UBX7_YEAST - dbPTM
UBX7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBX7_YEAST
UniProt AC P38349
Protein Name UBX domain-containing protein 7
Gene Name UBX7
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 436
Subcellular Localization Endoplasmic reticulum .
Protein Description Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway..
Protein Sequence MLEALFRDSVEEAINDSIKEGVVLAVYNTARDDQWLKSWFKGDDVSLDTLAEHSIWLRLVKDTEQFQLFEQVFPNVVVPSIYLIRAGKIELIIQGEDDRHWEKLLACIGIKDKKAGESSSRETNPGLAREEKSSRDVHRKNARERIAETTLEIQRREQLKQRKLAEEERERIIRLVRADRAERKALDETHHRTLDDDKPLDVHDYIKDAQKLHSSKCVLQIRMTDGKTLKHEFNSSETLNDVRKWVDVNRTDGDCPYSFHRGIPRVTFKDSDELKTLETLELTPRSALLLKPLETQNSGLSVTGMEGPSLLGRLYKGFSTWWHNDKDPEVTSQREETSKPNRHEVRSSTPLSGAASSSCFQYNNVREPVQSSAHASPMLTPSGTRYPSETNLTTSRSVSPNVFQFVNNDHQEDPEDPTTFNGNNVHLEKKKDEDKK
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
19UbiquitinationEAINDSIKEGVVLAV
HHHHHHHHCCCEEEE		52.9822106047
37UbiquitinationARDDQWLKSWFKGDD
CCCCHHHHHHHCCCC		42.5624961812
41UbiquitinationQWLKSWFKGDDVSLD
HHHHHHHCCCCCCHH		55.9917644757
61UbiquitinationSIWLRLVKDTEQFQL
CHHHHCCCCHHHHHH		64.6217644757
198AcetylationHRTLDDDKPLDVHDY
CCCCCCCCCCCHHHH		55.2524489116
198UbiquitinationHRTLDDDKPLDVHDY
CCCCCCCCCCCHHHH		55.2515699485
207AcetylationLDVHDYIKDAQKLHS
CCHHHHHHHHHHHHC		40.5624489116
207UbiquitinationLDVHDYIKDAQKLHS
CCHHHHHHHHHHHHC		40.5615699485
227UbiquitinationQIRMTDGKTLKHEFN
EEEECCCCEEEEECC		54.1923749301
230AcetylationMTDGKTLKHEFNSSE
ECCCCEEEEECCCCC		46.4424489116
230UbiquitinationMTDGKTLKHEFNSSE
ECCCCEEEEECCCCC		46.4417644757
244UbiquitinationETLNDVRKWVDVNRT
CHHHHHHHHHCCCCC		51.9517644757
269AcetylationGIPRVTFKDSDELKT
CCCCEEECCHHHHCE		47.1324489116
269UbiquitinationGIPRVTFKDSDELKT
CCCCEEECCHHHHCE		47.1317644757
275UbiquitinationFKDSDELKTLETLEL
ECCHHHHCEEEEEEE		49.3617644757
291AcetylationPRSALLLKPLETQNS
CCCEEEECCCCCCCC		47.7524489116
291UbiquitinationPRSALLLKPLETQNS
CCCEEEECCCCCCCC		47.7523749301
326UbiquitinationSTWWHNDKDPEVTSQ
CCCCCCCCCHHHCCC		79.2122817900
347PhosphorylationPNRHEVRSSTPLSGA
CCCHHCCCCCCCCCC		43.6828889911
348PhosphorylationNRHEVRSSTPLSGAA
CCHHCCCCCCCCCCC		24.3919779198
349PhosphorylationRHEVRSSTPLSGAAS
CHHCCCCCCCCCCCC		29.5128889911
352PhosphorylationVRSSTPLSGAASSSC
CCCCCCCCCCCCCCC		27.8219779198
356PhosphorylationTPLSGAASSSCFQYN
CCCCCCCCCCCCCCC		23.4227017623
371PhosphorylationNVREPVQSSAHASPM
CCCCCCCCCCCCCCC		29.7123749301
372PhosphorylationVREPVQSSAHASPML
CCCCCCCCCCCCCCC		13.6423749301
376PhosphorylationVQSSAHASPMLTPSG
CCCCCCCCCCCCCCC		10.8523749301
380PhosphorylationAHASPMLTPSGTRYP
CCCCCCCCCCCCCCC		14.7928889911
382PhosphorylationASPMLTPSGTRYPSE
CCCCCCCCCCCCCCC		47.7823749301
384PhosphorylationPMLTPSGTRYPSETN
CCCCCCCCCCCCCCC		31.2229688323
386PhosphorylationLTPSGTRYPSETNLT
CCCCCCCCCCCCCCC		15.7922890988
388PhosphorylationPSGTRYPSETNLTTS
CCCCCCCCCCCCCCC		48.3921082442
390PhosphorylationGTRYPSETNLTTSRS
CCCCCCCCCCCCCCC		39.6122890988
393PhosphorylationYPSETNLTTSRSVSP
CCCCCCCCCCCCCCC		25.4622890988
394PhosphorylationPSETNLTTSRSVSPN
CCCCCCCCCCCCCCC		25.8822890988
395PhosphorylationSETNLTTSRSVSPNV
CCCCCCCCCCCCCCE		19.8122890988
397PhosphorylationTNLTTSRSVSPNVFQ
CCCCCCCCCCCCEEE		27.0625752575
399PhosphorylationLTTSRSVSPNVFQFV
CCCCCCCCCCEEECC		16.4128889911
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 UBX7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBX7_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 UBX7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBX7_YEASTUBX7physical
14755638
UBX6_YEASTUBX6physical
14755638
CDC48_YEASTCDC48physical
14755638
SLY41_YEASTSLY41genetic
16269340
ERG2_YEASTERG2genetic
16269340
ERG6_YEASTERG6genetic
16269340
BFR1_YEASTBFR1genetic
16269340
DFM1_YEASTDFM1physical
18407841
CDC48_YEASTCDC48physical
15258615
ARP5_YEASTARP5physical
26656161
CTK1_YEASTCTK1genetic
27708008
RV161_YEASTRVS161genetic
27708008
BUD31_YEASTBUD31genetic
27708008
MTU1_YEASTSLM3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
YD180_YEASTYDL180Wgenetic
27708008
UBC5_YEASTUBC5genetic
27708008
IES1_YEASTIES1genetic
27708008
KA122_YEASTKAP122genetic
27708008
ATG1_YEASTATG1genetic
27708008
PDR11_YEASTPDR11genetic
27708008
POM33_YEASTPOM33genetic
27708008
ENV10_YEASTENV10genetic
27708008
ARPC3_YEASTARC18genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
UBX2_YEASTUBX2genetic
27708008
RAD14_YEASTRAD14genetic
27708008
RS7B_YEASTRPS7Bgenetic
27708008
YO036_YEASTYOL036Wgenetic
27708008
INO4_YEASTINO4genetic
27708008
ATX2_YEASTATX2genetic
27708008
IES4_YEASTIES4genetic
27708008
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBX7_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 THR-349; SER-376; SER-388;THR-393 AND SER-399, AND MASS SPECTROMETRY.
"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 THR-349, AND MASSSPECTROMETRY.

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