{"data":{"id":"us/37-cfr-appendix-f-to-subpart-g-of-part-1","jurisdiction":"us","citation":"37 CFR Appendix F to Subpart G of Part 1","heading":"Appendix F to Subpart G of Part 1—List of Feature Keys Related to Protein Sequences","body":"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).\nKey Description\nCONFLICT different papers report differing sequences.\nVARIANT authors report that sequence variants exist.\nVARSPLIC description of sequence variants produced by alternative splicing.\nMUTAGEN site which has been experimentally altered.\nMOD__RES post-translational modification of a residue.\nACETYLATION N-terminal or other.\nAMIDATION generally at the C-terminal of a mature active peptide.\nBLOCKED undetermined N- or C-terminal blocking group.\nFORMYLATION of the N-terminal methionine.\nGAMMA-CARBOXYGLUTAMIC ACID HYDROXYLATION of asparagine, aspartic acid, proline, or lysine.\nMETHYLATION generally of lysine or arginine.\nPHOSPHORYLATION of serine, threonine, tyrosine, aspartic acid or histidine.\nPYRROLIDONE CARBOXYLIC ACID N-terminal glutamate which has formed an internal cyclic lactam.\nSULFATATION generally of tyrosine.\nLIPID covalent binding of a lipidic moiety.\nMYRISTATE 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.\nPALMITATE palmitate group attached through a thioether bond to a cysteine residue or through an ester bond to a serine or threonine residue.\nFARNESYL farnesyl group attached through a thioether bond to a cysteine residue.\nGERANYL-GERANYL geranyl-geranyl group attached through a thioether bond to a cysteine residue.\nGPI-ANCHOR glycosyl-phosphatidylinositol (GPI) group linked to the alpha- carboxyl group of the C-terminal residue of the mature form of a protein.\nN-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.\nDISULFID 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.\nTHIOLEST thiolester bond; the `FROM' and `TO' endpoints represent the two residues which are linked by the thiolester bond.\nTHIOETH thioether bond; the `FROM' and `TO' endpoints represent the two residues which are linked by the thioether bond.\nCARBOHYD glycosylation site; the nature of the carbohydrate (if known) is given in the description field.\nMETAL binding site for a metal ion; the description field indicates the nature of the metal.\nBINDING binding site for any chemical group (co-enzyme, prosthetic group, etc.); the chemical nature of the group is given in the description field.\nSIGNAL extent of a signal sequence (prepeptide).\nTRANSIT extent of a transit peptide (mitochondrial, chloroplastic, or for a microbody).\nPROPEP extent of a propeptide.\nCHAIN extent of a polypeptide chain in the mature protein.\nPEPTIDE extent of a released active peptide.\nDOMAIN extent of a domain of interest on the sequence; the nature of that domain is given in the description field.\nCA__BIND extent of a calcium-binding region.\nDNA__BIND extent of a DNA-binding region.\nNP__BIND extent of a nucleotide phosphate binding region; the nature of the nucleotide phosphate is indicated in the description field.\nTRANSMEM extent of a transmembrane region.\nZN__FING extent of a zinc finger region.\nSIMILAR extent of a similarity with another protein sequence; precise information, relative to that sequence, is given in the description field.\nREPEAT extent of an internal sequence repetition.\nHELIX secondary structure: Helices, for example, Alpha-helix, 3(10) helix, or Pi-helix.\nSTRAND secondary structure: Beta-strand, for example, Hydrogen bonded beta-strand, or Residue in an isolated beta-bridge.\nTURN secondary structure Turns, for example, H-bonded turn (3-turn, 4-turn, or 5-turn).\nACT__SITE amino acid(s) involved in the activity of an enzyme.\nSITE any other interesting site on the sequence.\nINIT__MET the sequence is known to start with an initiator methionine.\nNON__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.\nNON__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.\nUNSURE uncertainties in the sequence; used to describe region(s) of a sequence for which the authors are unsure about the sequence assignment.","path":["Title 37—Patents, Trademarks, and Copyrights","CHAPTER I—UNITED STATES PATENT AND TRADEMARK OFFICE, DEPARTMENT OF COMMERCE","SUBCHAPTER A—GENERAL","PART 1—RULES OF PRACTICE IN PATENT CASES","Subpart G—Biotechnology Invention Disclosures"],"source_url":"https://www.ecfr.gov/api/versioner/v1/full/2026-08-25/title-37.xml","current_through":"2026-08-25","vintage":"","retrieved_at":"2026-08-27T02:25:45Z","sha256":"690e5bfe2bca944231b7a77fabb12f5998d198804c7615374206d76d48fc691a","source_id":"us-cfr","stale":true,"prev":"us/37-cfr-appendix-e-to-subpart-g-of-part-1","next":"us/37-cfr-appendix-g-to-subpart-g-of-part-1"},"notice":"GroundRules: Original legal text. Not legal advice."}