uncharacterized protein Dmel_CG9922, isoform B [Drosophila melanogaster]
huntingtin-interacting protein K( domain architecture ID 10198831)
huntingtin-interacting protein K (HYPK) is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity
List of domain hits
Name | Accession | Description | Interval | E-value | ||
UBA_HYPK | cd14361 | UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ... |
82-122 | 3.88e-11 | ||
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K, is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It is involved in regulating cell growth, cell cycle, unfolded protein response, and cell death. All members in this subfamily contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes. : Pssm-ID: 270544 Cd Length: 41 Bit Score: 53.67 E-value: 3.88e-11
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Name | Accession | Description | Interval | E-value | ||
UBA_HYPK | cd14361 | UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ... |
82-122 | 3.88e-11 | ||
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K, is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It is involved in regulating cell growth, cell cycle, unfolded protein response, and cell death. All members in this subfamily contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes. Pssm-ID: 270544 Cd Length: 41 Bit Score: 53.67 E-value: 3.88e-11
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HYPK_UBA | pfam19026 | HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ... |
82-122 | 6.59e-11 | ||
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK protein and its homologs. This domain in HYPK mediates a protein interaction with the Naa15 C-terminus. Pssm-ID: 436907 Cd Length: 41 Bit Score: 53.33 E-value: 6.59e-11
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Name | Accession | Description | Interval | E-value | ||
UBA_HYPK | cd14361 | UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ... |
82-122 | 3.88e-11 | ||
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K, is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It is involved in regulating cell growth, cell cycle, unfolded protein response, and cell death. All members in this subfamily contain an N-terminal ubiquitin-associated (UBA) that shows high sequence similarity with that of eukaryotic nascent polypeptide-associated complex proteins (NAC) which is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes. Pssm-ID: 270544 Cd Length: 41 Bit Score: 53.67 E-value: 3.88e-11
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HYPK_UBA | pfam19026 | HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ... |
82-122 | 6.59e-11 | ||
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK protein and its homologs. This domain in HYPK mediates a protein interaction with the Naa15 C-terminus. Pssm-ID: 436907 Cd Length: 41 Bit Score: 53.33 E-value: 6.59e-11
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UBA_NAC_like | cd14278 | UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and ... |
86-118 | 1.14e-03 | ||
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins; The family contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins found in archaea and bacteria. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. The family also includes huntingtin-interacting protein K (HYPK), also called Huntingtin yeast partner K or Huntingtin yeast two-hybrid protein K. It is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity. It may be involved in regulating cell growth, cell cycle, unfolded protein response and cell death. All members in this family contain an ubiquitin-associated (UBA) domain. Pssm-ID: 270464 [Multi-domain] Cd Length: 37 Bit Score: 34.38 E-value: 1.14e-03
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UBA_NAC_euk | cd14358 | UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and its ... |
87-117 | 7.97e-03 | ||
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and its homologs mainly found in eukaryotes; The subfamily contains nascent polypeptide-associated complex subunit alpha (NACA), putative NACA-like protein (NACP1), nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD), and similar proteins. NACA, also called NAC-alpha or Alpha-NAC, together with BTF3, also called Beta-NAC, form the nascent polypeptide-associated complex (NAC) which is a cytosolic protein chaperone that contacts the nascent polypeptide chains as they emerge from the ribosome. Besides, NACA has a high affinity for nucleic acids and exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. It is a cytokine-modulated specific transcript in the human TF-1 erythroleukemic cell line. It also acts as a transcriptional co-activator in osteoblasts by binding to phosphorylated c-Jun, a member of the activator-protein-1 (AP-1) family. Moreover, NACA binds to and regulates the adaptor protein Fas-associated death domain (FADD). In addition, NACA functions as a novel factor participating in the positive regulation of human erythroid-cell differentiation. The biological function of NACP1 (also called Alpha-NAC pseudogene 1 or NAC-alpha pseudogene 1) and NACAD remain unclear. All family members contain an NAC domain and a C-terminal ubiquitin-associated (UBA) domain. Pssm-ID: 270541 [Multi-domain] Cd Length: 37 Bit Score: 32.21 E-value: 7.97e-03
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