Q9UL15 · BAG5_HUMAN
- ProteinBAG family molecular chaperone regulator 5
- GeneBAG5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids447 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Co-chaperone for HSP/HSP70 proteins. It functions as a nucleotide-exchange factor promoting the release of ADP from HSP70, thereby activating HSP70-mediated protein refolding (PubMed:20223214).
Has an essential role in maintaining proteostasis at junctional membrane complexes (JMC), where it may function as a scaffold between the HSPA8 chaperone and JMC proteins enabling correct, HSPA8-dependent JMC protein folding (By similarity).
Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity).
Has an essential role in maintaining proteostasis at junctional membrane complexes (JMC), where it may function as a scaffold between the HSPA8 chaperone and JMC proteins enabling correct, HSPA8-dependent JMC protein folding (By similarity).
Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBAG family molecular chaperone regulator 5
- Short namesBAG-5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UL15
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Cardiomyopathy, dilated, 2F (CMD2F)
- Note
- DescriptionA form of dilated cardiomyopathy, a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. CMD2F is an autosomal recessive, early-onset form.
- See alsoMIM:619747
Natural variants in CMD2F
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086932 | 197-447 | missing | in CMD2F | |
VAR_086933 | 390-447 | missing | in CMD2F; loss of interaction with HSPA8 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_058712 | 157 | in dbSNP:rs17854644 | |||
Sequence: C → W | ||||||
Natural variant | VAR_086932 | 197-447 | in CMD2F | |||
Sequence: Missing | ||||||
Natural variant | VAR_086933 | 390-447 | in CMD2F; loss of interaction with HSPA8 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 510 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000088872 | 1-447 | BAG family molecular chaperone regulator 5 | |||
Sequence: MDMGNQHPSISRLQEIQKEVKSVEQQVIGFSGLSDDKNYKKLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNANHPHRIEIQNIFEEAQSLVREKIVPFYNGGNCVTDEFEEGIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCMKKQPSLPLSEDAHPSVAKINFVMCEVNKARGVLIALLMGVNNNETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADTTKAFDLRQNHSILKIEKVLKRMREIKNELLQAQNPSELYLSSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYIDLKEALEKRKLFACEEHPSHKAVWNVLGNLSEIQGEVLSFDGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVRLAQNILSYLDLKSDEWEY |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the heart.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds to the ATPase domain of HSP/HSP70 chaperones. Binds PRKN. Interacts with HSPA8 and JPH2 (PubMed:35044787).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UL15 | BANP Q8N9N5 | 3 | EBI-356517, EBI-744695 | |
BINARY | Q9UL15 | CDCA7L Q96GN5 | 3 | EBI-356517, EBI-5278764 | |
BINARY | Q9UL15 | DES P17661 | 3 | EBI-356517, EBI-1055572 | |
BINARY | Q9UL15 | EFEMP1 Q12805 | 3 | EBI-356517, EBI-536772 | |
BINARY | Q9UL15 | FAM118B Q9BPY3 | 3 | EBI-356517, EBI-726822 | |
BINARY | Q9UL15 | GOLGA6A Q9NYA3 | 3 | EBI-356517, EBI-11163335 | |
BINARY | Q9UL15 | HSPA1B P08107 | 6 | EBI-356517, EBI-629985 | |
BINARY | Q9UL15 | KASH5 Q8N6L0 | 6 | EBI-356517, EBI-749265 | |
BINARY | Q9UL15 | KRTAP5-4 Q6L8H1 | 3 | EBI-356517, EBI-11963072 | |
BINARY | Q9UL15 | LCE2C Q5TA81 | 3 | EBI-356517, EBI-11973993 | |
BINARY | Q9UL15 | LRRK1 Q38SD2 | 3 | EBI-356517, EBI-1050422 | |
BINARY | Q9UL15 | LRRK2 Q5S007 | 12 | EBI-356517, EBI-5323863 | |
BINARY | Q9UL15 | MAD1L1 Q9Y6D9 | 9 | EBI-356517, EBI-742610 | |
BINARY | Q9UL15 | Q53FC7 | 2 | EBI-356517, EBI-9356749 | |
BINARY | Q9UL15 | THAP1 Q9NVV9 | 7 | EBI-356517, EBI-741515 | |
BINARY | Q9UL15 | TOM1 O60784-2 | 3 | EBI-356517, EBI-12117154 | |
BINARY | Q9UL15 | TRIM27 P14373 | 6 | EBI-356517, EBI-719493 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-86 | BAG 1 | ||||
Sequence: SISRLQEIQKEVKSVEQQVIGFSGLSDDKNYKKLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNA | ||||||
Domain | 95-167 | BAG 2 | ||||
Sequence: QNIFEEAQSLVREKIVPFYNGGNCVTDEFEEGIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCM | ||||||
Domain | 182-260 | BAG 3 | ||||
Sequence: SVAKINFVMCEVNKARGVLIALLMGVNNNETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEE | ||||||
Domain | 275-350 | BAG 4 | ||||
Sequence: SILKIEKVLKRMREIKNELLQAQNPSELYLSSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYIDLKE | ||||||
Domain | 365-442 | BAG 5 | ||||
Sequence: SHKAVWNVLGNLSEIQGEVLSFDGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVRLAQNILSYLDLKS |
Domain
The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9UL15-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length447
- Mass (Da)51,200
- Last updated2000-05-01 v1
- Checksum0D3F7EA6B612C1F5
Q9UL15-2
- Name2
- Differences from canonical
- 1-1: M → MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACETEHNKSM
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037996 | 1 | in isoform 2 | |||
Sequence: M → MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACETEHNKSM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF095195 EMBL· GenBank· DDBJ | AAD16124.2 EMBL· GenBank· DDBJ | mRNA | ||
AB020680 EMBL· GenBank· DDBJ | BAA74896.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL139300 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC044216 EMBL· GenBank· DDBJ | AAH44216.2 EMBL· GenBank· DDBJ | mRNA | ||
BC050551 EMBL· GenBank· DDBJ | AAH50551.1 EMBL· GenBank· DDBJ | mRNA |