Hras
entrez
293621
canonical
uniprot
P20171
canonical
ensembl
ENSRNOG00000016611
resolver
ensp
ENSRNOP00000022363
resolver
ensp
ENSRNOP00000069770
resolver
enst
ENSRNOT00000079464
resolver
genesymbol
Hras
resolver
genesymbol_syn
Hras1
resolver
uniprot
A0A8L2R1F7
resolver
uniprot
Q4KLL6
resolver
uniprot
Q5RJJ8
resolver
uniprot_entry
A0A8L2R1F7_RAT
resolver
uniprot_entry
RASH_RAT
resolver
uniprot_sec
Q4KLL6
resolver
uniprot_sec
Q5RJJ8
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 26; /note="N->G: Interacts and partially stimulates PLCE1; when associated with L-61."; /evidence="ECO:0000269|PubMed:11179219"; MUTAGEN 35; /note="T->S: No interaction and stimulation of PLCE1; when associated with L-61."; /evidence="ECO:0000269|PubMed:11179219"; MUTAGEN 37; /note="E->G: Reduced interaction and stimulation of PLCE1; when associated with L-61."; /evidence="ECO:0000269|PubMed:11179219"; MUTAGEN 38; /note="D->N: Reduced interaction and stimulation of PLCE1; when associated with L-61."; /evidence="ECO:0000269|PubMed:11179219"; MUTAGEN 40; /note="Y->C: No interaction and stimulation of PLCE1; when associated with L-61."; /evidence="ECO:0000269|PubMed:11179219"; MUTAGEN 61; /note="Q->L: Constitutively active. Constitutively interacts and stimulates PLCE1 phospholipase activity. Reduced interaction and stimulation of PLCE1; when associated with G-37 and N-38. No interaction and stimulation of PLCE1; when associated with S-35 and C-40. Interacts and partially stimulates PLCE1; when associated with G-26. Interacts but does not stimulate PLCE1; when associated with S-186."; /evidence="ECO:0000269|PubMed:11179219"; MUTAGEN 186; /note="C->S: Interacts but does not stimulate PLCE1; when associated with L-61."; /evidence="ECO:0000269|PubMed:11179219
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
11179219
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19319189
uniprot
proteins
pubmed
19878719
uniprot
proteins
pubmed
3023901
uniprot
proteins
pubmed
3027702
uniprot
proteins
pubmed
3290900
uniprot
proteins
sequence_length
189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19878719}. 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 (By similarity). The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form. {ECO:0000250}.
uniprot
proteins