37 C.F.R. § app F to Subpart G of Part 1
Current through November 30, 2024
Source: World Intellectual Property Organization (WIPO) Handbook on Industrial Property Information and Documentation, Standard ST.25: Standard for the Presentation of Nucleotide and Amino Acid Sequence Listings in Patent Applications (2009).
| Key | Description |
| CONFLICT | different papers report differing sequences. |
| VARIANT | authors report that sequence variants exist. |
| VARSPLIC | description of sequence variants produced by alternative splicing. |
| MUTAGEN | site which has been experimentally altered. |
| MOD__RES | post-translational modification of a residue. |
| ACETYLATION | N-terminal or other. |
| AMIDATION | generally at the C-terminal of a mature active peptide. |
| BLOCKED | undetermined N- or C-terminal blocking group. |
| FORMYLATION | of the N-terminal methionine. |
| GAMMA-CARBOXYGLUTAMIC ACID HYDROXYLATION | of asparagine, aspartic acid, proline, or lysine. |
| METHYLATION | generally of lysine or arginine. |
| PHOSPHORYLATION | of serine, threonine, tyrosine, aspartic acid or histidine. |
| PYRROLIDONE CARBOXYLIC ACID | N-terminal glutamate which has formed an internal cyclic lactam. |
| SULFATATION | generally of tyrosine. |
| LIPID | covalent binding of a lipidic moiety. |
| MYRISTATE | myristate group attached through an amide bond to the N-terminal glycine residue of the mature form of a protein or to an internal lysine residue. |
| PALMITATE | palmitate group attached through a thioether bond to a cysteine residue or through an ester bond to a serine or threonine residue. |
| FARNESYL | farnesyl group attached through a thioether bond to a cysteine residue. |
| GERANYL-GERANYL | geranyl-geranyl group attached through a thioether bond to a cysteine residue. |
| GPI-ANCHOR | glycosyl-phosphatidylinositol (GPI) group linked to the alpha- carboxyl group of the C-terminal residue of the mature form of a protein. |
| N-ACYL DIGLYCERIDE | N-terminal cysteine of the mature form of a prokaryotic lipoprotein with an amide-linked fatty acid and a glyceryl group to which two fatty acids are linked by ester linkages. |
| DISULFID | disulfide bond; the `FROM' and `TO' endpoints represent the two residues which are linked by an intra-chain disulfide bond; if the `FROM' and `TO' endpoints are identical, the disulfide bond is an interchain one and the description field indicates the nature of the cross-link. |
| THIOLEST | thiolester bond; the `FROM' and `TO' endpoints represent the two residues which are linked by the thiolester bond. |
| THIOETH | thioether bond; the `FROM' and `TO' endpoints represent the two residues which are linked by the thioether bond. |
| CARBOHYD | glycosylation site; the nature of the carbohydrate (if known) is given in the description field. |
| METAL | binding site for a metal ion; the description field indicates the nature of the metal. |
| BINDING | binding site for any chemical group (co-enzyme, prosthetic group, etc.); the chemical nature of the group is given in the description field. |
| SIGNAL | extent of a signal sequence (prepeptide). |
| TRANSIT | extent of a transit peptide (mitochondrial, chloroplastic, or for a microbody). |
| PROPEP | extent of a propeptide. |
| CHAIN | extent of a polypeptide chain in the mature protein. |
| PEPTIDE | extent of a released active peptide. |
| DOMAIN | extent of a domain of interest on the sequence; the nature of that domain is given in the description field. |
| CA__BIND | extent of a calcium-binding region. |
| DNA__BIND | extent of a DNA-binding region. |
| NP__BIND | extent of a nucleotide phosphate binding region; the nature of the nucleotide phosphate is indicated in the description field. |
| TRANSMEM | extent of a transmembrane region. |
| ZN__FING | extent of a zinc finger region. |
| SIMILAR | extent of a similarity with another protein sequence; precise information, relative to that sequence, is given in the description field. |
| REPEAT | extent of an internal sequence repetition. |
| HELIX | secondary structure: Helices, for example, Alpha-helix, 3(10) helix, or Pi-helix. |
| STRAND | secondary structure: Beta-strand, for example, Hydrogen bonded beta-strand, or Residue in an isolated beta-bridge. |
| TURN | secondary structure Turns, for example, H-bonded turn (3-turn, 4-turn, or 5-turn). |
| ACT__SITE | amino acid(s) involved in the activity of an enzyme. |
| SITE | any other interesting site on the sequence. |
| INIT__MET | the sequence is known to start with an initiator methionine. |
| NON__TER | the residue at an extremity of the sequence is not the terminal residue; if applied to position 1, this signifies that the first position is not the N-terminus of the complete molecule; if applied to the last position, it signifies that this position is not the C-terminus of the complete molecule; there is no description field for this key. |
| NON__CONS | non consecutive residues; indicates that two residues in a sequence are not consecutive and that there are a number of unsequenced residues between them. |
| UNSURE | uncertainties in the sequence; used to describe region(s) of a sequence for which the authors are unsure about the sequence assignment. |
37 C.F.R. app F to Subpart G of Part 1
Part 2 is placed in the separate grouping of parts pertaining to trademarks regulations.
Part 6 is placed in the separate grouping of parts pertaining to trademarks regulations.
Part 7 is placed in the separate grouping of parts pertaining to trademarks regulations.
Part 1 is placed in the separate grouping of parts pertaining to patents regulations.
Part 3 pertaining to both patents and trademarks is placed in the grouping pertaining to patents regulations.
Part 4 is placed in the separate grouping of parts pertaining to patents regulations.
Part 5 is placed in the separate grouping of parts pertaining to patents regulations.