• integral component of membrane • endoplasmic reticulum membrane • endoplasmic reticulum • membrane
Biological process
• dolichol-linked oligosaccharide biosynthetic process • mannosylation • protein glycosylation
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
56052
208211
Ensembl
ENSG00000033011
ENSMUSG00000039427
UniProt
Q9BT22
Q921Q3
RefSeq (mRNA)
NM_019109 NM_001330504
NM_145362
RefSeq (protein)
NP_001317433 NP_061982
NP_663337
Location (UCSC)
Chr 16: 5.03 – 5.09 Mb
Chr 16: 5.23 – 5.24 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Chitobiosyldiphosphodolichol beta-mannosyltransferase is an enzyme that is encoded by the ALG1 gene [5] whose structure and function has been conserved from yeast to man.[6][7]
Contents
1Function
2References
3Further reading
4External links
Function[edit]
The biosynthesis of lipid-linked oligosaccharides is highly conserved among eukaryotes and is catalyzed by 14 glycosyltransferases in an ordered stepwise manner. The Alg1 mannosyltransferase I (MT I) catalyzes the first mannosylation step in this process.[6]
References[edit]
^ abcGRCh38: Ensembl release 89: ENSG00000033011 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000039427 - Ensembl, May 2017
^Couto JR, Huffaker TC, Robbins PW (1984). "Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway". J. Biol. Chem. 259 (1): 378–82. PMID 6368538.
^Takahashi T, Honda R, Nishikawa Y (Mar 2000). "Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1". Glycobiology. 10 (3): 321–7. doi:10.1093/glycob/10.3.321. PMID 10704531.
Couto JR, Huffaker TC, Robbins PW (January 1984). "Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway". J. Biol. Chem. 259 (1): 378–82. PMID 6368538.
Gao XD, Nishikawa A, Dean N (June 2004). "Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum". Glycobiology. 14 (6): 559–70. doi:10.1093/glycob/cwh072. PMID 15044395.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Kranz C, Denecke J, Lehle L, et al. (2004). "Congenital Disorder of Glycosylation Type Ik (CDG-Ik): A Defect of Mannosyltransferase I". Am. J. Hum. Genet. 74 (3): 545–51. doi:10.1086/382493. PMC 1182267. PMID 14973782.
Schwarz M, Thiel C, Lübbehusen J, et al. (2004). "Deficiency of GDP-Man:GlcNAc2-PP-Dolichol Mannosyltransferase Causes Congenital Disorder of Glycosylation Type Ik". Am. J. Hum. Genet. 74 (3): 472–81. doi:10.1086/382492. PMC 1182261. PMID 14973778.
Grubenmann CE, Frank CG, Hülsmeier AJ, et al. (2004). "Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik". Hum. Mol. Genet. 13 (5): 535–42. doi:10.1093/hmg/ddh050. PMID 14709599.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
External links[edit]
GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview
Human ALG1 genome location and ALG1 gene details page in the UCSC Genome Browser.
Full-time equivalent From Wikipedia, the free encyclopedia Jump to navigation Jump to search Full-time equivalent ( FTE ) or whole time equivalent ( WTE ) is a unit that indicates the workload of an employed person (or student) in a way that makes workloads or class loads comparable [1] across various contexts. FTE is often used to measure a worker's or student's involvement in a project, or to track cost reductions in an organization. An FTE of 1.0 is equivalent to a full-time worker or student, while an FTE of 0.5 signals half of a full work or school load. [2] Contents 1 U.S. Federal Government 2 In education 2.1 Example 3 Notes 4 References U.S. Federal Government [ edit ] In the U.S. Federal Government, FTE is defined by the Government Accountability Office (GAO) as the number of total hours worked divided by the maximum number of compensable hours in a full-time schedule as
Bicuculline From Wikipedia, the free encyclopedia Jump to navigation Jump to search Bicuculline Clinical data ATC code none Identifiers IUPAC name (6 R )-6-[(5 S )-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5- g ]isoquinolin-5-yl]furo[3,4- e ][1,3]benzodioxol-8(6 H )-one CAS Number 485-49-4 Y PubChem CID 10237 IUPHAR/BPS 2312 ChemSpider 9820 Y UNII Y37615DVKC ChEBI CHEBI:3092 N ChEMBL ChEMBL417990 N ECHA InfoCard 100.006.927 Chemical and physical data Formula C 20 H 17 N O 6 Molar mass 367.352 g/mol 3D model (JSmol) Interactive image Melting point 215 °C (419 °F) SMILES O=C1O[C@H](c3c1c2OCOc2cc3)[C@@H]5c4cc6OCOc6cc4CCN5C InChI InChI=1S/C20H17NO6/c1-21-5-4-10-6-14-15(25-8-24-14)7-12(10)17(21)18-11-2-3-13-19(26-9-23-13)16(11)20(22)27-18/h2-3,6-7,17-18H,4-5,8-9H2,1H3/t17-,18+/m0/s1 Y Key:IYGYMKDQCDOMRE-ZWKOTPCHSA-N
Clash Royale CLAN TAG
