
407PhosphorylationEDEFLINSDDEM---
HHCCCCCCCCCC---		39.1722369663
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 CUE5_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 CUE5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCS7_YEASTSCS7genetic
16269340
TRS85_YEASTTRS85genetic
16269340
ALG6_YEASTALG6genetic
16269340
HRD1_YEASTHRD1genetic
16269340
PGA3_YEASTPGA3genetic
16269340
ATX2_YEASTATX2genetic
16269340
KEX1_YEASTKEX1genetic
16269340
AP3S_YEASTAPS3genetic
16269340
PFD2_YEASTGIM4genetic
16269340
AP3B_YEASTAPL6genetic
16269340
GAS1_YEASTGAS1genetic
16269340
BFR1_YEASTBFR1genetic
16269340
RIC1_YEASTRIC1genetic
16269340
CUE5_YEASTCUE5physical
18467557
SIN3_YEASTSIN3genetic
19547744
ATG8_YEASTATG8physical
25042851
UBI4P_YEASTUBI4physical
25042851
CHK1_YEASTCHK1genetic
27708008
TRS85_YEASTTRS85genetic
27708008
VAM7_YEASTVAM7genetic
27708008
STB5_YEASTSTB5genetic
27708008
GVP36_YEASTGVP36genetic
27708008
ICE2_YEASTICE2genetic
27708008
CTK1_YEASTCTK1genetic
27708008
YRA2_YEASTYRA2genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
SPEE_YEASTSPE3genetic
27708008
DSK2_YEASTDSK2physical
27477278
ATG8_YEASTATG8physical
27477278
PSB7_YEASTPRE4physical
27477278
PRS7_YEASTRPT1physical
27477278
RPN5_YEASTRPN5physical
27477278
RPN8_YEASTRPN8physical
27477278
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CUE5_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-21; SER-36; THR-50;SER-60; THR-70; SER-91; THR-167; SER-220; SER-244; SER-309; THR-346;SER-348; SER-351; THR-352; THR-364; THR-369; THR-383; THR-384; THR-386AND SER-407, 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-11; SER-36; THR-50;THR-70; THR-167; SER-348; SER-351; THR-352; THR-364; THR-367; THR-384AND SER-407, 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-91 AND THR-384, 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: PROTEIN SEQUENCE OF 60-88; 214-232; 373-387 AND 396-411,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-220; THR-384 ANDSER-407, UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-396,AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-364 AND THR-367, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"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: PROTEIN SEQUENCE OF 60-88; 214-232; 373-387 AND 396-411,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-220; THR-384 ANDSER-407, UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-396,AND MASS SPECTROMETRY.

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