Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
PH02Gene35289
View in Genome Browser
Position
hic_scaffold_3:103087877-103090852 (-)
2975bp
Gene Type
gene
Gene Description (Protein Product)
Replication protein A 32 kDa subunit
Organism
Phyllostachys edulis
Also AS AT2G24490

Gene Structure

upstream:
Get Sequence

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
PH02Gene49568 At4g28440-like
PH02Gene38997 At4g28440-like
PH02Gene47669 DNA polymerase subunit Cdc27
Regulatory gene
PH02Gene00239 zinc finger
PH02Gene00552 Zinc-finger double-stranded RNA-binding
PH02Gene00687 Domain of unknown function (DUF966)

Load All Networks

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
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0000228 nuclear chromosome CC
GO:0000278 mitotic cell cycle BP
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005634 nucleus CC
GO:0005657 replication fork CC
GO:0005662 DNA replication factor A complex CC
GO:0005694 chromosome CC
GO:0006139 nucleobase-containing compound metabolic process BP
GO:0006259 DNA metabolic process BP
GO:0006260 DNA replication BP
GO:0006261 DNA-templated DNA replication BP
GO:0006269 DNA replication, synthesis of RNA primer BP
GO:0006281 DNA repair BP
GO:0006310 DNA recombination BP
GO:0006725 cellular aromatic compound metabolic process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006974 cellular response to DNA damage stimulus BP
GO:0007049 cell cycle BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009058 biosynthetic process BP
GO:0009059 macromolecule biosynthetic process BP
GO:0009892 negative regulation of metabolic process BP
GO:0009987 cellular process BP
GO:0010468 regulation of gene expression BP
GO:0010605 negative regulation of macromolecule metabolic process BP
GO:0010629 negative regulation of gene expression BP
GO:0016070 RNA metabolic process BP
GO:0016458 obsolete gene silencing BP
GO:0018130 heterocycle biosynthetic process BP
GO:0019222 regulation of metabolic process BP
GO:0019438 aromatic compound biosynthetic process BP
GO:0022402 cell cycle process BP
GO:0030894 replisome CC
GO:0031974 membrane-enclosed lumen CC
GO:0031981 nuclear lumen CC
GO:0032774 RNA biosynthetic process BP
GO:0032991 protein-containing complex CC
GO:0032993 protein-DNA complex CC
GO:0033260 nuclear DNA replication BP
GO:0033554 cellular response to stress BP
GO:0034641 cellular nitrogen compound metabolic process BP
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0034654 nucleobase-containing compound biosynthetic process BP
GO:0035861 site of double-strand break CC
GO:0043170 macromolecule metabolic process BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043228 non-membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043232 intracellular non-membrane-bounded organelle CC
GO:0043233 organelle lumen CC
GO:0043596 nuclear replication fork CC
GO:0043601 nuclear replisome CC
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044249 cellular biosynthetic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044271 cellular nitrogen compound biosynthetic process BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044427 obsolete chromosomal part CC
GO:0044428 obsolete nuclear part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044454 obsolete nuclear chromosome part CC
GO:0044464 obsolete cell part CC
GO:0044786 cell cycle DNA replication BP
GO:0046483 heterocycle metabolic process BP
GO:0048519 negative regulation of biological process BP
GO:0050789 regulation of biological process BP
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0060255 regulation of macromolecule metabolic process BP
GO:0065007 biological regulation BP
GO:0070013 intracellular organelle lumen CC
GO:0071704 organic substance metabolic process BP
GO:0090304 nucleic acid metabolic process BP
GO:0090734 site of DNA damage CC
GO:1901360 organic cyclic compound metabolic process BP
GO:1901362 organic cyclic compound biosynthetic process BP
GO:1901576 organic substance biosynthetic process BP
GO:1902295 synthesis of RNA primer involved in cell cycle DNA replication BP
GO:1902318 synthesis of RNA primer involved in nuclear cell cycle DNA replication BP
GO:1902969 mitotic DNA replication BP
GO:1902981 synthesis of RNA primer involved in mitotic DNA replication BP
GO:1903047 mitotic cell cycle process BP
KEGG Term Name Description
map03440 Homologous recombination Homologous recombination (HR) is essential for the accurate repair of DNA double-strand breaks (DSBs), potentially lethal lesions. HR takes place in the late S-G2 phase of the cell cycle and involves the generation of a single-stranded region of DNA, followed by strand invasion, formation of a Holliday junction, DNA synthesis using the intact strand as a template, branch migration and resolution. It is investigated that RecA/Rad51 family proteins play a central role. The breast cancer susceptibility protein Brca2 and the RecQ helicase BLM (Bloom syndrome mutated) are tumor suppressors that maintain genome integrity, at least in part, through HR.
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.
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.