DPH2_YEAST - dbPTM
DPH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPH2_YEAST
UniProt AC P32461
Protein Name 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000305}
Gene Name DPH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 534
Subcellular Localization Cytoplasm .
Protein Description Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2..
Protein Sequence MEVAPALSTTQSDVAFQKVETHEIDRSSYLGPCYNSDELMQLISAYYNVEPLVGYLEQHPEYQNVTLQFPDDLIKDSSLIVRLLQSKFPHGKIKFWVLADTAYSACCVDEVAAEHVHAEVVVHFGDACLNAIQNLPVVYSFGTPFLDLALVVENFQRAFPDLSSKICLMANAPFSKHLSQLYNILKGDLHYTNIIYSQVNTSAVEEKFVTILDTFHVPEDVDQVGVFEKNSVLFGQHDKADNISPEDYHLFHLTTPQDPRLLYLSTVFQSVHIFDPALPGMVTGPFPSLMRRYKYMHVARTAGCIGILVNTLSLRNTRETINELVKLIKTREKKHYLFVVGKPNVAKLANFEDIDIWCILGCSQSGIIVDQFNEFYKPIITPYELNLALSEEVTWTGKWVVDFRDAIDEIEQNLGGQDTISASTTSDEPEFDVVRGRYTSTSRPLRALTHLELEAADDDDSKQLTTRHTASGAVIKGTVSTSASALQNRSWKGLGSDFDSTEVDNTGADIEEGISGVARGYGFDREDAMKKENK
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
8PhosphorylationMEVAPALSTTQSDVA
CCCCCCCCCCHHHCC		31.3630377154
9PhosphorylationEVAPALSTTQSDVAF
CCCCCCCCCHHHCCE		29.7030377154
10PhosphorylationVAPALSTTQSDVAFQ
CCCCCCCCHHHCCEE		23.7730377154
12PhosphorylationPALSTTQSDVAFQKV
CCCCCCHHHCCEEEE		31.7728889911
18AcetylationQSDVAFQKVETHEID
HHHCCEEEEEECCCC		35.2724489116
21PhosphorylationVAFQKVETHEIDRSS
CCEEEEEECCCCHHH		28.0030377154
78PhosphorylationDDLIKDSSLIVRLLQ
CHHHCCCHHHHHHHH		32.0528889911
175PhosphorylationLMANAPFSKHLSQLY
HHHCCCHHHHHHHHH		20.3630377154
191PhosphorylationILKGDLHYTNIIYSQ
HHHCCHHHCCEEEEE		14.5829650682
192PhosphorylationLKGDLHYTNIIYSQV
HHCCHHHCCEEEEEC		14.8129650682
196PhosphorylationLHYTNIIYSQVNTSA
HHHCCEEEEECCCHH		6.8329650682
197PhosphorylationHYTNIIYSQVNTSAV
HHCCEEEEECCCHHH		19.7629650682
201PhosphorylationIIYSQVNTSAVEEKF
EEEEECCCHHHHHHH		21.1429650682
210PhosphorylationAVEEKFVTILDTFHV
HHHHHHEEHHHHCCC		20.9622369663
214PhosphorylationKFVTILDTFHVPEDV
HHEEHHHHCCCCCCC		16.5222369663
449PhosphorylationSRPLRALTHLELEAA
CCCHHHHEEEEEEEC		24.3530377154
469PhosphorylationKQLTTRHTASGAVIK
CCCEEEEECCCCEEE		21.1620377248
471PhosphorylationLTTRHTASGAVIKGT
CEEEEECCCCEEEEE		28.5728889911
480PhosphorylationAVIKGTVSTSASALQ
CEEEEEEECCHHHHH		19.2428889911
481PhosphorylationVIKGTVSTSASALQN
EEEEEEECCHHHHHC		24.7930377154
484PhosphorylationGTVSTSASALQNRSW
EEEECCHHHHHCCCC		29.3130377154
496PhosphorylationRSWKGLGSDFDSTEV
CCCCCCCCCCCCCCC		39.9021440633
500PhosphorylationGLGSDFDSTEVDNTG
CCCCCCCCCCCCCCC		26.8519779198
501PhosphorylationLGSDFDSTEVDNTGA
CCCCCCCCCCCCCCC		41.7019779198
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 DPH2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPH2_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 DPH2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYPH_YEASTCPR1physical
16554755
HSP7E_YEASTECM10physical
16554755
MNN1_YEASTMNN1physical
16554755
TRX2_YEASTTRX2physical
16554755
HSP77_YEASTSSC1physical
16554755
TRX1_YEASTTRX1physical
16554755
DPH1_YEASTDPH1physical
18719252
DPH1_YEASTDPH1physical
23645155
EIF3J_YEASTHCR1genetic
27708008
INO4_YEASTINO4genetic
27708008
RV161_YEASTRVS161genetic
27708008
PAT1_YEASTPAT1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
EF2_YEASTEFT2genetic
27708008
SAP1_YEASTSAP1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
NEM1_YEASTNEM1genetic
27708008
LSM1_YEASTLSM1genetic
27708008
MNN11_YEASTMNN11genetic
27708008
CYP7_YEASTCPR7genetic
27708008
YK58_YEASTYKR078Wgenetic
27708008
SWI6_YEASTSWI6genetic
27708008
DCR2_YEASTDCR2genetic
27708008
ROM2_YEASTROM2genetic
27708008
SRC1_YEASTSRC1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
MDM38_YEASTMDM38genetic
27708008
ENB1_YEASTENB1genetic
27708008
MRX11_YEASTYPL041Cgenetic
27708008
DAP1_YEASTDAP1genetic
27708008
CG12_YEASTCLN2genetic
27708008
YP260_YEASTYPL260Wgenetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
COG3_YEASTCOG3genetic
29674565
SWC5_YEASTSWC5genetic
29674565
LCB2_YEASTLCB2genetic
29674565
TRS23_YEASTTRS23genetic
29674565
EF2_YEASTEFT2genetic
29674565
COG7_YEASTCOG7genetic
29674565
NBP35_YEASTNBP35genetic
29674565
YG36_YEASTYGR126Wgenetic
29674565
CHO2_YEASTCHO2genetic
29674565
APQ12_YEASTAPQ12genetic
29674565
ATC7_YEASTNEO1genetic
29674565
EXO70_YEASTEXO70genetic
29674565
RS21B_YEASTRPS21Bgenetic
29674565
CYP7_YEASTCPR7genetic
29674565
HOC1_YEASTHOC1genetic
29674565
BET3_YEASTBET3genetic
29674565
CFT2_YEASTCFT2genetic
29674565
NU188_YEASTNUP188genetic
29674565
ERG5_YEASTERG5genetic
29674565
RNA1_YEASTRNA1genetic
29674565
SFL1_YEASTSFL1genetic
29674565
GGPPS_YEASTBTS1genetic
29674565
HSP7F_YEASTSSE1genetic
29674565
YAR1_YEASTYAR1genetic
29674565
SPT2_YEASTSPT2genetic
29674565
YCH1_YEASTYCH1genetic
29674565
ARP4_YEASTARP4genetic
29674565
NAP1_YEASTNAP1genetic
29674565
ENT4_YEASTENT4genetic
29674565
OST6_YEASTOST6genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPH2_YEAST

loading...

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-496, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory