DCW1_YEAST - dbPTM
DCW1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCW1_YEAST
UniProt AC P36091
Protein Name Mannan endo-1,6-alpha-mannosidase DCW1
Gene Name DCW1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 449
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor . GPI-anchored plasma membrane protein (GPI-PMP).
Protein Description Required for normal synthesis of the cell wall..
Protein Sequence MLVNKVIGLLGVLFATRFTNAVELDLDNYESLQNATSLIAYGLMDYYTGNQYGKTVGMFSDPYYWWEAGGAWGCMLDYWFFMDNDTYNDEIIAAMIHQAGDDNDYIPLNQSTTEGNDDQAFWGIAAMTAAERNFTNPPENEPQWLYLAQAVFNTMALRWDADSCGGGLRWQIFVWNSGYDYKNTVSNGALFHIAARLARYTGNQTYVDWAEKVYEWMVGVNLISNGTYKYVYDGVSIDDNCTKVTSYQWTYNQGLLLAGSAYLYNFTGSDLWHTRTKEFLNASQVFFHDGIVYEAACQGPNSCNTDQRSFKAYFARFLGVTAQLVPETRNQIMSWLNTSAIAAAKSCSGGTDGHTCGLNWFNGTWDGMYGLGEQMSALEVMVNTRALDKPAPYTAENGGSSVGDGAAGTQAQPTNLAPLNITKGSKAGAGIITAVIGISIVACALWLVF
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
34N-linked_GlycosylationDNYESLQNATSLIAY
CCHHHHHHHHHHHHH
50.94-
84N-linked_GlycosylationDYWFFMDNDTYNDEI
EEEEEECCCCCCHHH
31.56-
109N-linked_GlycosylationDNDYIPLNQSTTEGN
CCCEECCCCCCCCCC
28.53-
133N-linked_GlycosylationAMTAAERNFTNPPEN
HHHHHHHCCCCCCCC
39.33-
203N-linked_GlycosylationRLARYTGNQTYVDWA
HHHHHHCCCCCCHHH
24.18-
224PhosphorylationMVGVNLISNGTYKYV
HHCCEEEECCEEEEE
32.1628889911
225N-linked_GlycosylationVGVNLISNGTYKYVY
HCCEEEECCEEEEEE
39.57-
228PhosphorylationNLISNGTYKYVYDGV
EEEECCEEEEEECCE
11.1729650682
240N-linked_GlycosylationDGVSIDDNCTKVTSY
CCEEECCCCCEEEEE
31.45-
265N-linked_GlycosylationAGSAYLYNFTGSDLW
ECEEEEEECCCCCCC
25.96-
281N-linked_GlycosylationTRTKEFLNASQVFFH
CCCHHHHCHHHEEEC
42.75-
337N-linked_GlycosylationNQIMSWLNTSAIAAA
HHHHHHHCHHHHHHH
26.23-
362N-linked_GlycosylationTCGLNWFNGTWDGMY
CCCCCCCCCCCCCCC
38.30-
400PhosphorylationYTAENGGSSVGDGAA
CCCCCCCCCCCCCCC
24.2128889911
401PhosphorylationTAENGGSSVGDGAAG
CCCCCCCCCCCCCCC
33.1328889911
420N-linked_GlycosylationPTNLAPLNITKGSKA
CCCCCCCCCCCCCCC
38.53-
428GPI-anchorITKGSKAGAGIITAV
CCCCCCCCCHHHHHH
28.24-

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 DCW1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCW1_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 DCW1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DFG5_YEASTDFG5genetic
12421307
OSTD_YEASTSWP1physical
18467557
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
DFG5_YEASTDFG5genetic
23891562
SLG1_YEASTSLG1genetic
23891562
TLG2_YEASTTLG2genetic
23891562
CCW12_YEASTCCW12genetic
23891562
MSMO_YEASTERG25genetic
23891562
ELO3_YEASTELO3genetic
23891562
ETR1_YEASTETR1genetic
27708008
PUT4_YEASTPUT4genetic
27708008
FLC2_YEASTFLC2genetic
27708008
YJ66_YEASTYJR096Wgenetic
27708008
RT109_YEASTRTT109genetic
27708008
DFG5_YEASTDFG5genetic
27708008
STI1_YEASTSTI1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCW1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND SER-401, ANDMASS SPECTROMETRY.

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