Basic Information
Gene ID
JhiChr07G10393.g
Position
chr7:3689457-3708552 (-)
19095bp
Gene Type
gene
Gene Description (Protein Product)
Protein transport protein Sec24-like
Organism
Also AS AT3G07100

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
JhiChr13G10157.g transport) protein
JhiChr08G10798.g transport protein

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Annotation

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


Pathway
GO Term Description GO Category
GO:0000003 reproduction BP
GO:0006275 regulation of DNA replication BP
GO:0006996 organelle organization BP
GO:0007029 endoplasmic reticulum organization BP
GO:0007030 Golgi organization BP
GO:0007276 gamete generation BP
GO:0008150 biological_process BP
GO:0008156 negative regulation of DNA replication BP
GO:0008361 regulation of cell size BP
GO:0009889 regulation of biosynthetic process BP
GO:0009890 negative regulation of biosynthetic process BP
GO:0009892 negative regulation of metabolic process BP
GO:0009987 cellular process BP
GO:0010256 endomembrane system organization BP
GO:0010556 regulation of macromolecule biosynthetic process BP
GO:0010558 negative regulation of macromolecule biosynthetic process BP
GO:0010564 regulation of cell cycle process BP
GO:0010605 negative regulation of macromolecule metabolic process BP
GO:0010948 negative regulation of cell cycle process BP
GO:0016043 cellular component organization BP
GO:0019219 regulation of nucleobase-containing compound metabolic process BP
GO:0019222 regulation of metabolic process BP
GO:0019953 sexual reproduction BP
GO:0022414 reproductive process BP
GO:0031323 regulation of cellular metabolic process BP
GO:0031324 negative regulation of cellular metabolic process BP
GO:0031326 regulation of cellular biosynthetic process BP
GO:0031327 negative regulation of cellular biosynthetic process BP
GO:0032501 multicellular organismal process BP
GO:0032504 multicellular organism reproduction BP
GO:0032535 regulation of cellular component size BP
GO:0032875 regulation of DNA endoreduplication BP
GO:0032876 negative regulation of DNA endoreduplication BP
GO:0044703 multi-organism reproductive process BP
GO:0045786 negative regulation of cell cycle BP
GO:0045934 negative regulation of nucleobase-containing compound metabolic process BP
GO:0048232 male gamete generation BP
GO:0048519 negative regulation of biological process BP
GO:0048523 negative regulation of cellular process BP
GO:0048609 multicellular organismal reproductive process BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0051052 regulation of DNA metabolic process BP
GO:0051053 negative regulation of DNA metabolic process BP
GO:0051171 regulation of nitrogen compound metabolic process BP
GO:0051172 negative regulation of nitrogen compound metabolic process BP
GO:0051704 obsolete multi-organism process BP
GO:0051726 regulation of cell cycle BP
GO:0060255 regulation of macromolecule metabolic process BP
GO:0065007 biological regulation BP
GO:0065008 regulation of biological quality BP
GO:0071840 cellular component organization or biogenesis BP
GO:0080090 regulation of primary metabolic process BP
GO:0080119 ER body organization BP
GO:0090066 regulation of anatomical structure size BP
GO:0090329 regulation of DNA-templated DNA replication BP
GO:2000104 negative regulation of DNA-templated DNA replication BP
GO:2000112 regulation of cellular macromolecule biosynthetic process BP
GO:2000113 negative regulation of cellular macromolecule biosynthetic process BP
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.