UBA2_YEAST - dbPTM
UBA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA2_YEAST
UniProt AC P52488
Protein Name Ubiquitin-activating enzyme E1-like
Gene Name UBA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 636
Subcellular Localization Nucleus.
Protein Description The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1..
Protein Sequence MPRETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNSKLVPYQGNVMDISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRSTPSQPIHCIVWAKNFLFNQLFASETSGNEDDNNQDWGTDDAEEIKRIKQETNELYELQKIIISRDASRIPEILNKLFIQDINKLLAIENLWKTRTKPVPLSDSQINTPTKTAQSASNSVGTIQEQISNFINITQKLMDRYPKEQNHIEFDKDDADTLEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYTDLNMAFTAKASNLSQNRYLSNPKLAPPNKNCPVCSKVCRGVIKLSSDCLNKMKLSDFVVLIREKYSYPQDISLLDASNQRLLFDYDFEDLNDRTLSEINLGNGSIILFSDEEGDTMIRKAIELFLDVDDELPCNTCSLPDVEVPLIKANNSPSKNEEEEKNEKGADVVATTNSHGKDGIVILDDDEGEITIDAEPINGSKKRPVDTEISEAPSNKRTKLVNEPTNSDIVELD
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
204PhosphorylationLFNQLFASETSGNED
HHHHHHCCCCCCCCC		33.7930377154
282PhosphorylationRTKPVPLSDSQINTP
CCCCCCCCHHHCCCC		29.1922369663
284PhosphorylationKPVPLSDSQINTPTK
CCCCCCHHHCCCCCH		29.5922369663
288PhosphorylationLSDSQINTPTKTAQS
CCHHHCCCCCHHHHH		33.6822369663
290PhosphorylationDSQINTPTKTAQSAS
HHHCCCCCHHHHHHH		38.7022369663
292PhosphorylationQINTPTKTAQSASNS
HCCCCCHHHHHHHCC		32.1929136822
295PhosphorylationTPTKTAQSASNSVGT
CCCHHHHHHHCCCHH		31.0629136822
297PhosphorylationTKTAQSASNSVGTIQ
CHHHHHHHCCCHHHH		34.5829136822
299PhosphorylationTAQSASNSVGTIQEQ
HHHHHHCCCHHHHHH		21.3029136822
302PhosphorylationSASNSVGTIQEQISN
HHHCCCHHHHHHHHH		19.8229136822
308PhosphorylationGTIQEQISNFINITQ
HHHHHHHHHHHHHHH		25.9429136822
357AcetylationHIFNIPMKSVFDIKQ
HHHCCCCCCCCCHHH		37.8124489116
396AcetylationLRVLNLLKYAPTTKY
HHHHHHHHCCCCCCC		42.4024489116
402AcetylationLKYAPTTKYTDLNMA
HHCCCCCCCCCCHHH		48.9422865919
411PhosphorylationTDLNMAFTAKASNLS
CCCHHHHEEECCCCC		20.0827738172
415PhosphorylationMAFTAKASNLSQNRY
HHHEEECCCCCCCCC		37.2819823750
418PhosphorylationTAKASNLSQNRYLSN
EEECCCCCCCCCCCC		29.6519823750
422PhosphorylationSNLSQNRYLSNPKLA
CCCCCCCCCCCCCCC		23.2519823750
424PhosphorylationLSQNRYLSNPKLAPP
CCCCCCCCCCCCCCC		42.0019823750
439PhosphorylationNKNCPVCSKVCRGVI
CCCCCHHHHHHHHHH		28.4928889911
498PhosphorylationFEDLNDRTLSEINLG
CCCCCCCCCCEEECC		37.1828889911
500PhosphorylationDLNDRTLSEINLGNG
CCCCCCCCEEECCCC		35.5028889911
513PhosphorylationNGSIILFSDEEGDTM
CCCEEEEECCCCCHH		40.4428889911
555PhosphorylationPLIKANNSPSKNEEE
CEEECCCCCCCCHHH		30.2927738172
557PhosphorylationIKANNSPSKNEEEEK
EECCCCCCCCHHHHH		48.1924930733
574PhosphorylationKGADVVATTNSHGKD
CCCCEEEECCCCCCC		18.2030377154
575PhosphorylationGADVVATTNSHGKDG
CCCEEEECCCCCCCE		25.6130377154
577PhosphorylationDVVATTNSHGKDGIV
CEEEECCCCCCCEEE		31.3730377154
622AcetylationAPSNKRTKLVNEPTN
CCCCCCCCCCCCCCC		55.2422865919
628PhosphorylationTKLVNEPTNSDIVEL
CCCCCCCCCCCCCCC		40.9722369663
630PhosphorylationLVNEPTNSDIVELD-
CCCCCCCCCCCCCC-		31.0622369663
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 UBA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA2_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 UBA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBA2_YEASTUBA2physical
7629121
UFD1_YEASTUFD1physical
9236779
RHC31_YEASTAOS1physical
9312010
RHC31_YEASTAOS1physical
16554755
ULP2_YEASTULP2genetic
10905345
RHC31_YEASTAOS1genetic
10905345
SMT3_YEASTSMT3genetic
10905345
HSP7F_YEASTSSE1physical
19536198
HSP71_YEASTSSA1physical
19536198
DOA10_YEASTSSM4genetic
20388728
UBC9_YEASTUBC9physical
21209884
IMB5_YEASTKAP114genetic
22562154
UBC9_YEASTUBC9physical
9341106
UBC_HUMANUBCphysical
26876099
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBA2_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 THR-288 AND SER-439, ANDMASS SPECTROMETRY.

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