Amino acid distributions around O-linked glycosylation sites
To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most promine...
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| Veröffentlicht in: | Biochemical journal 1991-04, Vol.275 (2), p.529-534 |
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| container_title | Biochemical journal |
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| creator | WILSON, I. B. H GAVEL, Y VON HEIJNE, G |
| description | To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data. |
| doi_str_mv | 10.1042/bj2750529 |
| format | Article |
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B. H ; GAVEL, Y ; VON HEIJNE, G</creator><creatorcontrib>WILSON, I. B. H ; GAVEL, Y ; VON HEIJNE, G</creatorcontrib><description>To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2750529</identifier><identifier>PMID: 2025231</identifier><language>eng</language><publisher>Colchester: Portland Press</publisher><subject>Acetylgalactosamine ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Databases, Factual ; Fundamental and applied biological sciences. 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B. H</creatorcontrib><creatorcontrib>GAVEL, Y</creatorcontrib><creatorcontrib>VON HEIJNE, G</creatorcontrib><title>Amino acid distributions around O-linked glycosylation sites</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data.</description><subject>Acetylgalactosamine</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Databases, Factual</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Glycoproteins - chemistry</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Proteins</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE9LwzAYh4Moc04PfgChFwUP1TdpkqYgwhj-g8Eueg5Jms7MrplJK-zbu7ky9ZTD8_C84YfQOYYbDJTc6gXJGTBSHKAhpjmkIifiEA2BcJpyIPgYncS4AMAUKAzQgABhJMNDdDdeusYnyrgyKV1sg9Nd63wTExV815TJLK1d82HLZF6vjY_rWm1xEl1r4yk6qlQd7Vn_jtDb48Pr5Dmdzp5eJuNpaijnbaoN55hozDCvMOZCVSVmtDA5qZgWRgPXnHFNDANLraoKTrW2hRAqE5CJLBuh-1131emlLY1t2qBquQpuqcJaeuXkf9K4dzn3XxJjBvATuOoDwX92NrZy6aKxda0a67soBTDKi1xsxOudaIKPMdhqfwSD3E4t91Nv3Iu_v9qb_bYbftlzFY2qq6Aa4-JvsMhBcEGzb5B7hrY</recordid><startdate>19910415</startdate><enddate>19910415</enddate><creator>WILSON, I. B. 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H ; GAVEL, Y ; VON HEIJNE, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466t-bc6612b1516f1168afd1549c72f5b8cb06b656b2c50e4eaf964bbe988a3803833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Acetylgalactosamine</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Databases, Factual</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Glycoproteins - chemistry</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Proteins</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WILSON, I. B. H</creatorcontrib><creatorcontrib>GAVEL, Y</creatorcontrib><creatorcontrib>VON HEIJNE, G</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WILSON, I. B. H</au><au>GAVEL, Y</au><au>VON HEIJNE, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid distributions around O-linked glycosylation sites</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1991-04-15</date><risdate>1991</risdate><volume>275</volume><issue>2</issue><spage>529</spage><epage>534</epage><pages>529-534</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data.</abstract><cop>Colchester</cop><pub>Portland Press</pub><pmid>2025231</pmid><doi>10.1042/bj2750529</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1991-04, Vol.275 (2), p.529-534 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Acetylgalactosamine Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Databases, Factual Fundamental and applied biological sciences. Psychology Glycoproteins Glycoproteins - chemistry Glycosylation Humans Proteins Sequence Homology, Nucleic Acid |
| title | Amino acid distributions around O-linked glycosylation sites |
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