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There are several matches for 'probable chaperone'.
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7648 matches
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organism
protein
1)
Homo sapiens
C1GALT1C1 - C1GALT1-specific
chaperone
1;
Probable
chaperone
required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.
Probably
acts as a specific molecular
chaperone
assisting the folding/stability of core 1 beta-3- galactosyltransferase (C1GALT1).
[a.k.a. AAQ89005.1, NP_001011551, R-HSA-3781865]
2)
Homo sapiens
HSPB1 - Heat shock protein beta-1; Small heat shock protein which functions as a molecular
chaperone
probably
maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular
chaperone
activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
[a.k.a. R-HSA-162582, CAB004439, B2R4N8]
3)
Homo sapiens
HSPB6 - Heat shock protein beta-6; Small heat shock protein which functions as a molecular
chaperone
probably
maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ
chaperone
-like activity.
[a.k.a. 5LTW, 5OKF, ENSP00000004982]
4)
Homo sapiens
RTP4 - Receptor-transporting protein 4;
Probable
chaperone
protein which facilitates trafficking and functional cell surface expression of some G-protein coupled receptors (GPCRs). Promotes functional expression of the bitter taste receptor TAS2R16. Also promotes functional expression of the opioid receptor heterodimer OPRD1-OPRM1 (By similarity).
[a.k.a. R-HSA-388396, R-HSA-162582, Receptor transporter protein 4]
5)
Homo sapiens
DNAJB4 - DnaJ homolog subfamily B member 4;
Probable
chaperone
. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
[a.k.a. uc001dij.4, Q9UDY4, ENSP00000359799]
6)
Homo sapiens
MKKS - McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin;
Probable
molecular
chaperone
that assists the folding of proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis. Belongs to the TCP-1 chaperonin family.
[a.k.a. NM_170784, EAX10344.1, NM_170784.2]
7)
Homo sapiens
RCN3 - Reticulocalbin-3;
Probable
molecular
chaperone
assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant- associated protein D/SP-D and the lipid transporter ABCA3 (By similarity). By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis (By similarity). Has an anti-fibrotic activity by negatively r [...]
[a.k.a. BC013436, UPI0002A4735D, CCDS12771.1]
8)
Homo sapiens
BBS10 - Bardet-Biedl syndrome 10 protein;
Probable
molecular
chaperone
that assists the folding of proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation. Belongs to the TCP-1 chaperonin family.
[a.k.a. ENSP00000497413, NP_078961, R-HSA-1852241]
9)
Homo sapiens
HSP90AA1 - Heat shock protein HSP 90-alpha; 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 which is essential for its
chaperone
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. Engages with a ra [...]
[a.k.a. R-HSA-1643713, R-HSA-196854, ENSP00000216281]
10)
Homo sapiens
TIMM8B - Mitochondrial import inner membrane translocase subunit Tim8 B;
Probable
mitochondrial intermembrane
chaperone
that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a
chaperone
-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
[a.k.a. HPA041173, DDP2, OMIM:606659]
11)
Homo sapiens
PDILT - Protein disulfide-isomerase-like protein of the testis;
Probable
redox-inactive
chaperone
involved in spermatogenesis; Belongs to the protein disulfide isomerase family.
[a.k.a. NP_777584, 4NWY, XP_011544068.1]
12)
Homo sapiens
DNAJB7 - DnaJ homolog subfamily B member 7;
Probably
acts as a co-
chaperone
.
[a.k.a. AAL40391.1, CCDS14008, CR456468]
13)
Homo sapiens
CNNM4 - Metal transporter CNNM4;
Probable
metal transporter. The interaction with the metal ion
chaperone
COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function.
[a.k.a. AB046812, XM_005263914, ENSG00000158158]
14)
Homo sapiens
NPM2 - Nucleoplasmin-2; Core histones
chaperone
involved in chromatin reprogramming, specially during fertilization and early embryonic development.
Probably
involved in sperm DNA decondensation during fertilization. Belongs to the nucleoplasmin family.
[a.k.a. XM_017012949.2, NPM2-209, XP_016868437]
15)
Homo sapiens
CHORDC1 - Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication,
probably
by inhibiting the kinase activity of ROCK2. Proposed to act as co-
chaperone
for HSP90. May play a role in the regulation of NOD1 via a HSP90
chaperone
complex. In vitro, has intrinsic
chaperone
activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis.
[a.k.a. NM_001144073, ENST00000311547, UPI00004052A7]
16)
Homo sapiens
PPIL2 - RING-type E3 ubiquitin-protein ligase PPIL2; Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'- linked polyubiquitination of proteins could target them for proteasomal degradation. May also function as a
chaperone
, playing a role in transport to the cell membrane of BSG/Basigin for instance.
Probable
inactive PPIase with no peptidyl- prolyl cis-trans isomerase activity. Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.
[a.k.a. R-HSA-202733, XM_005261448.4, XM_017028705]
17)
Homo sapiens
FKBP8 - Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a
chaperone
for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex
probably
interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.
[a.k.a. NM_012181.4, Q53GU3, ENST00000608443]
18)
Homo sapiens
HSP90AB1 - Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...]
[a.k.a. R-HSA-69278, ENSG00000096384, P08238]
19)
Homo sapiens
RSAD1 - Radical S-adenosyl methionine domain-containing protein 1, mitochondrial; May be a heme
chaperone
, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity (
Probable
). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine (By similarity); Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
[a.k.a. CCDS11569, NR_130911, OTTHUMG00000162126]
20)
Homo sapiens
COQ10A - Coenzyme Q-binding protein COQ10 homolog A, mitochondrial; Required for the function of coenzyme Q in the respiratory chain. May serve as a
chaperone
or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (
Probable
); Belongs to the COQ10 family.
[a.k.a. ENST00000433805, ENSP00000446723, HGNC:26515]
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