26 items (Homo sapiens) - STRING network view

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	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)
	STUB1	STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates- ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 th [...] (303 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)
	DNAJB1	DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP (340 aa)
	PEBP4	phosphatidylethanolamine-binding protein 4; Seems to promote cellular resistance to TNF-induced apoptosis by inhibiting activation of the Raf-1/MEK/ERK pathway, JNK and phosphatidylethanolamine externalization (227 aa)
	SDCBP	syndecan binding protein (syntenin); Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (298 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)
	SLC6A3	solute carrier family 6 (neurotransmitter transporter, dopamine), member 3; Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals (620 aa)
	CCT2	chaperonin 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)
	HSPA4	heat shock 70kDa protein 4 (840 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)
	GPR37	G protein-coupled receptor 37 (endothelin receptor type B-like); Orphan receptor. May have a unique functional role in the central nervous system (613 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)
	TCP1	t-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)
	PACRG	PARK2 co-regulated; Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited. May play an important role in the formation of Lewy bodies and protection of dopaminergic neurons against Parkinson disease (296 aa)
	UBE2G2	ubiquitin-conjugating enzyme E2G 2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-linked polyubiquitination. Involved in endoplasmic reticulum- associated degradation (ERAD) (165 aa)
	PICK1	protein interacting with PRKCA 1; Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate heteromeric ASIC1/ASIC3 channel (415 aa)
	LYPD2	LY6/PLAUR domain containing 2 (125 aa)
	PARK2	parkinson protein 2, E3 ubiquitin protein ligase (parkin) (465 aa)
	HSPA1A	heat shock 70kDa protein 1A (641 aa)
	SYVN1	synovial apoptosis inhibitor 1, synoviolin; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons f [...] (617 aa)
	DNAJA1	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria (397 aa)
	PSAP	prosaposin (524 aa)
	UBE2G1	ubiquitin-conjugating enzyme E2G 1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 48’-, as well as ’Lys-63’-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4 (170 aa)
	GRIP1	glutamate receptor interacting protein 1; May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons (1076 aa)
	SAG	S-antigen; retina and pineal gland (arrestin); Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated- phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase (405 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
CCT2	DNAJA1	ENSP00000299300	ENSP00000369127	chaperonin 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	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	0.570
CCT2	DNAJB1	ENSP00000299300	ENSP00000254322	chaperonin 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	DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP	0.578
CCT2	GPR37	ENSP00000299300	ENSP00000306449	chaperonin 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	G protein-coupled receptor 37 (endothelin receptor type B-like); Orphan receptor. May have a unique functional role in the central nervous system	0.450
CCT2	HSPA1A	ENSP00000299300	ENSP00000364802	chaperonin 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	heat shock 70kDa protein 1A	0.757
CCT2	HSPA4	ENSP00000299300	ENSP00000302961	chaperonin 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	heat shock 70kDa protein 4	0.772
CCT2	HSPA8	ENSP00000299300	ENSP00000227378	chaperonin 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	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	0.789
CCT2	PACRG	ENSP00000299300	ENSP00000337946	chaperonin 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	PARK2 co-regulated; Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited. May play an important role in the formation of Lewy bodies and protection of dopaminergic neurons against Parkinson disease	0.450
CCT2	PARK2	ENSP00000299300	ENSP00000355865	chaperonin 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	parkinson protein 2, E3 ubiquitin protein ligase (parkin)	0.450
CCT2	TCP1	ENSP00000299300	ENSP00000317334	chaperonin 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	t-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	0.999
DNAJA1	CCT2	ENSP00000369127	ENSP00000299300	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	chaperonin 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	0.570
DNAJA1	DNAJB1	ENSP00000369127	ENSP00000254322	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP	0.773
DNAJA1	GPR37	ENSP00000369127	ENSP00000306449	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	G protein-coupled receptor 37 (endothelin receptor type B-like); Orphan receptor. May have a unique functional role in the central nervous system	0.765
DNAJA1	HSPA1A	ENSP00000369127	ENSP00000364802	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	heat shock 70kDa protein 1A	0.954
DNAJA1	HSPA4	ENSP00000369127	ENSP00000302961	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	heat shock 70kDa protein 4	0.933
DNAJA1	HSPA8	ENSP00000369127	ENSP00000227378	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	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	0.999
DNAJA1	PACRG	ENSP00000369127	ENSP00000337946	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	PARK2 co-regulated; Suppresses cell death induced by accumulation of unfolded Pael receptor (Pael-R, a substrate of Parkin). Facilitates the formation of inclusions consisting of Pael-R, molecular chaperones, protein degradation molecules and itself when proteasome is inhibited. May play an important role in the formation of Lewy bodies and protection of dopaminergic neurons against Parkinson disease	0.461
DNAJA1	PARK2	ENSP00000369127	ENSP00000355865	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	parkinson protein 2, E3 ubiquitin protein ligase (parkin)	0.902
DNAJA1	PSAP	ENSP00000369127	ENSP00000378394	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	prosaposin	0.649
DNAJA1	STUB1	ENSP00000369127	ENSP00000219548	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates- ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 th [...]	0.528
DNAJA1	TCP1	ENSP00000369127	ENSP00000317334	DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria	t-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	0.650

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