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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 | PGRMC1 | progesterone receptor membrane component 1; Receptor for progesterone (By similarity) (195 aa) | ||
 | RPS12 | ribosomal protein S12 (132 aa) | ||
 | ISL1 | ISL LIM homeobox 1; Binds and regulates the promoters of the insulin, glucagon and somatostatin genes. Involved in the specificarion of motor neurons in cooperation with LHX3 and LDB1 (By similarity) (349 aa) | ||
 | RPS4Y1 | ribosomal protein S4, Y-linked 1 (263 aa) | ||
 | RPL36 | ribosomal protein L36 (105 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) | ||
 | 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) | ||
 | RPL3L | ribosomal protein L3-like (407 aa) | ||
 | RPS11 | ribosomal protein S11 (158 aa) | ||
 | RPS27A | ribosomal protein S27a (156 aa) | ||
 | RPL37 | ribosomal protein L37; Binds to the 23S rRNA (By similarity) (97 aa) | ||
 | RPL30 | ribosomal protein L30 (115 aa) | ||
 | RPL26 | ribosomal protein L26 (145 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) | ||
 | 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) | ||
 | RPL13 | ribosomal protein L13 (211 aa) | ||
 | RPL15 | ribosomal protein L15 (204 aa) | ||
 | RPL38 | ribosomal protein L38 (70 aa) | ||
 | RPS14 | ribosomal protein S14 (151 aa) | ||
 | RPL4 | ribosomal protein L4 (427 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) | ||
 | MBOAT4 | membrane bound O-acyltransferase domain containing 4; Mediates the octanoylation of ghrelin at ’Ser-3’. Can use a variety of fatty acids as substrates including octanoic acid, decanoic acid and tetradecanoic acid (435 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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