{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P01112","secondaryAccessions":["B5BUA0","Q14080","Q6FHV9","Q9BR65","Q9UCE2"],"uniProtkbId":"RASH_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1986-07-21","entryVersion":281,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"GTPase HRas"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9020151"}],"value":"3.6.5.2"}]},"alternativeNames":[{"fullName":{"value":"H-Ras-1"}},{"fullName":{"value":"Ha-Ras"}},{"fullName":{"value":"Transforming protein p21"}},{"fullName":{"value":"c-H-ras"}},{"fullName":{"value":"p21ras"}}],"contains":[{"recommendedName":{"fullName":{"value":"GTPase HRas, N-terminally processed"}}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"HRAS"},"synonyms":[{"value":"HRAS1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12740440"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14500341"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22821884"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40934300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9020151"}],"value":"Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151). Recognized by LZTR1 that mediates its ubiquitination by a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (PubMed:40934300)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9020151"}]}},{"texts":[{"value":"Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20171"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q61411"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10369681"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10608844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11022048"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11257115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11598133"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11980706"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14500341"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17230191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18596699"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35522713"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35768504"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36175670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40934300"}],"value":"In its GTP-bound form interacts with PLCE1 (PubMed:11022048). Interacts with TBC1D10C (PubMed:17230191). Interacts with RGL3 (By similarity). Interacts with HSPD1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (By similarity). Forms a signaling complex with RASGRP1 and DGKZ (PubMed:11257115). Interacts with RASSF5 (PubMed:18596699). Interacts with PDE6D (PubMed:11980706). Interacts with IKZF3 (PubMed:10369681). Interacts with RACK1 (PubMed:14500341). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (PubMed:10608844, PubMed:11598133). Interacts (active GTP-bound form) with both SHOC2 and PP1c (all isoforms) to form a tertiary complex; SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS (PubMed:35768504, PubMed:35831509, PubMed:36175670). Interacts (GTP-bound form) with MAPKAP1/SIN1; inhibiting H-Ras/HRAS activity (PubMed:35522713). Interacts (GDP-bound form) with LZTR1; this interaction mediates HRAS ubiquitination by BCR E3 ligase complex (PubMed:40934300)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q99996-3","geneName":"AKAP9","intActId":"EBI-11022349"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"P53677-2","geneName":"AP3M2","intActId":"EBI-12177015"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"P10398","geneName":"ARAF","intActId":"EBI-365961"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9NXL2-1","geneName":"ARHGEF38","intActId":"EBI-18172597"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9UII2","geneName":"ATP5IF1","intActId":"EBI-718459"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9H7T9","geneName":"AUNIP","intActId":"EBI-10693257"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q00994","geneName":"BEX3","intActId":"EBI-741753"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9H2G9","geneName":"BLZF1","intActId":"EBI-2548012"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"P15056","geneName":"BRAF","intActId":"EBI-365980"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q7Z569","geneName":"BRAP","intActId":"EBI-349900"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q5PSV4","geneName":"BRMS1L","intActId":"EBI-5666615"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9ULD4-2","geneName":"BRPF3","intActId":"EBI-23662416"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q96LL4","geneName":"C8orf48","intActId":"EBI-751596"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q86X55","geneName":"CARM1","intActId":"EBI-2339854"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q96HB5","geneName":"CCDC120","intActId":"EBI-744556"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q49A88-3","geneName":"CCDC14","intActId":"EBI-12105646"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q96GN5-2","geneName":"CDCA7L","intActId":"EBI-9091443"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"P24941","geneName":"CDK2","intActId":"EBI-375096"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"O95674","geneName":"CDS2","intActId":"EBI-3913685"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9H3R5","geneName":"CENPH","intActId":"EBI-1003700"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q9Y4F5-3","geneName":"CEP170B","intActId":"EBI-12950757"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q86XR8","geneName":"CEP57","intActId":"EBI-308614"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01112","intActId":"EBI-350145"},"interactantTwo":{"uniProtKBAccession":"Q494V2-2","geneName":"CFAP100","intActId":"E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A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi"}],"commentType":"PTM"},{"texts":[{"value":"S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation"}],"commentType":"PTM"},{"texts":[{"value":"The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29239724"}],"value":"Fatty-acylated at Lys-170"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30442762"}],"value":"Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19744486"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8626575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8626586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9632667"}],"value":"(Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL (PubMed:19744486, PubMed:8626575, PubMed:8626586, PubMed:9632667). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to inhibit Ras signaling (PubMed:8626575, PubMed:8626586, PubMed:9632667)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Costello syndrome","diseaseAccession":"DI-01437","acronym":"CSTLO","description":"A rare condition characterized by prenatally increased growth, postnatal growth deficiency, intellectual disability, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities.","diseaseCrossReference":{"database":"MIM","id":"218040"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16170316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16329078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16443854"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17054105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18039947"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18247425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19995790"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Congenital myopathy with excess of muscle spindles","diseaseAccession":"DI-01411","acronym":"CMEMS","description":"Variant of Costello syndrome.","diseaseCrossReference":{"database":"MIM","id":"218040"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17412879"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Thyroid cancer, non-medullary, 2","diseaseAccession":"DI-04532","acronym":"NMTC2","description":"A form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms.","diseaseCrossReference":{"database":"MIM","id":"188470"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12727991"}]},"note":{"texts":[{"value":"Disease susceptibility is associated with variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3670300"}],"value":"Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Bladder cancer","diseaseAccession":"DI-02612","acronym":"BLC","description":"A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. 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