UBP7_YEAST - dbPTM
UBP7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP7_YEAST
UniProt AC P40453
Protein Name Ubiquitin carboxyl-terminal hydrolase 7
Gene Name UBP7
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1071
Subcellular Localization Cytoplasm .
Protein Description Involved in the sorting of ubiquitinated cargo proteins at the multivesicular body (MVB)..
Protein Sequence MLDDDKGTAMHPHITPFTPEYSNELLRRVQDLYHEDIKHYYPQLKLEKLLDLLEHTEYLFELYLDSIHHDRPNDALTAFIIGCYYVFLIIPQSLQFQTRNKSYSIYTDLKKMYENEMNMTNVVLMVKKEIGVVLDESVKHGAGIEHRITKKRAFSVPADDLSGQVASLSLDTAAPQDHGLKGTFTEDDAEQSSPVWTAPNLEPNDQLKLALLPEVIPTPAFREPERKTSVPVRPSVLLEDVPSIYHEDDTSFASLNPPFREITADRSVTHRKDSYHSVYMVDSGNLKEDNDDLFNVENDGFIQSLDILQKQSIITAPELFSILSNRVEREKVLLIDLRIPQRSAINHIVAPNLVNVDPNLLWDKQTNTPIYKDDILEHLLKENENFINRNKFDYIVYYTDVKTFMTINFDYAFIFFYLMLTSQKTPLTTVPTTLLGGYEKWKKTLHSYAQEYHISIEDYLYRPYSQKARLQQEQQQQQQQPDSQDSFSAKESSTKVPEPPSWKPPDLPIRLRKRPPPPPPVSMPTTPEIPPPLPPKIMVHSQVSSISRKPPIPAKQHVKKEQLNSNEIIQRKRQHQHQHYDQQILQPQRAYNIPTIERSPNVYVSLSITGLRNLGNTCYINSMIQCLFAAKTFRTLFISSKYKSYLQPIRSNGSHYSPKLSNSLSMLFNKMYLNGGCSVVPTGFLKVINQLRPDLKIPDDQQDTQEFLMILLDRLHDELSDQQHVANDYPNLLLYNADALKVSNNEYKHWFDKNVIGNGISPIDDIFQGQMENSLQCKRCGYTTFNYSTFYVLSLAIPRRSMKLSKLGRSTEKRVKLEDCINMFTSDEVLSGENAWDCPRCGPTASVSTSVSALENEPSIVKSKKKKSRFFTLHTGTKRRHLDFFGDGITEGHNSNNNNTTIFERERSRSPFRMLGGSGKRSSSSTPFSTGGNDSNNSSDYKNKKLTTVKTINFVTLPKILVIHLSRFYYDLTKKNNTVVTYPLILNIILKNNDTMKYKLFGVVNHTGTLISGHYTSLVNKDLEHNVNIGRSKWYYFDDEVVKADRKHGSDKNLKISSSDVYVLFYERVYD
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
113PhosphorylationYTDLKKMYENEMNMT
HHHHHHHHHCCCCCC		25.2027017623
155PhosphorylationITKKRAFSVPADDLS
CCCCCCEECCHHHCC		26.6320377248
183PhosphorylationQDHGLKGTFTEDDAE
CCCCCCCCCCCCCHH		26.2924961812
185PhosphorylationHGLKGTFTEDDAEQS
CCCCCCCCCCCHHHC		38.0419779198
192PhosphorylationTEDDAEQSSPVWTAP
CCCCHHHCCCCEECC		28.2821440633
193PhosphorylationEDDAEQSSPVWTAPN
CCCHHHCCCCEECCC		24.1425521595
197PhosphorylationEQSSPVWTAPNLEPN
HHCCCCEECCCCCCC		32.2524961812
229PhosphorylationREPERKTSVPVRPSV
CCCCCCCCCCCCHHH		27.7119779198
235PhosphorylationTSVPVRPSVLLEDVP
CCCCCCHHHHHCCCC		18.1619779198
243PhosphorylationVLLEDVPSIYHEDDT
HHHCCCCCCCCCCCC		35.3119779198
250PhosphorylationSIYHEDDTSFASLNP
CCCCCCCCCCHHCCC		37.7619779198
251PhosphorylationIYHEDDTSFASLNPP
CCCCCCCCCHHCCCC		26.3019779198
274PhosphorylationSVTHRKDSYHSVYMV
CCCCCCCCCCEEEEE		27.9930377154
275PhosphorylationVTHRKDSYHSVYMVD
CCCCCCCCCEEEEEE		14.3028889911
277PhosphorylationHRKDSYHSVYMVDSG
CCCCCCCEEEEEECC		13.5028889911
483PhosphorylationQQQQQPDSQDSFSAK
HHHHCCCHHHCCCHH		42.4430377154
486PhosphorylationQQPDSQDSFSAKESS
HCCCHHHCCCHHHCC		17.2920377248
488PhosphorylationPDSQDSFSAKESSTK
CCHHHCCCHHHCCCC		42.2421440633
549UbiquitinationQVSSISRKPPIPAKQ
CCCCCCCCCCCCHHH		48.6423749301
599PhosphorylationNIPTIERSPNVYVSL
CCCCCCCCCCEEEEE		14.1827017623
603PhosphorylationIERSPNVYVSLSITG
CCCCCCEEEEEEEEC		7.3127017623
654PhosphorylationQPIRSNGSHYSPKLS
HCCCCCCCCCCCCHH		24.4121440633
908PhosphorylationTIFERERSRSPFRML
EEEEEHHCCCCCHHC		32.1528889911
918PhosphorylationPFRMLGGSGKRSSSS
CCHHCCCCCCCCCCC		39.0728889911
922PhosphorylationLGGSGKRSSSSTPFS
CCCCCCCCCCCCCCC		37.7520377248
923PhosphorylationGGSGKRSSSSTPFST
CCCCCCCCCCCCCCC		32.1320377248
924PhosphorylationGSGKRSSSSTPFSTG
CCCCCCCCCCCCCCC		39.2022369663
925PhosphorylationSGKRSSSSTPFSTGG
CCCCCCCCCCCCCCC		41.8920377248
926PhosphorylationGKRSSSSTPFSTGGN
CCCCCCCCCCCCCCC		30.2420377248
929PhosphorylationSSSSTPFSTGGNDSN
CCCCCCCCCCCCCCC		27.6127214570
930PhosphorylationSSSTPFSTGGNDSNN
CCCCCCCCCCCCCCC		49.8722369663
935PhosphorylationFSTGGNDSNNSSDYK
CCCCCCCCCCCHHHC		41.7427214570
938PhosphorylationGGNDSNNSSDYKNKK
CCCCCCCCHHHCCCC		28.9227214570
941PhosphorylationDSNNSSDYKNKKLTT
CCCCCHHHCCCCCCC		20.5727017623
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 UBP7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP7_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 UBP7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BBC1_YEASTBBC1physical
16554755
PPR1_YEASTPPR1physical
16554755
HSE1_YEASTHSE1physical
17079730
DPB3_YEASTDPB3genetic
20093466
ARF1_YEASTARF1genetic
20093466
MAF1_YEASTMAF1genetic
20093466
RV167_YEASTRVS167genetic
20093466
RL24A_YEASTRPL24Agenetic
20093466
RS10A_YEASTRPS10Agenetic
20093466
VHS1_YEASTVHS1physical
21460040
SECU_YEASTPDS1physical
22072716
MAF1_YEASTMAF1genetic
27708008
RV167_YEASTRVS167genetic
27708008
RTF1_YEASTRTF1genetic
27708008
ASK10_YEASTASK10genetic
27708008
MAL13_YEASTMAL13genetic
27708008
CSF1_YEASTCSF1genetic
27708008
RAD17_YEASTRAD17genetic
26740628
MRC1_YEASTMRC1genetic
26740628
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP7_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-155 AND SER-924, ANDMASS SPECTROMETRY.

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