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) | ||
 | RPL6 | ribosomal protein L6; Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I (288 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) | ||
 | SSB | Sjogren syndrome antigen B (autoantigen La); Binds to the 3’ poly(U) terminii of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (408 aa) | ||
 | TRAM1 | translocation associated membrane protein 1; Stimulatory or required for the translocation of secretory proteins across the ER membrane (374 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) | ||
 | 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) | ||
 | RPS11 | ribosomal protein S11 (158 aa) | ||
 | RPL37 | ribosomal protein L37; Binds to the 23S rRNA (By similarity) (97 aa) | ||
 | RPL30 | ribosomal protein L30 (115 aa) | ||
 | RPL29 | ribosomal protein L29 (159 aa) | ||
 | SSR2 | signal sequence receptor, beta (translocon-associated protein beta); 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 (183 aa) | ||
 | RPS23 | ribosomal protein S23 (143 aa) | ||
 | RPL13 | ribosomal protein L13 (211 aa) | ||
 | RPL38 | ribosomal protein L38 (70 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) | ||
 | PRKDC | protein kinase, DNA-activated, catalytic polypeptide (4127 aa) | ||
 | RPS15A | ribosomal protein S15a (130 aa) | ||
 | RPLP2 | ribosomal protein, large, P2; Plays an important role in the elongation step of protein synthesis (115 aa) | ||
 | XRCC4 | X-ray repair complementing defective repair in Chinese hamster cells 4; Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (336 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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