"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PS50238"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 149345, 'pathways': 0, 'proteins': 148881, 'proteomes': 3622, 'sets': 0, 'structural_models': {'alphafold': 112448, 'bfvd': 0}, 'structures': 66, 'taxa': 10307}"	"{}"	"[{'text': '<p>Small G proteins of the Rho family, which includes Rho, Rac and Cdc42,\nregulate phosphorylation pathways that control a range of biological functions\nincluding cytoskeleton formation and cell proliferation. Rho proteins act as\nmolecular switches, with an active GTP-bound form and an inactive GDP-bound\nform. The inactive GDP bound form is promoted by GTPase-activating proteins\n(GAPs). GAP proteins specific for Rho contain a conserved region of around 200\namino-acid residues, the Rho-GAP domain. This domain can accelerate the GTP\nhydrolysis activity of Rho by five orders of magnitude [[cite:PUB00018225]]. RhoGAP domains are\nusually associated with other signaling modules like SH2,\nSH3 or PH.\n\nLike other GAP domains Rho-GAP is exclusively helical (nine helices) [[cite:PUB00004251]]. The core of the domain forms a four-helix bundle. The most\nconserved residues across the family are located on the bundle face that\ninteracts with the G protein [[cite:PUB00004258]]. Rho-GAP domain like Ras-GAP supplies an\narginine residue in trans into the active site of the G protein which confers\na self-stimulatory GAP activity through homophilic interaction [[cite:PUB00018226]].\n\nSome of the proteins containing a RhoGAP domain are listed below:\n\n - Mammalian  ARAP  1,2 and 3 proteins, a family of GTPase activating proteins\n   that  contains  both  a RhoGAP and a ARFGAP domains. They\n   can  regulate  Rho or ARF G proteins according to their localization in the\n   cell.\n - Vertebrate Beta-chimaerin protein, a GTPase activating protein for the Rho-\n   like GTPase Rac.\n - Mammalian  Nadrin  protein,  a  neuron-specific  GTPase-activating  protein\n   involved in regulated exocytosis.\n - Mammalian unconventional myosin-9b.\n - Mammalian  breakpoint  cluster  region  protein (BCR) and Drosophila Rotund\n   protein, GTPase-activating proteins for Rac and Cdc42.\n - Mammalian Rho-GAP hematopoietic protein C1.\n - Mammalian   Rho-GTPase-activating   protein   6.   It  promotes  continuous\n   elongation  of  cytoplasmic processes during cell motility and simultaneous\n   retraction of the cell body changing the cell morphology.\n - Mammalian   phosphatidylinositol  3-kinase  regulatory  alpha  subunit,  an\n   adapter  subunit  of the phosphatidylinositol  3-kinase  (PI3K).  It  has a\n   critical role in signal transduction pathways originating from a variety of\n   membrane-bound receptors.\n - Mammalian  Inositol polyphosphate 5-phosphatase OCRL-1 (EC 3.1.3.-). It may\n   function  in lysosomal membrane trafficking by regulating the specific pool\n   of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes.\n - Mammalian  type  II  inositol-1,4,5-trisphosphate 5-phosphatase involved in\n   signal-terminating reaction (EC 3.1.3.56.).\n - Yeast LRG1 and SAC7 proteins, the two major Rho GTPase-activating proteins.\n   The SAC7 protein is involved in assembly of actin.\n - Yeast  BEM2 protein, a GTPase activating protein involved in the control of\n   cellular morphogenesis.\n\nThe profile we developed covers the whole domain.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR000198"	False	False	False	"{'PUB00018225': {'PMID': 9631293, 'ISBN': None, 'volume': '8', 'issue': '2', 'year': 1998, 'title': 'GTPase-activating proteins and their complexes.', 'URL': None, 'raw_pages': '195-201', 'medline_journal': 'Curr Opin Struct Biol', 'ISO_journal': 'Curr. Opin. Struct. Biol.', 'authors': ['Gamblin SJ', 'Smerdon SJ.'], 'DOI_URL': 'http://dx.doi.org/10.1016/S0959-440X(98)80038-9'}, 'PUB00004251': {'PMID': 9009196, 'ISBN': None, 'volume': '385', 'issue': '6615', 'year': 1997, 'title': 'The structure of the GTPase-activating domain from p50rhoGAP.', 'URL': None, 'raw_pages': '458-61', 'medline_journal': 'Nature', 'ISO_journal': 'Nature', 'authors': ['Barrett T', 'Xiao B', 'Dodson EJ', 'Dodson G', 'Ludbrook SB', 'Nurmahomed K', 'Gamblin SJ', 'Musacchio A', 'Smerdon SJ', 'Eccleston JF.'], 'DOI_URL': 'http://dx.doi.org/10.1038/385458a0'}, 'PUB00004258': {'PMID': 9262406, 'ISBN': None, 'volume': '388', 'issue': '6643', 'year': 1997, 'title': 'Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP.', 'URL': None, 'raw_pages': '693-7', 'medline_journal': 'Nature', 'ISO_journal': 'Nature', 'authors': ['Rittinger K', 'Walker PA', 'Eccleston JF', 'Nurmahomed K', 'Owen D', 'Laue E', 'Gamblin SJ', 'Smerdon SJ.'], 'DOI_URL': 'http://dx.doi.org/10.1038/41805'}, 'PUB00018226': {'PMID': 9338791, 'ISBN': None, 'volume': '389', 'issue': '6652', 'year': 1997, 'title': 'Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue.', 'URL': None, 'raw_pages': '758-62', 'medline_journal': 'Nature', 'ISO_journal': 'Nature', 'authors': ['Rittinger K', 'Walker PA', 'Eccleston JF', 'Smerdon SJ', 'Gamblin SJ.'], 'DOI_URL': 'http://dx.doi.org/10.1038/39651'}}"	""	"{'name': 'Rho GTPase-activating proteins domain profile', 'short': 'RHOGAP'}"	""	"{'accession': '2osa', 'name': 'The Rho-GAP domain of human N-chimaerin'}"	""	"profile"	"domain"	""