LKHA4_YEAST - dbPTM
LKHA4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LKHA4_YEAST
UniProt AC Q10740
Protein Name Leucine aminopeptidase 2 {ECO:0000303|PubMed:6352682}
Gene Name LAP2 {ECO:0000303|PubMed:6352682}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 671
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro)..
Protein Sequence MFLLPFVIRHSSSIYLPTLRFRGLLTVISRNIHISTPHKMLPLSIEQRRPSRSPEYDQSTLSNYKDFAVLHTDLNLSVSFEKSAISGSVTFQLKKLHEGKNKSDELHLDTSYLDVQEVHIDGSKADFQIEQRKEPLGSRLVINNASCNDNFTLNIQFRTTDKCTALQWLNSKQTKGGKPYVFSQLEAIHARSLFPCFDTPSVKSTFTASIESPLPVVFSGIRIEDTSKDTNIYRFEQKVPIPAYLIGIASGDLSSAPIGPRSTVYTEPFRLKDCQWEFENDVEKFIQTAEKIIFEYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDRSNIDVIAHELAHSWSGNLVTNCSWNHFWLNEGWTVYLERRIIGAIHGEPTRHFSALIGWSDLQNSIDSMKDPERFSTLVQNLNDNTDPDDAFSTVPYEKGFNLLFHLETILGGKAEFDPFIRHYFKKFAKKSLDTFQFLDTLYEFYPEKKEILDSVDWETWLYKPGMPPRPHFITALADNVYQLADKWVEMAQHLKTTEDFRSEFNAIDIKDFNSNQLVLFLETLTQNGHSNKKPKDFDWAKFPVASRALLDIYQDNIVKSQNAEVVFKMFKFQIFAKLQEEYKHLADWLGTVGRMKFVRPGYRLLNSVDRRLALATFDKFKDTYHPICKALVKQDLGL
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
44PhosphorylationPHKMLPLSIEQRRPS
CCCCCCCCHHHCCCC		23.3421440633
51PhosphorylationSIEQRRPSRSPEYDQ
CHHHCCCCCCCCCCH		43.5122369663
53PhosphorylationEQRRPSRSPEYDQST
HHCCCCCCCCCCHHH		26.8120377248
56PhosphorylationRPSRSPEYDQSTLSN
CCCCCCCCCHHHHHC		23.7522369663
59PhosphorylationRSPEYDQSTLSNYKD
CCCCCCHHHHHCCCC		28.5522369663
60PhosphorylationSPEYDQSTLSNYKDF
CCCCCHHHHHCCCCE		28.6822369663
62PhosphorylationEYDQSTLSNYKDFAV
CCCHHHHHCCCCEEE		37.9022369663
64PhosphorylationDQSTLSNYKDFAVLH
CHHHHHCCCCEEEEE		14.4622369663
77PhosphorylationLHTDLNLSVSFEKSA
EECEEEEEEEEECCC		18.0327017623
79PhosphorylationTDLNLSVSFEKSAIS
CEEEEEEEEECCCCC		25.0627017623
138PhosphorylationQRKEPLGSRLVINNA
ECCCCCCCCEEEECC		30.0828889911
178AcetylationSKQTKGGKPYVFSQL
CCCCCCCCCEECHHH		41.6722865919
228UbiquitinationIRIEDTSKDTNIYRF
EEEEECCCCCCCEEE		71.3323749301
574AcetylationPKDFDWAKFPVASRA
CCCCCHHHCCHHHHH		46.0424489116
616AcetylationAKLQEEYKHLADWLG
HHHHHHHHHHHHHHH		35.1124489116
652AcetylationLALATFDKFKDTYHP
HHHHHHHHHHHHCHH		50.5524489116
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 LKHA4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LKHA4_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 LKHA4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PFKA1_YEASTPFK1physical
11805826
EF2_YEASTEFT2physical
16554755
SYEC_YEASTGUS1physical
16554755
MAOM_YEASTMAE1physical
16554755
CHS5_YEASTCHS5physical
16554755
BCH1_YEASTBCH1physical
16554755
AAD3_YEASTAAD3genetic
27708008
RKM4_YEASTRKM4genetic
27708008
YRA2_YEASTYRA2genetic
27708008
INO4_YEASTINO4genetic
27708008
CY1_YEASTCYT1genetic
27708008
VPS5_YEASTVPS5genetic
27708008
MPC54_YEASTMPC54genetic
27708008
ULS1_YEASTULS1genetic
27708008
SRL1_YEASTSRL1genetic
27708008
ETFD_YEASTCIR2genetic
27708008
YPQ3_YEASTRTC2genetic
27708008
REI1_YEASTREI1genetic
27708008
SNF5_YEASTSNF5genetic
27708008
RNQ1_YEASTRNQ1genetic
27708008
ATG22_YEASTATG22genetic
27708008
RDS1_YEASTRDS1genetic
27708008
ARO1_YEASTARO1genetic
27708008
MZM1_YEASTMZM1genetic
27708008
VFA1_YEASTVFA1genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
POG1_YEASTPOG1genetic
27708008
MCM22_YEASTMCM22genetic
27708008
PRY2_YEASTPRY2genetic
27708008
CAF4_YEASTCAF4genetic
27708008
ASI1_YEASTASI1genetic
27708008
LAG2_YEASTLAG2genetic
27708008
PDR5_YEASTPDR5genetic
27708008
MKK1_YEASTMKK1genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
CTF19_YEASTCTF19genetic
27708008
ARGI_YEASTCAR1genetic
27708008
BEM4_YEASTBEM4genetic
27708008
MRL1_YEASTMRL1genetic
27708008
AXL1_YEASTAXL1genetic
27708008
YP174_YEASTYPR174Cgenetic
27708008
BANP_HUMANBANPphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LKHA4_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 SER-51, AND MASSSPECTROMETRY.

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