STRINGSTRING
K5UK65_PHACS K5UK65_PHACS K5UZF6_PHACS K5UZF6_PHACS K5V2E2_PHACS K5V2E2_PHACS K5V5B5_PHACS K5V5B5_PHACS K5V6R6_PHACS K5V6R6_PHACS K5VDT2_PHACS K5VDT2_PHACS K5VE65_PHACS K5VE65_PHACS K5VH12_PHACS K5VH12_PHACS K5VJ07_PHACS K5VJ07_PHACS K5VS56_PHACS K5VS56_PHACS K5VUJ1_PHACS K5VUJ1_PHACS K5VUN4_PHACS K5VUN4_PHACS K5VVN0_PHACS K5VVN0_PHACS K5VWQ4_PHACS K5VWQ4_PHACS K5W141_PHACS K5W141_PHACS K5W1N7_PHACS K5W1N7_PHACS K5W2D0_PHACS K5W2D0_PHACS K5W2S8_PHACS K5W2S8_PHACS K5W505_PHACS K5W505_PHACS K5W581_PHACS K5W581_PHACS K5W5J5_PHACS K5W5J5_PHACS K5W5P3_PHACS K5W5P3_PHACS K5W760_PHACS K5W760_PHACS CLP1 CLP1 K5W880_PHACS K5W880_PHACS K5W9K6_PHACS K5W9K6_PHACS K5W9U6_PHACS K5W9U6_PHACS K5WAL0_PHACS K5WAL0_PHACS K5WAQ1_PHACS K5WAQ1_PHACS K5WAR0_PHACS K5WAR0_PHACS K5WBM6_PHACS K5WBM6_PHACS K5WCH1_PHACS K5WCH1_PHACS K5WEA6_PHACS K5WEA6_PHACS K5WG30_PHACS K5WG30_PHACS K5WG40_PHACS K5WG40_PHACS K5WJC3_PHACS K5WJC3_PHACS K5WJF5_PHACS K5WJF5_PHACS K5WJR8_PHACS K5WJR8_PHACS K5WPB1_PHACS K5WPB1_PHACS K5X3W9_PHACS K5X3W9_PHACS K5X7W4_PHACS K5X7W4_PHACS K5X8B7_PHACS K5X8B7_PHACS K5X9H4_PHACS K5X9H4_PHACS K5X9M9_PHACS K5X9M9_PHACS K5X9X3_PHACS K5X9X3_PHACS K5XEI0_PHACS K5XEI0_PHACS K5XEN7_PHACS K5XEN7_PHACS
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:
K5UK65_PHACSUncharacterized protein. (1210 aa)
K5UZF6_PHACSSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. (705 aa)
K5V2E2_PHACSSmg4_UPF3 domain-containing protein. (475 aa)
K5V5B5_PHACSUncharacterized protein; Belongs to the DEAD box helicase family. (470 aa)
K5V6R6_PHACSSerine/threonine-protein phosphatase. (304 aa)
K5VDT2_PHACSUncharacterized protein. (296 aa)
K5VE65_PHACSUncharacterized protein. (702 aa)
K5VH12_PHACSRRM domain-containing protein. (165 aa)
K5VJ07_PHACSUncharacterized protein. (149 aa)
K5VS56_PHACSUncharacterized protein. (869 aa)
K5VUJ1_PHACSUncharacterized protein. (568 aa)
K5VUN4_PHACSAAA domain-containing protein. (1067 aa)
K5VVN0_PHACSNuclear cap-binding protein subunit 2. (225 aa)
K5VWQ4_PHACSCleavage and polyadenylation specificity factor subunit 5; Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The [...] (204 aa)
K5W141_PHACSPWI domain-containing protein. (452 aa)
K5W1N7_PHACSUncharacterized protein. (311 aa)
K5W2D0_PHACSSerine/threonine-protein phosphatase; Belongs to the PPP phosphatase family. (332 aa)
K5W2S8_PHACSUncharacterized protein. (606 aa)
K5W505_PHACSUncharacterized protein. (338 aa)
K5W581_PHACSUncharacterized protein. (1079 aa)
K5W5J5_PHACSCID domain-containing protein. (620 aa)
K5W5P3_PHACSCleavage and polyadenylation specificity factor subunit 2. (951 aa)
K5W760_PHACSProtein DOM34 homolog; May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non- functional ribosomes and degrade damaged mRNAs. (419 aa)
CLP1mRNA cleavage and polyadenylation factor CLP1; Required for endonucleolytic cleavage during polyadenylation- dependent pre-mRNA 3'-end formation. (501 aa)
K5W880_PHACSPolyadenylate-binding protein; Binds the poly(A) tail of mRNA. Belongs to the polyadenylate-binding protein type-1 family. (672 aa)
K5W9K6_PHACSmRNA cap 0 methyltransferase domain-containing protein. (700 aa)
K5W9U6_PHACSUncharacterized protein. (437 aa)
K5WAL0_PHACSeRF1_1 domain-containing protein. (438 aa)
K5WAQ1_PHACSWD_REPEATS_REGION domain-containing protein. (527 aa)
K5WAR0_PHACSUncharacterized protein. (594 aa)
K5WBM6_PHACSCPSF_A domain-containing protein. (1417 aa)
K5WCH1_PHACSRRM domain-containing protein. (302 aa)
K5WEA6_PHACSRRM domain-containing protein. (220 aa)
K5WG30_PHACSRRM domain-containing protein. (234 aa)
K5WG40_PHACSUncharacterized protein. (785 aa)
K5WJC3_PHACSPoly(A) polymerase; Polymerase that creates the 3'-poly(A) tail of mRNA's. (556 aa)
K5WJF5_PHACSUncharacterized protein; Belongs to the DEAD box helicase family. (396 aa)
K5WJR8_PHACSProtein phosphatase PP2A regulatory subunit B; Belongs to the phosphatase 2A regulatory subunit B family. (448 aa)
K5WPB1_PHACSSerine/threonine-protein phosphatase. (489 aa)
K5X3W9_PHACSRRM domain-containing protein. (224 aa)
K5X7W4_PHACSSuf domain-containing protein. (806 aa)
K5X8B7_PHACSTr-type G domain-containing protein. (605 aa)
K5X9H4_PHACSMIF4G domain-containing protein. (869 aa)
K5X9M9_PHACSUncharacterized protein. (246 aa)
K5X9X3_PHACSRRM domain-containing protein. (203 aa)
K5XEI0_PHACSUncharacterized protein. (260 aa)
K5XEN7_PHACSFip1 domain-containing protein. (603 aa)
Your Current Organism:
Phanerochaete carnosa
NCBI taxonomy Id: 650164
Other names: P. carnosa HHB-10118-sp, Phanerochaete carnosa HHB-10118-sp
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.