STRINGSTRING
A0A1V6Q207 A0A1V6Q207 A0A1V6Q2Q0 A0A1V6Q2Q0 A0A1V6Q380 A0A1V6Q380 A0A1V6Q3I1 A0A1V6Q3I1 A0A1V6Q3Y9 A0A1V6Q3Y9 A0A1V6Q481 A0A1V6Q481 A0A1V6Q487 A0A1V6Q487 A0A1V6Q4T3 A0A1V6Q4T3 A0A1V6Q516 A0A1V6Q516 A0A1V6Q544 A0A1V6Q544 A0A1V6Q6J4 A0A1V6Q6J4 A0A1V6Q732 A0A1V6Q732 A0A1V6Q7F9 A0A1V6Q7F9 A0A1V6Q880 A0A1V6Q880 A0A1V6QAN5 A0A1V6QAN5 A0A1V6QBR3 A0A1V6QBR3 A0A1V6QCN1 A0A1V6QCN1 A0A1V6QCR4 A0A1V6QCR4 A0A1V6QDP3 A0A1V6QDP3 A0A1V6QEF6 A0A1V6QEF6 A0A1V6QFL5 A0A1V6QFL5 A0A1V6QHQ0 A0A1V6QHQ0 A0A1V6QIU1 A0A1V6QIU1 A0A1V6QQD7 A0A1V6QQD7 A0A1V6QNS5 A0A1V6QNS5 A0A1V6QNH9 A0A1V6QNH9 A0A1V6QN44 A0A1V6QN44 A0A1V6QL77 A0A1V6QL77 A0A1V6QKT5 A0A1V6QKT5 A0A1V6QKT2 A0A1V6QKT2 A0A1V6QKH7 A0A1V6QKH7 A0A1V6QKG0 A0A1V6QKG0 A0A1V6QJY9 A0A1V6QJY9 A0A1V6QJN0 A0A1V6QJN0 A0A1V6QJL9 A0A1V6QJL9 A0A1V6QJD5 A0A1V6QJD5 A0A1V6PCH0 A0A1V6PCH0 A0A1V6PEY2 A0A1V6PEY2 A0A1V6PI88 A0A1V6PI88 A0A1V6PJL2 A0A1V6PJL2 A0A1V6PK28 A0A1V6PK28 A0A1V6PP53 A0A1V6PP53 A0A1V6PPZ8 A0A1V6PPZ8 A0A1V6PQQ6 A0A1V6PQQ6 A0A1V6PR03 A0A1V6PR03 A0A1V6PR20 A0A1V6PR20 A0A1V6PR52 A0A1V6PR52 A0A1V6PR84 A0A1V6PR84 A0A1V6PS70 A0A1V6PS70 A0A1V6PSE3 A0A1V6PSE3 A0A1V6PSI3 A0A1V6PSI3 A0A1V6PSK5 A0A1V6PSK5 A0A1V6PST1 A0A1V6PST1 A0A1V6PT38 A0A1V6PT38 A0A1V6PTD7 A0A1V6PTD7 A0A1V6PTG1 A0A1V6PTG1 A0A1V6PTP8 A0A1V6PTP8 A0A1V6PTS2 A0A1V6PTS2 A0A1V6PU17 A0A1V6PU17 A0A1V6PU93 A0A1V6PU93 A0A1V6PUA6 A0A1V6PUA6 A0A1V6PW78 A0A1V6PW78 A0A1V6PWF2 A0A1V6PWF2 A0A1V6PWM9 A0A1V6PWM9 A0A1V6PWX6 A0A1V6PWX6 A0A1V6PXK3 A0A1V6PXK3 A0A1V6PYU0 A0A1V6PYU0 A0A1V6PZE9 A0A1V6PZE9 A0A1V6PZS5 A0A1V6PZS5 A0A1V6PZS6 A0A1V6PZS6 A0A1V6Q006 A0A1V6Q006 A0A1V6Q0C3 A0A1V6Q0C3 A0A1V6Q0Y2 A0A1V6Q0Y2 A0A1V6Q1W1 A0A1V6Q1W1
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:
A0A1V6Q207Uncharacterized protein. (70 aa)
A0A1V6Q2Q0Vacuolar protein sorting-associated protein 27; Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. (698 aa)
A0A1V6Q380Tubulin alpha chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Belongs to the tubulin family. (450 aa)
A0A1V6Q3I1FAD-binding FR-type domain-containing protein. (694 aa)
A0A1V6Q3Y9Uncharacterized protein; Belongs to the DEAD box helicase family. (482 aa)
A0A1V6Q481Uncharacterized protein. (1075 aa)
A0A1V6Q487PHD-type domain-containing protein. (510 aa)
A0A1V6Q4T3Uncharacterized protein. (248 aa)
A0A1V6Q516Uncharacterized protein. (725 aa)
A0A1V6Q544Ferric oxidoreductase domain-containing protein. (713 aa)
A0A1V6Q6J4Uncharacterized protein; Belongs to the V-ATPase proteolipid subunit family. (200 aa)
A0A1V6Q732Uncharacterized protein. (697 aa)
A0A1V6Q7F9FAD-binding FR-type domain-containing protein. (655 aa)
A0A1V6Q880t-SNARE coiled-coil homology domain-containing protein. (388 aa)
A0A1V6QAN5Uncharacterized protein. (726 aa)
A0A1V6QBR3Uncharacterized protein; Belongs to the synaptobrevin family. (215 aa)
A0A1V6QCN1Uncharacterized protein. (2490 aa)
A0A1V6QCR4Uncharacterized protein. (510 aa)
A0A1V6QDP3V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (159 aa)
A0A1V6QEF6Uncharacterized protein. (345 aa)
A0A1V6QFL5V-type proton ATPase subunit a; Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. (855 aa)
A0A1V6QHQ0Uncharacterized protein; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. (1818 aa)
A0A1V6QIU1FAD-binding FR-type domain-containing protein. (576 aa)
A0A1V6QQD7Uncharacterized protein. (558 aa)
A0A1V6QNS5PH domain-containing protein. (1418 aa)
A0A1V6QNH9Uncharacterized protein. (263 aa)
A0A1V6QN44Protein kinase domain-containing protein. (1274 aa)
A0A1V6QL77V-type proton ATPase subunit; Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores; Belongs to the V-ATPase V0D/AC39 subunit family. (363 aa)
A0A1V6QKT5Tubulin beta chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. (447 aa)
A0A1V6QKT2Uncharacterized protein. (261 aa)
A0A1V6QKH7Uncharacterized protein. (317 aa)
A0A1V6QKG0V-type proton ATPase subunit H; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. (473 aa)
A0A1V6QJY9Uncharacterized protein. (563 aa)
A0A1V6QJN0FAD-binding FR-type domain-containing protein. (596 aa)
A0A1V6QJL9V-type proton ATPase subunit C; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (390 aa)
A0A1V6QJD5F-box domain-containing protein. (572 aa)
A0A1V6PCH0Uncharacterized protein. (250 aa)
A0A1V6PEY2Uncharacterized protein. (423 aa)
A0A1V6PI88Uncharacterized protein. (518 aa)
A0A1V6PJL2Uncharacterized protein. (658 aa)
A0A1V6PK28Tubulin alpha chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. (430 aa)
A0A1V6PP53Uncharacterized protein. (517 aa)
A0A1V6PPZ8TPR_REGION domain-containing protein. (555 aa)
A0A1V6PQQ6Uncharacterized protein. (629 aa)
A0A1V6PR03NAD_binding_2 domain-containing protein. (103 aa)
A0A1V6PR20Uncharacterized protein. (121 aa)
A0A1V6PR52V-type proton ATPase subunit F; Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (124 aa)
A0A1V6PR84CFEM domain-containing protein. (414 aa)
A0A1V6PS70Uncharacterized protein. (600 aa)
A0A1V6PSE3Uncharacterized protein. (284 aa)
A0A1V6PSI3Uncharacterized protein. (231 aa)
A0A1V6PSK5Uncharacterized protein. (75 aa)
A0A1V6PST1Uncharacterized protein. (247 aa)
A0A1V6PT38Plug_translocon domain-containing protein. (478 aa)
A0A1V6PTD7FAD-binding FR-type domain-containing protein. (741 aa)
A0A1V6PTG1Uncharacterized protein. (320 aa)
A0A1V6PTP8V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (158 aa)
A0A1V6PTS2Phosphatidylinositol 3-kinase VPS34. (899 aa)
A0A1V6PU17FAD-binding FR-type domain-containing protein. (619 aa)
A0A1V6PU93Uncharacterized protein. (418 aa)
A0A1V6PUA6Uncharacterized protein. (199 aa)
A0A1V6PW78Vacuolar proton pump subunit B; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase; Belongs to the ATPase alpha/beta chains family. (498 aa)
A0A1V6PWF2Uncharacterized protein. (206 aa)
A0A1V6PWM9Uncharacterized protein. (205 aa)
A0A1V6PWX6Uncharacterized protein. (4321 aa)
A0A1V6PXK3Uncharacterized protein. (266 aa)
A0A1V6PYU0Uncharacterized protein. (311 aa)
A0A1V6PZE9FAD-binding FR-type domain-containing protein. (687 aa)
A0A1V6PZS5zf-Tim10_DDP domain-containing protein. (90 aa)
A0A1V6PZS6FAD-binding FR-type domain-containing protein. (781 aa)
A0A1V6Q006NAD_binding_2 domain-containing protein. (327 aa)
A0A1V6Q0C3Uncharacterized protein. (217 aa)
A0A1V6Q0Y2Coronin; Belongs to the WD repeat coronin family. (597 aa)
A0A1V6Q1W1FAD-binding FR-type domain-containing protein. (842 aa)
Your Current Organism:
Penicillium antarcticum
NCBI taxonomy Id: 416450
Other names: CBS 100492, FRR 4989, P. antarcticum
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