H3A9U3_LATCH protein (Latimeria chalumnae) - STRING interaction network

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H3A9U3_LATCH

PMSR domain-containing protein. (121 aa)

Predicted Functional Partners:

LOC102347712

0.861

LOC102354290

0.853

M3XI97_LATCH

0.776

TXN2

0.723

MSRB2

0.705

MSRB1

0.663

RP1L1

0.639

NUDT18

0.613

MFHAS1

0.590

MTMR9

0.590

Your Current Organism:

Latimeria chalumnae

NCBI taxonomy Id: 7897
Other names: L. chalumnae, coelacanth

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
H3A9U3_LATCH	LOC102347712	ENSLACP00000006414	ENSLACP00000002294	PMSR domain-containing protein.	Thioredoxin; Belongs to the thioredoxin family.	0.861
H3A9U3_LATCH	LOC102354290	ENSLACP00000006414	ENSLACP00000003364	PMSR domain-containing protein.	Uncharacterized protein.	0.853
H3A9U3_LATCH	M3XI97_LATCH	ENSLACP00000006414	ENSLACP00000022453	PMSR domain-containing protein.	Thioredoxin domain-containing protein.	0.776
H3A9U3_LATCH	MFHAS1	ENSLACP00000006414	ENSLACP00000000624	PMSR domain-containing protein.	Malignant fibrous histiocytoma amplified sequence 1.	0.590
H3A9U3_LATCH	MSRB1	ENSLACP00000006414	ENSLACP00000013022	PMSR domain-containing protein.	Methionine sulfoxide reductase B1.	0.663
H3A9U3_LATCH	MSRB2	ENSLACP00000006414	ENSLACP00000016069	PMSR domain-containing protein.	Peptide-methionine (R)-S-oxide reductase; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues.	0.705
H3A9U3_LATCH	MTMR9	ENSLACP00000006414	ENSLACP00000012589	PMSR domain-containing protein.	Myotubularin related protein 9.	0.590
H3A9U3_LATCH	NUDT18	ENSLACP00000006414	ENSLACP00000019444	PMSR domain-containing protein.	Nudix hydrolase 18; Belongs to the Nudix hydrolase family.	0.613
H3A9U3_LATCH	RP1L1	ENSLACP00000006414	ENSLACP00000006929	PMSR domain-containing protein.	Uncharacterized protein.	0.639
H3A9U3_LATCH	TXN2	ENSLACP00000006414	ENSLACP00000003526	PMSR domain-containing protein.	Thioredoxin 2.	0.723
LOC102347712	H3A9U3_LATCH	ENSLACP00000002294	ENSLACP00000006414	Thioredoxin; Belongs to the thioredoxin family.	PMSR domain-containing protein.	0.861
LOC102347712	LOC102354290	ENSLACP00000002294	ENSLACP00000003364	Thioredoxin; Belongs to the thioredoxin family.	Uncharacterized protein.	0.584
LOC102347712	MSRB1	ENSLACP00000002294	ENSLACP00000013022	Thioredoxin; Belongs to the thioredoxin family.	Methionine sulfoxide reductase B1.	0.676
LOC102347712	MSRB2	ENSLACP00000002294	ENSLACP00000016069	Thioredoxin; Belongs to the thioredoxin family.	Peptide-methionine (R)-S-oxide reductase; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues.	0.855
LOC102347712	TXN2	ENSLACP00000002294	ENSLACP00000003526	Thioredoxin; Belongs to the thioredoxin family.	Thioredoxin 2.	0.973
LOC102354290	H3A9U3_LATCH	ENSLACP00000003364	ENSLACP00000006414	Uncharacterized protein.	PMSR domain-containing protein.	0.853
LOC102354290	LOC102347712	ENSLACP00000003364	ENSLACP00000002294	Uncharacterized protein.	Thioredoxin; Belongs to the thioredoxin family.	0.584
LOC102354290	M3XI97_LATCH	ENSLACP00000003364	ENSLACP00000022453	Uncharacterized protein.	Thioredoxin domain-containing protein.	0.443
LOC102354290	MSRB1	ENSLACP00000003364	ENSLACP00000013022	Uncharacterized protein.	Methionine sulfoxide reductase B1.	0.632
LOC102354290	MSRB2	ENSLACP00000003364	ENSLACP00000016069	Uncharacterized protein.	Peptide-methionine (R)-S-oxide reductase; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues.	0.632