General information | DisProt: | DP00167 | Name: | Ras-related protein Rap-2a | Synonym(s): | RAP2A_HUMAN
RbBP-30
RAP2A
| First appeared in release: | Release 2.1 (03/14/2005) | UniProt: | P10114 | UniGene: | Hs.508480 | SwissProt: | RAP2A_HUMAN | TrEMBL: | | NCBI (GI): | 131852 | Source organism: | Homo sapiens (Human) | Sequence length: | 183 | Percent disordered: | 13% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG - 60 TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL - 120 ESEREVSSSE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC - 180 NIQ
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Functional narrative |
Rap2A is a member the small GTPase super family and the Ras family. Rap2A is involved with multiple signal transduction cascades that regulate cell growth and differentiation. Rap2A cycles between the binding partners GDP and GTP with the assistance of guanine nucleotide exchange factors and GTPase activating proteins. Switches I and II in this protein undergo conformational changes depending upon the partner bound. L3, a loop located between two beta sheets is consistently disordered and functions as a linker or hinge region to assist in binding and overall flexibility of this protein.
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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: | Switch I | Location: | 32 - 36 | Length: | 5 | Region sequence: |
YDPTI | Modification type: | Complex
Fragment
| PDB: | 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
Molecular recognition effectors
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (pH: 7.5; protein (per mL) 10 mg; PEG 4000 19 %; magnesium chloride 100 mM; Tris 100 mM)
| References:
- Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I. "Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS." EMBO J. 1997; 16(18): 5582-91. PubMed: 9312017
| Comments:
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Region 2 | Type: | Disordered - Extended | Name: | L3 Loop | Location: | 45 - 55 | Length: | 11 | Region sequence: |
EVDSSPSVLEI | Modification type: | Complex
Fragment
Native
| PDB: | 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S | Structural/functional type: | Function arises from the disordered state | Functional classes: | Entropic chain
| Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (pH: 8; LiSO4 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)
- X-ray crystallography (pH: 8; MgCl2 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)
| References:
- Menetrey J, Cherfils J. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Proteins. 1999; 37(3): 465-473. PubMed: 10591105
| Comments:
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Region 3 | Type: | Disordered - Extended | Name: | Switch II | Location: | 60 - 63 | Length: | 4 | Region sequence: |
GTEQ | Modification type: | Complex
Fragment
| PDB: | 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (pH: 7.5; magnesium chloride 100 mM; PEG 4000 19 %; protein (per mL) 10 mg; Tris 100 mM)
| References:
- Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I. "Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS." EMBO J. 1997; 16(18): 5582-91. PubMed: 9312017
| Comments:
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Region 4 | Type: | Disordered - Extended | Name: | Switch II | Location: | 62 - 63 | Length: | 2 | Region sequence: |
EQ | Modification type: | Complex
Fragment
Native
| PDB: | 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (pH: 8; LiSO4 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)
- X-ray crystallography (pH: 8; MgCl2 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)
| References:
- Menetrey J, Cherfils J. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Proteins. 1999; 37(3): 465-473. PubMed: 10591105
| Comments:
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Region 5 | Type: | Disordered - Extended | Name: | Switch II | Location: | 62 - 66 | Length: | 5 | Region sequence: |
EQFAS | Modification type: | Complex
Fragment
Native
| PDB: | 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (pH: 8; LiSO4 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)
- X-ray crystallography (pH: 8; MgCl2 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)
| References:
- Menetrey J, Cherfils J. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Proteins. 1999; 37(3): 465-473. PubMed: 10591105
| Comments:
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