PPGR - Gene Detail

Basic Information

Gene ID	Bpev01.c4863.g0001 View in Genome Browser
Position	Contig4863:52-1780 (-) 1728bp
Gene Type	gene
Gene Description (Protein Product)	Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system
Organism	Betula pendula
Also AS	AT4G28620

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

Bpev01.c5492.g0005 Belongs to the ABC transporter superfamily

Bpev01.c5492.g0002 Oligopeptide transport system permease protein OppC

Bpev01.c5492.g0001 probably responsible for the translocation of the substrate across the membrane

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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:0000166	nucleotide binding	MF
GO:0003674	molecular_function	MF
GO:0005215	transporter activity	MF
GO:0005488	binding	MF
GO:0005524	ATP binding	MF
GO:0005575	cellular_component	CC
GO:0005623	obsolete cell	CC
GO:0005886	plasma membrane	CC
GO:0006810	transport	BP
GO:0008144	obsolete drug binding	MF
GO:0008150	biological_process	BP
GO:0015232	heme transmembrane transporter activity	MF
GO:0015886	heme transport	BP
GO:0016020	membrane	CC
GO:0017076	purine nucleotide binding	MF
GO:0022857	transmembrane transporter activity	MF
GO:0030554	adenyl nucleotide binding	MF
GO:0032553	ribonucleotide binding	MF
GO:0032555	purine ribonucleotide binding	MF
GO:0032559	adenyl ribonucleotide binding	MF
GO:0035639	purine ribonucleoside triphosphate binding	MF
GO:0036094	small molecule binding	MF
GO:0043167	ion binding	MF
GO:0043168	anion binding	MF
GO:0044464	obsolete cell part	CC
GO:0051179	localization	BP
GO:0051181	obsolete cofactor transport	BP
GO:0051184	obsolete cofactor transmembrane transporter activity	MF
GO:0051234	establishment of localization	BP
GO:0055085	transmembrane transport	BP
GO:0071702	organic substance transport	BP
GO:0071705	nitrogen compound transport	BP
GO:0071944	cell periphery	CC
GO:0097159	organic cyclic compound binding	MF
GO:0097367	carbohydrate derivative binding	MF
GO:1901265	nucleoside phosphate binding	MF
GO:1901363	heterocyclic compound binding	MF
GO:1901678	iron coordination entity transport	BP

KEGG Term	Name	Description
map02010	ABC transporters	The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD).
map02010	ABC transporters	The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD).