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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Your Input:
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 | RPS5 | ribosomal protein S5 (204 aa) | ||
 | SRP54 | signal recognition particle 54kDa; 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) | ||
 | RPL18A | ribosomal protein L18a (176 aa) | ||
 | SEC61B | Sec61 beta subunit; Necessary for protein translocation in the endoplasmic reticulum (96 aa) | ||
 | RPS12 | ribosomal protein S12 (132 aa) | ||
 | SPCS1 | signal peptidase complex subunit 1 homolog (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) (169 aa) | ||
 | RPN2 | ribophorin II; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (631 aa) | ||
 | SSR1 | signal sequence receptor, alpha (286 aa) | ||
 | RPS4Y1 | ribosomal protein S4, Y-linked 1 (263 aa) | ||
 | RPS16 | ribosomal protein S16 (146 aa) | ||
 | RPL36 | ribosomal protein L36 (105 aa) | ||
 | RPL27 | ribosomal protein L27 (136 aa) | ||
 | RPL35 | ribosomal protein L35 (123 aa) | ||
 | TRAM1 | translocation associated membrane protein 1; Stimulatory or required for the translocation of secretory proteins across the ER membrane (374 aa) | ||
 | RPL8 | ribosomal protein L8 (257 aa) | ||
 | SPCS2 | signal peptidase complex subunit 2 homolog (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) (226 aa) | ||
 | SSR3 | signal sequence receptor, gamma (translocon-associated protein gamma); TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins (185 aa) | ||
 | RPL26L1 | ribosomal protein L26-like 1 (145 aa) | ||
 | SRP14 | signal recognition particle 14kDa (homologous Alu RNA binding 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) | ||
 | SEC11A | SEC11 homolog A (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) (179 aa) | ||
 | RPL3L | ribosomal protein L3-like (407 aa) | ||
 | SRP9 | signal recognition particle 9kDa; 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) | ||
 | SRP68 | signal recognition particle 68kDa; 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) | ||
 | SRP72 | signal recognition particle 72kDa; 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 (671 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | SRP19 | signal recognition particle 19kDa; Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP (144 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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