STRINGSTRING
A0A1V6PPX7 A0A1V6PPX7 A0A1V6PQ62 A0A1V6PQ62 A0A1V6PRF2 A0A1V6PRF2 A0A1V6PS42 A0A1V6PS42 A0A1V6PSK1 A0A1V6PSK1 A0A1V6PT23 A0A1V6PT23 A0A1V6PU29 A0A1V6PU29 A0A1V6PWB4 A0A1V6PWB4 A0A1V6PXX6 A0A1V6PXX6 A0A1V6PYS9 A0A1V6PYS9 A0A1V6PYY7 A0A1V6PYY7 A0A1V6PZH5 A0A1V6PZH5 MRI1 MRI1 A0A1V6Q0V9 A0A1V6Q0V9 A0A1V6Q1F1 A0A1V6Q1F1 A0A1V6Q296 A0A1V6Q296 A0A1V6Q3Z5 A0A1V6Q3Z5 A0A1V6Q402 A0A1V6Q402 A0A1V6Q5B0 A0A1V6Q5B0 A0A1V6Q7J1 A0A1V6Q7J1 A0A1V6Q7S4 A0A1V6Q7S4 A0A1V6QBD2 A0A1V6QBD2 A0A1V6QBN4 A0A1V6QBN4 A0A1V6QBP4 A0A1V6QBP4 A0A1V6QBW6 A0A1V6QBW6 A0A1V6QC79 A0A1V6QC79 A0A1V6QD32 A0A1V6QD32 A0A1V6QDD2 A0A1V6QDD2 A0A1V6QDI9 A0A1V6QDI9 A0A1V6QDJ5 A0A1V6QDJ5 A0A1V6QDN3 A0A1V6QDN3 A0A1V6QJB3 A0A1V6QJB3 A0A1V6QP34 A0A1V6QP34
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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A0A1V6PPX7DNA topoisomerase 2; Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double- strand breaks. (1726 aa)
A0A1V6PQ62Glucose-6-phosphate isomerase; Belongs to the GPI family. (585 aa)
A0A1V6PRF21-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase. (256 aa)
A0A1V6PS42Protein disulfide-isomerase. (516 aa)
A0A1V6PSK1Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (162 aa)
A0A1V6PT23NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. (237 aa)
A0A1V6PU29Peptidylprolyl isomerase. (122 aa)
A0A1V6PWB4Glucose-6-phosphate 1-epimerase; Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P). (319 aa)
A0A1V6PXX6Triosephosphate isomerase. (281 aa)
A0A1V6PYS9Multifunctional tryptophan biosynthesis protein; Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities. (752 aa)
A0A1V6PYY7Mannose-6-phosphate isomerase. (461 aa)
A0A1V6PZH5Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (415 aa)
MRI1Methylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily. (382 aa)
A0A1V6Q0V9FK506-binding protein. (478 aa)
A0A1V6Q1F1Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (457 aa)
A0A1V6Q296Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (484 aa)
A0A1V6Q3Z5Phosphoacetylglucosamine mutase; Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins. Belongs to the phosphohexose mutase family. (539 aa)
A0A1V6Q402Phosphomannomutase; Involved in the synthesis of the GDP-mannose and dolichol- phosphate-mannose required for a number of critical mannosyl transfer reactions. (268 aa)
A0A1V6Q5B0DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus r [...] (870 aa)
A0A1V6Q7J1Terpene cyclase/mutase family member; Belongs to the terpene cyclase/mutase family. (664 aa)
A0A1V6Q7S4Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (288 aa)
A0A1V6QBD2Triosephosphate isomerase. (249 aa)
A0A1V6QBN4NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. (685 aa)
A0A1V6QBP4Chorismate mutase. (266 aa)
A0A1V6QBW6Peptidylprolyl isomerase. (121 aa)
A0A1V6QC79UDP-glucose 4-epimerase; Belongs to the NAD(P)-dependent epimerase/dehydratase family. (371 aa)
A0A1V6QD32Peptidyl-prolyl cis-trans isomerase. (127 aa)
A0A1V6QDD2Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (173 aa)
A0A1V6QDI9Peptidylprolyl isomerase. (115 aa)
A0A1V6QDJ5DNA topoisomerase; Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. Belongs to the type IA topoisomerase family. (628 aa)
A0A1V6QDN3Peptidylprolyl isomerase. (132 aa)
A0A1V6QJB3Ribulose-phosphate 3-epimerase; Belongs to the ribulose-phosphate 3-epimerase family. (251 aa)
A0A1V6QP34Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (209 aa)
Your Current Organism:
Penicillium antarcticum
NCBI taxonomy Id: 416450
Other names: CBS 100492, FRR 4989, P. antarcticum
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