Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
ACSA_36378.g
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Position
acsa_381:37843409-37845714 (+)
2305bp
Gene Type
gene
Gene Description (Protein Product)
B-cell receptor-associated protein
Organism
Acer saccharum
Also AS AT5G42570

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
ACSA_37011.g B-cell receptor-associated protein
ACSA_37677.g Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser Thr consensus motif in nascent polypeptide chains
ACSA_38010.g Carbon-nitrogen hydrolase
Regulatory gene
ACSA_00040.g Transcription factor
ACSA_00250.g Transcription factor
ACSA_00309.g Zinc-finger homeodomain protein

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
KEGG Pathway
KEGG Term Name Description
map04141 Protein processing in endoplasmic reticulum The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.