General information | DisProt: | DP00617 | Name: | 26S proteasome complex subunit DSS1 | Synonym(s): | DSS1_HUMAN
DSS1
Deleted in split hand/split foot protein 1
Split hand/foot malformation type 1 protein
Split hand/foot deleted protein 1
Brh2-interacting protein Dss1
| First appeared in release: | Release 5.3 (09/21/2010) | UniProt: | P60896 | UniGene: | | SwissProt: | DSS1_HUMAN | TrEMBL: | | NCBI (GI): | | Source organism: | Homo Sapiens (Human) | Sequence length: | 70 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MSEKKQPVDL GLLEEDDEFE EFPAEDWAGL DEDEDAHVWE DNWDDDNVED DFSNQLRAEL - 60 EKHGYKMETS
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Functional narrative |
Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Interacts with the C-terminal of BRCA2.
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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 - Extended | Name: | N-terminal domain | Location: | 1 - 25 | Length: | 25 | Region sequence: |
MSEKKQPVDLGLLEEDDEFEEFPAE | Modification type: | Complex
Native
| PDB: | 1MIU:B, 1IYJ:A, 1MJE:B | Structural/functional type: | Function arises from the disordered state | Functional classes: | Chaperones
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (277 K; pH: 8; CaCL2; DTT; NaCl; PEG 4000; Tris-HCl)
| References:
There are no documents referencing this region. | Comments:Region 1 contains a BRCA2 binding site (aa 7-25); these residues are highly conserved (Yang 2002)
Main reference: Yang H et al (2002) PMID 12228710.
The PDB structures from Yang et al. (2002) show DSS1 in complex with BRCA2 (1IJY and 1MIU), and a complex of DSS1-BRCA2-ssDNA (1MJE).
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Region 2 | Type: | Disordered - Extended | Name: | | Location: | 26 - 36 | Length: | 11 | Region sequence: |
DWAGLDEDEDA | Modification type: | Complex
Native
| PDB: | 1IYJ:A, 1MIU:B, 1MJE:B | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; pH: 8; CaCL2; DTT; NaCl; PEG 4000; Tris-HCl)
| References:
There are no documents referencing this region. | Comments:Main reference: Yang H et al (2002) PMID 12228710.
The PDB structures from Yang et al. (2002) show DSS1 in complex with BRCA2 (1IJY and 1MIU), and a complex of DSS1-BRCA2-ssDNA (1MJE).
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Region 3 | Type: | Disordered - Extended | Name: | C-terminal domain | Location: | 37 - 70 | Length: | 34 | Region sequence: |
HVWEDNWDDDNVEDDFSNQLRAELEKHGYKMETS | Modification type: | Complex
Native
| PDB: | 1IYJ:A, 1MIU:B, 1MJE:B | Structural/functional type: | Function arises from the disordered state | Functional classes: | Chaperones
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (277 K; pH: 8; CaCL2; DTT; NaCl; PEG 4000; Tris-HCl)
| References:
There are no documents referencing this region. | Comments:Main reference: Yang H et al (2002) PMID 12228710.
The PDB structures from Yang et al. (2002) show DSS1 in complex with BRCA2 (1IJY and 1MIU), and a complex of DSS1-BRCA2-ssDNA (1MJE).
Region 3 contains a BRCA2 binding site (aa 37-63); these residues are highly conserved (Yang 2002)
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Comments |
Main reference: Yang H et al (2002) PMID 12228710.
The PDB structures from Yang et al. (2002) show DSS1 in complex with BRCA2 (1IJY and 1MIU), and a complex of DSS1-BRCA2-ssDNA (1MJE).
Sent for AV 9-15-2010 (PMID 12228710)
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