Hras
entrez
15461
canonical
uniprot
Q61411
canonical
ensembl
ENSMUSG00000025499
resolver
ensp
ENSMUSP00000026572
resolver
ensp
ENSMUSP00000095570
resolver
ensp
ENSMUSP00000132110
resolver
ensp
ENSMUSP00000170908
resolver
ensp
ENSMUSP00000170909
resolver
ensp
ENSMUSP00000170924
resolver
ensp
ENSMUSP00000170926
resolver
genesymbol
Hras
resolver
genesymbol_syn
Hras1
resolver
uniprot
F7BIB2
resolver
uniprot
Q6P716
resolver
uniprot
Q80WD2
resolver
uniprot
Q811B9
resolver
uniprot_entry
RASH_MOUSE
resolver
uniprot_sec
F7BIB2
resolver
uniprot_sec
Q6P716
resolver
uniprot_sec
Q80WD2
resolver
uniprot_sec
Q811B9
resolver
activity_regulation
ACTIVITY REGULATION: 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).
uniprot
proteins
amino_acid_sequence
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (By similarity). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Recognized by LZTR1 that mediates its ubiquitination by a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (By similarity). {ECO:0000250|UniProtKB:P01112}.
uniprot
proteins
mass_dalton
21298
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="Q->R: Found in chemically induced liver tumors."; /evidence="ECO:0000269|PubMed:7526162
uniprot
proteins
post_translational_modification
PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01112}.; PTM: S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation. {ECO:0000250|UniProtKB:P01112}.; PTM: 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. {ECO:0000250|UniProtKB:P01112}.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250}.; PTM: 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. {ECO:0000250|UniProtKB:P01112}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10869344
uniprot
proteins
pubmed
1347942
uniprot
proteins
pubmed
14500341
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16580637
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19906996
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7526162
uniprot
proteins
pubmed
8922043
uniprot
proteins
sequence_length
189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20171}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the plasma membrane and the Golgi apparatus. The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). {ECO:0000250}.
uniprot
proteins