ALG3_HUMAN - dbPTM
ALG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALG3_HUMAN
UniProt AC Q92685
Protein Name Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
Gene Name ALG3
Organism Homo sapiens (Human).
Sequence Length 438
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol..
Protein Sequence MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWVIHRVAYTEIDWKAYMAEVEGVINGTYDYTQLQGDTGPLVYPAGFVYIFMGLYYATSRGTDIRMAQNIFAVLYLATLLLVFLIYHQTCKVPPFVFFFMCCASYRVHSIFVLRLFNDPVAMVLLFLSINLLLAQRWGWGCCFFSLAVSVKMNVLLFAPGLLFLLLTQFGFRGALPKLGICAGLQVVLGLPFLLENPSGYLSRSFDLGRQFLFHWTVNWRFLPEALFLHRAFHLALLTAHLTLLLLFALCRWHRTGESILSLLRDPSKRKVPPQPLTPNQIVSTLFTSNFIGICFSRSLHYQFYVWYFHTLPYLLWAMPARWLTHLLRLLVLGLIELSWNTYPSTSCSSAALHICHAVILLQLWLGPQPFPKSTQHSKKAH
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
11PhosphorylationGLRKRGRSGSAAQAE
CCCCCCCCCCHHHHH
39.6729255136
13PhosphorylationRKRGRSGSAAQAEGL
CCCCCCCCHHHHHHH
22.9829255136
22UbiquitinationAQAEGLCKQWLQRAW
HHHHHHHHHHHHHHH
49.9421890473
166PhosphorylationCASYRVHSIFVLRLF
HHHHHHHCHHHHHHC
18.1846162275
312PhosphorylationALCRWHRTGESILSL
HHHHHHHCCHHHHHH
32.2021406692
315PhosphorylationRWHRTGESILSLLRD
HHHHCCHHHHHHHCC
30.1221406692
318PhosphorylationRTGESILSLLRDPSK
HCCHHHHHHHCCCCC
24.5621406692
325UbiquitinationSLLRDPSKRKVPPQP
HHHCCCCCCCCCCCC
62.7221890473
355PhosphorylationIGICFSRSLHYQFYV
HHHHHHHCHHHHHHH
20.4928450419
358PhosphorylationCFSRSLHYQFYVWYF
HHHHCHHHHHHHHHH
12.9528450419
361PhosphorylationRSLHYQFYVWYFHTL
HCHHHHHHHHHHHHH
3.7328450419
364PhosphorylationHYQFYVWYFHTLPYL
HHHHHHHHHHHHHHH
3.8728450419
367PhosphorylationFYVWYFHTLPYLLWA
HHHHHHHHHHHHHHH
21.3828450419
370PhosphorylationWYFHTLPYLLWAMPA
HHHHHHHHHHHHCCH
19.9628450419

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 ALG3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALG3_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 ALG3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GFAP_HUMANGFAPphysical
26186194
AL3B1_HUMANALDH3B1physical
26186194
T10IP_HUMANTSGA10IPphysical
26186194
KLH14_HUMANKLHL14physical
26186194
CREB3_HUMANCREB3physical
21516116
T10IP_HUMANTSGA10IPphysical
28514442
KLH14_HUMANKLHL14physical
28514442
GFAP_HUMANGFAPphysical
28514442
AL3B1_HUMANALDH3B1physical
28514442

Drug and Disease Associations
Kegg Disease
H00118 Congenital disorders of glycosylation (CDG) type I
OMIM Disease
601110Congenital disorder of glycosylation 1D (CDG1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALG3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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-13, AND MASSSPECTROMETRY.

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