| General information | | DisProt: | DP00384 | | Name: | High mobility group protein B1 | | Synonym(s): | HMGB1_MOUSE
High mobility group protein 1
HMG-1
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P63158 | | UniGene: | Mm.207047 | | SwissProt: | HMGB1_MOUSE | | TrEMBL: | | | NCBI (GI): | 52783747 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 215 | | Percent disordered: | 28% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF - 60
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL - 120
SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK - 180
SKKKKEEEDD EEDEEDEEEE EEEEDEDEEE DDDDE
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| Functional narrative |
Binds preferentially single-stranded DNA and unwinds double stranded DNA. Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells.
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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 | | Name: | | | Location: | 2 - 4 | | Length: | 3 | | Region sequence: |
GKG | | Modification type: | Native
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR) (293 K; DTT 10 mM; NaCl 150 mM; Phosphate buffer (pH 5.0) 10 mM)
| References:
- Knapp S, Muller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. "The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes." Biochemistry. 2004; 43(38): 11992-7. PubMed: 15379539
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 82 - 90 | | Length: | 9 | | Region sequence: |
KGETKKKFK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR) (293 K; DTT 10 mM; NaCl 150 mM; Phosphate buffer (pH 5.0) 10 mM)
| References:
- Knapp S, Muller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. "The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes." Biochemistry. 2004; 43(38): 11992-7. PubMed: 15379539
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 167 - 185 | | Length: | 19 | | Region sequence: |
KPDAAKKGVVKAEKSKKKK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR) (293 K; DTT 10 mM; NaCl 150 mM; Phosphate buffer (pH 5.0) 10 mM)
| References:
- Knapp S, Muller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. "The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes." Biochemistry. 2004; 43(38): 11992-7. PubMed: 15379539
| Comments:
|
| Region 4 | | Type: | Disordered | | Name: | acidic tail | | Location: | 186 - 215 | | Length: | 30 | | Region sequence: |
EEEDDEEDEEDEEEEEEEEDEDEEEDDDDE | | Modification type: | Native
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR) (293 K; DTT 10 mM; NaCl 150 mM; Phosphate buffer (pH 5.0) 10 mM)
| References:
- Knapp S, Muller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. "The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes." Biochemistry. 2004; 43(38): 11992-7. PubMed: 15379539
| Comments:
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| Comments |
Additional UniGene ID: Mm.313345
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