Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
PtJG25850
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Position
chr11:808508908-808585429 (+)
76521bp
Gene Type
gene
Gene Description (Protein Product)
F-actin-capping protein subunit beta
Organism
Pinus tabuliformis
Also AS AT1G71790

Gene Structure

upstream:
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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
PtQG03750 WASH complex subunit 7
PtXG23290 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
PtXG16880 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
Regulatory gene
Pt0G01630 dof zinc finger protein
Pt0G07980 dof zinc finger protein
Pt0G30270 G patch domain-containing 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
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0000902 cell morphogenesis BP
GO:0003674 molecular_function MF
GO:0003779 actin binding MF
GO:0005488 binding MF
GO:0005515 protein binding 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:0006950 response to stress BP
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:0008092 cytoskeletal protein binding MF
GO:0008150 biological_process BP
GO:0008290 F-actin capping protein complex CC
GO:0009266 response to temperature stimulus BP
GO:0009408 response to heat BP
GO:0009628 response to abiotic stimulus BP
GO:0009653 anatomical structure morphogenesis BP
GO:0009987 cellular process BP
GO:0010639 negative regulation of organelle organization BP
GO:0015629 actin cytoskeleton CC
GO:0016043 cellular component organization BP
GO:0030029 actin filament-based process BP
GO:0030036 actin cytoskeleton organization BP
GO:0030832 regulation of actin filament length BP
GO:0030833 regulation of actin filament polymerization BP
GO:0030834 regulation of actin filament depolymerization BP
GO:0030835 negative regulation of actin filament depolymerization BP
GO:0030837 negative regulation of actin filament polymerization BP
GO:0031333 negative regulation of protein-containing complex assembly BP
GO:0032271 regulation of protein polymerization BP
GO:0032272 negative regulation of protein polymerization BP
GO:0032502 developmental process 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:0032989 cellular component morphogenesis BP
GO:0032991 protein-containing complex CC
GO:0033043 regulation of organelle organization BP
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:0043242 negative regulation of protein-containing complex disassembly BP
GO:0043244 regulation of protein-containing complex disassembly BP
GO:0043254 regulation of protein-containing complex assembly BP
GO:0044087 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:0044464 obsolete cell part CC
GO:0044877 protein-containing complex binding MF
GO:0048519 negative regulation of biological process BP
GO:0048523 negative regulation of cellular process BP
GO:0048856 anatomical structure development BP
GO:0048869 cellular developmental process BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051015 actin filament binding MF
GO:0051016 barbed-end actin filament capping BP
GO:0051128 regulation of cellular component organization BP
GO:0051129 negative regulation of cellular component organization BP
GO:0051493 regulation of cytoskeleton organization BP
GO:0051494 negative regulation of cytoskeleton organization BP
GO:0051693 actin filament capping BP
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:0097435 supramolecular fiber organization BP
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:1901879 regulation of protein depolymerization BP
GO:1901880 negative regulation of protein depolymerization BP
GO:1902903 regulation of supramolecular fiber organization BP
GO:1902904 negative 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.