PPGR - Gene Detail

Basic Information

Gene ID	Pop_G18G019063 View in Genome Browser
Position	chrG18:2244741-2247068 (-) 2327bp
Gene Type	gene
Gene Description (Protein Product)	Functions as component of the Arp2 3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks
Organism	Populus alba x Populus glandulosa
Also AS	Potri.018G123100AT1G60430Potri.018G123100.v4.1

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

Pop_G18G080184 GPI mannosyltransferase

Pop_UnG060154 Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome

Pop_G18G033707 phosphatase 2C

Regulatory gene

Pop_A01G002215 NAC domain-containing protein

Pop_A01G003796 isoform X1

Pop_A01G003952 transcription factor

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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)

Select Expression

Pathway

GO Term	Description	GO Category
GO:0003674	molecular_function	MF
GO:0005198	structural molecule activity	MF
GO:0005200	structural constituent of cytoskeleton	MF
GO:0005575	cellular_component	CC
GO:0005622	intracellular anatomical structure	CC
GO:0005623	obsolete cell	CC
GO:0005856	cytoskeleton	CC
GO:0005884	actin filament	CC
GO:0005885	Arp2/3 protein complex	CC
GO:0006996	organelle organization	BP
GO:0007010	cytoskeleton organization	BP
GO:0007015	actin filament organization	BP
GO:0008064	regulation of actin polymerization or depolymerization	BP
GO:0008150	biological_process	BP
GO:0009987	cellular process	BP
GO:0010638	positive regulation of organelle organization	BP
GO:0015629	actin cytoskeleton	CC
GO:0016043	cellular component organization	BP
GO:0030027	lamellipodium	CC
GO:0030029	actin filament-based process	BP
GO:0030036	actin cytoskeleton organization	BP
GO:0030424	axon	CC
GO:0030426	growth cone	CC
GO:0030427	site of polarized growth	CC
GO:0030832	regulation of actin filament length	BP
GO:0030833	regulation of actin filament polymerization	BP
GO:0030838	positive regulation of actin filament polymerization	BP
GO:0031252	cell leading edge	CC
GO:0031334	positive regulation of protein-containing complex assembly	BP
GO:0031941	filamentous actin	CC
GO:0032271	regulation of protein polymerization	BP
GO:0032273	positive regulation of protein polymerization	BP
GO:0032535	regulation of cellular component size	BP
GO:0032956	regulation of actin cytoskeleton organization	BP
GO:0032970	regulation of actin filament-based process	BP
GO:0032991	protein-containing complex	CC
GO:0033043	regulation of organelle organization	BP
GO:0033267	obsolete axon part	CC
GO:0034314	Arp2/3 complex-mediated actin nucleation	BP
GO:0042995	cell projection	CC
GO:0043005	neuron projection	CC
GO:0043226	organelle	CC
GO:0043228	non-membrane-bounded organelle	CC
GO:0043229	intracellular organelle	CC
GO:0043232	intracellular non-membrane-bounded organelle	CC
GO:0043254	regulation of protein-containing complex assembly	BP
GO:0044087	regulation of cellular component biogenesis	BP
GO:0044089	positive regulation of cellular component biogenesis	BP
GO:0044422	obsolete organelle part	CC
GO:0044424	obsolete intracellular part	CC
GO:0044430	obsolete cytoskeletal part	CC
GO:0044446	obsolete intracellular organelle part	CC
GO:0044463	obsolete cell projection part	CC
GO:0044464	obsolete cell part	CC
GO:0045010	actin nucleation	BP
GO:0048518	positive regulation of biological process	BP
GO:0048522	positive regulation of cellular process	BP
GO:0050789	regulation of biological process	BP
GO:0050794	regulation of cellular process	BP
GO:0051128	regulation of cellular component organization	BP
GO:0051130	positive regulation of cellular component organization	BP
GO:0051493	regulation of cytoskeleton organization	BP
GO:0051495	positive regulation of cytoskeleton organization	BP
GO:0061850	growth cone leading edge	CC
GO:0065007	biological regulation	BP
GO:0065008	regulation of biological quality	BP
GO:0071840	cellular component organization or biogenesis	BP
GO:0090066	regulation of anatomical structure size	BP
GO:0090723	obsolete growth cone part	CC
GO:0090725	peripheral region of growth cone	CC
GO:0097435	supramolecular fiber organization	BP
GO:0097458	obsolete neuron part	CC
GO:0099080	supramolecular complex	CC
GO:0099081	supramolecular polymer	CC
GO:0099512	supramolecular fiber	CC
GO:0099513	polymeric cytoskeletal fiber	CC
GO:0110053	regulation of actin filament organization	BP
GO:0120025	plasma membrane bounded cell projection	CC
GO:0120038	obsolete plasma membrane bounded cell projection part	CC
GO:0150034	distal axon	CC
GO:1902903	regulation of supramolecular fiber organization	BP
GO:1902905	positive regulation of supramolecular fiber organization	BP

KEGG Term	Name	Description
map04144	Endocytosis	Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type.
map01100	Metabolic pathways	-
map00563	Glycosylphosphatidylinositol(GPI)-anchor biosynthesis	Cell surface proteins can be attached to the cell membrane via the glycolipid structure called glycosylphosphatidylinositol (GPI) anchor. Hundreds of GPI-anchored proteins have been identified in many eukaryotes ranging from protozoa and fungi to mammals. All protein-linked GPI anchors share a common core structure, characterized by the substructure Man (a1-4) GlcN (a1-6) myo-inositol-1P-lipid. Biosynthesis of GPI anchors proceeds in three stages: (i) preassembly of a GPI precursor in the ER membrane, (ii) attachment of the GPI to the C-terminus of a newly synthesized protein in the lumen of the ER, and (iii) lipid remodeling and/or carbohydrate side-chain modifications in the ER and the Golgi. Defects of GPI anchor biosynthesis gene result in a genetic disorder, paroxysmal nocturnal hemoglobinuria.