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MRPS12 MRPS12 THUMPD2 THUMPD2 DIS3L2 DIS3L2 THUMPD3 THUMPD3 ARF6 ARF6 QTRTD1 QTRTD1 QTRT1 QTRT1 UBC UBC EIF4A1 EIF4A1 RPS23 RPS23 CRYAB CRYAB EIF4A2 EIF4A2 EIF4A3 EIF4A3 NEDD8 NEDD8 DIS3L DIS3L HELZ2 HELZ2 DIS3 DIS3
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
CRYABcrystallin, alpha B; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (175 aa)
QTRT1queuine tRNA-ribosyltransferase 1; Exchanges the guanine residue with 7-aminomethyl-7- deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By similarity) (403 aa)
NEDD8neural precursor cell expressed, developmentally down-regulated 8; Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C- APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins (81 aa)
EIF4A3eukaryotic translation initiation factor 4A3; ATP-dependent RNA helicase. Component of a splicing- dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction [...] (411 aa)
QTRTD1queuine tRNA-ribosyltransferase domain containing 1; Interacts with QTRT1 to form an active queuine tRNA- ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine) (By similarity) (415 aa)
EIF4A1eukaryotic translation initiation factor 4A1; ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5’-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (406 aa)
RPS23ribosomal protein S23 (143 aa)
ARF6ADP-ribosylation factor 6; GTP-binding protein involved in protein trafficking; regulates endocytic recycling and cytoskeleton remodeling. May modulate vesicle budding and uncoating within the Golgi apparatus. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in the regulation of dendritic spine development (By similarity). Contributes to the regulation of dendritic branching and filopodia extension (175 aa)
MRPS12mitochondrial ribosomal protein S12 (138 aa)
DIS3L2DIS3 mitotic control homolog (S. cerevisiae)-like 2; Ribonuclease that plays a critical role in RNA metabolism. It is essential for correct mitosis, and negatively regulates cell proliferation (885 aa)
DIS3LDIS3 mitotic control homolog (S. cerevisiae)-like; Putative cytoplasm-specific catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3’ untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA (1054 aa)
EIF4A2eukaryotic translation initiation factor 4A2; ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5’-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (407 aa)
THUMPD3THUMP domain containing 3 (507 aa)
UBCubiquitin C (685 aa)
DIS3DIS3 mitotic control homolog (S. cerevisiae) (958 aa)
HELZ2helicase with zinc finger 2, transcriptional coactivator; Helicase that acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA (2649 aa)
THUMPD2THUMP domain containing 2 (503 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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