| General information | | DisProt: | DP00546 | | Name: | Huntingtin-interacting protein K [Isoform 1] | | Synonym(s): | HYPK_HUMAN
Huntingtin yeast partner K
HYPK
| | First appeared in release: | Release 4.0 (06/23/2008) | | UniProt: | Q9NX55-1 | | UniGene: | Hs.631692 | | SwissProt: | HYPK_HUMAN | | TrEMBL: | | | NCBI (GI): | 74719419 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 175 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MTGFLLPPAS RASRTGAERR CGPGPAPPPP RAEAVSVAGS RREVGLMRRR GEIDMATEGD - 60
VELELETETS GPERPPEKPR KHDSGAADLE RVTDYAEEKE IQSSNLETAM SVIGDRRSRE - 120
QKAKQEREKE LAKVTIKKED LELIMTEMEI SRAAAERSLR EHMGNVVEAL IALTN
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| Functional narrative |
HYPK is a Huntingtin interacting protein with no known functional characterization. However, the N-terminus region is believed to belong to the intrinsically unstructured family of proteins.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Pre-Molten Globule | | Name: | | | Location: | 1 - 175 | | Length: | 175 | | Region sequence: |
MTGFLLPPASRASRTGAERRCGPGPAPPPPRAEAVSVAGSRREVGLMRRRGEIDMATEGD
VELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSRE
QKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the pre-molten globule state
| | Functional classes: | | | Functional subclasses: | | Detection methods:
- Sensitivity to proteolysis
- Size exclusion/gel filtration chromatography
- Circular dichroism (CD) spectroscopy, far-UV
| References:
- Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. "Huntingtin interacting protein HYPK is intrinsically unstructured." Proteins. 2008; 71(4): 1686-98. PubMed: 18076027
| Comments:
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| References |
- Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. "Huntingtin interacting protein HYPK is intrinsically unstructured." Proteins. 2008; 71(4): 1686-98. PubMed: 18076027
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