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Genes / Proteins / Lipids Glycans / Glycoconjugates Glycomes Pathways / Interactions / Diseases / Organisms
Nucleus-vacuole junction protein 2
Summary
- UniProt ID
- Q06833
- Gene Symbol
-
- NVJ2
- Organism
- Saccharomyces cerevisiae S288C
Annotation
- Keyword
-
- Endoplasmic reticulum
- Glycoprotein
- Lipid transport
- Lipid-binding
- Nucleus
- Phosphoprotein
- Reference proteome
- Signal-anchor
- Transmembrane helix
- Gene Ontology (GO)
| GO Term |
|---|
| mitochondrion-endoplasmic reticulum membrane tethering |
| ER to Golgi ceramide transport |
| phospholipid transport |
| GO Term |
|---|
| lipid transporter activity |
| lipid binding |
Sequence
MASLKVFLAVYLLGGITFLPLVLFTLYKIHLLYSNLKSASKKELDHDTADEIDEKTRLLARDIDPEFKARKLEEQLGVKVFNKGWITVTKQYYYHSSEVAVILKNSNNNKDSDTALQEQILQRTDLKKKQRFFAVLRHGNLFLYKDDSQNANLVHAISLQNRFITIWPRFDELGKEELPDASLFTKRTCIAIFKNDLVSIDSKNHNVILPHFDPLTSAESNNGDISTNDTTHEYQSQFHSSNQFFLYFDNNMDKEDWYYQLINASKNSNSLSTGLLDPNVSANAAHLKTKDMLQLIQDINSTENQLTTKWLNALLGRLFLSLQQTDTLNKFIHEKICKKLNKIKTPGFLDDLVVEKVDVGDSAPLFTSPELLELSPEGSTKIAIDVQYRGNLTIIIATKASINLGSRFKQREVSLQLSIKIKEFSGPLLFLIKPPPSNRIWYAFRTEPIMDFEIEPIVSSSKLSYNVVTNAIKSKFAEAVKESLVVPFMDDIVFYPTPNEVYRGGIWEEQDPEAAARARTAAAASDMNNTSAKEHLEALQEGGMKTQSRIKKALRPERKKENLKDLVDASGVATKTTTQTTVTTATNDDVSSSENSTKSRKYFKNSIKKIGRWYKDNVGNSSDTEDMDEIDVQDKKNDDSADERESDNPILTSNPKMISNRRPVPRRPSQPLNTLSPKLEGRKEKDTENFPVPPSASNMNASKMFANKENRKFSVSSNDSQNSLKNGDPHVKASKLESSQAFVKKTSQNRFNDGFFKQDLEFEEQREPKL
Glycosylation Sites
| Position | Description | PubMed ID | GlyTouCan ID | Source |
|---|---|---|---|---|
| 228 | N-linked (GlcNAc...) asparagine |
|
||
| 263 | N-linked (GlcNAc...) asparagine |
|
||
| 279 | N-linked (GlcNAc...) asparagine |
|
||
| 300 | N-linked (GlcNAc...) asparagine |
|
||
| 391 | N-linked (GlcNAc...) asparagine |
|
||
| 528 | N-linked (GlcNAc...) asparagine |
|
||
| 529 | N-linked (GlcNAc...) asparagine |
|
||
| 595 | N-linked (GlcNAc...) asparagine |
|
||
| 620 | N-linked (GlcNAc...) asparagine |
|
||
| 700 | N-linked (GlcNAc...) asparagine |
|
Feature
: Glycosylation Site from GlyGen
: Glycosylation Site from UniProt
