about
CalreticulinHeat shock protein 1 (chaperonin)Heat shock protein 1 (chaperonin 10)CalnexinHeat shock protein 8Serine (or cysteine) peptidase inhibitor, clade H, member 1CLN3 lysosomal/endosomal transmembrane protein, batteninPeptidylprolyl isomerase BPeptidylprolyl isomerase CCrystallin alpha BST13 Hsp70 interacting proteinDnaJ heat shock protein family (Hsp40) member B5Coiled-coil domain containing 115RuvB like AAA ATPase 2UDP-glucose glycoprotein glucosyltransferase 1Lectin, mannose binding 1Endoplasmic reticulum to nucleus signaling 2Peptidylprolyl isomerase EPeptidylprolyl isomerase FAryl hydrocarbon receptor interacting protein like 1Chaperonin containing TCP1 subunit 2Bardet-Biedl syndrome 12McKusick-Kaufman syndromeGlutaredoxin and cysteine rich domain containing 2Zinc finger FYVE-type containing 21NudC domain containing 3DnaJ (Hsp40) homolog, subfamily A, member 3 variantPutative heat shock protein HSP 90-beta 4Putative heat shock protein HSP 90-beta-3Putative heat shock protein HSP 90-beta 2DnaJ heat shock protein family (Hsp40) member A2Heat shock protein 90 alpha family class A member 1Alpha hemoglobin stabilizing proteinPhosphoinositide kinase, FYVE-type zinc finger containingHeat shock protein family A (Hsp70) member 13T-complex 1Caseinolytic mitochondrial matrix peptidase chaperone subunit XHeat shock protein family A (Hsp70) member 9Calreticulin 3GrpE like 2, mitochondrial
P680
Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequenceNucleolar protein B23 has molecular chaperone activitiesIdentification and characterization of AFG3L2, a novel paraplegin-related geneIsolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteinsMutations in a new photoreceptor-pineal gene on 17p cause Leber congenital amaurosisCharacterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemiaMolecular chaperone properties of serum amyloid P componentEndoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein responseThe importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coliLHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumHLA-B2702 (77-83/83-77) peptide binds to beta-tubulin on human NK cells and blocks their cytotoxic capacityIdentification and characterization of a human mitochondrial homologue of the bacterial co-chaperone GrpECytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycleSerine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicingA new feature on the cholesterol-lowering landscapeAn abundant erythroid protein that stabilizes free alpha-haemoglobinDisassembly of transcriptional regulatory complexes by molecular chaperonesChaperones and folding of MHC class I molecules in the endoplasmic reticulumSpastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloproteaseCharacterisation of a new human and murine member of the DnaJ family of proteinsFunctional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperoneThe p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathwayA novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese familyIsolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10Positional cloning of the gene for X-linked retinitis pigmentosa 2Meckel-Gruber syndrome protein MKS3 is required for endoplasmic reticulum-associated degradation of surfactant protein CMutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIIIPrefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperoninGenomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoterPeptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilinIdentification of the key structural motifs involved in HspB8/HspB6-Bag3 interactionThe chaperone activity of clusterin is dependent on glycosylation and redox environment
P921
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P680
Q22001507-88B45D88-FC2D-4159-B302-55D82E746DAFQ22009438-18C24ABC-010C-4205-A46E-2212A74D7977Q22010227-5EE18E1A-A0B9-4146-8283-3274FB9C9754Q22010678-23873478-B376-4A18-8966-93833870C938Q22010998-CABAB000-E80B-4330-A882-05D201CC7985Q22011147-DB6A47E9-663E-4805-A9FB-79B9CAAD9A00Q22254102-4843DCF9-C03A-4B00-9856-D4ADE3BC2DE8Q22254117-65965A7F-2D7A-4050-B74F-9E97D7A7D12BQ24290435-3845A032-66B8-4BE3-AC7F-615D3095341FQ24290571-0569B727-644D-4DBB-98EC-054E50194400Q24290637-16066F9C-B171-4501-AD7D-741B1874DF9FQ24291143-AC5299E3-077A-46CE-A09B-5B0596586639Q24291628-869FDFE1-1C6C-49F0-929E-E41F580F746AQ24291847-808EFC38-1149-4966-AF63-6D5F95CC587CQ24291946-585AEF8F-82CD-4297-A24E-44D23125BB74Q24299833-91423441-930C-49CF-AF14-C7FB584F8C10Q24300055-A1904643-A8FE-4333-81AB-9CDF8E339FDBQ24303969-5E43593D-E84B-4358-BD13-4AEA45B289AFQ24309083-024767E1-FAE5-4588-AAD4-D1BF8E44F740Q24311879-76CB6C48-B846-4E9C-B047-67A654CB46ABQ24316265-237078C1-5935-4472-AE97-B81798CF4A13Q24317200-504CA973-ADC0-4F83-8E0D-EE650E6F1EC1Q24319909-6AC393E2-445C-4C79-80B4-2E9587523FBBQ24320040-99282979-63E6-4DB2-9017-93625564CF66Q24320121-9FD8B168-EE3F-4DF1-9547-83D24119335EQ24322014-DF57457C-43C3-4F6D-B12D-AEDF6688F569Q24323014-24D74A7C-D2E3-40D9-AB00-C37CF0308D19Q24336195-B3DCBD18-F613-44E3-B607-F08B227D1FCAQ24336409-E44D82AD-E49B-4C4B-922B-0E67DC67FDECQ24336991-D8491792-7442-4CDC-89C1-DD29AAEF3EBDQ24338951-E0DF5ECF-9B41-4998-8CA7-16E6ADCFFE8BQ28115657-C0D8A099-0114-4154-BB90-3120ECAE0142Q85997507-9E734691-D59A-479F-93FE-9E89989E4A71
P921
description
Interacting selectively and non-covalently with an unfolded protein.
@en
moleculaire functie
@nl
name
unfolded protein binding
@en
type
label
unfolded protein binding
@en
altLabel
GO:0051082
@en
prefLabel
unfolded protein binding
@en
P279
P2888
P686
GO:0051082