Summary: RhoGAP domain
This is the Wikipedia entry entitled "RhoGAP domain". More...
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RhoGAP domain Edit Wikipedia article
Structure of Phospholipase A2.
Human proteins containing this domain
ABR; ARHGAP1; ARHGAP10; ARHGAP11A; ARHGAP11B; ARHGAP12; ARHGAP15; ARHGAP17; ARHGAP18; ARHGAP19; ARHGAP20; ARHGAP21; ARHGAP22; ARHGAP23; ARHGAP24; ARHGAP25; ARHGAP26; ARHGAP27; ARHGAP28; ARHGAP29; ARHGAP30; ARHGAP4; ARHGAP5; ARHGAP6; ARHGAP8; ARHGAP9; BCR; BPGAP1; C1[disambiguation needed]; C5orf5; CDGAP; CENTD1; CENTD2; CENTD3; CHN1; CHN2; DEPDC1; DEPDC1A; DEPDC1B; DLC1; FAM13A1; FKSG42; GMIP; GRLF1; HMHA1; INPP5B; KIAA1688; LOC553158; MYO9A; MYO9B; OCRL; OPHN1; PIK3R1; PIK3R2; PRR5; RACGAP1; RACGAP1P; RALBP1; RICH2; RICS; SH3BP1; SLIT1; SNX26; SRGAP1; SRGAP2; SRGAP3; STARD13; STARD8; SYDE1; SYDE2;
- Musacchio, A.; Cantley, L. C.; Harrison, S. C. (1996). "Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit". Proceedings of the National Academy of Sciences of the United States of America 93 (25): 14373–14378. PMC 26139. PMID 8962058.
- Barrett, T.; Xiao, B.; Dodson, E. J.; Dodson, G.; Ludbrook, S. B.; Nurmahomed, K.; Gamblin, S. J.; Musacchio, A.; Smerdon, S. J.; Eccleston, J. F. (1997). "The structure of the GTPase-activating domain from p50rhoGAP". Nature 385 (6615): 458–461. doi:10.1038/385458a0. PMID 9009196.
- Gamblin, S. J.; Rittinger, K.; Walker, P. A.; Eccleston, J. F.; Nurmahomed, K.; Owen, D.; Laue, E.; Smerdon, S. J. (1997). "Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP". Nature 388 (6643): 693–697. doi:10.1038/41805. PMID 9262406.
- Boguski, M. S.; McCormick, F. (1993). "Proteins regulating Ras and its relatives". Nature 366 (6456): 643–654. doi:10.1038/366643a0. PMID 8259209.
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RhoGAP domain Provide feedback
GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
Musacchio A, Cantley LC, Harrison SC; , Proc Natl Acad Sci U S A 1996;93:14373-14378.: Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. PUBMED:8962058 EPMC:8962058
Barrett T, Xiao B, Dodson EJ, Dodson G, Ludbrook SB, Nurmahomed K, Gamblin SJ, Musacchio A, Smerdon SJ, Eccleston JF; , Nature 1997;385:458-461.: The structure of the GTPase-activating domain from p50rhoGAP. PUBMED:9009196 EPMC:9009196
Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ; , Nature 1997;388:693-697.: Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. PUBMED:9262406 EPMC:9262406
Internal database links
|Similarity to PfamA using HHSearch:||DUF1708|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000198Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins. This entry is a Rho/Rac/Cdc42-like GAP domain, that is found in a wide variety of large, multi-functional proteins [PUBMED:9009196]. A number of structure are known for this family [PUBMED:9009196, PUBMED:8962058, PUBMED:9262406]. The domain is composed of seven alpha helices. This domain is also known as the breakpoint cluster region-homology (BH) domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||intracellular (GO:0005622)|
|Biological process||signal transduction (GO:0007165)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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Superfamily contains BCR-homology GTPase activation domain (BH-domain) and p120GAP domain-like, including the GAP related domain of neurofibromin, families.
The clan contains the following 3 members:DUF1708 RasGAP RhoGAP
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
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Curation and family details
|Author:||Ponting C, Schultz J, Bork P|
|Number in seed:||87|
|Number in full:||7538|
|Average length of the domain:||147.00 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||17.80 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||22|
|Download:||download the raw HMM for this family|
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The tree shows the occurrence of this domain across different species. More...
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the RhoGAP domain has been found. There are 36 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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