STRINGSTRING
T15H9.6 T15H9.6 W04A4.5 W04A4.5 pap-1 pap-1 Y48G10A.4 Y48G10A.4 inst-1 inst-1 aos-1 aos-1 dic-1 dic-1 F10B5.8 F10B5.8 F19F10.12 F19F10.12 symk-1 symk-1 ubc-9 ubc-9 F43G6.5 F43G6.5 cdk-9 cdk-9 smo-1 smo-1 R02D3.4 R02D3.4 ulp-1 ulp-1 uba-2 uba-2
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:
T15H9.6Poly(A) polymerase; Polymerase that creates the 3'-poly(A) tail of mRNA's. (554 aa)
W04A4.5INTegrator complex Subunit homolog. (1071 aa)
pap-1Poly(A) polymerase; Polymerase that creates the 3'-poly(A) tail of mRNA's. (655 aa)
Y48G10A.4INTegrator complex Subunit homolog. (977 aa)
inst-1INTegrator complex Subunit homolog. (1884 aa)
aos-1SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable). (350 aa)
dic-1VWFA domain-containing protein. (872 aa)
F10B5.8INTegrator complex Subunit homolog. (608 aa)
F19F10.12Beta-Casp domain-containing protein. (646 aa)
symk-1SYMpleKin cleavage and polyadenylation factor. (1143 aa)
ubc-9SUMO-conjugating enzyme UBC9; Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1 and the Polycomb protein sop-2. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates. Belongs to the ubiquitin-conjugating enzyme family. (166 aa)
F43G6.5Poly(A) polymerase; Polymerase that creates the 3'-poly(A) tail of mRNA's. (554 aa)
cdk-9Probable cyclin-dependent kinase 9; Essential member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (C- terminal domain) of the large subunit of RNA polymerase II (RNAP II) and spt-5. (478 aa)
smo-1Small ubiquitin-related modifier; Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic dev [...] (91 aa)
R02D3.4INTegrator complex Subunit homolog. (782 aa)
ulp-1Sentrin-specific protease; Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form. (697 aa)
uba-2SUMO-activating enzyme subunit uba-2; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable). (582 aa)
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.