KHSE_YEAST - dbPTM
KHSE_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KHSE_YEAST
UniProt AC P17423
Protein Name Homoserine kinase
Gene Name THR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 357
Subcellular Localization
Protein Description Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate..
Protein Sequence MVRAFKIKVPASSANIGPGYDVLGVGLSLFLELDVTIDSSQAQETNDDPNNCKLSYTKESEGYSTVPLRSDANLITRTALYVLRCNNIRNFPSGTKVHVSNPIPLGRGLGSSGAAVVAGVILGNEVAQLGFSKQRMLDYCLMIERHPDNITAAMMGGFCGSFLRDLTPQEVERREIPLAEVLPEPSGGEDTGLVPPLPPTDIGRHVKYQWNPAIKCIAIIPQFELSTADSRGVLPKAYPTQDLVFNLQRLAVLTTALTMDPPNADLIYPAMQDRVHQPYRKTLIPGLTEILSCVTPSTYPGLLGICLSGAGPTILALATENFEEISQEIINRFAKNGIKCSWKLLEPAYDGASVEQQ
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
58AcetylationNCKLSYTKESEGYST
CCEEEEEECCCCCCC		51.5124489116
58UbiquitinationNCKLSYTKESEGYST
CCEEEEEECCCCCCC		51.5123749301
133UbiquitinationVAQLGFSKQRMLDYC
HHHCCCCHHHHHHHH		39.4024961812
167PhosphorylationGSFLRDLTPQEVERR
HHHHHHCCHHHHHHC		27.5028889911
207AcetylationTDIGRHVKYQWNPAI
CCCCHHCCCCCCCCH		26.1224489116
207UbiquitinationTDIGRHVKYQWNPAI
CCCCHHCCCCCCCCH		26.1223749301
236AcetylationDSRGVLPKAYPTQDL
CCCCCCCCCCCCHHH		57.2924489116
236UbiquitinationDSRGVLPKAYPTQDL
CCCCCCCCCCCCHHH		57.2923749301
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 KHSE_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KHSE_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 KHSE_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_YEASTPOL30genetic
17314980
SAS3_YEASTSAS3genetic
17314980
PP4R2_YEASTPSY4genetic
17314980
UBP13_YEASTUBP13genetic
17314980
KHSE_YEASTTHR1physical
11283351
DNM1_YEASTDNM1physical
18467557
KHSE_YEASTTHR1physical
18719252
TWF1_YEASTTWF1genetic
19269370
SIP4_YEASTSIP4genetic
19269370
ADK_YEASTADO1genetic
19269370
SPO14_YEASTSPO14genetic
19269370
RFA2_YEASTRFA2genetic
19269370
ALAT_YEASTALT2genetic
16941010
AGX1_YEASTAGX1genetic
16941010
AK_YEASTHOM3genetic
20305002
FKBP_YEASTFPR1genetic
20305002
UBP4_YEASTDOA4genetic
20305002
ALY1_YEASTALY1genetic
20305002
HUA1_YEASTHUA1genetic
20305002
SSH1_YEASTSSH1genetic
20305002
TAT1_YEASTTAT1genetic
20305002
PRS8_YEASTRPT6genetic
20305002
PRS10_YEASTRPT4genetic
20305002
PSB1_YEASTPRE3genetic
20305002
DHOM_YEASTHOM6genetic
20305002
SNG1_YEASTSNG1genetic
20424846
ELO3_YEASTELO3genetic
22808036
RIR1_YEASTRNR1genetic
23518504
UBC9_HUMANUBE2Iphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KHSE_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-167, AND MASSSPECTROMETRY.

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