Variant position: 644 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 664 The length of the canonical sequence.
Location on the sequence:
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 RSYRSVGGSGGG-SFGDNLVT RSYLLGNSSPRTQ--SPQNCSIM
Mouse RSFRSVGGSGGG-SFGDNLVT RSYLLGNSSPRSQ--SSQNC
Rat RSFRSVGGSGGG-SFGDNLVT RSYLLGNSSPRTQ--SSQNC
Pig RSYRSVGGSGGG-SFGDNLVT RSYLLGNSRPRTQ--SPQNC
Chicken RGYRSS----GG-GIGEGLLG RSYVLGGAGPRRQAPAPQGC
Xenopus laevis RTYRSTGGTSGGSGLGESPVT RNFIVGN-GQRAQV-APQNC
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
1 – 661 Prelamin-A/C
1 – 646 Lamin-A/C
384 – 664 Tail
628 – 628 Phosphoserine
632 – 632 Phosphoserine
636 – 636 Phosphoserine
652 – 652 Phosphoserine
661 – 661 Cysteine methyl ester
661 – 661 S-farnesyl cysteine
573 – 664 Missing. In isoform C.
607 – 656 Missing. In isoform 6.
664 – 664 M -> IQEMGMRWEVEEGRRKVSLSCLP. In isoform 4.
644 – 644 R -> A. Does not affect tail cleavage.
647 – 647 L -> R. Completely inhibits tail cleavage.
648 – 648 L -> A. Completely inhibits tail cleavage.
650 – 650 N -> A. Partially inhibits tail cleavage.
661 – 661 C -> S. Loss of interaction with NARF. Abolishes farnesylation.
Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.
Barrowman J.; Hamblet C.; Kane M.S.; Michaelis S.;
PLoS ONE 7:E32120-E32120(2012)
Cited for: MUTAGENESIS OF ARG-644; LEU-647; LEU-648; ASN-650 AND CYS-661; CHARACTERIZATION OF VARIANT HGPS CYS-644;
Novel lamin A/C gene (LMNA) mutations in atypical progeroid syndromes.
Csoka A.B.; Cao H.; Sammak P.J.; Constantinescu D.; Schatten G.P.; Hegele R.A.;
J. Med. Genet. 41:304-308(2004)
Cited for: VARIANT HGPS CYS-644; VARIANTS ILE-10 AND VAL-578;
Novel LMNA mutations in patients with Emery-Dreifuss muscular dystrophy and functional characterization of four LMNA mutations.
Scharner J.; Brown C.A.; Bower M.; Iannaccone S.T.; Khatri I.A.; Escolar D.; Gordon E.; Felice K.; Crowe C.A.; Grosmann C.; Meriggioli M.N.; Asamoah A.; Gordon O.; Gnocchi V.F.; Ellis J.A.; Mendell J.R.; Zammit P.S.;
Hum. Mutat. 32:152-167(2011)
Cited for: VARIANTS EDMD2 SER-39; CYS-45; PRO-150; PRO-189; ARG-190 INS; LEU-206; TRP-249; GLN-249; PRO-268; PRO-271; PRO-294; PRO-295; PRO-303; GLN-355 DEL; LYS-358; LYS-361; LYS-386; ASP-449; TRP-453; PRO-454; TYR-461; ARG-467; PRO-527; LYS-528; ARG-528; SER-541; PRO-541; SER-602 AND CYS-644; CHARACTERIZATION OF VARIANTS EDMD2 PRO-25; TRP-249; ILE-456 AND PRO-541;
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.