YHT1_YEAST - dbPTM
YHT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YHT1_YEAST
UniProt AC P38835
Protein Name PH domain-containing protein YHR131C
Gene Name YHR131C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 850
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MALPIEGKLSMANNRIERLKSPSSSSTCSMDEVLITSSNNSSSICLETMRQLPREGVSGQINIIKETAASSSSHAALFIKQDLYEHIDPLPAYPPSYDLVNPNKEVRFPIFGDTAPCPKSSLPPLYAPAVYELTLISLKLERLSPYEISSNRSWRNFIIEINSTQLNFYHIDESLTKHIRNYSSGETKSEKEDRIHSDLVHRSDQSQHLHHRLFTLPTRSASEFKKADQERISYRVKRDRSRYLTDEALYKSFTLQNARFGIPTDYTKKSFVLRMSCESEQFLLRFSHIDDMIDWSMYLSIGISVSLDLEVREYPDYRIVPRRRRRRRRRRRRRRHTHRSESSMGSFSQRFIRSNSRPDLIQRYSTGSSTNNNTTIRERSNTFTAGLLDHYCTGLSKTPTEALISSAASGESSDNSTLGSTRSLSGCSASRSIASRSLKFKIKNFFRPKNSSRTEKLHRLRSNSSNLNSVIETEEDDEHHESSGGDHPEPGVPVNTTIKVERPMHRNRAISMPQRQSLRRAISEEVVPIKFPNSTVGESVHSPSPIEHLSVDGCEIMLQSQNAVMKEELRSVASNLVANERDEASIRPKPQSSSIYLSGLAPNGESATDLSQSSRSLCLTNRDAEINDDESATETDEDENDGETDEYAGDDTNDDTDDSNIGYAYGSESDYSCLIEERIRNRRRASSTLSCFSNIPYGTDDIKWKPAIKEISRRRYLRDSLKCIKPFLDSNDCLGKVIYIPVSGPTFETSNKIHFSNRQSLQKQKNHFLKGFIVGPTALIELNCKNKNAIVGTTKDAEDHGEDDGDGDDGEDDDDDDDDDDDDDDDEDDDDDDDDDDDDDDDDDDGQITA
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
8AcetylationMALPIEGKLSMANNR
CCCCCCCEEHHCCCH		25.3025381059
8UbiquitinationMALPIEGKLSMANNR
CCCCCCCEEHHCCCH		25.3024961812
343PhosphorylationHTHRSESSMGSFSQR
HHCCCCCCCCHHHHH		24.1023749301
346PhosphorylationRSESSMGSFSQRFIR
CCCCCCCHHHHHHHH		17.0623749301
354PhosphorylationFSQRFIRSNSRPDLI
HHHHHHHCCCCCCHH		34.0522369663
356PhosphorylationQRFIRSNSRPDLIQR
HHHHHCCCCCCHHHH		46.5722369663
364PhosphorylationRPDLIQRYSTGSSTN
CCCHHHHHCCCCCCC		8.3322369663
365PhosphorylationPDLIQRYSTGSSTNN
CCHHHHHCCCCCCCC		28.6022369663
366PhosphorylationDLIQRYSTGSSTNNN
CHHHHHCCCCCCCCC		31.9522369663
368PhosphorylationIQRYSTGSSTNNNTT
HHHHCCCCCCCCCCC		33.7922369663
369PhosphorylationQRYSTGSSTNNNTTI
HHHCCCCCCCCCCCE		36.1822369663
370PhosphorylationRYSTGSSTNNNTTIR
HHCCCCCCCCCCCEE		43.6022369663
382PhosphorylationTIRERSNTFTAGLLD
CEECHHCCCCHHHHH		24.4928889911
416PhosphorylationSGESSDNSTLGSTRS
CCCCCCCCCCCCCCC		29.9628889911
423PhosphorylationSTLGSTRSLSGCSAS
CCCCCCCCCCCCCCC		27.2928889911
432PhosphorylationSGCSASRSIASRSLK
CCCCCCHHHHHHCCC		21.7328889911
464PhosphorylationLHRLRSNSSNLNSVI
HHHHHHCCCCCCCCE		23.1123749301
465PhosphorylationHRLRSNSSNLNSVIE
HHHHHCCCCCCCCEE		49.9723749301
473PhosphorylationNLNSVIETEEDDEHH
CCCCCEECCCCCCCC		33.2824961812
482PhosphorylationEDDEHHESSGGDHPE
CCCCCCCCCCCCCCC		29.9023749301
483PhosphorylationDDEHHESSGGDHPEP
CCCCCCCCCCCCCCC		43.7524961812
496PhosphorylationEPGVPVNTTIKVERP
CCCCCCCCEEEEECC		30.0823749301
497PhosphorylationPGVPVNTTIKVERPM
CCCCCCCEEEEECCC		17.3824961812
511PhosphorylationMHRNRAISMPQRQSL
CCCCCCCCCHHHHHH		24.3528152593
523PhosphorylationQSLRRAISEEVVPIK
HHHHHHHHCCCCCCC		27.0722890988
574PhosphorylationEELRSVASNLVANER
HHHHHHHHHHHCCCC		28.6528889911
606PhosphorylationGLAPNGESATDLSQS
CCCCCCCCHHCCCHH		37.5623749301
616PhosphorylationDLSQSSRSLCLTNRD
CCCHHHHCCCCCCCC		25.9422369663
620PhosphorylationSSRSLCLTNRDAEIN
HHHCCCCCCCCCCCC		27.4928889911
686PhosphorylationIRNRRRASSTLSCFS
HHCCCCCCCCCHHHC		23.2623749301
688PhosphorylationNRRRASSTLSCFSNI
CCCCCCCCCHHHCCC		21.8623749301
690PhosphorylationRRASSTLSCFSNIPY
CCCCCCCHHHCCCCC		17.1323749301
693PhosphorylationSSTLSCFSNIPYGTD
CCCCHHHCCCCCCCC		37.8723749301
703UbiquitinationPYGTDDIKWKPAIKE
CCCCCCCCCHHHHHH		57.0423749301
722UbiquitinationRYLRDSLKCIKPFLD
HHHHHHHHHHHHHCC		37.5523749301
725UbiquitinationRDSLKCIKPFLDSND
HHHHHHHHHHCCCCC		38.9122817900
730PhosphorylationCIKPFLDSNDCLGKV
HHHHHCCCCCCCCEE		36.3923749301
736UbiquitinationDSNDCLGKVIYIPVS
CCCCCCCEEEEEECC		16.7124961812
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YHT1_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 YHT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSP5_YEASTRSP5physical
16554755
CSK21_YEASTCKA1physical
16554755
RSP5_YEASTRSP5physical
18719252
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YHT1_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-356, AND MASSSPECTROMETRY.

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