A6R68_09652 protein (Neotoma lepida) - STRING interaction network

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Score

A6R68_09652

Uncharacterized protein. (126 aa)

Predicted Functional Partners:

A6R68_22852

0.992

A6R68_02684

0.981

A6R68_04428

0.979

A6R68_13453

0.979

A6R68_19410

0.976

A6R68_12036

0.955

A6R68_20857

0.940

A6R68_21231

0.927

A6R68_03091

0.924

A6R68_12283

0.918

Your Current Organism:

Neotoma lepida

NCBI taxonomy Id: 56216
Other names: N. lepida, desert woodrat

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A6R68_02684	A6R68_03091	A0A1A6GSX6	A0A1A6GR67	Uncharacterized protein.	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	0.940
A6R68_02684	A6R68_04428	A0A1A6GSX6	A0A1A6GNU1	Uncharacterized protein.	Plug_translocon domain-containing protein.	0.841
A6R68_02684	A6R68_09652	A0A1A6GSX6	A0A1A6FZ69	Uncharacterized protein.	Uncharacterized protein.	0.981
A6R68_02684	A6R68_12036	A0A1A6GSX6	A0A1A6H4W9	Uncharacterized protein.	Uncharacterized protein.	0.954
A6R68_02684	A6R68_12283	A0A1A6GSX6	A0A1A6H3H9	Uncharacterized protein.	Uncharacterized protein.	0.684
A6R68_02684	A6R68_13453	A0A1A6GSX6	A0A1A6H0R5	Uncharacterized protein.	Plug_translocon domain-containing protein.	0.841
A6R68_02684	A6R68_19410	A0A1A6GSX6	A0A1A6HJP7	Uncharacterized protein.	TPR_REGION domain-containing protein.	0.953
A6R68_02684	A6R68_20857	A0A1A6GSX6	A0A1A6HRT2	Uncharacterized protein.	Uncharacterized protein.	0.965
A6R68_02684	A6R68_22852	A0A1A6GSX6	A0A1A6HYS4	Uncharacterized protein.	SRP54 domain-containing protein.	0.975
A6R68_03091	A6R68_02684	A0A1A6GR67	A0A1A6GSX6	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Uncharacterized protein.	0.940
A6R68_03091	A6R68_04428	A0A1A6GR67	A0A1A6GNU1	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Plug_translocon domain-containing protein.	0.498
A6R68_03091	A6R68_09652	A0A1A6GR67	A0A1A6FZ69	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Uncharacterized protein.	0.924
A6R68_03091	A6R68_12036	A0A1A6GR67	A0A1A6H4W9	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Uncharacterized protein.	0.999
A6R68_03091	A6R68_12283	A0A1A6GR67	A0A1A6H3H9	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Uncharacterized protein.	0.755
A6R68_03091	A6R68_13453	A0A1A6GR67	A0A1A6H0R5	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Plug_translocon domain-containing protein.	0.498
A6R68_03091	A6R68_19410	A0A1A6GR67	A0A1A6HJP7	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	TPR_REGION domain-containing protein.	0.999
A6R68_03091	A6R68_20857	A0A1A6GR67	A0A1A6HRT2	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	Uncharacterized protein.	0.999
A6R68_03091	A6R68_22852	A0A1A6GR67	A0A1A6HYS4	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	SRP54 domain-containing protein.	0.999
A6R68_04428	A6R68_02684	A0A1A6GNU1	A0A1A6GSX6	Plug_translocon domain-containing protein.	Uncharacterized protein.	0.841
A6R68_04428	A6R68_03091	A0A1A6GNU1	A0A1A6GR67	Plug_translocon domain-containing protein.	Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.	0.498