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STRINGSTRING
CTSB CTSB TIPRL TIPRL TUBB8 TUBB8 CCT6B CCT6B HSPA5 HSPA5 IGBP1 IGBP1 DNAJA2 DNAJA2 HSP90AB1 HSP90AB1 UBL4A UBL4A TCP1 TCP1 CCT2 CCT2 HSPD1 HSPD1 UBA1 UBA1 PFDN2 PFDN2 UBC UBC HSP90AA1 HSP90AA1 TUBB6 TUBB6 PFDN5 PFDN5 RUVBL1 RUVBL1 SMC3 SMC3 PFDN4 PFDN4 ELAVL1 ELAVL1 METTL21B METTL21B BAG2 BAG2 NTPCR NTPCR KIAA1967 KIAA1967
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:
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)
METTL21Bmethyltransferase like 21B; Protein-lysine methyltransferase (By similarity) (226 aa)
KIAA1967KIAA1967 (923 aa)
DNAJA2DnaJ (Hsp40) homolog, subfamily A, member 2; Co-chaperone of Hsc70 (412 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)
RUVBL1RuvB-like 1 (E. coli); May be able to bind plasminogen at cell surface and enhance plasminogen activation (456 aa)
TUBB6tubulin, beta 6 class V; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity) (446 aa)
HSPA5heat 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)
HSP90AB1heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (724 aa)
CCT6Bchaperonin containing TCP1, subunit 6B (zeta 2); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity) (530 aa)
TUBB8tubulin, beta 8 class VIII; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity) (444 aa)
PFDN5prefoldin subunit 5; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC (154 aa)
HSP90AA1heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (854 aa)
UBA1ubiquitin-like modifier activating enzyme 1; Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP (1058 aa)
HSPD1heat shock 60kDa protein 1 (chaperonin); Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (573 aa)
CTSBcathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis (339 aa)
UBCubiquitin C (685 aa)
IGBP1immunoglobulin (CD79A) binding protein 1; Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of PP2A, PP4 and PP6 phosphatases catalytic subunits by protecting them from degradative polyubiquitination until they associate with regulatory subunits (339 aa)
SMC3structural maintenance of chromosomes 3; Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement (1217 aa)
NTPCRnucleoside-triphosphatase, cancer-related; Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency (190 aa)
TIPRLTIP41, TOR signaling pathway regulator-like (S. cerevisiae); May be a allosteric regulator of serine/threonine- protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C)-TIPRL complex does not show phosphatase activity. May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair (272 aa)
PFDN2prefoldin subunit 2; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (154 aa)
UBL4Aubiquitin-like 4A; Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40- it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting (157 aa)
BAG2BCL2-associated athanogene 2; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (211 aa)
PFDN4prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (134 aa)
ELAVL1ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R); Involved in 3’-UTR ARE-mediated MYC stabilization. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, HUR binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA and AUUUUUA motifs. Binds preferentially to the 5’-UUUU[AG]UUU-3’ motif in vitro (326 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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