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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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 to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
NPM3Nucleoplasmin-3; Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning. Modulates the histone chaperone function and the RNA-binding activity of nucleolar phosphoprotein B23/NPM. Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM ; Belongs to the nucleoplasmin family. (178 aa)    
Predicted Functional Partners:
NPM1
Nucleophosmin; Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. M [...]
   
 
0.999
NPM2
Nucleoplasmin-2; Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. Belongs to the nucleoplasmin family.
   
 
0.999
NCL
Nucleolin; Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG- 3' repeats more tightly than the telomeric single-stranded DNA 5'- TTAGGG-3' repeats.
   
 
 0.915
NEPRO
Nucleolus and neural progenitor protein; May play a role in cortex development as part of the Notch signaling pathway. Downstream of Notch may repress the expression of proneural genes and inhibit neuronal differentiation thereby maintaining neural progenitors. May also play a role in preimplentation embryo development.
   
   0.865
RPL26L1
Ribosomal protein L26 like 1; Belongs to the universal ribosomal protein uL24 family.
   
   0.828
RPL36AL
Ribosomal protein L36a like; Belongs to the eukaryotic ribosomal protein eL42 family.
   
 
 0.822
PPAN-P2RY11
PPAN-P2RY11 readthrough; Belongs to the G-protein coupled receptor 1 family.
   
   0.819
RPL3
60S ribosomal protein L3; The L3 protein is a component of the large subunit of cytoplasmic ribosomes.
   
 
 0.818
RECQL4
ATP-dependent DNA helicase Q4; DNA-dependent ATPase. May modulate chromosome segregation. Belongs to the helicase family. RecQ subfamily.
   
   0.814
LAS1L
Ribosomal biogenesis protein LAS1L; Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.
   
   0.800
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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