DPM1_HUMAN - dbPTM
DPM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPM1_HUMAN
UniProt AC O60762
Protein Name Dolichol-phosphate mannosyltransferase subunit 1
Gene Name DPM1
Organism Homo sapiens (Human).
Sequence Length 260
Subcellular Localization Endoplasmic reticulum.
Protein Description Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex..
Protein Sequence MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
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
2Acetylation------MASLEVSRS
------CCCCCCCCC		23.8722814378
3Phosphorylation-----MASLEVSRSP
-----CCCCCCCCCC		24.6225159151
7Phosphorylation-MASLEVSRSPRRSR
-CCCCCCCCCCCCCC		20.0529255136
9PhosphorylationASLEVSRSPRRSRRE
CCCCCCCCCCCCCCE		18.4329255136
13PhosphorylationVSRSPRRSRRELEVR
CCCCCCCCCCEEEEC		36.6517081983
21PhosphorylationRRELEVRSPRQNKYS
CCEEEECCCCCCCCE		29.6125159151
26UbiquitinationVRSPRQNKYSVLLPT
ECCCCCCCCEEEECC		30.4821890473
26UbiquitinationVRSPRQNKYSVLLPT
ECCCCCCCCEEEECC		30.4821890473
27PhosphorylationRSPRQNKYSVLLPTY
CCCCCCCCEEEECCC		16.1528152594
28PhosphorylationSPRQNKYSVLLPTYN
CCCCCCCEEEECCCC		14.1128152594
33PhosphorylationKYSVLLPTYNERENL
CCEEEECCCCHHCCC		38.6628152594
34PhosphorylationYSVLLPTYNERENLP
CEEEECCCCHHCCCC		17.0628152594
58PhosphorylationFSESGINYEIIIIDD
HHHCCCCEEEEEECC		13.4425332170
71PhosphorylationDDGSPDGTRDVAEQL
CCCCCCCCHHHHHHH		30.9525332170
80UbiquitinationDVAEQLEKIYGSDRI
HHHHHHHHHHCCCCE		50.2321890473
80UbiquitinationDVAEQLEKIYGSDRI
HHHHHHHHHHCCCCE		50.2321890473
82PhosphorylationAEQLEKIYGSDRILL
HHHHHHHHCCCCEEE		22.9629496907
95UbiquitinationLLRPREKKLGLGTAY
EECCCHHCCCCCCHH		42.9321890473
95UbiquitinationLLRPREKKLGLGTAY
EECCCHHCCCCCCHH		42.9321890473
100PhosphorylationEKKLGLGTAYIHGMK
HHCCCCCCHHHCCCC		22.7225404012
102PhosphorylationKLGLGTAYIHGMKHA
CCCCCCHHHCCCCCC		8.0325404012
110PhosphorylationIHGMKHATGNYIIIM
HCCCCCCCCCEEEEE		26.1925404012
113PhosphorylationMKHATGNYIIIMDAD
CCCCCCCEEEEEECC		8.5425404012
136UbiquitinationPEFIRKQKEGNFDIV
HHHHHHHCCCCEEEC		71.30-
136MalonylationPEFIRKQKEGNFDIV
HHHHHHHCCCCEEEC		71.3026320211
149UbiquitinationIVSGTRYKGNGGVYG
ECCCCEEECCCCEEC		42.4821890473
149UbiquitinationIVSGTRYKGNGGVYG
ECCCCEEECCCCEEC		42.4821890473
149MethylationIVSGTRYKGNGGVYG
ECCCCEEECCCCEEC		42.48-
155PhosphorylationYKGNGGVYGWDLKRK
EECCCCEECCCHHHH		18.7729496907
160UbiquitinationGVYGWDLKRKIISRG
CEECCCHHHHHHHHC		49.5321890473
172PhosphorylationSRGANFLTQILLRPG
HHCCCHHHHHHHCCC		14.9329978859
174AcetylationGANFLTQILLRPGAS
CCCHHHHHHHCCCCC		3.0919608861
197AcetylationYRKEVLEKLIEKCVS
HCHHHHHHHHHHHHH		51.0719608861
232UbiquitinationGEVPISFVDRVYGES
CCCCCCHHHHHHCCC		3.5219608861
232AcetylationGEVPISFVDRVYGES
CCCCCCHHHHHHCCC		3.5219608861
234MethylationVPISFVDRVYGESKL
CCCCHHHHHHCCCCC		20.46-
236UbiquitinationISFVDRVYGESKLGG
CCHHHHHHCCCCCCH		18.97-
240UbiquitinationDRVYGESKLGGNEIV
HHHHCCCCCCHHHHH		47.0121890473
240UbiquitinationDRVYGESKLGGNEIV
HHHHCCCCCCHHHHH		47.0121890473
248PhosphorylationLGGNEIVSFLKGLLT
CCHHHHHHHHHHHHH		30.4428857561
269Methylation----------------
----------------		-
275Ubiquitination----------------------
----------------------		-
283Phosphorylation------------------------------
------------------------------		-
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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:16280320
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPM1_HUMAN !!
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 DPM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT16_HUMANZBTB16physical
16169070
DPM2_HUMANDPM2physical
10835346
DPM3_HUMANDPM3physical
10835346
CHIP_HUMANSTUB1physical
16280320
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608799Congenital disorder of glycosylation 1E (CDG1E)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPM1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-7 AND SER-9,ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-21, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-7 AND SER-9,ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.

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