ALG8_HUMAN - dbPTM
ALG8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALG8_HUMAN
UniProt AC Q9BVK2
Protein Name Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
Gene Name ALG8
Organism Homo sapiens (Human).
Sequence Length 526
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity)..
Protein Sequence MAALTIATGTGNWFSALALGVTLLKCLLIPTYHSTDFEVHRNWLAITHSLPISQWYYEATSEWTLDYPPFFAWFEYILSHVAKYFDQEMLNVHNLNYSSSRTLLFQRFSVIFMDVLFVYAVRECCKCIDGKKVGKELTEKPKFILSVLLLWNFGLLIVDHIHFQYNGFLFGLMLLSIARLFQKRHMEGAFLFAVLLHFKHIYLYVAPAYGVYLLRSYCFTANKPDGSIRWKSFSFVRVISLGLVVFLVSALSLGPFLALNQLPQVFSRLFPFKRGLCHAYWAPNFWALYNALDKVLSVIGLKLKFLDPNNIPKASMTSGLVQQFQHTVLPSVTPLATLICTLIAILPSIFCLWFKPQGPRGFLRCLTLCALSSFMFGWHVHEKAILLAILPMSLLSVGKAGDASIFLILTTTGHYSLFPLLFTAPELPIKILLMLLFTIYSISSLKTLFRKEKPLFNWMETFYLLGLGPLEVCCEFVFPFTSWKVKYPFIPLLLTSVYCAVGITYAWFKLYVSVLIDSAIGKTKKQ
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
35PhosphorylationLIPTYHSTDFEVHRN
HCCCCCCCCHHHHHH
31.2524719451
49PhosphorylationNWLAITHSLPISQWY
HHHHHEECCCHHHHH
27.4722251617
53PhosphorylationITHSLPISQWYYEAT
HEECCCHHHHHHHCC
16.8422251625
61PhosphorylationQWYYEATSEWTLDYP
HHHHHCCCCCCCCCC
37.8822251633
138PhosphorylationKKVGKELTEKPKFIL
CCCCHHHHCCCHHHH
42.9529083192
216PhosphorylationYGVYLLRSYCFTANK
HHHHHHHHHHEECCC
26.6546162311
223UbiquitinationSYCFTANKPDGSIRW
HHHEECCCCCCCEEC
41.8621906983
231UbiquitinationPDGSIRWKSFSFVRV
CCCCEECCCCCHHHH
31.6021890473
231UbiquitinationPDGSIRWKSFSFVRV
CCCCEECCCCCHHHH
31.6021890473
273UbiquitinationFSRLFPFKRGLCHAY
HHHHCCCCCCCCCCC
45.88-
302UbiquitinationVLSVIGLKLKFLDPN
HHHHHCCCCEECCCC
44.40-
304UbiquitinationSVIGLKLKFLDPNNI
HHHCCCCEECCCCCC
42.1521890473
304UbiquitinationSVIGLKLKFLDPNNI
HHHCCCCEECCCCCC
42.1521890473
440PhosphorylationLMLLFTIYSISSLKT
HHHHHHHHHHHHHHH
9.2629496907
443PhosphorylationLFTIYSISSLKTLFR
HHHHHHHHHHHHHHH
24.5524719451
444PhosphorylationFTIYSISSLKTLFRK
HHHHHHHHHHHHHHC
32.0129496907
511PhosphorylationTYAWFKLYVSVLIDS
HHHHHHHHHHHHHHH
7.4146162317

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 ALG8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALG8_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 ALG8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ULA1_HUMANNAE1physical
21988832
KS6A5_HUMANRPS6KA5physical
21988832

Drug and Disease Associations
Kegg Disease
H00118 Congenital disorders of glycosylation (CDG) type I
OMIM Disease
608104Congenital disorder of glycosylation 1H (CDG1H)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALG8_HUMAN

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Related Literatures of Post-Translational Modification

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