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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | TARBP1 | TAR (HIV-1) RNA binding protein 1; Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs. In case of infection by HIV-1, it binds to the loop region of TAR RNA, a region also bound by RNA polymerase II. Binding of TARBP1 and RNA polymerase II to HIV-1 TAR RNA is mutually exclusive, suggesting that TARBP1 may function alone or in conjunction with HIV-1 Tat to disengage RNA polymerase II from HIV-1 TAR RNA. May act by methylating HIV-1 TAR RNA (1621 aa) | ||
 | SNX8 | sorting nexin 8; May be involved in several stages of intracellular trafficking. May play a role in intracellular protein transport from early endosomes to the trans-Golgi network (465 aa) | ||
 | DDX5 | DEAD (Asp-Glu-Ala-Asp) box helicase 5; Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation a [...] (614 aa) | ||
 | DDX39A | DEAD (Asp-Glu-Ala-Asp) box polypeptide 39A; Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus (427 aa) | ||
 | MRM1 | mitochondrial rRNA methyltransferase 1 homolog (S. cerevisiae); Probably methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S) (By similarity) (353 aa) | ||
 | QTRT1 | queuine 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) | ||
 | DDX18 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 18; Probable RNA-dependent helicase (670 aa) | ||
 | QTRTD1 | queuine 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) | ||
 | EIF4A1 | eukaryotic 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) | ||
 | TPX2 | TPX2, microtubule-associated, homolog (Xenopus laevis); Spindle assembly factor. Required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at ’Thr-288’ and protects this residue against dephosphorylation (747 aa) | ||
 | KCTD19 | potassium channel tetramerisation domain containing 19 (926 aa) | ||
 | RNMTL1 | RNA methyltransferase like 1; Probable RNA methyltransferase (By similarity) (420 aa) | ||
 | DDX10 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 10; Putative ATP-dependent RNA helicase (875 aa) | ||
 | MRPL1 | mitochondrial ribosomal protein L1 (325 aa) | ||
 | EIF4A2 | eukaryotic 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) | ||
 | DDX59 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 59 (619 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | DDX21 | DEAD (Asp-Glu-Ala-Asp) box helicase 21; Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Functions as cofactor for JUN-activated transcription. Involved in rRNA processing (783 aa) | ||
 | TRMT1 | tRNA methyltransferase 1 homolog (S. cerevisiae); Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups (659 aa) | ||
 | RPL10A | ribosomal protein L10a (217 aa) | ||
 | DDX39B | DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B (428 aa) | ||
 | TDRD12 | tudor domain containing 12 (395 aa) | ||
 | THUMPD2 | THUMP domain containing 2 (503 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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