25 items (Homo sapiens) - STRING network view

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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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	NCALD	neurocalcin delta; May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three calcium ions (193 aa)
	HSPA8	heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (646 aa)
	HSPA2	heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (639 aa)
	HSPBP1	HSPA (heat shock 70kDa) binding protein, cytoplasmic cochaperone 1; Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR (359 aa)
	FAM86B2	family with sequence similarity 86, member B2 (330 aa)
	LNX1	ligand of numb-protein X 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65 (By similarity) (728 aa)
	METTL21C	methyltransferase like 21C; Protein-lysine methyltransferase (264 aa)
	HSPA4L	heat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity) (839 aa)
	HSPA9	heat shock 70kDa protein 9 (mortalin) (679 aa)
	HSPA4	heat shock 70kDa protein 4 (840 aa)
	EEF2	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (858 aa)
	HSPA6	heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity) (643 aa)
	HSPH1	heat shock 105kDa/110kDa protein 1; Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity) (858 aa)
	ATRIP	ATR interacting protein (791 aa)
	HSPA5	heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (654 aa)
	CCDC88A	coiled-coil domain containing 88A (1870 aa)
	DYNC1H1	dynein, cytoplasmic 1, heavy chain 1; Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (4646 aa)
	FAM86C1	family with sequence similarity 86, member C1 (165 aa)
	BAG3	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity (575 aa)
	METTL21D	methyltransferase like 21D; Protein-lysine N-methyltransferase that specifically trimethylates ’Lys-315’ of VCP/p97 (229 aa)
	METTL21A	methyltransferase like 21A; Protein-lysine methyltransferase (218 aa)
	C5orf54	chromosome 5 open reading frame 54 (594 aa)
	EFTUD2	elongation factor Tu GTP binding domain containing 2; Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP (972 aa)
	FAM86A	family with sequence similarity 86, member A (330 aa)
	FAM86B1	family with sequence similarity 86, member B1 (330 aa)

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ATRIP	METTL21A	ENSP00000323099	ENSP00000385481	ATR interacting protein	methyltransferase like 21A; Protein-lysine methyltransferase	0.686
BAG3	HSPA2	ENSP00000358081	ENSP00000247207	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity	heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage	0.640
BAG3	HSPA4	ENSP00000358081	ENSP00000302961	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity	heat shock 70kDa protein 4	0.997
BAG3	HSPA5	ENSP00000358081	ENSP00000324173	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity	heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER	0.586
BAG3	HSPA6	ENSP00000358081	ENSP00000310219	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity	heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity)	0.715
BAG3	HSPA8	ENSP00000358081	ENSP00000227378	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity	heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex	0.990
BAG3	HSPH1	ENSP00000358081	ENSP00000318687	BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity	heat shock 105kDa/110kDa protein 1; Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity)	0.531
C5orf54	METTL21A	ENSP00000386184	ENSP00000385481	chromosome 5 open reading frame 54	methyltransferase like 21A; Protein-lysine methyltransferase	0.688
EEF2	FAM86A	ENSP00000307940	ENSP00000398502	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	family with sequence similarity 86, member A	0.784
EEF2	HSPA2	ENSP00000307940	ENSP00000247207	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage	0.575
EEF2	HSPA4	ENSP00000307940	ENSP00000302961	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 4	0.518
EEF2	HSPA4L	ENSP00000307940	ENSP00000296464	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity)	0.508
EEF2	HSPA5	ENSP00000307940	ENSP00000324173	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER	0.666
EEF2	HSPA6	ENSP00000307940	ENSP00000310219	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity)	0.643
EEF2	HSPA8	ENSP00000307940	ENSP00000227378	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex	0.881
EEF2	HSPA9	ENSP00000307940	ENSP00000297185	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 70kDa protein 9 (mortalin)	0.552
EEF2	HSPH1	ENSP00000307940	ENSP00000318687	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	heat shock 105kDa/110kDa protein 1; Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity)	0.458
EEF2	NCALD	ENSP00000307940	ENSP00000220931	eukaryotic translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	neurocalcin delta; May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. Binds three calcium ions	0.478
EFTUD2	HSPA2	ENSP00000392094	ENSP00000247207	elongation factor Tu GTP binding domain containing 2; Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP	heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage	0.541
EFTUD2	HSPA4	ENSP00000392094	ENSP00000302961	elongation factor Tu GTP binding domain containing 2; Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP	heat shock 70kDa protein 4	0.445

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