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RUVBL2 RUVBL2 TTI1 TTI1 HSPA4 HSPA4 POLR2E POLR2E RUVBL1 RUVBL1 TUBA1A TUBA1A UBC UBC SMG1 SMG1 RPS3 RPS3 UPF1 UPF1 SMG8 SMG8 MAGOH MAGOH SMG9 SMG9 RPS23 RPS23 RPS2 RPS2 RPL4 RPL4 RPL34 RPL34 RPL11 RPL11 UPF2 UPF2 RPL19 RPL19 RPL35A RPL35A EIF4A3 EIF4A3 RPL27 RPL27 RPL7 RPL7 UPF3A UPF3A SMG6 SMG6
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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.
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small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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query proteins and first shell of interactors
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white nodes:
second shell of interactors
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Edges represent protein-protein associations
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experimentally determined
Predicted Interactions
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POLR2Epolymerase (RNA) II (DNA directed) polypeptide E, 25kDa; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the low [...] (210 aa)
RPL19ribosomal protein L19 (196 aa)
RPL27ribosomal protein L27 (136 aa)
UPF1UPF1 regulator of nonsense transcripts homolog (yeast); RNA-dependent helicase and ATPase required for nonsense- mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1- eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (loc [...] (1118 aa)
SMG6smg-6 homolog, nonsense mediated mRNA decay factor (C. elegans); Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5’- (GTGTGG)(4)GTGT-3’ telomeric DNA, but not to a telomerase RNA template component (TER) (1419 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)
SMG9smg-9 homolog, nonsense mediated mRNA decay factor (C. elegans); Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8 (520 aa)
RPS23ribosomal protein S23 (143 aa)
SMG8smg-8 homolog, nonsense mediated mRNA decay factor (C. elegans); Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required to mediate the recruitment of SMG1 to the ribosome-SURF complex and to suppress SMG1 kinase activity until the ribosome-SURF complex locates the exon junction complex (EJC). Acts as a regulator of kinase activity (991 aa)
TUBA1Atubulin, alpha 1a; 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 (By similarity) (451 aa)
HSPA4heat shock 70kDa protein 4 (840 aa)
RPL4ribosomal protein L4 (427 aa)
RUVBL1RuvB-like 1 (E. coli); May be able to bind plasminogen at cell surface and enhance plasminogen activation (456 aa)
RPL7ribosomal protein L7; Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs (248 aa)
RPS2ribosomal protein S2 (293 aa)
UBCubiquitin C (685 aa)
UPF2UPF2 regulator of nonsense transcripts homolog (yeast) (1272 aa)
MAGOHmago-nashi homolog, proliferation-associated (Drosophila); 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 in the mature mR [...] (146 aa)
TTI1TELO2 interacting protein 1; Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell gr [...] (1089 aa)
RPL11ribosomal protein L11; Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity) (178 aa)
UPF3AUPF3 regulator of nonsense transcripts homolog A (yeast); Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2- UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. However, UPF3A is shown to be only marginally active in NMD as compared to UPF3B. Binds spliced mRNA [...] (476 aa)
RPL34ribosomal protein L34 (117 aa)
RPL35Aribosomal protein L35a; Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site (110 aa)
SMG1smg-1 homolog, phosphatidylinositol 3-kinase-related kinase (C. elegans); Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex asso [...] (3661 aa)
RPS3ribosomal protein S3 (243 aa)
RUVBL2RuvB-like 2 (E. coli); Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (5’ to 3’) activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity (463 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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