HIS2_YEAST - dbPTM
HIS2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIS2_YEAST
UniProt AC P00815
Protein Name Histidine biosynthesis trifunctional protein
Gene Name HIS4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 799
Subcellular Localization
Protein Description
Protein Sequence MVLPILPLIDDLASWNSKKEYVSLVGQVLLDGSSLSNEEILQFSKEEEVPLVALSLPSGKFSDDEIIAFLNNGVSSLFIASQDAKTAEHLVEQLNVPKERVVVEENGVFSNQFMVKQKFSQDKIVSIKKLSKDMLTKEVLGEVRTDRPDGLYTTLVVDQYERCLGLVYSSKKSIAKAIDLGRGVYYSRSRNEIWIKGETSGNGQKLLQISTDCDSDALKFIVEQENVGFCHLETMSCFGEFKHGLVGLESLLKQRLQDAPEESYTRRLFNDSALLDAKIKEEAEELTEAKGKKELSWEAADLFYFALAKLVANDVSLKDVENNLNMKHLKVTRRKGDAKPKFVGQPKAEEEKLTGPIHLDVVKASDKVGVQKALSRPIQKTSEIMHLVNPIIENVRDKGNSALLEYTEKFDGVKLSNPVLNAPFPEEYFEGLTEEMKEALDLSIENVRKFHAAQLPTETLEVETQPGVLCSRFPRPIEKVGLYIPGGTAILPSTALMLGVPAQVAQCKEIVFASPPRKSDGKVSPEVVYVAEKVGASKIVLAGGAQAVAAMAYGTETIPKVDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADEDADVDFVASDLLSQAEHGIDSQVILVGVNLSEKKIQEIQDAVHNQALQLPRVDIVRKCIAHSTIVLCDGYEEALEMSNQYAPEHLILQIANANDYVKLVDNAGSVFVGAYTPESCGDYSSGTNHTLPTYGYARQYSGANTATFQKFITAQNITPEGLENIGRAVMCVAKKEGLDGHRNAVKIRMSKLGLIPKDFQ
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
137AcetylationLSKDMLTKEVLGEVR
HCHHHCCHHHHCCCC		41.6924489116
1762-HydroxyisobutyrylationSSKKSIAKAIDLGRG
CCHHHHHHHHHCCCC		44.18-
176AcetylationSSKKSIAKAIDLGRG
CCHHHHHHHHHCCCC		44.1824489116
196AcetylationSRNEIWIKGETSGNG
CCCEEEEEEECCCCC		35.3824489116
242UbiquitinationMSCFGEFKHGLVGLE
HHHHCCHHHHHHCHH		32.2517644757
250PhosphorylationHGLVGLESLLKQRLQ
HHHHCHHHHHHHHHH		44.0022369663
253UbiquitinationVGLESLLKQRLQDAP
HCHHHHHHHHHHCCC		38.3717644757
253AcetylationVGLESLLKQRLQDAP
HCHHHHHHHHHHCCC		38.3724489116
263PhosphorylationLQDAPEESYTRRLFN
HHCCCCHHHHHHHHC		30.0922369663
264PhosphorylationQDAPEESYTRRLFND
HCCCCHHHHHHHHCC		13.9322369663
265PhosphorylationDAPEESYTRRLFNDS
CCCCHHHHHHHHCCH		20.7022369663
272PhosphorylationTRRLFNDSALLDAKI
HHHHHCCHHHHHHHH		23.1722369663
278UbiquitinationDSALLDAKIKEEAEE
CHHHHHHHHHHHHHH		54.7117644757
278AcetylationDSALLDAKIKEEAEE
CHHHHHHHHHHHHHH		54.7124489116
280AcetylationALLDAKIKEEAEELT
HHHHHHHHHHHHHHH		49.1224489116
2802-HydroxyisobutyrylationALLDAKIKEEAEELT
HHHHHHHHHHHHHHH		49.12-
2902-HydroxyisobutyrylationAEELTEAKGKKELSW
HHHHHHHCCCHHCCH		66.10-
318AcetylationVANDVSLKDVENNLN
HHCCCCHHHHHHCCC		52.8224489116
327AcetylationVENNLNMKHLKVTRR
HHHCCCCCEEEEEEC		44.7224489116
341AcetylationRKGDAKPKFVGQPKA
CCCCCCCCCCCCCHH		52.5625381059
352AcetylationQPKAEEEKLTGPIHL
CCHHHHHHCCCCEEE		55.4124489116
363AcetylationPIHLDVVKASDKVGV
CEEEEEEECCCHHCH		41.8624489116
367UbiquitinationDVVKASDKVGVQKAL
EEEECCCHHCHHHHH		38.0922817900
3672-HydroxyisobutyrylationDVVKASDKVGVQKAL
EEEECCCHHCHHHHH		38.09-
372UbiquitinationSDKVGVQKALSRPIQ
CCHHCHHHHHCCCCH		49.2223749301
380UbiquitinationALSRPIQKTSEIMHL
HHCCCCHHHHHHHHH		55.5317644757
409AcetylationALLEYTEKFDGVKLS
HHHHHHHHCCCEECC		40.7424489116
416PhosphorylationKFDGVKLSNPVLNAP
HCCCEECCCCCCCCC		33.1121440633
519PhosphorylationFASPPRKSDGKVSPE
EECCCCCCCCCCCHH		53.5322369663
524PhosphorylationRKSDGKVSPEVVYVA
CCCCCCCCHHHEEEE		20.8722369663
533AcetylationEVVYVAEKVGASKIV
HHEEEEECCCCCEEE		35.9124489116
537PhosphorylationVAEKVGASKIVLAGG
EEECCCCCEEEECCH		19.5827017623
553PhosphorylationQAVAAMAYGTETIPK
HHHHHHHHCCCCCCC		16.1122369663
555PhosphorylationVAAMAYGTETIPKVD
HHHHHHCCCCCCCHH		19.7822369663
557PhosphorylationAMAYGTETIPKVDKI
HHHHCCCCCCCHHHC		42.2822369663
563AcetylationETIPKVDKILGPGNQ
CCCCCHHHCCCCCCC		42.7024489116
563UbiquitinationETIPKVDKILGPGNQ
CCCCCHHHCCCCCCC		42.7023749301
576UbiquitinationNQFVTAAKMYVQNDT
CCCEEEEEEHHCCCC		28.4417644757
739PhosphorylationTYGYARQYSGANTAT
CCCCCHHCCCCCHHH		11.9722369663
740PhosphorylationYGYARQYSGANTATF
CCCCHHCCCCCHHHH		24.0822369663
744PhosphorylationRQYSGANTATFQKFI
HHCCCCCHHHHHHHH		26.9222369663
746PhosphorylationYSGANTATFQKFITA
CCCCCHHHHHHHHHH		25.2622369663
773AcetylationRAVMCVAKKEGLDGH
HHHHHHHHHCCCCCC		30.8425381059
774AcetylationAVMCVAKKEGLDGHR
HHHHHHHHCCCCCCC		47.4825381059
796AcetylationSKLGLIPKDFQ----
HHHCCCCCCCC----		65.2724489116
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 HIS2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIS2_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 HIS2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHH1_YEASTDHH1physical
11805826
PDC1_YEASTPDC1physical
11805826
METK1_YEASTSAM1physical
11805826
TBA3_YEASTTUB3physical
11805826
SPT2_YEASTSPT2genetic
2991744
SPT3_YEASTSPT3genetic
6326126
H4_YEASTHHF1genetic
9171362
EBS1_YEASTEBS1genetic
16467471
FMP48_YEASTFMP48physical
20489023
IF5_YEASTTIF5genetic
20584985
TAF12_YEASTTAF12genetic
9844638
H2A1_YEASTHTA1genetic
9844638
H2B1_YEASTHTB1genetic
9844638
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HIS2_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-265, AND MASSSPECTROMETRY.

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