UniProtKB/Swiss-Prot PTM Description

The soluble form derives from the membrane form by proteolytic processing, N-linked glycan is a mixture of high mannose and complex type. Glycan structure does not influence binding affinity to CD40, Not O-glycosylated

Glycosylation Sites

Position Structures Description Evidence
ASN-240 Associated Structures: 12 global GlycoSuite
Site-Specific Information

A number of glycan structures have been assigned to specific glycosylation sites

Position Structures Description Evidence
ASN-240 Associated Structures: 12 Site specific GlycoSuite

Notes

Accompanying information sourced from GlycoSuiteDB

  1. ASN-240 [ONLY POSSIBLE EXTRACELLULAR ASN-GLYCOSYLATION SITE
  2. ASN-240 [ONLY POSSIBLE EXTRACELLULAR ASN-GLYCOSYLATION SITE

Sequence

MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL

References 1

  1. Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells

    Khandekar, Silverman, Wells-Marani, Bacon, Birrell, Brigham-Burke, DeMarini, Jonak, Camilleri, Fishman-Lobell

    PubMed: 11676606 Year: 2001