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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 | OSGEP | O-sialoglycoprotein endopeptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (By similarity) (335 aa) | ||
 | TMSB10 | thymosin beta 10; Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity) (44 aa) | ||
 | FTSJ2 | FtsJ RNA methyltransferase homolog 2 (E. coli); Probable methyltransferase (246 aa) | ||
 | HELB | helicase (DNA) B; Unwinds duplex DNA with 5’-3’ polarity. Has single- strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates. During S phase, may facilitate cellular recovery from replication stress (1087 aa) | ||
 | MBD4 | methyl-CpG binding domain protein 4; Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G-T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G-U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein (580 aa) | ||
 | DNAJC10 | DnaJ (Hsp40) homolog, subfamily C, member 10 (793 aa) | ||
 | OSGEPL1 | O-sialoglycoprotein endopeptidase-like 1; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (By similarity) (414 aa) | ||
 | PIF1 | PIF1 5’-to-3’ DNA helicase homolog (S. cerevisiae); DNA-dependent ATPase and DNA helicase inhibiting telomerase activity by unwinding DNA/RNA duplex formed by telomerase RNA and telomeric DNA in a 5’ to 3’ polarity. Negatively regulates telomere length and such inhibition requires its ATPase activity. Tightly cell cycle regulated and expressed in late S/G2 phase (641 aa) | ||
 | EFTUD1 | elongation factor Tu GTP binding domain containing 1; Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits (1120 aa) | ||
 | EIF2B5 | eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa; Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP (721 aa) | ||
 | SPIN2B | spindlin family, member 2B; Involved in the regulation of cell cycle progression, this activity is related to the inhibition of apoptosis following the removal of essential growth factors (258 aa) | ||
 | GFM2 | G elongation factor, mitochondrial 2; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation (779 aa) | ||
 | PGM2L1 | phosphoglucomutase 2-like 1; Glucose 1,6-bisphosphate synthase using 1,3- bisphosphoglycerate as a phosphate donor and a series of 1- phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1- phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5- bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities (622 aa) | ||
 | EEF2 | eukaryotic translation elongation 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 (858 aa) | ||
 | FTSJ1 | FtsJ RNA methyltransferase homolog 1 (E. coli) (329 aa) | ||
 | UPP1 | uridine phosphorylase 1; Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (310 aa) | ||
 | RBBP9 | retinoblastoma binding protein 9; May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta1 through interaction with retinoblastoma and the subsequent displacement of E2F-1 (186 aa) | ||
 | YRDC | yrdC domain containing (E. coli); May regulate the activity of some transporters (By similarity) (279 aa) | ||
 | SPIN1 | spindlin 1; May play a role in cell-cycle regulation during the transition from gamete to embryo (By similarity) (262 aa) | ||
 | VPS29 | vacuolar protein sorting 29 homolog (S. cerevisiae); Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Has low protein phosphatase activity towards a serine-phosphorylated peptide derived from IGF2R (in vitro) (186 aa) | ||
 | RPL23A | ribosomal protein L23a; This protein binds to a specific region on the 26S rRNA (By similarity) (156 aa) | ||
 | EFTUD2 | elongation factor Tu GTP binding domain containing 2; Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP (972 aa) | ||
 | FTSJ3 | FtsJ homolog 3 (E. coli); Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation (847 aa) | ||
 | TOP2B | topoisomerase (DNA) II beta 180kDa; Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Indirectly involved in vitamin D- coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR- mediated transrepression of the CYP27B1 gene (1621 aa) | ||
 | TOP2A | topoisomerase (DNA) II alpha 170kDa (1531 aa) | ||
 | GFM1 | G elongation factor, mitochondrial 1; Mitochondrial GTPase that 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. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of m [...] (751 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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