Sequence information
Variant position: 12 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 189 The length of the canonical sequence.
Location on the sequence:
MTEYKLVVVGA
G GVGKSALTIQLIQNHFVDEY
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human MTEYKLVVVGAG GVGKSALTIQLIQNHFVDEY
Mouse MTEYKLVVVGAG GVGKSALTIQLIQNHFVDEY
Rat MTEYKLVVVGAG GVGKSALTIQLIQNHFVDEY
Chicken MTEYKLVVVGAG GVGKSALTIQLIQNHFVDEY
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
1 – 186
GTPase HRas
Initiator methionine
1 – 1
Removed; alternate
Chain
2 – 186
GTPase HRas, N-terminally processed
Nucleotide binding
10 – 17
GTP
Modified residue
1 – 1
N-acetylmethionine; in GTPase HRas; alternate
Modified residue
2 – 2
N-acetylthreonine; in GTPase HRas, N-terminally processed
Mutagenesis
17 – 17
S -> N. Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2.
Mutagenesis
26 – 26
N -> G. Loss of interaction with PLCE1; when associated with V-12.
Mutagenesis
29 – 29
V -> A. No effect on interaction with PLCE1; when associated with V-12.
Mutagenesis
32 – 32
Y -> F. Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12.
Beta strand
12 – 15
Literature citations
Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras.
Song C.; Hu C.-D.; Masago M.; Kariya K.; Yamawaki-Kataoka Y.; Shibatohge M.; Wu D.; Satoh T.; Kataoka T.;
J. Biol. Chem. 276:2752-2757(2001)
Cited for: INTERACTION WITH PLCE1; CHARACTERIZATION OF VARIANT VAL-12; MUTAGENESIS OF SER-17; ASN-26; VAL-29; TYR-32; PRO-34; THR-35; GLU-37; ASP-38 AND SER-39;
Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease.
Liu F.; Iqbal K.; Grundke-Iqbal I.; Rossie S.; Gong C.X.;
J. Biol. Chem. 280:1790-1796(2005)
Cited for: CHARACTERIZATION OF CSTLO VARIANT VAL-12;
Germline mutations in HRAS proto-oncogene cause Costello syndrome.
Aoki Y.; Niihori T.; Kawame H.; Kurosawa K.; Ohashi H.; Tanaka Y.; Filocamo M.; Kato K.; Suzuki Y.; Kure S.; Matsubara Y.;
Nat. Genet. 37:1038-1040(2005)
Cited for: VARIANTS CSTLO ALA-12; SER-12; VAL-12 AND ASP-13;
Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation.
van der Burgt I.; Kupsky W.; Stassou S.; Nadroo A.; Barroso C.; Diem A.; Kratz C.P.; Dvorsky R.; Ahmadian M.R.; Zenker M.;
J. Med. Genet. 44:459-462(2007)
Cited for: VARIANTS CMEMS VAL-12; SER-12; LYS-22 AND LYS-63;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.