Summary: RhoGAP domain
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This is the Wikipedia entry entitled "RhoGAP domain". More...
RhoGAP domain Edit Wikipedia article
RhoGAP domain | |||||||||||
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Identifiers | |||||||||||
Symbol | RhoGAP | ||||||||||
Pfam | PF00620 | ||||||||||
InterPro | IPR000198 | ||||||||||
SMART | RhoGAP | ||||||||||
SCOP2 | 1rgb / SCOPe / SUPFAM | ||||||||||
OPM protein | 1xa6 | ||||||||||
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RhoGAP domain is an evolutionary conserved protein domain of GTPase activating proteins towards Rho/Rac/Cdc42-like small GTPases.
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; 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; TAGAP;
References
- [1]. Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. Musacchio A, Cantley LC, Harrison SC; Proc Natl Acad Sci U S A 1996;93:14373-14378. PMIDÂ 8962058
- [2]. The structure of the GTPase-activating domain from p50rhoGAP. 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. PMIDÂ 9009196
- [3]. Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ; Nature 1997;388:693-697. PMIDÂ 9262406
- [4]. Proteins regulating Ras and its relatives. Boguski MS, McCormick F; Nature 1993;366:643-654. PMIDÂ 8259209
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
RhoGAP domain Provide feedback
GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
Literature references
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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
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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
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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
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Boguski MS, McCormick F; , Nature 1993;366:643-654.: Proteins regulating Ras and its relatives. PUBMED:8259209 EPMC:8259209
Internal database links
SCOOP: | DNA_pol_phi Msb1-Mug8_dom Nod1 Tra1_central |
Similarity to PfamA using HHSearch: | Msb1-Mug8_dom |
External database links
HOMSTRAD: | RhoGAP |
SCOP: | 1rgb |
SMART: | RhoGAP |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000198
Members 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.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Biological process | signal transduction (GO:0007165) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan GAP (CL0409), which has the following description:
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:
Msb1-Mug8_dom RasGAP RhoGAPAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (83) |
Full (54694) |
Representative proteomes | UniProt (87465) |
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RP15 (7503) |
RP35 (18331) |
RP55 (40878) |
RP75 (55679) |
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HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (83) |
Full (54694) |
Representative proteomes | UniProt (87465) |
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RP15 (7503) |
RP35 (18331) |
RP55 (40878) |
RP75 (55679) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | SMART |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Ponting CP |
Number in seed: | 83 |
Number in full: | 54694 |
Average length of the domain: | 143.2 aa |
Average identity of full alignment: | 27 % |
Average coverage of the sequence by the domain: | 15.7 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 149 | ||||||||||||
Family (HMM) version: | 30 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 78 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.