UniProtKB/Swiss-Prot PTM Description

The lysosomal precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins, N-linked glycans show a high degree of microheterogeneity, The one residue extended Saposin-B-Val is only found in 5% of the chains

Glycosylation Sites

Position Structures Description Evidence
ASN-215 Associated Structures: 52 global GlycoSuite
Position Structures Description Evidence
ASN-332 Associated Structures: 17 global GlycoSuite
Position Structures Description Evidence
ASN-426 Associated Structures: 4 global GlycoSuite
Position Structures Description Evidence
ASN-80, ASN-101 Associated Structures: 17 global GlycoSuite
Site-Specific Information

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

Position Structures Description Evidence
ASN-215 Associated Structures: 1 Site specific GlycoSuite

Notes

Accompanying information sourced from GlycoSuiteDB

  1. ASN-215 [KLEINSCHMIDT ET AL. (1988) BIOL. CHEM. HOPPE SEYLER 369:1361-1365
  2. EXCEPT IN METACHROMATIC LEUKODYSTROPHY WHERE MUTATION THR-217 TO I-217 [KRETZ ET AL. (1990) PNAS 87:2541-2544
  3. OR MUTATION ASN-215 TO K-215 [REGIS ET AL (1999) EUR. J. HUM. GENET. 7:125-130
  4. ASN-426 [FURST ET AL. (1988) BIOL. CHEM. HOPPE SEYLER 369:317-328
  5. ASN-80 & ASN-101 [MORIMOTO ET AL. (1989) PNAS 86:3389-3393
  6. ASN-332 [KLEINSCHMIDT ET AL. (1987) BIOL. CHEM. HOPPE SEYLER 368:1571-1578

Sequence

MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN