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Genes / Proteins / Lipids Glycans / Glycoconjugates Glycomes Pathways / Interactions / Diseases / Organisms
bZIP transcription factor 17
Summary
- UniProt ID
- O22208
- Gene Symbol
-
- BZIP17
- Organism
- Arabidopsis thaliana (thale cress)
External Links
Annotation
- Keyword
-
- Activator
- DNA-binding
- Endoplasmic reticulum
- Glycoprotein
- Golgi apparatus
- Nucleus
- Reference proteome
- Stress response
- Transcription regulation
- Transmembrane helix
- Gene Ontology (GO)
| GO Term |
|---|
| regulation of DNA-templated transcription |
| positive regulation of DNA-templated transcription |
| hyperosmotic salinity response |
| GO Term |
|---|
| Golgi membrane |
| nucleus |
| endoplasmic reticulum |
| endoplasmic reticulum membrane |
| GO Term |
|---|
| transcription cis-regulatory region binding |
| DNA-binding transcription factor activity |
| sequence-specific DNA binding |
Sequence
MAEPITKEQPPPPAPDPNSTYPPPSDFDSISIPPLDDHFSDQTPIGELMSDLGFPDGEFELTFDGMDDLYFPAENESFLIPINTSNQEQFGDFTPESESSGISGDCIVPKDADKTITTSGCINRESPRDSDDRCSGADHNLDLPTPLSSQGSGNCGSDVSEATNESSPKSRNVAVDQKVKVEEAATTTTSITKRKKEIDEDLTDESRNSKYRRSGEDADASAVTGEEDEKKRARLMRNRESAQLSRQRKKHYVEELEEKVRNMHSTITDLNGKISYFMAENATLRQQLGGNGMCPPHLPPPPMGMYPPMAPMPYPWMPCPPYMVKQQGSQVPLIPIPRLKPQNTLGTSKAKKSESKKSEAKTKKVASISFLGLLFCLFLFGALAPIVNVNYGGISGAFYGNYRSNYITDQIYSQHRDRVLDTSRSGAGTGVSNSNGMHRGRDSDRGARKNISATESSVTPGNGSEPLVASLFVPRNDKLVKIDGNLIINSILASEKAVASRKASESKERKADLMISKDYTPALPLPDVGRTEELAKHLYRSKAEKQKALSSGSADTLKDQVKTKAANGEMQQWFREGVAGPMFSSGMCTEVFQFDVSSTSGAIIPAATNVSAEHGKNTTDTHKQQNRRILRGLPIPLPGSDFNLTKEHQRNSSSKEIKPASSMVVSVLVDPREGGDGDIDGMIGGPKSLSRVFVVVLLDSAKYVTYSCVLPRSGAPHLVTT
Glycosylation Sites
| Position | Description | PubMed ID | GlyTouCan ID | Source |
|---|---|---|---|---|
| 450 | N-linked (GlcNAc...) asparagine |
|
||
| 462 | N-linked (GlcNAc...) asparagine |
|
||
| 609 | N-linked (GlcNAc...) asparagine |
|
||
| 617 | N-linked (GlcNAc...) asparagine |
|
||
| 643 | N-linked (GlcNAc...) asparagine |
|
||
| 651 | N-linked (GlcNAc...) asparagine |
|
Feature
: Glycosylation Site from GlyGen
: Glycosylation Site from UniProt
