| General information | | DisProt: | DP00459 | | Name: | Rho GTPase-activating protein 1 | | Synonym(s): | RHG01_HUMAN
Rho-type GTPase-activating protein 1
Rho-related small GTPase protein activator
GTPase-activating protein rhoOGAP
p50-RhoGAP
CDC42 GTPase-activating protein
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | Q07960 | | UniGene: | Hs.138860 | | SwissProt: | RHG01_HUMAN | | TrEMBL: | | | NCBI (GI): | 3024550 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 439 | | Percent disordered: | 8% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPELVTHLKW - 60
DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY - 120
TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF - 180
KFGQKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ - 240
QFGVSLQHLQ EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG - 300
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV PATLQVLQTL - 360
PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT - 420
KFLLDHQGEL FPSPDPSGL
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| Functional narrative |
GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.
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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: | 198 - 231 | | Length: | 34 | | Region sequence: |
HVKLEQLGIPRQVLKYDDFLKSTQKSPATAPKPM | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; PEG 8K (3%); sodium cacodylate (pH 6.7) 170 mM; zinc acetate 30 mM)
- X-ray crystallography (291 K; HEPES (pH 7.5) 0.1 M; MPD 5 %; PEG 6K (10%))
| References:
- Barrett T, Xiao B, Dodson EJ, Dodson G, Ludbrook SB, Nurmahomed K, Gamblin SJ, Musacchio A, Smerdon SJ, Eccleston JF. "The structure of the GTPase-activating domain from p50rhoGAP." Nature. 1997; 385(6615): 458-61. PubMed: 9009196
| Comments:Residues 1-34 of the fragment correspond to residues 198-231 of the full-length protein.
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| References |
- Lancaster CA, Taylor-Harris PM, Self AJ, Brill S, van Erp HE, Hall A. "Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases." J Biol Chem. 1994; 269(2): 1137-42. PubMed: 8288572
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| Comments |
In the experiment, the crystal structure of a 242-residue C-terminal fragment of p50-rhoGAP was determined. Residues 1-242 of the fragment correspond to residues 198-439 of the full length protein.
According to the paper, there are 8 residues missing from the F-G loop. These residues were not specified.
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