DPH1_YEAST - dbPTM
DPH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPH1_YEAST
UniProt AC P40487
Protein Name 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305}
Gene Name DPH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 425
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 MSGSTESKKQPRRRFIGRKSGNSNNDKLTTVAENGNEIIHKQKSRIALGRSVNHVPEDILNDKELNEAIKLLPSNYNFEIHKTVWNIRKYNAKRIALQMPEGLLIYSLIISDILEQFCGVETLVMGDVSYGACCIDDFTARALDCDFIVHYAHSCLVPIDVTKIKVLYVFVTINIQEDHIIKTLQKNFPKGSRIATFGTIQFNPAVHSVRDKLLNDEEHMLYIIPPQIKPLSRGEVLGCTSERLDKEQYDAMVFIGDGRFHLESAMIHNPEIPAFKYDPYNRKFTREGYDQKQLVEVRAEAIEVARKGKVFGLILGALGRQGNLNTVKNLEKNLIAAGKTVVKIILSEVFPQKLAMFDQIDVFVQVACPRLSIDWGYAFNKPLLTPYEASVLLKKDVMFSEKYYPMDYYEAKGYGRGETPKHAIE
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
44PhosphorylationEIIHKQKSRIALGRS
CEEHCCHHHHCCCCC
26.8217287358
51PhosphorylationSRIALGRSVNHVPED
HHHCCCCCCCCCCHH
26.0224961812
63AcetylationPEDILNDKELNEAIK
CHHHCCHHHHHHHHH
64.1324489116
289PhosphorylationRKFTREGYDQKQLVE
CCCCCCCCCHHHHEE
15.5027017623
332AcetylationNTVKNLEKNLIAAGK
HHHHHHHHHHHHCCH
61.2924489116
340PhosphorylationNLIAAGKTVVKIILS
HHHHCCHHHHHHHHH
29.6119795423
403PhosphorylationDVMFSEKYYPMDYYE
CCCCCCCCCCCCHHC
14.5627017623
404PhosphorylationVMFSEKYYPMDYYEA
CCCCCCCCCCCHHCC
11.8027017623
408PhosphorylationEKYYPMDYYEAKGYG
CCCCCCCHHCCCCCC
9.2827017623

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 DPH1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPH1_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 DPH1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IPYR_YEASTIPP1physical
16554755
MNN1_YEASTMNN1physical
16554755
IF4A_YEASTTIF2physical
16554755
ELM1_YEASTELM1physical
16554755
DPH2_YEASTDPH2physical
16554755
TRX1_YEASTTRX1physical
16554755
STM1_YEASTSTM1physical
16554755
CORO_YEASTCRN1physical
16554755
ADH3_YEASTADH3physical
16554755
HSC82_YEASTHSC82physical
16554755
VDAC1_YEASTPOR1physical
16554755
ZEO1_YEASTZEO1physical
16554755
DPH2_YEASTDPH2physical
16429126
RIR2_YEASTRNR2physical
16429126
DPH2_YEASTDPH2physical
11283351
DPH2_YEASTDPH2physical
23645155
DPH5_YEASTDPH5genetic
23645155
DPH2_YEASTDPH2physical
24422557
SWI6_YEASTSWI6genetic
27708008
PAT1_YEASTPAT1genetic
27708008
EF2_YEASTEFT2genetic
27708008
AK_YEASTHOM3genetic
27708008
SNF6_YEASTSNF6genetic
27708008
VPS53_YEASTVPS53genetic
27708008
SRC1_YEASTSRC1genetic
27708008
BUL2_YEASTBUL2genetic
27708008
DPH2_HUMANDPH2physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPH1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.

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