Variant position: 334 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 453 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 DAFDGFDFGDDPSDKFFTSH NGMQFSTWDNDNDKFEGNCAE
Mouse DAFDGYDFGDDPSDKFFTSH NGMQFSTWDNDNDKFEGNCAE
Rat DAFDGYDFGDDPSDKFFTSH NGMHFSTWDNDNDKFEGNCAE
Bovine DAFDGYDFGDDSSDKFFTSH NGMQFSTWDSDNDKYDGNCAE
Xenopus laevis DAFDGFDFGDDPSDKFYTSH NGMQFSTFDKDNDKFDGNCAE
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
27 – 453 Fibrinogen gamma chain
170 – 416 Fibrinogen C-terminal
334 – 334 N-linked (GlcNAc...); in variant Asahi
Gene analyses of abnormal fibrinogens with a mutation in the gamma chain.
Mimuro J.; Muramatsu S.; Maekawa H.; Sakata Y.; Kaneko M.; Yoshitake S.; Okuma M.; Ito Y.; Takeda Y.; Matsuda M.;
Int. J. Hematol. 56:129-134(1992)
Cited for: VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3 TYR-356;
Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site.
Yoshida N.; Terukina S.; Okuma M.; Moroi M.; Aoki N.; Matsuda M.;
J. Biol. Chem. 263:13848-13856(1988)
Cited for: VARIANT KYOTO-1 LYS-334;
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