ALG1 |
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Identifikatori |
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Alijasi | ALG1 |
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Spoljašnji ID | OMIM: 605907 MGI: 2384774 HomoloGene: 5387 GeneCards: ALG1 |
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Genska lokacija (miš) |
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![Chromosome 16 (mouse)](//upload.wikimedia.org/wikipedia/commons/thumb/2/28/Ideogram_house_mouse_chromosome_16.svg/260px-Ideogram_house_mouse_chromosome_16.svg.png) | Hr. | Chromosome 16 (mouse)[1] |
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| Band | 16|16 A1 | Start | 5,051,485 bp[1] |
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Kraj | 5,062,776 bp[1] |
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Genska ontologija |
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Molecular function | • transferase activity • glycosyltransferase activity • mannosyltransferase activity • chitobiosyldiphosphodolichol beta-mannosyltransferase activity
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Cellular component | • саставни део мембране • endoplasmic reticulum membrane • ендоплазматични ретикулум • мембрана
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Biological process | • dolichol-linked oligosaccharide biosynthetic process • mannosylation • GO:0033578, GO:0033577, GO:0033575, GO:0033576 protein glycosylation
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Sources:Amigo / QuickGO |
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Ortolozi |
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Vrste | Čovek | Miš |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | | |
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Location (UCSC) | n/a | Chr 16: 5.05 – 5.06 Mb |
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PubMed search | [2] | [3] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Hitobiozildifosfodolihol beta-manoziltransferaza je enzim koji je kodiran ALG1 genom.[4] Njena struktura i funkcija je očuvana od nižih ka višim organizmima.[5][6]
Funkcija
Biosinteza oligosaharida vezanih za lipide je visoko očuvana među eukariotima i katalizovana je od strane 14 glikoziltransferaza na uređen postupni način. Alg1 manoziltransferaza I (MT I) katalizuje prvi korak manozilacije u ovom procesu.[5] Klinički, nedostatak ALG1 kod ljudi dovodi do ALG1-CDG, urođenog poremećaja glikozilacije.[7]
Reference
- ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000039427 - Ensembl, May 2017
- ^ „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ „Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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. doi:10.1016/S0021-9258(17)43670-2
. - ^ а б „Entrez Gene: ALG1 asparagine-linked glycosylation 1 homolog (S. cerevisiae, beta-1,4-mannosyltransferase)”.
- ^ Takahashi T, Honda R, Nishikawa Y (март 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. PMID 10704531. doi:10.1093/glycob/10.3.321. CS1 одржавање: Формат датума (веза)
- ^ „# 608540 CONGENITAL DISORDER OF GLYCOSYLATION, TYPE Ik; CDG1K”. Johns Hopkins University. Приступљено 2019-05-01.
Literatura
- Couto JR, Huffaker TC, Robbins PW (јануар 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. doi:10.1016/S0021-9258(17)43670-2
. CS1 одржавање: Формат датума (веза) - Gao XD, Nishikawa A, Dean N (јун 2004). „Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum”. Glycobiology. 14 (6): 559—70. PMID 15044395. doi:10.1093/glycob/cwh072
. CS1 одржавање: Формат датума (веза) - 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. PMID 16303743. doi:10.1093/dnares/12.2.117
. - 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. PMC 528928
. PMID 15489334. doi:10.1101/gr.2596504. - 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. PMC 1182267
. PMID 14973782. doi:10.1086/382493. - 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. PMC 1182261
. PMID 14973778. doi:10.1086/382492. - 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. PMID 14709599. doi:10.1093/hmg/ddh050
. - 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. PMC 403697
. PMID 12975309. doi:10.1101/gr.1293003. - 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. Bibcode:2002PNAS...9916899M. PMC 139241
. PMID 12477932. doi:10.1073/pnas.242603899
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Spoljašnje veze
- 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.
2.4.1: Heksozil- transferaze | |
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2.4.2: Pentozil- transferaze | |
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2.4.99: Sijalil transferaze | |
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