O-GLYCBASE version 2.0: a revised database of O-glycosylated proteins

Jan Hansen; Ole Lund; Kristoffer Rapacki; Søren Brunak

O-GLYCBASE version 2.0: a revised database of O-glycosylated proteins

Jan Hansen, Ole Lund, Kristoffer Rapacki, Søren Brunak

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

O-GLYCBASE is an updated database of information on glycoproteins and their O-linked glycosylation sites. Entries are compiled and revised from the literature, and from the SWISS-PROT database. Entries include information about species, sequence, glycosylation sites and glycan type. O-GLYCBASE is now fully cross-referenced to the SWISS-PROT, PIR, PROSITE, PDB, EMBL, HSSP, LISTA and MIM databases. Compared with version 1.0 the number of entries have increased by 34%. Revision of the O-glycan assignment was performed on 20% of the entries. Sequence logos displaying the acceptor specificity patterns for the GalNAc, mannose and GlcNAc transferases are shown. The O-GLYCBASE database is available through WWW or by anonymous FTP.

Original language	English
Journal	Nucleic Acids Research
Volume	25
Issue number	1
Pages (from-to)	278-282
ISSN	0305-1048
Publication status	Published - 1997

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@article{5b61c207aba343278a473e17aeb353f3,

title = "O-GLYCBASE version 2.0: a revised database of O-glycosylated proteins",

abstract = "O-GLYCBASE is an updated database of information on glycoproteins and their O-linked glycosylation sites. Entries are compiled and revised from the literature, and from the SWISS-PROT database. Entries include information about species, sequence, glycosylation sites and glycan type. O-GLYCBASE is now fully cross-referenced to the SWISS-PROT, PIR, PROSITE, PDB, EMBL, HSSP, LISTA and MIM databases. Compared with version 1.0 the number of entries have increased by 34%. Revision of the O-glycan assignment was performed on 20% of the entries. Sequence logos displaying the acceptor specificity patterns for the GalNAc, mannose and GlcNAc transferases are shown. The O-GLYCBASE database is available through WWW or by anonymous FTP.",

author = "Jan Hansen and Ole Lund and Kristoffer Rapacki and S{\o}ren Brunak",

year = "1997",

language = "English",

volume = "25",

pages = "278--282",

journal = "Nucleic Acids Research",

issn = "0305-1048",

publisher = "Oxford University Press",

number = "1",

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TY - JOUR

T1 - O-GLYCBASE version 2.0: a revised database of O-glycosylated proteins

AU - Hansen, Jan

AU - Lund, Ole

AU - Rapacki, Kristoffer

AU - Brunak, Søren

PY - 1997

Y1 - 1997

N2 - O-GLYCBASE is an updated database of information on glycoproteins and their O-linked glycosylation sites. Entries are compiled and revised from the literature, and from the SWISS-PROT database. Entries include information about species, sequence, glycosylation sites and glycan type. O-GLYCBASE is now fully cross-referenced to the SWISS-PROT, PIR, PROSITE, PDB, EMBL, HSSP, LISTA and MIM databases. Compared with version 1.0 the number of entries have increased by 34%. Revision of the O-glycan assignment was performed on 20% of the entries. Sequence logos displaying the acceptor specificity patterns for the GalNAc, mannose and GlcNAc transferases are shown. The O-GLYCBASE database is available through WWW or by anonymous FTP.

AB - O-GLYCBASE is an updated database of information on glycoproteins and their O-linked glycosylation sites. Entries are compiled and revised from the literature, and from the SWISS-PROT database. Entries include information about species, sequence, glycosylation sites and glycan type. O-GLYCBASE is now fully cross-referenced to the SWISS-PROT, PIR, PROSITE, PDB, EMBL, HSSP, LISTA and MIM databases. Compared with version 1.0 the number of entries have increased by 34%. Revision of the O-glycan assignment was performed on 20% of the entries. Sequence logos displaying the acceptor specificity patterns for the GalNAc, mannose and GlcNAc transferases are shown. The O-GLYCBASE database is available through WWW or by anonymous FTP.

M3 - Journal article

VL - 25

SP - 278

EP - 282

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 1

ER -