BLH1_YEAST - dbPTM
BLH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLH1_YEAST
UniProt AC Q01532
Protein Name Cysteine proteinase 1, mitochondrial
Gene Name LAP3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 483
Subcellular Localization Isoform Cytoplasmic: Cytoplasm.
Isoform Mitochondrial: Mitochondrion.
Protein Description The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities..
Protein Sequence MLPTSVSRSLYLKTFRSHLLRAPQIVLKRMSSSIDISKINSWNKEFQSDLTHQLATTVLKNYNADDALLNKTRLQKQDNRVFNTVVSTDSTPVTNQKSSGRCWLFAATNQLRLNVLSELNLKEFELSQAYLFFYDKLEKANYFLDQIVSSADQDIDSRLVQYLLAAPTEDGGQYSMFLNLVKKYGLIPKDLYGDLPYSTTASRKWNSLLTTKLREFAETLRTALKERSADDSIIVTLREQMQREIFRLMSLFMDIPPVQPNEQFTWEYVDKDKKIHTIKSTPLEFASKYAKLDPSTPVSLINDPRHPYGKLIKIDRLGNVLGGDAVIYLNVDNETLSKLVVKRLQNNKAVFFGSHTPKFMDKKTGVMDIELWNYPAIGYNLPQQKASRIRYHESLMTHAMLITGCHVDETSKLPLRYRVENSWGKDSGKDGLYVMTQKYFEEYCFQIVVDINELPKELASKFTSGKEEPIVLPIWDPMGALAK
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
4Phosphorylation----MLPTSVSRSLY
----CCCCCCCHHHH		37.4928889911
5Phosphorylation---MLPTSVSRSLYL
---CCCCCCCHHHHH		19.0228889911
7Phosphorylation-MLPTSVSRSLYLKT
-CCCCCCCHHHHHHH		18.8728889911
12PhosphorylationSVSRSLYLKTFRSHL
CCCHHHHHHHHHHHH		5.2319779198
31PhosphorylationQIVLKRMSSSIDISK
HHHHHHHHCCCCHHH		25.6022369663
32PhosphorylationIVLKRMSSSIDISKI
HHHHHHHCCCCHHHH		23.2120377248
33PhosphorylationVLKRMSSSIDISKIN
HHHHHHCCCCHHHHH		19.5722369663
41PhosphorylationIDISKINSWNKEFQS
CCHHHHHHCCHHHHH		35.1828152593
42UbiquitinationDISKINSWNKEFQSD
CHHHHHHCCHHHHHH		18.5423749301
44AcetylationSKINSWNKEFQSDLT
HHHHHCCHHHHHHHH		54.3624489116
48PhosphorylationSWNKEFQSDLTHQLA
HCCHHHHHHHHHHHH		39.6519779198
68UbiquitinationNYNADDALLNKTRLQ
HCCCCHHHHCCHHHH		7.5324961812
71AcetylationADDALLNKTRLQKQD
CCHHHHCCHHHHHCC		34.6824489116
71UbiquitinationADDALLNKTRLQKQD
CCHHHHCCHHHHHCC		34.68-
84PhosphorylationQDNRVFNTVVSTDST
CCCCEEEEEEECCCC		15.7222369663
87PhosphorylationRVFNTVVSTDSTPVT
CEEEEEEECCCCCCC		23.3522369663
88PhosphorylationVFNTVVSTDSTPVTN
EEEEEEECCCCCCCC		23.5122369663
90PhosphorylationNTVVSTDSTPVTNQK
EEEEECCCCCCCCCC		34.4022369663
91PhosphorylationTVVSTDSTPVTNQKS
EEEECCCCCCCCCCC		25.2922369663
94PhosphorylationSTDSTPVTNQKSSGR
ECCCCCCCCCCCCCC		32.8922369663
189AcetylationKKYGLIPKDLYGDLP
HHHCCCCHHHCCCCC		54.0624489116
197PhosphorylationDLYGDLPYSTTASRK
HHCCCCCCCCCCHHH		26.4127017623
199PhosphorylationYGDLPYSTTASRKWN
CCCCCCCCCCHHHHH		22.1227017623
210PhosphorylationRKWNSLLTTKLREFA
HHHHHHHHHHHHHHH		27.4627017623
267PhosphorylationPNEQFTWEYVDKDKK
CCCCCEEEEECCCCC		32.4018407956
288AcetylationTPLEFASKYAKLDPS
CCCHHHHHHCCCCCC		45.8824489116
291AcetylationEFASKYAKLDPSTPV
HHHHHHCCCCCCCCC		50.7824489116
296PhosphorylationYAKLDPSTPVSLIND
HCCCCCCCCCHHHCC		32.8527214570
310AcetylationDPRHPYGKLIKIDRL
CCCCCCCCEEEEECC		40.9925381059
354PhosphorylationNKAVFFGSHTPKFMD
CCEEEECCCCCHHHC		21.0222369663
356PhosphorylationAVFFGSHTPKFMDKK
EEEECCCCCHHHCCC		29.8522369663
358AcetylationFFGSHTPKFMDKKTG
EECCCCCHHHCCCCC		55.2524489116
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 BLH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLH1_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 BLH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATB_YEASTVMA2physical
16554755
GAL7_YEASTGAL7genetic
21589890
RPB1_YEASTRPO21genetic
27708008
NBP35_YEASTNBP35genetic
27708008
YHS2_YEASTCIA2genetic
27708008
TAD3_YEASTTAD3genetic
27708008
FUN30_YEASTFUN30genetic
27708008
GEM1_YEASTGEM1genetic
27708008
SIF2_YEASTSIF2genetic
27708008
THRC_YEASTTHR4genetic
27708008
MTU1_YEASTSLM3genetic
27708008
SAC3_YEASTSAC3genetic
27708008
VMA21_YEASTVMA21genetic
27708008
CHO2_YEASTCHO2genetic
27708008
CBP4_YEASTCBP4genetic
27708008
FLX1_YEASTFLX1genetic
27708008
PBS2_YEASTPBS2genetic
27708008
MDM35_YEASTMDM35genetic
27708008
APE2_YEASTAPE2genetic
27708008
RM49_YEASTMRP49genetic
27708008
TPO5_YEASTTPO5genetic
27708008
COX12_YEASTCOX12genetic
27708008
UPS2_YEASTUPS2genetic
27708008
ELO3_YEASTELO3genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
RCF2_YEASTRCF2genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
HMI1_YEASTHMI1genetic
27708008
CY1_YEASTCYT1genetic
27708008
MNE1_YEASTMNE1genetic
27708008
MSC6_YEASTMSC6genetic
27708008
YME1_YEASTYME1genetic
27708008
MSS18_YEASTMSS18genetic
27708008
KAR3_YEASTKAR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BLH1_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-296 AND THR-356, ANDMASS SPECTROMETRY.

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