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GTF2B GTF2B CSNK2A1 CSNK2A1 COIL COIL NOLC1 NOLC1 NOP56 NOP56 POLR1A POLR1A FBL FBL RRS1 RRS1 NHP2L1 NHP2L1 RPS14 RPS14 NOP58 NOP58
"NOLC1" - nucleolar and coiled-body phosphoprotein 1 in Homo sapiens
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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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protein of unknown 3D structure
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second shell of interactors
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Predicted Interactions
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NOLC1nucleolar and coiled-body phosphoprotein 1; Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I (699 aa)    
Predicted Functional Partners:
NOP56
NOP56 ribonucleoprotein homolog (yeast); Involved in the early to middle stages of 60S ribosomal subunit biogenesis (594 aa)
      score_image score_image   score_image   0.995
NOP58
NOP58 ribonucleoprotein homolog (yeast); Required for 60S ribosomal subunit biogenesis (By similarity) (529 aa)
      score_image score_image   score_image   0.995
FBL
fibrillarin; Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2’- hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (321 aa)
      score_image score_image   score_image   0.988
CSNK2A1
casein kinase 2, alpha 1 polypeptide; Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly che [...] (391 aa)
        score_image   score_image   0.984
POLR1A
polymerase (RNA) I polypeptide A, 194kDa; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of [...] (1720 aa)
      score_image score_image   score_image   0.975
COIL
coilin; Is a component of the nuclear coiled bodies (CBS) which are involved in the function or assembly/disassembly of nucleoplasmic snRNPs. During mitosis, CBS disassemble, coinciding with a mitotic-specific phosphorylation of p80 coilin (576 aa)
        score_image   score_image   0.974
NHP2L1
NHP2 non-histone chromosome protein 2-like 1 (S. cerevisiae); Binds to the 5’-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding (128 aa)
      score_image score_image   score_image   0.955
RRS1
RRS1 ribosome biogenesis regulator homolog (S. cerevisiae); Involved in ribosome biogenesis (By similarity) (365 aa)
      score_image score_image   score_image   0.954
GTF2B
general transcription factor IIB; General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II (316 aa)
        score_image   score_image   0.930
RPS14
ribosomal protein S14 (151 aa)
        score_image   score_image   0.890
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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