ALG1_HUMAN - dbPTM
ALG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALG1_HUMAN
UniProt AC Q9BT22
Protein Name Chitobiosyldiphosphodolichol beta-mannosyltransferase
Gene Name ALG1
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER..
Protein Sequence MAASCLVLLALCLLLPLLLLGGWKRWRRGRAARHVVAVVLGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLGSMHSPFRARSEPEDPVTERSAFTERDAGSGLVTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFPDPAGKLNQFRKNLRESQQLRWDESWVQTVLPLVMDT
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
46PhosphorylationVLGDVGRSPRMQYHA
EECCCCCCHHHHHHH
15.7821712546
68UbiquitinationFSVTLLGFCNSKPHD
CEEEEEHHCCCCCCH
3.4422817900
72UbiquitinationLLGFCNSKPHDELLQ
EEHHCCCCCCHHHHH
32.1721890473
72UbiquitinationLLGFCNSKPHDELLQ
EEHHCCCCCCHHHHH
32.1721890473
106UbiquitinationRVFQYGVKVVLQAMY
HHHHHHHHHHHHHHH
23.4321890473
106UbiquitinationRVFQYGVKVVLQAMY
HHHHHHHHHHHHHHH
23.4321890473
112UbiquitinationVKVVLQAMYLLWKLM
HHHHHHHHHHHHHHH
1.2421890473
112UbiquitinationVKVVLQAMYLLWKLM
HHHHHHHHHHHHHHH
1.2421890473
113PhosphorylationKVVLQAMYLLWKLMW
HHHHHHHHHHHHHHC
11.1428634298
125UbiquitinationLMWREPGAYIFLQNP
HHCCCCCEEEEECCC
12.64-
125UbiquitinationLMWREPGAYIFLQNP
HHCCCCCEEEEECCC
12.6421987572
179UbiquitinationHPLVLLAKWYEKFFG
CHHHHHHHHHHHHHH
50.7222817900
183UbiquitinationLLAKWYEKFFGRLSH
HHHHHHHHHHHHHHH
30.2321890473
217UbiquitinationRAVTVYDKPASFFKE
EEEEEECCCHHHHCC
25.4621890473
223UbiquitinationDKPASFFKETPLDLQ
CCCHHHHCCCCCCHH
59.6822817900
236UbiquitinationLQHRLFMKLGSMHSP
HHHHHHHHHCCCCCC
42.2221987572
239PhosphorylationRLFMKLGSMHSPFRA
HHHHHHCCCCCCCCC
24.6118691976
242PhosphorylationMKLGSMHSPFRARSE
HHHCCCCCCCCCCCC
19.6626931382
284UbiquitinationPALLVSSTSWTEDED
CEEEEECCCCCCCCC
22.3021963094
284UbiquitinationPALLVSSTSWTEDED
CEEEEECCCCCCCCC
22.30-
322UbiquitinationLVCVITGKGPLREYY
EEEEEECCCHHHHHH
49.02-
382UbiquitinationLPMKVVDMFGCCLPV
CCHHHHHHHCCCHHH
1.7821963094
395UbiquitinationPVCAVNFKCLHELVK
HHHHHCHHHHHHHHH
30.5921963094

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 ALG1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALG1_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 ALG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ALG1_HUMAN !!

Drug and Disease Associations
Kegg Disease
H00118 Congenital disorders of glycosylation (CDG) type I
OMIM Disease
608540Congenital disorder of glycosylation 1K (CDG1K)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALG1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-242, AND MASSSPECTROMETRY.

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