Sequence information
Variant position: 144 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 3661 The length of the canonical sequence.
Location on the sequence:
GSRALATKDMRKSQERSMSY
S DESRLSNLLRRITREDDRDR
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 GSRALATKDMRKSQERSMSYS DESRLSNLLRRITREDDRDR
Mouse GSRALATKDMRKSQERSMSYS DESRLSNLLRRITREDDRDR
Zebrafish GNRALATKDMRKSQDRPLAHS EESRLANLLRRASREDDRER
Caenorhabditis elegans LA------------------G KVIRLVGVL-----------
Drosophila HRKAYQCKGDTIN---PMANG EDLRLSKIIRRLINENNPTV
Slime mold TATATAITPTPIT----TSQS TSSSMLNLPLKVGKE-----
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 – 3661
Serine/threonine-protein kinase SMG1
Region
1 – 1977
Interaction with SMG8 and SMG9
Region
116 – 144
Disordered
Alternative sequence
1 – 1269
Missing. In isoform 4.
Alternative sequence
1 – 630
Missing. In isoform 3.
Beta strand
143 – 148
Literature citations
The mRNA surveillance protein hSMG-1 functions in genotoxic stress response pathways in mammalian cells.
Brumbaugh K.M.; Otterness D.M.; Geisen C.; Oliveira V.; Brognard J.; Li X.; Lejeune F.; Tibbetts R.S.; Maquat L.E.; Abraham R.T.;
Mol. Cell 14:585-598(2004)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2); FUNCTION; PHOSPHORYLATION OF TP53; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; ACTIVITY REGULATION; MUTAGENESIS OF ASP-2335; VARIANTS CYS-144 AND LYS-612;
Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-35; CYS-126; CYS-144; TYR-151; ASN-160; VAL-167; GLY-320; SER-465; ARG-546; SER-588; LYS-612; CYS-753; CYS-809; CYS-812; ILE-829; ASP-832; GLY-952; SER-969; LEU-1016; GLN-1029; SER-1072; HIS-1103; ARG-1275; PRO-1292; VAL-1332; PRO-1358; THR-1418; CYS-2171; SER-2258; LYS-2345; GLU-2730; SER-2889; ALA-2899; THR-3239 AND GLN-3583;
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.