STRINGSTRING
A0A1V6PXP8 A0A1V6PXP8 A0A1V6PXS9 A0A1V6PXS9 A0A1V6PYJ0 A0A1V6PYJ0 A0A1V6PZ04 A0A1V6PZ04 A0A1V6PZT9 A0A1V6PZT9 A0A1V6PZU3 A0A1V6PZU3 A0A1V6PZZ2 A0A1V6PZZ2 A0A1V6Q009 A0A1V6Q009 A0A1V6Q0I5 A0A1V6Q0I5 A0A1V6Q0U0 A0A1V6Q0U0 A0A1V6Q1M1 A0A1V6Q1M1 A0A1V6Q1R4 A0A1V6Q1R4 A0A1V6Q1R6 A0A1V6Q1R6 A0A1V6Q290 A0A1V6Q290 A0A1V6Q2G7 A0A1V6Q2G7 PAN2 PAN2 A0A1V6Q2Z9 A0A1V6Q2Z9 A0A1V6Q409 A0A1V6Q409 A0A1V6Q4G2 A0A1V6Q4G2 A0A1V6Q4P5 A0A1V6Q4P5 A0A1V6Q4Z4 A0A1V6Q4Z4 A0A1V6Q522 A0A1V6Q522 A0A1V6Q5Y5 A0A1V6Q5Y5 A0A1V6Q689 A0A1V6Q689 A0A1V6Q6Y9 A0A1V6Q6Y9 A0A1V6Q762 A0A1V6Q762 A0A1V6Q7S4 A0A1V6Q7S4 A0A1V6QPP4 A0A1V6QPP4 A0A1V6QPN9 A0A1V6QPN9 A0A1V6QPI8 A0A1V6QPI8 A0A1V6QPG5 A0A1V6QPG5 A0A1V6QNX3 A0A1V6QNX3 A0A1V6QNS2 A0A1V6QNS2 A0A1V6QNG1 A0A1V6QNG1 A0A1V6QN75 A0A1V6QN75 A0A1V6QN56 A0A1V6QN56 A0A1V6QMS0 A0A1V6QMS0 A0A1V6QN27 A0A1V6QN27 A0A1V6QML4 A0A1V6QML4 A0A1V6QML1 A0A1V6QML1 A0A1V6QLW8 A0A1V6QLW8 A0A1V6QJP7 A0A1V6QJP7 A0A1V6QIG6 A0A1V6QIG6 A0A1V6QHR4 A0A1V6QHR4 A0A1V6QHE2 A0A1V6QHE2 A0A1V6QGS5 A0A1V6QGS5 A0A1V6QG94 A0A1V6QG94 A0A1V6QF56 A0A1V6QF56 A0A1V6QF35 A0A1V6QF35 A0A1V6QEK3 A0A1V6QEK3 A0A1V6QE97 A0A1V6QE97 A0A1V6QE72 A0A1V6QE72 A0A1V6QDT5 A0A1V6QDT5 A0A1V6QDE4 A0A1V6QDE4 A0A1V6QD81 A0A1V6QD81 A0A1V6QD23 A0A1V6QD23 A0A1V6QBY7 A0A1V6QBY7 A0A1V6QBR2 A0A1V6QBR2 A0A1V6QBQ4 A0A1V6QBQ4 A0A1V6QBN4 A0A1V6QBN4 A0A1V6QBL7 A0A1V6QBL7 LSM3 LSM3 A0A1V6QAC8 A0A1V6QAC8 A0A1V6QAB3 A0A1V6QAB3 A0A1V6Q9F2 A0A1V6Q9F2 A0A1V6Q937 A0A1V6Q937 LSM8 LSM8 A0A1V6Q8X0 A0A1V6Q8X0 LSM5 LSM5 A0A1V6Q806 A0A1V6Q806 A0A1V6PPF5 A0A1V6PPF5 A0A1V6PQP3 A0A1V6PQP3 A0A1V6PRW4 A0A1V6PRW4 A0A1V6PS91 A0A1V6PS91 A0A1V6PSN0 A0A1V6PSN0 A0A1V6PT23 A0A1V6PT23 A0A1V6PTP0 A0A1V6PTP0 A0A1V6PTY5 A0A1V6PTY5 A0A1V6PU14 A0A1V6PU14 A0A1V6PU89 A0A1V6PU89 A0A1V6PV13 A0A1V6PV13 A0A1V6PVB7 A0A1V6PVB7 A0A1V6PVI2 A0A1V6PVI2 A0A1V6PVQ4 A0A1V6PVQ4 A0A1V6PW05 A0A1V6PW05 A0A1V6PW10 A0A1V6PW10 A0A1V6PW92 A0A1V6PW92 A0A1V6PXD1 A0A1V6PXD1 A0A1V6PXL5 A0A1V6PXL5 A0A1V6PXN1 A0A1V6PXN1
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.
Node Color
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
A0A1V6PXP8NOT2_3_5 domain-containing protein. (491 aa)
A0A1V6PXS9Uncharacterized protein; Belongs to the heat shock protein 70 family. (668 aa)
A0A1V6PYJ0ATP-dependent 6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily. (784 aa)
A0A1V6PZ04Uncharacterized protein. (486 aa)
A0A1V6PZT9Enolase_N domain-containing protein. (96 aa)
A0A1V6PZU3Uncharacterized protein. (1436 aa)
A0A1V6PZZ2Uncharacterized protein. (598 aa)
A0A1V6Q009Enolase_C domain-containing protein. (197 aa)
A0A1V6Q0I5Uncharacterized protein. (1195 aa)
A0A1V6Q0U0CobW C-terminal domain-containing protein. (572 aa)
A0A1V6Q1M1Uncharacterized protein. (288 aa)
A0A1V6Q1R4RNB domain-containing protein. (1086 aa)
A0A1V6Q1R6Sm domain-containing protein. (92 aa)
A0A1V6Q290T-complex protein 1 subunit delta. (536 aa)
A0A1V6Q2G7Uncharacterized protein. (550 aa)
PAN2PAN2-PAN3 deadenylation complex catalytic subunit PAN2; Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent [...] (1168 aa)
A0A1V6Q2Z9Uncharacterized protein. (250 aa)
A0A1V6Q409Uncharacterized protein. (438 aa)
A0A1V6Q4G2T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (562 aa)
A0A1V6Q4P5Uncharacterized protein. (315 aa)
A0A1V6Q4Z4PH domain-containing protein. (1278 aa)
A0A1V6Q522Uncharacterized protein. (643 aa)
A0A1V6Q5Y5Polyadenylate-binding protein; Binds the poly(A) tail of mRNA. Belongs to the polyadenylate-binding protein type-1 family. (738 aa)
A0A1V6Q689YL1_C domain-containing protein. (793 aa)
A0A1V6Q6Y93'-5' exonuclease domain-containing protein. (1321 aa)
A0A1V6Q762Uncharacterized protein. (735 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)
A0A1V6QPP4Uncharacterized protein. (1343 aa)
A0A1V6QPN9Uncharacterized protein. (1449 aa)
A0A1V6QPI8Uncharacterized protein. (566 aa)
A0A1V6QPG5Uncharacterized protein. (358 aa)
A0A1V6QNX3Uncharacterized protein; Belongs to the chaperonin (HSP60) family. (1638 aa)
A0A1V6QNS2Sec2p domain-containing protein. (285 aa)
A0A1V6QNG1Uncharacterized protein. (539 aa)
A0A1V6QN75RNase_PH domain-containing protein. (317 aa)
A0A1V6QN56ANK_REP_REGION domain-containing protein. (752 aa)
A0A1V6QMS0Uncharacterized protein. (329 aa)
A0A1V6QN27Uncharacterized protein. (578 aa)
A0A1V6QML4Endo/exonuclease/phosphatase domain-containing protein. (748 aa)
A0A1V6QML1Uncharacterized protein. (503 aa)
A0A1V6QLW8T-complex protein 1 subunit gamma. (539 aa)
A0A1V6QJP7RNB domain-containing protein. (1360 aa)
A0A1V6QIG6Uncharacterized protein. (530 aa)
A0A1V6QHR4Uncharacterized protein; Belongs to the DEAD box helicase family. (512 aa)
A0A1V6QHE2Uncharacterized protein. (389 aa)
A0A1V6QGS5Uncharacterized protein. (480 aa)
A0A1V6QG945'-3' exoribonuclease 1; Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. (1395 aa)
A0A1V6QF56Uncharacterized protein. (392 aa)
A0A1V6QF35TPR_REGION domain-containing protein. (396 aa)
A0A1V6QEK3Uncharacterized protein. (388 aa)
A0A1V6QE97Nudix hydrolase domain-containing protein. (192 aa)
A0A1V6QE72Uncharacterized protein; Belongs to the RNR ribonuclease family. (1032 aa)
A0A1V6QDT52-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2; Belongs to the DPH1/DPH2 family. DPH2 subfamily. (567 aa)
A0A1V6QDE4Uncharacterized protein. (851 aa)
A0A1V6QD81Uncharacterized protein. (536 aa)
A0A1V6QD23RNase_PH domain-containing protein. (268 aa)
A0A1V6QBY7PAT1 domain-containing protein. (811 aa)
A0A1V6QBR2ANK_REP_REGION domain-containing protein. (606 aa)
A0A1V6QBQ4Uncharacterized protein. (236 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)
A0A1V6QBL7Nudix hydrolase domain-containing protein. (857 aa)
LSM3U6 snRNA-associated Sm-like protein LSm3; Binds specifically to the 3'-terminal U-tract of U6 snRNA. (95 aa)
A0A1V6QAC8HRDC domain-containing protein. (754 aa)
A0A1V6QAB3ABC transporter domain-containing protein. (283 aa)
A0A1V6Q9F2Uncharacterized protein. (2309 aa)
A0A1V6Q937Uncharacterized protein. (540 aa)
LSM8U6 snRNA-associated Sm-like protein LSm8; Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. (98 aa)
A0A1V6Q8X0Uncharacterized protein. (272 aa)
LSM5U6 snRNA-associated Sm-like protein LSm5; Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA. (83 aa)
A0A1V6Q806Uncharacterized protein. (1074 aa)
A0A1V6PPF5cobW domain-containing protein. (399 aa)
A0A1V6PQP3Sm domain-containing protein. (578 aa)
A0A1V6PRW4Uncharacterized protein. (757 aa)
A0A1V6PS91Uncharacterized protein. (247 aa)
A0A1V6PSN0RNase_PH domain-containing protein. (394 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)
A0A1V6PTP0CCHC-type domain-containing protein. (1209 aa)
A0A1V6PTY5F-box domain-containing protein. (563 aa)
A0A1V6PU14Uncharacterized protein. (324 aa)
A0A1V6PU89Uncharacterized protein. (181 aa)
A0A1V6PV13RRM domain-containing protein. (1025 aa)
A0A1V6PVB7Uncharacterized protein. (738 aa)
A0A1V6PVI2Uncharacterized protein. (808 aa)
A0A1V6PVQ4ECR1_N domain-containing protein. (391 aa)
A0A1V6PW05Uncharacterized protein. (224 aa)
A0A1V6PW10RNase_PH domain-containing protein. (386 aa)
A0A1V6PW92Uncharacterized protein. (1845 aa)
A0A1V6PXD12-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. (435 aa)
A0A1V6PXL5Uncharacterized protein. (2043 aa)
A0A1V6PXN1Importin N-terminal domain-containing protein. (1048 aa)
Your Current Organism:
Penicillium antarcticum
NCBI taxonomy Id: 416450
Other names: CBS 100492, FRR 4989, P. antarcticum
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.