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Conserved domains on  [gi|27229055|ref|NP_080594|]
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huntingtin-interacting protein K [Mus musculus]

Protein Classification

huntingtin-interacting protein K( domain architecture ID 16075013)

huntingtin-interacting protein K (HYPK) is an intrinsically unstructured Huntingtin (HTT)-interacting protein with chaperone-like activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HYPK_UBA pfam19026
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ...
 88-128 3.91e-14

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: 61.80  E-value: 3.91e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 27229055    88 VTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41
 
Name Accession Description Interval E-value
HYPK_UBA pfam19026
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ...
 88-128 3.91e-14

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: 61.80  E-value: 3.91e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 27229055    88 VTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41
UBA_HYPK cd14361
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ...
 88-128 4.08e-14

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: 61.76  E-value: 4.08e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 27229055  88 VTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:cd14361   1 VKVKKEDVELIVNELEVSKAQAERALREHNGDVVKALRALI 41
 
Name Accession Description Interval E-value
HYPK_UBA pfam19026
HYPK UBA domain; This entry represents the UBA domain found at the C-terminus of the HYPK ...
 88-128 3.91e-14

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: 61.80  E-value: 3.91e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 27229055    88 VTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:pfam19026   1 VKVKKEDVELIMTELEVSKAKAERALREHGGDVVAALRALL 41
UBA_HYPK cd14361
UBA-like domain found in Huntingtin-interacting protein K (HYPK) and similar proteins; HYPK, ...
 88-128 4.08e-14

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: 61.76  E-value: 4.08e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 27229055  88 VTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:cd14361   1 VKVKKEDVELIVNELEVSKAQAERALREHNGDVVKALRALI 41
UBA_NAC_like cd14278
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and ...
 92-128 1.93e-09

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: 49.40  E-value: 1.93e-09
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 27229055  92 KEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:cd14278   1 EEDIELVMSQTGVSREEAIKALRENKGDVVDAILELT 37
UBA_NAC_euk cd14358
UBA-like domain found in nascent polypeptide-associated complex subunit alpha (NACA) and its ...
 93-128 8.62e-05

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: 37.60  E-value: 8.62e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 27229055  93 EDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:cd14358   2 KDIELVMQQANVSRAKAVKALKENDNDIVNAIMELT 37
UBA_NACAD cd14416
UBA-like domain found in nascent polypeptide-associated complex subunit alpha ...
 90-128 6.97e-03

UBA-like domain found in nascent polypeptide-associated complex subunit alpha domain-containing protein 1 (NACAD); The subfamily includes a group of uncharacterized proteins mainly found in vertebrates. Their biological function remains unknown, but they show high sequence similarity to the nascent polypeptide-associated complex (NAC) subunit alpha (NACA) that exists as part of several protein complexes playing a role in proliferation, apoptosis, or degradation. Like NACA, NACAD contains an NAC domain and a C-terminal ubiquitin-associated (UBA) domain.


Pssm-ID: 270599  Cd Length: 44  Bit Score: 32.74  E-value: 6.97e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 27229055  90 IKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALT 128
Cdd:cd14416   5 LEVRDIELVMAQANVSRAKAVRALRHNNNDIVNAIMELT 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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