ALG2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Alpha-1,3-mannosyltransferase ALG2''' is an [[enzyme]] that is encoded by the ''ALG2'' [[gene]].<ref name="pmid18400550">{{cite journal | vauthors = Jackson BJ, Kukuruzinska MA, Robbins P | title = Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation | journal = Glycobiology | volume = 3 | issue = 4 | pages = 357–64 | date = August 1993 | pmid = 8400550 | pmc =  | doi = 10.1093/glycob/3.4.357 }}</ref>  Mutations in the human gene are associated with congenital defects in glycosylation <ref name="ThielSchwarz2003">{{cite journal | vauthors = Thiel C, Schwarz M, Peng J, Grzmil M, Hasilik M, Braulke T, Kohlschütter A, von Figura K, Lehle L, Körner C | title = A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis | journal = The Journal of Biological Chemistry | volume = 278 | issue = 25 | pages = 22498–505 | date = June 2003 | pmid = 12684507 | doi = 10.1074/jbc.M302850200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85365| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)
| HGNCid = 23159
| Symbol = ALG2
| AltSymbols =; CDGIi; FLJ14511; hALPG2
| OMIM = 607905
| ECnumber = 
| Homologene = 5930
| MGIid = 1914731
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0009058 |text = biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 85365
    | Hs_Ensembl = ENSG00000119523
    | Hs_RefseqProtein = NP_149078
    | Hs_RefseqmRNA = NM_033087
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 101018529
    | Hs_GenLoc_end = 101024057
    | Hs_Uniprot = Q9H553
    | Mm_EntrezGene = 56737
    | Mm_Ensembl = ENSMUSG00000039740
    | Mm_RefseqmRNA = NM_019998
    | Mm_RefseqProtein = NP_064382
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 47490934
    | Mm_GenLoc_end = 47495425
    | Mm_Uniprot = Q9JJA8
  }}
}}
'''Asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)''', also known as '''ALG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85365| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the glycosyltransferase 1 family. The encoded protein acts as an alpha 1,3 mannosyltransferase, mannosylating Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. Defects in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ii).<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the glycosyltransferase 1 family. The encoded protein acts as an alpha 1,3 mannosyltransferase, mannosylating Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. Defects in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ii).<ref name="entrez">{{cite web | title = Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85365| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ALG2 has been shown to [[Protein-protein interaction|interact]] with  [[ANXA7]]<ref name=pmid12445460>{{cite journal | vauthors = Satoh H, Nakano Y, Shibata H, Maki M | title = The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner | journal = Biochimica et Biophysica Acta | volume = 1600 | issue = 1-2 | pages = 61–7 | date = November 2002 | pmid = 12445460 | doi = 10.1016/S1570-9639(02)00445-4 }}</ref> and [[ANXA11]].<ref name=pmid12445460/>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Jaeken J | title = Congenital disorders of glycosylation (CDG): update and new developments | journal = Journal of Inherited Metabolic Disease | volume = 27 | issue = 3 | pages = 423–6 | year = 2005 | pmid = 15272470 | doi = 10.1023/B:BOLI.0000031221.44647.9e }}
| citations =
* {{cite journal | vauthors = Jaeken J, Carchon H | title = Congenital disorders of glycosylation: a booming chapter of pediatrics | journal = Current Opinion in Pediatrics | volume = 16 | issue = 4 | pages = 434–9 | date = August 2004 | pmid = 15273506 | doi = 10.1097/01.mop.0000133636.56790.4a }}
*{{cite journal | author=Jaeken J |title=Congenital disorders of glycosylation (CDG): update and new developments. |journal=J. Inherit. Metab. Dis. |volume=27 |issue= 3 |pages= 423-6 |year= 2005 |pmid= 15272470 |doi= }}
* {{cite journal | vauthors = Satoh H, Shibata H, Nakano Y, Kitaura Y, Maki M | title = ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner | journal = Biochemical and Biophysical Research Communications | volume = 291 | issue = 5 | pages = 1166–72 | date = March 2002 | pmid = 11883939 | doi = 10.1006/bbrc.2002.6600 }} NB ALG-2 is NOT the protein product of the ALG2 gene.
*{{cite journal | author=Jaeken J, Carchon H |title=Congenital disorders of glycosylation: a booming chapter of pediatrics. |journal=Curr. Opin. Pediatr. |volume=16 |issue= 4 |pages= 434-9 |year= 2004 |pmid= 15273506 |doi= }}
* {{cite journal | vauthors = Satoh H, Nakano Y, Shibata H, Maki M | title = The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner | journal = Biochimica et Biophysica Acta | volume = 1600 | issue = 1-2 | pages = 61–7 | date = November 2002 | pmid = 12445460 | doi = 10.1016/S1570-9639(02)00445-4 }} NB ALG-2 is NOT the protein product of the ALG2 gene.
*{{cite journal | author=Satoh H, Shibata H, Nakano Y, ''et al.'' |title=ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 5 |pages= 1166-72 |year= 2002 |pmid= 11883939 |doi= 10.1006/bbrc.2002.6600 }}
* {{cite journal | vauthors = Hansen C, Tarabykina S, la Cour JM, Lollike K, Berchtold MW | title = The PEF family proteins sorcin and grancalcin interact in vivo and in vitro | journal = FEBS Letters | volume = 545 | issue = 2-3 | pages = 151–4 | date = June 2003 | pmid = 12804766 | doi = 10.1016/S0014-5793(03)00518-0 }}
*{{cite journal | author=Satoh H, Nakano Y, Shibata H, Maki M |title=The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner. |journal=Biochim. Biophys. Acta |volume=1600 |issue= 1-2 |pages= 61-7 |year= 2002 |pmid= 12445460 |doi= }}
* {{cite journal | vauthors = Shibata H, Yamada K, Mizuno T, Yorikawa C, Takahashi H, Satoh H, Kitaura Y, Maki M | title = The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1 | journal = Journal of Biochemistry | volume = 135 | issue = 1 | pages = 117–28 | date = January 2004 | pmid = 14999017 | doi = 10.1093/jb/mvh014 }} NB ALG-2 is NOT the protein product of the ALG2 gene.
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Katoh K, Suzuki H, Terasawa Y, Mizuno T, Yasuda J, Shibata H, Maki M | title = The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B | journal = The Biochemical Journal | volume = 391 | issue = Pt 3 | pages = 677–85 | date = November 2005 | pmid = 16004603 | pmc = 1276969 | doi = 10.1042/BJ20050398 }} NB ALG-2 is NOT the protein product of the ALG2 gene.
*{{cite journal  | author=Thiel C, Schwarz M, Peng J, ''et al.'' |title=A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis. |journal=J. Biol. Chem. |volume=278 |issue= 25 |pages= 22498-505 |year= 2003 |pmid= 12684507 |doi= 10.1074/jbc.M302850200 }}
* {{cite journal | vauthors = Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T | title = Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries | journal = DNA Research | volume = 12 | issue = 2 | pages = 117–26 | year = 2007 | pmid = 16303743 | doi = 10.1093/dnares/12.2.117 }}
*{{cite journal | author=Hansen C, Tarabykina S, la Cour JM, ''et al.'' |title=The PEF family proteins sorcin and grancalcin interact in vivo and in vitro. |journal=FEBS Lett. |volume=545 |issue= 2-3 |pages= 151-4 |year= 2003 |pmid= 12804766 |doi=  }}
* {{cite journal | vauthors = Draeby I, Woods YL, la Cour JM, Mollerup J, Bourdon JC, Berchtold MW | title = The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane | journal = Archives of Biochemistry and Biophysics | volume = 467 | issue = 1 | pages = 87–94 | date = November 2007 | pmid = 17889823 | pmc = 2691584 | doi = 10.1016/j.abb.2007.07.028 }} NB ALG-2 is NOT the protein product of the ALG2 gene.
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Shibata H, Yamada K, Mizuno T, ''et al.'' |title=The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1. |journal=J. Biochem. |volume=135 |issue= 1 |pages= 117-28 |year= 2004 |pmid= 14999017 |doi=  }}
*{{cite journal  | author=Humphray SJ, Oliver K, Hunt AR, ''et al.'' |title=DNA sequence and analysis of human chromosome 9. |journal=Nature |volume=429 |issue= 6990 |pages= 369-74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Katoh K, Suzuki H, Terasawa Y, ''et al.'' |title=The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B. |journal=Biochem. J. |volume=391 |issue= Pt 3 |pages= 677-85 |year= 2006 |pmid= 16004603 |doi= 10.1042/BJ20050398 }}
*{{cite journal | author=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Draeby I, Woods YL, la Cour JM, ''et al.'' |title=The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane. |journal=Arch. Biochem. Biophys. |volume=467 |issue= 1 |pages= 87-94 |year= 2007 |pmid= 17889823 |doi= 10.1016/j.abb.2007.07.028 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* [https://www.ncbi.nlm.nih.gov/books/NBK1332/  GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
* {{UCSC gene info|ALG2}}
 
 
{{Glycosyltransferases}}
 
{{gene-9-stub}}

Latest revision as of 17:58, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Alpha-1,3-mannosyltransferase ALG2 is an enzyme that is encoded by the ALG2 gene.[1] Mutations in the human gene are associated with congenital defects in glycosylation [2][3]

Function

This gene encodes a member of the glycosyltransferase 1 family. The encoded protein acts as an alpha 1,3 mannosyltransferase, mannosylating Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. Defects in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ii).[3]

Interactions

ALG2 has been shown to interact with ANXA7[4] and ANXA11.[4]

References

  1. ↑ Jackson BJ, Kukuruzinska MA, Robbins P (August 1993). "Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation". Glycobiology. 3 (4): 357–64. doi:10.1093/glycob/3.4.357. PMID 8400550.
  2. ↑ Thiel C, Schwarz M, Peng J, Grzmil M, Hasilik M, Braulke T, Kohlschütter A, von Figura K, Lehle L, Körner C (June 2003). "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis". The Journal of Biological Chemistry. 278 (25): 22498–505. doi:10.1074/jbc.M302850200. PMID 12684507.
  3. ↑ 3.0 3.1 "Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)".
  4. ↑ 4.0 4.1 Satoh H, Nakano Y, Shibata H, Maki M (November 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochimica et Biophysica Acta. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.

Further reading

External links


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