MCD4_YEAST - dbPTM
MCD4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCD4_YEAST
UniProt AC P36051
Protein Name GPI ethanolamine phosphate transferase 1
Gene Name MCD4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 919
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Golgi apparatus membrane
Multi-pass membrane protein. Vacuole membrane
Multi-pass membrane protein.
Protein Description Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. Ethanolamine phosphate on the alpha-1,4-linked mannose is essential for further mannosylation by GPI10 and is necessary for an efficient recognition of GPI lipids and GPI proteins by the GPI transamidase, for the efficient transport of GPI anchored proteins from endoplasmic reticulum to Golgi and for the physiological incorporation of ceramides into GPI anchors by lipid remodeling. Also involved in non-mitochondrial ATP movements across membrane and participates in Golgi and endoplasmic reticulum function, Also required for the incorporation of BGL2 into the cell wall..
Protein Sequence MWNKTRTTLLAVGVLFHLFYLWSIFDIYFISPLVHGMSPYQSTPTPPAKRLFLIVGDGLRADTTFDKVTHPVSGKTEFLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKGWKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPNKVDTWMYDHTFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWGAGLNKPVHNPFPVSDNYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELPIAYIDGKESDKLAALYNNARSILEQYLVKQDEVIDSQFFYKEYFKFVEKSHSHYLEEIETLIQRISEGENYLEQEAITLTEELMQITLEGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQKASPLSHAVFGSIGILLNWILFYQHSPFNFYMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGTSPWKRVLITISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGVRELSVNILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKIHSRINSYTRAIFAIQISLVAAMLAVTHRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPNNDYKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMVQWIEIENKIKEMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDPFLMGALLMLKLIIPYGLLSTCLGILNLKLNFKDYTISSLIISMSDILSLNFFYLLRTEGSWLDIGITISNYCLAILSSLFMLILEVLGHVLLKNVIIQDKTKKTQ
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
75AcetylationVTHPVSGKTEFLAPF
CCCCCCCCHHHHHHH		37.0624489116
90N-linked_GlycosylationIRSLVMNNATYGISH
HHHHHHCCCCCCCCC		18.63-
104PhosphorylationHTRMPTESRPGHVAM
CCCCCCCCCCCCEEE		46.3728889911
138N-linked_GlycosylationVNFDSFFNQSTHTYS
CCHHHHHCCCCCEEE		32.65-
198N-linked_GlycosylationHLDQLFHNSTLNSTL
HHHHHHCCCCCCCCC		29.38-
202N-linked_GlycosylationLFHNSTLNSTLDYEI
HHCCCCCCCCCCEEE		32.79-
254AcetylationQIPILIDKVNKFFAD
CCCCHHHHHHHHCCC		40.4924489116
286N-linked_GlycosylationSHGDGHPNNTRTPLV
CCCCCCCCCCCCCEE		57.75-
312N-linked_GlycosylationNPFPVSDNYTENWEL
CCCCCCCCCCCCCCC		37.81-
334PhosphorylationVKQADIASLMSYLIG
CCHHHHHHHHHHHHC		25.5728889911
337PhosphorylationADIASLMSYLIGVNY
HHHHHHHHHHHCCCC		23.2928889911
338PhosphorylationDIASLMSYLIGVNYP
HHHHHHHHHHCCCCC		6.5928889911
344PhosphorylationSYLIGVNYPKNSVGE
HHHHCCCCCCCCCCC		17.1228889911
543AcetylationSVLRSGIKEFFKGTS
HHHHHHHHHHHCCCC		52.5824489116
848PhosphorylationLKLNFKDYTISSLII
CCCCCCCCCHHHHEE		13.4328889911
851PhosphorylationNFKDYTISSLIISMS
CCCCCCHHHHEEEHH		15.9928889911
852PhosphorylationFKDYTISSLIISMSD
CCCCCHHHHEEEHHH		21.5328889911
858PhosphorylationSSLIISMSDILSLNF
HHHEEEHHHHHHCCE		18.0828889911
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 MCD4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCD4_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 MCD4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECM33_YEASTECM33genetic
12441642
PSD1_YEASTPSD1genetic
12441642
SGPL_YEASTDPL1genetic
12441642
TMEDA_YEASTERV25physical
18467557
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
ELO3_YEASTELO3physical
16093310
YOP1_YEASTYOP1physical
16093310
TMEDA_YEASTERV25physical
22615397
BEM1_YEASTBEM1genetic
23891562
HOC1_YEASTHOC1genetic
23891562
HAC1_YEASTHAC1genetic
23891562
ERV14_YEASTERV14genetic
23891562
SUR1_YEASTSUR1genetic
23891562
ATG7_YEASTATG7genetic
25519895
ATG14_YEASTATG14genetic
25519895
ATG1_YEASTATG1genetic
25519895
CHO2_YEASTCHO2genetic
25519895
ECT1_YEASTECT1genetic
25519895
PSD2_YEASTPSD2genetic
25519895
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCD4_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-104, AND MASSSPECTROMETRY.

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