PPGR - Gene Detail

Basic Information

Gene ID	PH02Gene28774 View in Genome Browser
Position	hic_scaffold_14:100761005-100766803 (-) 5798bp
Gene Type	gene
Gene Description (Protein Product)	60Kd inner membrane protein
Organism	Phyllostachys edulis
Also AS	AT2G28800

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

PH02Gene38708 The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity)

PH02Gene37782 SRP54-type protein, helical bundle domain

PH02Gene29996 SRP54-type protein, GTPase domain

Regulatory gene

PH02Gene01001 ethylene-responsive transcription factor

PH02Gene01222 AP2 domain

PH02Gene01223 AP2 domain

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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

KEGG Term	Name	Description
map03060	Protein export	The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role.