Basic Information
Gene ID
Position
GWHASIS00001973:1271384-1273929 (+)
2545bp
Gene Type
gene
Gene Description (Protein Product)
protein folding in endoplasmic reticulum
Organism
Also AS AT5G49540

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
EVM0027560 ER membrane protein complex subunit
EVM0032833 Belongs to the SecY SEC61-alpha family
EVM0028195 Lysine histidine transporter-like
Regulatory gene
EVM0000098 DnaJ homolog; subfamily C; member
EVM0001373 Transcriptional regulator
EVM0001481 Transcription factor

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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:0000045 autophagosome assembly BP
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0005789 endoplasmic reticulum membrane CC
GO:0006457 protein folding BP
GO:0006914 autophagy BP
GO:0006996 organelle organization BP
GO:0007033 vacuole organization BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009056 catabolic process BP
GO:0009987 cellular process BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016021 membrane CC
GO:0016043 cellular component organization BP
GO:0016236 macroautophagy BP
GO:0022406 membrane docking BP
GO:0022607 cellular component assembly BP
GO:0030176 obsolete integral component of endoplasmic reticulum membrane CC
GO:0031090 organelle membrane CC
GO:0031224 obsolete intrinsic component of membrane CC
GO:0031227 obsolete intrinsic component of endoplasmic reticulum membrane CC
GO:0031300 obsolete intrinsic component of organelle membrane CC
GO:0031301 obsolete integral component of organelle membrane CC
GO:0031984 organelle subcompartment CC
GO:0032991 protein-containing complex CC
GO:0034975 protein folding in endoplasmic reticulum BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0044085 cellular component biogenesis BP
GO:0044237 cellular metabolic process BP
GO:0044248 cellular catabolic process BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044425 obsolete membrane part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0051179 localization BP
GO:0051640 organelle localization BP
GO:0051641 cellular localization BP
GO:0061919 process utilizing autophagic mechanism BP
GO:0070925 organelle assembly BP
GO:0071840 cellular component organization or biogenesis BP
GO:0072546 EMC complex CC
GO:0097630 obsolete intrinsic component of omegasome membrane CC
GO:0097631 obsolete integral component of omegasome membrane CC
GO:0098588 bounding membrane of organelle CC
GO:0098796 membrane protein complex CC
GO:0098827 endoplasmic reticulum subcompartment CC
GO:0140056 organelle localization by membrane tethering BP
GO:1903349 omegasome membrane CC
GO:1905037 autophagosome organization BP
GO:1990456 mitochondrion-endoplasmic reticulum membrane tethering BP
GO:1990462 omegasome CC
KEGG Term Name Description
map03430 Mismatch repair DNA mismatch repair (MMR) is a highly conserved biological pathway that plays a key role in maintaining genomic stability. MMR corrects DNA mismatches generated during DNA replication, thereby preventing mutations from becoming permanent in dividing cells. MMR also suppresses homologous recombination and was recently shown to play a role in DNA damage signaling. Defects in MMR are associated with genome-wide instability, predisposition to certain types of cancer including HNPCC, resistance to certain chemotherapeutic agents, and abnormalities in meiosis and sterility in mammalian systems.
map03420 Nucleotide excision repair Nucleotide excision repair (NER) is a mechanism to recognize and repair bulky DNA damage caused by compounds, environmental carcinogens, and exposure to UV-light. In humans hereditary defects in the NER pathway are linked to at least three diseases: xeroderma pigmentosum (XP), Cockayne syndrome (CS), and trichothiodystrophy (TTD). The repair of damaged DNA involves at least 30 polypeptides within two different sub-pathways of NER known as transcription-coupled repair (TCR-NER) and global genome repair (GGR-NER). TCR refers to the expedited repair of lesions located in the actively transcribed strand of genes by RNA polymerase II (RNAP II). In GGR-NER the first step of damage recognition involves XPC-hHR23B complex together with XPE complex (in prokaryotes, uvrAB complex). The following steps of GGR-NER and TCR-NER are similar.
map03410 Base excision repair Base excision repair (BER) is the predominant DNA damage repair pathway for the processing of small base lesions, derived from oxidation and alkylation damages. BER is normally defined as DNA repair initiated by lesion-specific DNA glycosylases and completed by either of the two sub-pathways: short-patch BER where only one nucleotide is replaced and long-patch BER where 2-13 nucleotides are replaced. Each sub-pathway of BER relies on the formation of protein complexes that assemble at the site of the DNA lesion and facilitate repair in a coordinated fashion. This process of complex formation appears to provide an increase in specificity and efficiency to the BER pathway, thereby facilitating the maintenance of genome integrity by preventing the accumulation of highly toxic repair intermediates.
map03030 DNA replication A complex network of interacting proteins and enzymes is required for DNA replication. Generally, DNA replication follows a multistep enzymatic pathway. At the DNA replication fork, a DNA helicase (DnaB or MCM complex) precedes the DNA synthetic machinery and unwinds the duplex parental DNA in cooperation with the SSB or RPA. On the leading strand, replication occurs continuously in a 5 to 3 direction, whereas on the lagging strand, DNA replication occurs discontinuously by synthesis and joining of short Okazaki fragments. In prokaryotes, the leading strand replication apparatus consists of a DNA polymerase (pol III core), a sliding clamp (beta), and a clamp loader (gamma delta complex). The DNA primase (DnaG) is needed to form RNA primers. Normally, during replication of the lagging-strand DNA template, an RNA primer is removed either by an RNase H or by the 5 to 3 exonuclease activity of DNA pol I, and the DNA ligase joins the Okazaki fragments. In eukaryotes, three DNA polymerases (alpha, delta, and epsilon) have been identified. DNA primase forms a permanent complex with DNA polymerase alpha. PCNA and RFC function as a clamp and a clamp loader. FEN 1 and RNase H1 remove the RNA from the Okazaki fragments and DNA ligase I joins the DNA.