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GFPT1 GFPT1 RPL4 RPL4 NAA50 NAA50 FARSB FARSB CCT5 CCT5 GARS GARS SFPQ SFPQ SARS SARS RPS27A RPS27A EEF2 EEF2 FARSA FARSA FUS FUS HNRNPD HNRNPD TARSL2 TARSL2 SARS2 SARS2 TARS TARS AURKA AURKA TOMM34 TOMM34 CHEK1 CHEK1 AHNAK AHNAK UBLCP1 UBLCP1 FHOD1 FHOD1 AARSD1 AARSD1 ENSG00000108825 ENSG00000108825 TARBP1 TARBP1 TPD52L2 TPD52L2
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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TARBP1Probable methyltransferase TARBP1; 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; Armadillo-like helical domain containing (1621 aa)
AURKAAurora kinase A; Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDE [...] (403 aa)
TPD52L2Tumor protein D52 like 2 (229 aa)
SARSSerine--tRNA ligase, cytoplasmic; Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction- serine is first activated by ATP to form Ser- AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at ’Lys-16’ (H4K16) [...] (514 aa)
NAA50N-alpha-acetyltransferase 50; N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine. Has a broad substrate specificity- able to acetylate the initiator methionine of most peptides, except for those with a proline in second position. Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins. Autoacetylates in vivo. The relevance of N-epsilon-acetyltransferase activity is however unclear- able to acetylate H4 in vitro, but this result has not been confirmed in vivo. [...] (169 aa)
FUSRNA-binding protein FUS; Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single- stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity; Belongs to the RRM TET family (526 aa)
FHOD1FH1/FH2 domain-containing protein 1; Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing; Armadillo-like helical domain containing (1164 aa)
RPS27AUbiquitin-40S ribosomal protein S27a; Ubiquitin- Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked- Lys-6-linked may be inv [...] (156 aa)
CCT5T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (541 aa)
FARSBphenylalanyl-tRNA synthetase beta subunit; Aminoacyl tRNA synthetases, Class II (589 aa)
UBLCP1Ubiquitin-like domain-containing CTD phosphatase 1; Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome; CTD family phosphatases (318 aa)
EEF2Elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily (858 aa)
RPL4L ribosomal proteins (427 aa)
HNRNPDHeterogeneous nuclear ribonucleoprotein D0; Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3’-UTR of many proto- oncogenes and cytokine mRNAs. Also binds to double- and single- stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5’-UUAG-3’ sequence and also weaker to the single-stranded 5’-TTAGGG-3’ telomeric DNA repeat. Binds RNA oligonucleotides with 5’-UUAGGG-3’ repeats more tightly than the telomeric single-s [...] (355 aa)
FARSAphenylalanyl-tRNA synthetase alpha subunit; Aminoacyl tRNA synthetases, Class II (508 aa)
TARSL2Probable threonine--tRNA ligase 2, cytoplasmic; threonyl-tRNA synthetase like 2; Belongs to the class-II aminoacyl-tRNA synthetase family (802 aa)
SFPQSplicing factor, proline- and glutamine-rich; DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphory [...] (707 aa)
GFPT1Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1; Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1 (699 aa)
TOMM34Mitochondrial import receptor subunit TOM34; Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state; Tetratricopeptide repeat domain containing (309 aa)
AHNAKNeuroblast differentiation-associated protein AHNAK; May be required for neuronal cell differentiation; PDZ domain containing (5890 aa)
GARSGlycine--tRNA ligase; Catalyzes the ligation of glycine to the 3’-end of its cognate tRNA. Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs; Belongs to the class-II aminoacyl-tRNA synthetase family (739 aa)
TARSThreonine--tRNA ligase, cytoplasmic; Aminoacyl tRNA synthetases, Class II (756 aa)
CHEK1Serine/threonine-protein kinase Chk1; Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at ’Ser-178’ and ’Thr-507’ and pho [...] (476 aa)
AARSD1Alanyl-tRNA editing protein Aarsd1; Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) (412 aa)
ENSG00000108825PTGES3L-AARSD1 readthrough; Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) (586 aa)
SARS2Serine--tRNA ligase, mitochondrial; Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec); Aminoacyl tRNA synthetases, Class II (520 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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