RASSF7 _ HRAS1
- Known as:
- RASSF7 _ HRAS1
- Catalog number:
- Y213912
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- RASSF7 _ HRAS1
Related genes to: RASSF7 _ HRAS1
- Gene:
- HRAS NIH gene
- Name:
- HRas proto-oncogene, GTPase
- Previous symbol:
- HRAS1
- Synonyms:
- -
- Chromosome:
- 11p15.5
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2019-04-23
- Gene:
- RASSF7 NIH gene
- Name:
- Ras association domain family member 7
- Previous symbol:
- C11orf13
- Synonyms:
- HRC1, HRAS1
- Chromosome:
- 11p15.5
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-18
- Date modifiied:
- 2016-01-29
Related products to: RASSF7 _ HRAS1
Anti- RASSF7 HRAS1 AntibodyAnti- RASSF7 (Ras association (RalGDS AF-6) domain family 7) AntibodyAntibodies: RASSF7 _ HRAS1 HOST: Goat Clonality: pAbC11orf13,Homo sapiens,HRAS1-related cluster protein 1,HRC1,Human,Ras association domain-containing protein 7,RASSF7CLIA c-H-ras,GTPase HRas,Ha-Ras,Homo sapiens,HRAS,HRAS1,H-Ras-1,Human,p21ras,Transforming protein p21CLIA c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,Mouse,Mus musculus,p21ras,Transforming protein p21CLIA c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,p21ras,Rat,Rattus norvegicus,Transforming protein p21CLIA Chicken,c-H-ras,Gallus gallus,GTPase HRas,HRAS1,H-Ras-1,p21ras,Transforming protein p21ELISA c-H-ras,GTPase HRas,Ha-Ras,Homo sapiens,HRAS,HRAS1,H-Ras-1,Human,p21ras,Transforming protein p21ELISA c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,Mouse,Mus musculus,p21ras,Transforming protein p21ELISA c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,p21ras,Rat,Rattus norvegicus,Transforming protein p21ELISA Chicken,c-H-ras,Gallus gallus,GTPase HRas,HRAS1,H-Ras-1,p21ras,Transforming protein p21ELISA kit c-H-ras,GTPase HRas,Ha-Ras,Homo sapiens,HRAS,HRAS1,H-Ras-1,Human,p21ras,Transforming protein p21ELISA kit c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,Mouse,Mus musculus,p21ras,Transforming protein p21ELISA kit c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,p21ras,Rat,Rattus norvegicus,Transforming protein p21 Related articles to: RASSF7 _ HRAS1
- RAS effectors specifically interact with GTP-bound RAS proteins to link extracellular signals to downstream signaling pathways. These interactions rely on two types of domains, called RAS-binding (RB) and RAS association (RA) domains, which share common structural characteristics. Although the molecular nature of RAS-effector interactions is well-studied for some proteins, most of the RA/RB-domain-containing proteins remain largely uncharacterized. Here, we searched through human proteome databases, extracting 41 RA domains in 39 proteins and 16 RB domains in 14 proteins, each of which can specifically select at least one of the 25 members in the RAS family. We next comprehensively investigated the sequence-structure-function relationship between different representatives of the RAS family, including HRAS, RRAS, RALA, RAP1B, RAP2A, RHEB1, and RIT1, with all members of RA domain family proteins (RASSFs) and the RB-domain-containing CRAF. The binding affinity for RAS-effector interactions, determined using fluorescence polarization, broadly ranged between high (0.3 μM) and very low (500 μM) affinities, raising interesting questions about the consequence of these variable binding affinities in the regulation of signaling events. Sequence and structural alignments pointed to two interaction hotspots in the RA/RB domains, consisting of an average of 19 RAS-binding residues. Moreover, we found novel interactions between RRAS1, RIT1, and RALA and RASSF7, RASSF9, and RASSF1, respectively, which were systematically explored in sequence-structure-property relationship analysis, and validated by mutational analysis. These data provide a set of distinct functional properties and putative biological roles that should now be investigated in the cellular context. - Source: PubMed
Publication date: 2021/04/28
Rezaei Adariani SoheilaKazemein Jasemi Neda SBazgir FarhadWittich ChristophAmin EhsanSeidel Claus A MDvorsky RadovanAhmadian Mohammad R - Small guanosine triphosphatases (GTPases) of the RAS superfamily signal by directly binding to multiple downstream effector proteins. Effectors are defined by a folded RAS-association (RA) domain that binds exclusively to GTP-loaded (activated) RAS, but the binding specificities of most RA domains toward more than 160 RAS superfamily GTPases have not been characterized. Ten RA domain family (RASSF) proteins comprise the largest group of related effectors and are proposed to couple RAS to the proapoptotic Hippo pathway. Here, we showed that RASSF1-6 formed complexes with the Hippo kinase ortholog MST1, whereas RASSF7-10 formed oligomers with the p53-regulating effectors ASPP1 and ASPP2. Moreover, only RASSF5 bound directly to activated HRAS and KRAS, and RASSFs did not augment apoptotic induction downstream of RAS oncoproteins. Structural modeling revealed that expansion of the RASSF effector family in vertebrates included amino acid substitutions to key residues that direct GTPase-binding specificity. We demonstrated that the tumor suppressor RASSF1A formed complexes with the RAS-related GTPases GEM, REM1, REM2, and the enigmatic RASL12. Furthermore, interactions between RASSFs and RAS GTPases blocked YAP1 nuclear localization. Thus, these simple scaffolds link the activation of diverse RAS family small G proteins to Hippo or p53 regulation. - Source: PubMed
Publication date: 2020/10/13
Dhanaraman ThillaivillalanSingh SwatiKilloran Ryan CSingh AnamikaXu XingjianShifman Julia MSmith Matthew J