UBX5_YEAST - dbPTM
UBX5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBX5_YEAST
UniProt AC Q06682
Protein Name UBX domain-containing protein 5
Gene Name UBX5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 500
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway..
Protein Sequence MSEGKVDEFMAITGADDAAIATQFIEMADGNLNTAISLFFENGGAALLSSNNTPTPSNSTPMAPTSVDSDADAQLAERLQREAYQQQQPDQDYVRPPDEARHEVLTETSGFPISYGGIGGRFEPLHRVNDMFDEGRPESIFNQRLDDTNTNTYINDNSSDSLDSEEENDDDEYEYVEEPVIELDEDGNIKEYTKLVRKPKTISKEQKLALLFRPPFSIMSKLDLDAAKQKARAKQKWIMINIQDSGIFQCQALNRDLWSSRPVKTIIKENFVFLQYQYESRNAQPYLQFYHLNNKDDLPHIAILDPITGERVKQWNRVVPIPEQFISEINEFLASFSLDPKVPNPTVNEPLPKVDPTTLTEEQQMELAIKESLNNNSSKSNQEEVPSTGEEQKRVQEPDPFSTIEARVHPEPPNKPGITTRIQIRTGDGSRLVRRFNALEDTVRTIYEVIKTEMDGFADSRFTLNDHQREDLIDKLNMTIADAGLKNSSLLLEKLDPEIE
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
69PhosphorylationMAPTSVDSDADAQLA
CCCCCCCCHHHHHHH		32.3227214570
139PhosphorylationFDEGRPESIFNQRLD
CCCCCCHHHHHCCCC		34.8522369663
220PhosphorylationRPPFSIMSKLDLDAA
CCCCCHHHHCCHHHH		28.5330377154
228UbiquitinationKLDLDAAKQKARAKQ
HCCHHHHHHHHHHHC		54.7923749301
230UbiquitinationDLDAAKQKARAKQKW
CHHHHHHHHHHHCCE		38.8522817900
353UbiquitinationTVNEPLPKVDPTTLT
CCCCCCCCCCCCCCC		67.9423749301
372PhosphorylationMELAIKESLNNNSSK
HHHHHHHHHHCCCCC		31.2529136822
377PhosphorylationKESLNNNSSKSNQEE
HHHHHCCCCCCCCCC		41.0729136822
378PhosphorylationESLNNNSSKSNQEEV
HHHHCCCCCCCCCCC		42.0829136822
379UbiquitinationSLNNNSSKSNQEEVP
HHHCCCCCCCCCCCC		53.9323749301
380PhosphorylationLNNNSSKSNQEEVPS
HHCCCCCCCCCCCCC		45.7722369663
387PhosphorylationSNQEEVPSTGEEQKR
CCCCCCCCCHHHHHC		54.9723749301
388PhosphorylationNQEEVPSTGEEQKRV
CCCCCCCCHHHHHCC		42.4125752575
393UbiquitinationPSTGEEQKRVQEPDP
CCCHHHHHCCCCCCC		58.7923749301
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 UBX5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBX5_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 UBX5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC48_YEASTCDC48physical
16554755
CSK2B_YEASTCKB1genetic
20093466
SNX4_YEASTSNX4genetic
20093466
DCOR_YEASTSPE1genetic
20093466
SAM37_YEASTSAM37genetic
20093466
GBLP_YEASTASC1genetic
20093466
CDC48_YEASTCDC48physical
21211725
NPL4_YEASTNPL4physical
21211725
UFD1_YEASTUFD1physical
21211725
CUL3_YEASTCUL3physical
21211725
CDC53_YEASTCDC53physical
22466964
CDC48_YEASTCDC48physical
22466964
CDC48_YEASTCDC48physical
15258615
ARP5_YEASTARP5physical
26656161
MRM2_YEASTMRM2genetic
27708008
VMA21_YEASTVMA21genetic
27708008
DIC1_YEASTDIC1genetic
27708008
CSK2B_YEASTCKB1genetic
27708008
ASK10_YEASTASK10genetic
27708008
NPR3_YEASTNPR3genetic
27708008
DCOR_YEASTSPE1genetic
27708008
UBX2_YEASTUBX2genetic
27708008
TSA1_YEASTTSA1genetic
27708008
SAM37_YEASTSAM37genetic
27708008
DOM34_YEASTDOM34genetic
27708008
RS28A_YEASTRPS28Agenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBX5_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-69 AND SER-139, 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-139, AND MASSSPECTROMETRY.

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