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STRINGSTRING
SPCS2 SPCS2 RPL35 RPL35 RPL27 RPL27 SRP54 SRP54 RPN1 RPN1 RPS27A RPS27A RPL37 RPL37 SRP14 SRP14 RPL26L1 RPL26L1 RPL36 RPL36 RPS12 RPS12 CCT4 CCT4 RPL6 RPL6 SSR1 SSR1 RPL26 RPL26 RPL19 RPL19 SSR2 SSR2 RPS5 RPS5 RPL30 RPL30 CCT2 CCT2 RPS23 RPS23 RPL29 RPL29 RPL18A RPL18A RPS11 RPS11 SEC11A SEC11A TCP1 TCP1
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 protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
RPS5ribosomal protein S5 (204 aa)
RPL6ribosomal protein L6; Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I (288 aa)
SRP54signal 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)
RPL18Aribosomal protein L18a (176 aa)
RPL19ribosomal protein L19 (196 aa)
RPS12ribosomal protein S12 (132 aa)
SSR1signal sequence receptor, alpha (286 aa)
RPL36ribosomal protein L36 (105 aa)
RPL27ribosomal protein L27 (136 aa)
RPL35ribosomal protein L35 (123 aa)
SPCS2signal 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)
RPL26L1ribosomal protein L26-like 1 (145 aa)
SRP14signal 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)
SEC11ASEC11 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)
RPS11ribosomal protein S11 (158 aa)
RPS27Aribosomal protein S27a (156 aa)
RPL37ribosomal protein L37; Binds to the 23S rRNA (By similarity) (97 aa)
RPL30ribosomal protein L30 (115 aa)
RPL26ribosomal protein L26 (145 aa)
RPL29ribosomal protein L29 (159 aa)
SSR2signal 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)
RPN1ribophorin I; 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 (607 aa)
RPS23ribosomal protein S23 (143 aa)
CCT2chaperonin containing TCP1, subunit 2 (beta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (535 aa)
TCP1t-complex 1; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (556 aa)
CCT4chaperonin containing TCP1, subunit 4 (delta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (539 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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