BAG family molecular chaperone regulator 1 isoform 1L [Mus musculus]
Protein Classification
Ubl_BAG1 and BAG domain-containing protein( domain architecture ID 10110639)
Ubl_BAG1 and BAG domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Ubl_BAG1 | cd01812 | ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ... |
154-231 | 4.86e-34 | ||
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain. : Pssm-ID: 340510 [Multi-domain] Cd Length: 77 Bit Score: 120.46 E-value: 4.86e-34
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| BAG | smart00264 | BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ... |
269-336 | 5.26e-10 | ||
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains : Pssm-ID: 214591 Cd Length: 79 Bit Score: 55.39 E-value: 5.26e-10
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| Name | Accession | Description | Interval | E-value | ||
| Ubl_BAG1 | cd01812 | ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ... |
154-231 | 4.86e-34 | ||
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain. Pssm-ID: 340510 [Multi-domain] Cd Length: 77 Bit Score: 120.46 E-value: 4.86e-34
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| BAG | smart00264 | BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ... |
269-336 | 5.26e-10 | ||
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains Pssm-ID: 214591 Cd Length: 79 Bit Score: 55.39 E-value: 5.26e-10
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| UBQ | smart00213 | Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
157-230 | 2.84e-08 | ||
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 50.34 E-value: 2.84e-08
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| ubiquitin | pfam00240 | Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
167-232 | 2.44e-05 | ||
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites. Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 41.77 E-value: 2.44e-05
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| BAG | pfam02179 | BAG domain; Domain present in Hsp70 regulators. |
264-333 | 1.28e-03 | ||
BAG domain; Domain present in Hsp70 regulators. Pssm-ID: 460475 [Multi-domain] Cd Length: 77 Bit Score: 37.21 E-value: 1.28e-03
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| Name | Accession | Description | Interval | E-value | ||
| Ubl_BAG1 | cd01812 | ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ... |
154-231 | 4.86e-34 | ||
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain. Pssm-ID: 340510 [Multi-domain] Cd Length: 77 Bit Score: 120.46 E-value: 4.86e-34
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| BAG | smart00264 | BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated ... |
269-336 | 5.26e-10 | ||
BAG domains, present in regulator of Hsp70 proteins; BAG domains, present in Bcl-2-associated athanogene 1 and silencer of death domains Pssm-ID: 214591 Cd Length: 79 Bit Score: 55.39 E-value: 5.26e-10
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| Ubl_ubiquitin_like | cd17039 | ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
157-228 | 6.84e-10 | ||
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation. Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 54.52 E-value: 6.84e-10
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| UBQ | smart00213 | Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
157-230 | 2.84e-08 | ||
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 50.34 E-value: 2.84e-08
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| Ubl_USP14_like | cd16104 | ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ... |
154-229 | 1.71e-07 | ||
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain. Pssm-ID: 340521 Cd Length: 75 Bit Score: 48.00 E-value: 1.71e-07
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| Ubl_UBFD1 | cd17047 | ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ... |
154-229 | 3.59e-07 | ||
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator. Pssm-ID: 340567 Cd Length: 70 Bit Score: 46.85 E-value: 3.59e-07
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| Ubl_UBLCP1 | cd01813 | ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ... |
154-229 | 1.08e-05 | ||
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism. Pssm-ID: 340511 Cd Length: 74 Bit Score: 42.94 E-value: 1.08e-05
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| ubiquitin | pfam00240 | Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
167-232 | 2.44e-05 | ||
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites. Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 41.77 E-value: 2.44e-05
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| Ubl_Dsk2p_like | cd16106 | ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ... |
180-228 | 1.91e-04 | ||
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes. Pssm-ID: 340523 [Multi-domain] Cd Length: 73 Bit Score: 39.54 E-value: 1.91e-04
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| Ubl_AtBAG1_like | cd17054 | ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, ... |
156-228 | 9.01e-04 | ||
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana Bcl-2-associated athanogenes AtBAG1, AtBAG2, AtBAG3, AtBAG4, and similar proteins; The family includes four Arabidopsis BAG family proteins (AtBAG1, AtBAG2, AtBAG3, AtBAG4) that have very similar domain organizations with a ubiquitin-like (Ubl) domain in the N-terminus and a BAG domain in the C-terminus. They may function as co-chaperones that regulate diverse cellular pathways, such as programmed cell death and stress responses. AtBAG1, AtBAG3, and AtBAG4 are predicted to localize in the cytoplasm, but the localization of AtBAG2 is the microbody. AtBAG4 can interact with Hsc70. The overexpression of AtBAG4 in tobacco plants confers tolerance to a wide range of abiotic stresses such as UV light, cold, oxidants, and salt treatments. Pssm-ID: 340574 Cd Length: 70 Bit Score: 37.40 E-value: 9.01e-04
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| BAG | pfam02179 | BAG domain; Domain present in Hsp70 regulators. |
264-333 | 1.28e-03 | ||
BAG domain; Domain present in Hsp70 regulators. Pssm-ID: 460475 [Multi-domain] Cd Length: 77 Bit Score: 37.21 E-value: 1.28e-03
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| Ubl2_FAT10 | cd17053 | ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ... |
162-228 | 1.34e-03 | ||
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain. Pssm-ID: 340573 Cd Length: 71 Bit Score: 36.94 E-value: 1.34e-03
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| Ubl_Ddi1_like | cd01796 | ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ... |
158-228 | 2.33e-03 | ||
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes. Pssm-ID: 340494 [Multi-domain] Cd Length: 73 Bit Score: 36.38 E-value: 2.33e-03
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