21 items (Penicillium antarcticum) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

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Others

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co-expression

protein homology

Your Input:
	A0A1V6Q0Y4	Uncharacterized protein. (242 aa)
	A0A1V6PTK5	Uncharacterized protein. (226 aa)
	A0A1V6PU96	AMP-binding domain-containing protein. (707 aa)
	A0A1V6PVY2	Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...] (227 aa)
	A0A1V6PWD5	Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...] (206 aa)
	A0A1V6PX60	BZIP domain-containing protein. (589 aa)
	A0A1V6PX88	HET domain-containing protein. (517 aa)
	A0A1V6PZ36	AMP-binding domain-containing protein. (698 aa)
	A0A1V6PZH9	Elongation of fatty acids protein. (543 aa)
	A0A1V6PSQ7	Uncharacterized protein. (921 aa)
	A0A1V6Q7X3	Uncharacterized protein. (244 aa)
	A0A1V6Q943	BZIP domain-containing protein. (331 aa)
	A0A1V6QCU7	Uncharacterized protein. (922 aa)
	A0A1V6QEA7	S5A_REDUCTASE domain-containing protein. (310 aa)
	A0A1V6QGN9	AMP-binding domain-containing protein. (563 aa)
	A0A1V6QHD0	Elongation of fatty acids protein. (343 aa)
	A0A1V6QNP8	Zn(2)-C6 fungal-type domain-containing protein. (708 aa)
	A0A1V6QPB8	Uncharacterized protein. (146 aa)
	A0A1V6P852	Uncharacterized protein. (220 aa)
	A0A1V6PPQ6	APH domain-containing protein. (346 aa)
	A0A1V6PSP2	Very-long-chain 3-oxoacyl-CoA reductase; Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids. (345 aa)

Your Current Organism:

Penicillium antarcticum

NCBI taxonomy Id: 416450
Other names: CBS 100492, FRR 4989, P. antarcticum

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Browse interactions in tabular form:

node1	node2	node1 annotation	node2 annotation	score
A0A1V6P852	A0A1V6PSP2	Uncharacterized protein.	Very-long-chain 3-oxoacyl-CoA reductase; Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.	0.821
A0A1V6P852	A0A1V6PTK5	Uncharacterized protein.	Uncharacterized protein.	0.631
A0A1V6P852	A0A1V6PZH9	Uncharacterized protein.	Elongation of fatty acids protein.	0.499
A0A1V6P852	A0A1V6Q0Y4	Uncharacterized protein.	Uncharacterized protein.	0.631
A0A1V6P852	A0A1V6Q7X3	Uncharacterized protein.	Uncharacterized protein.	0.631
A0A1V6P852	A0A1V6QEA7	Uncharacterized protein.	S5A_REDUCTASE domain-containing protein.	0.918
A0A1V6P852	A0A1V6QHD0	Uncharacterized protein.	Elongation of fatty acids protein.	0.682
A0A1V6P852	A0A1V6QPB8	Uncharacterized protein.	Uncharacterized protein.	0.631
A0A1V6PPQ6	A0A1V6PSP2	APH domain-containing protein.	Very-long-chain 3-oxoacyl-CoA reductase; Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.	0.821
A0A1V6PPQ6	A0A1V6PTK5	APH domain-containing protein.	Uncharacterized protein.	0.631
A0A1V6PPQ6	A0A1V6PWD5	APH domain-containing protein.	Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...]	0.582
A0A1V6PPQ6	A0A1V6PZH9	APH domain-containing protein.	Elongation of fatty acids protein.	0.499
A0A1V6PPQ6	A0A1V6Q0Y4	APH domain-containing protein.	Uncharacterized protein.	0.631
A0A1V6PPQ6	A0A1V6Q7X3	APH domain-containing protein.	Uncharacterized protein.	0.631
A0A1V6PPQ6	A0A1V6QEA7	APH domain-containing protein.	S5A_REDUCTASE domain-containing protein.	0.918
A0A1V6PPQ6	A0A1V6QHD0	APH domain-containing protein.	Elongation of fatty acids protein.	0.682
A0A1V6PPQ6	A0A1V6QPB8	APH domain-containing protein.	Uncharacterized protein.	0.631
A0A1V6PSP2	A0A1V6P852	Very-long-chain 3-oxoacyl-CoA reductase; Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.	Uncharacterized protein.	0.821
A0A1V6PSP2	A0A1V6PPQ6	Very-long-chain 3-oxoacyl-CoA reductase; Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.	APH domain-containing protein.	0.821
A0A1V6PSP2	A0A1V6PVY2	Very-long-chain 3-oxoacyl-CoA reductase; Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.	Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...]	0.950