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STRINGSTRING
SRP14 protein (human) - STRING interaction network
"SRP14" - Signal recognition particle 14 kDa protein in Homo sapiens
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
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SRP14Signal recognition particle 14 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (136 aa)    
Predicted Functional Partners:
SRP9
Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (86 aa)
     
  0.999
SRP68
Signal recognition particle subunit SRP68; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function (627 aa)
     
  0.999
SRP54
Signal recognition particle 54 kDa protein; Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein) (504 aa)
     
  0.999
SRP19
Signal recognition particle 19 kDa protein; Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP (144 aa)
     
  0.999
SRP72
Signal recognition particle subunit SRP72; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function; Belongs to the SRP72 family (671 aa)
     
  0.999
RPS17
Ribosomal protein S17 (135 aa)
     
    0.998
RPL30
Ribosomal protein L30; Belongs to the eukaryotic ribosomal protein eL30 family (115 aa)
     
  0.998
RPL27
60S ribosomal protein L27; Component of the large ribosomal subunit. Required for proper rRNA processing and maturation of 28S and 5.8S rRNAs (136 aa)
     
  0.998
RPS25
Ribosomal protein S25 (125 aa)
     
    0.998
RPS27
40S ribosomal protein S27; Component of the small ribosomal subunit. Required for proper rRNA processing and maturation of 18S rRNAs; Belongs to the eukaryotic ribosomal protein eS27 family (84 aa)
     
    0.998
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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