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Feature type and shape vocabulary

Every feature record has a type (see Load your own data). The viewer uses it to pick the feature’s default colour and shape from a table built into Nightingale, the library that draws the tracks. This page lists that table as shipped in @nightingale-elements/nightingale-track 5.11.1, the version the viewer draws with. It is generated from that package and kept in sync by drift tests, so it cannot silently diverge.

The first of these that applies wins:

  1. A colour or shape carried on the feature record itself. Some built-in kinds set one (InterPro domains get a colour per entry; PTMeXchange peptides are triangles); records from your own CSV, TSV or JSON file can set one with a color / shape column (or key); BED files cannot.
  2. The track’s rendering.color and rendering.shape, set on the track or inherited from its group or from defaults:. These apply to every feature in the track, whatever its type.
  3. The default for the feature’s type, from the table below.
  4. black and rectangle.

Colour and shape are resolved separately, so a track can set one and keep the other.

type is matched without regard to case, against either the type code (ACT_SITE) or the UniProt name (active site) listed in the table.

A type outside the table is drawn as a black rectangle. The viewer shows no error or warning; Nightingale only logs the type name to the browser console. Every unrecognised type looks the same, so a track that mixes two of them cannot tell them apart.

BED files have no type column, so every record read from a .bed file has type: BED and is drawn as a black rectangle unless its track sets rendering.

A lab marks its own hotspots with a type UniProt does not use:

type,start,end,description,score
HOTSPOT,132,140,Lab-defined mutational hotspot,0.87
HOTSPOT,601,612,Lab-defined mutational hotspot,0.64

On its own, each row draws as a black rectangle. Give the track a rendering block to choose the look instead:

accession: P05067
rows:
- id: hotspots
label: Hotspots
kind: features
data: ./hotspots.csv
rendering:
color: '#e67e22'
shape: roundRectangle

Because rendering applies to the whole track, it also overrides the defaults of any recognised types in the same file. Keep custom types in their own file and track so the recognised ones keep their colours.

45 type codes, in the order Nightingale’s type table lists them.

Type UniProt name Label Default shape Default colour Meaning
CHAIN chain Chain rectangle #CC9933 (aka mature region). This describes the extent of a polypeptide chain in the mature protein following processing
TRANSIT transit peptide Transit peptide rectangle #009966 This describes the extent of a transit peptide
INIT_MET initiator methionine Initiator methionine arrow #996633 This indicates that the initiator methionine is cleaved from the mature protein
PROPEP propeptide Propeptide rectangle #99CCCC Part of a protein that is cleaved during maturation or activation
PEPTIDE peptide Peptide rectangle #006699 The position and length of an active peptide in the mature protein
SIGNAL signal peptide Signal peptide rectangle #CC0033 N-terminal signal peptide
HELIX helix Helix rectangle #FF0066 The positions of experimentally determined helical regions
STRAND strand Beta strand rectangle #FFCC00 The positions of experimentally determined beta strands
TURN turn Turn rectangle #0571AF The positions of experimentally determined hydrogen-bonded turns
DISULFID disulfide bond Disulfide bond bridge #23B14D The positions of cysteine residues participating in disulphide bonds
CROSSLNK cross-link Cross-link bridge #FF6600 Covalent linkages of various types formed between two proteins or between two parts of the same protein
REGION region of interest Region of interest rectangle #B33E00 Regions in multifunctional enzymes or fusion proteins, or characteristics of a region, e.g., protein-protein interactions mediation
COILED coiled-coil region Coiled-coil region rectangle #006699 Coiled coils are built by two or more alpha-helices that wind around each other to form a supercoil
MOTIF short sequence motif Short sequence motif rectangle #402060 Short conserved sequence motif of biological significance
REPEAT repeat Repeat rectangle #9900FF Repeated sequence motifs or repeated domains within the protein
CA_BIND calcium-binding region Calcium-binding region rectangle #FF3399 Calcium-binding regions, such as the EF-hand motif
DNA_BIND DNA-binding region DNA binding rectangle #009933 DNA-binding domains such as AP2/ERF domain, the ETS domain, the Fork-Head domain, the HMG box and the Myb domain
DOMAIN other domain of interest Other domain of interest rectangle #9999FF Specific combination of secondary structures organized into a characteristic three-dimensional structure or fold
ZN_FING zinc finger region Zinc finger rectangle #990066 Small, functional, independently folded domain that coordinates one or more zinc ions
NP_BIND nucleotide-binding region Nucleotide-binding region rectangle #FF9900 (aka flavin-binding). Region in the protein which binds nucleotide phosphates
METAL metal ion-binding site Metal ion-binding site diamond #009900 Binding site for a metal ion
SITE other site of interest Other site of interest chevron #660033 Any interesting single amino acid site on the sequence
BINDING other binding site Other binding site rectangle #009999 Binding site for any chemical group (co-enzyme, prosthetic group, etc.)
ACT_SITE active site Active site circle #FF6666 Amino acid(s) directly involved in the activity of an enzyme
MOD_RES Post-translationally modified residue Modified residue triangle #000066 Modified residues such as phosphorylation, acetylation, acylation, methylation
LIPID lipid moiety-binding region Lipidation wave #99CC33 Covalently attached lipid group(s)
CARBOHYD glycosylation site Glycosylation hexagon #CC3366 Covalently attached glycan group(s)
COMPBIAS compositionally biased region Compositionally biased region rectangle #FF3366 Position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions
CONFLICT sequence conflict Sequence conflict rectangle #6633CC Sequence discrepancies of unknown origin
NON_CONS non-consecutive residues Non-adjacent residues doubleBar #FF0033 Indicates that two residues in a sequence are not consecutive and that there is an undetermined number of unsequenced residues between them
NON_TER non-terminal residue Non-terminal residue doubleBar #339933 The sequence is incomplete. The residue is not the terminal residue of the complete protein
UNSURE unsure residue Sequence uncertainty rectangle #33FF00 Regions of a sequence for which the authors are unsure about the sequence assignment
NON_STD non-standard amino acid Non-standard residue pentagon #330066 Non-standard amino acids (selenocysteine and pyrrolysine)
MUTAGEN mutagenesis site Mutagenesis rectangle #FF9900 Site which has been experimentally altered by mutagenesis
TOPO_DOM topological domain Topological domain rectangle #CC0000 Location of non-membrane regions of membrane-spanning proteins
TRANSMEM transmembrane region Transmembrane rectangle #CC00CC Extent of a membrane-spanning region
INTRAMEM intramembrane region Intramembrane rectangle #0000CC Extent of a region located in a membrane without crossing it
VAR_SEQ splice variant Splice variant rectangle #CC11CC —
VARIANT sequence variant Natural variant circle black Natural variant of the protein, including polymorphisms, variations between strains, isolates or cultivars, disease-associated mutations and RNA editing events
UNIQUE unique Unique peptide rectangle #fc3133 —
NON_UNIQUE non-unique Non-unique peptide rectangle #8585fc —
RESIDUE residue PTM residue rectangle #06038D —
EPITOPE epitope Epitopes rectangle #4ade33 —
ANTIGEN antigen Antibody binding sequences rectangle #996699 —
PDBE_COVER pdbe coverage PDBe 3D structure coverage rectangle #669966 —

rendering.shape takes one of these 22 names. The spellings (discontinuos) are Nightingale’s. Each is drawn below by the canvas track’s own drawing code: shapes that stretch across several residues, glyphs on one. 3 of them (leftEndedTag, rightEndedTag, doubleEndedTag) are declared but not drawn by the canvas track, and show a question mark instead. So does any other name: the config accepts any string for shape, and a misspelt one only shows up as a one-time warning naming it in the browser console.

Looks like Shape Drawn as Default for
rectangle Stretches to cover the feature CHAIN, TRANSIT, PROPEP, PEPTIDE, SIGNAL, HELIX, STRAND, TURN, REGION, COILED, MOTIF, REPEAT, CA_BIND, DNA_BIND, DOMAIN, ZN_FING, NP_BIND, BINDING, COMPBIAS, CONFLICT, UNSURE, MUTAGEN, TOPO_DOM, TRANSMEM, INTRAMEM, VAR_SEQ, UNIQUE, NON_UNIQUE, RESIDUE, EPITOPE, ANTIGEN, PDBE_COVER
roundRectangle Stretches to cover the feature —
bridge Stretches to cover the feature DISULFID, CROSSLNK
line Stretches to cover the feature —
diamond Fixed-size glyph; across more than one residue a line joins its ends METAL
chevron Fixed-size glyph; across more than one residue a line joins its ends SITE
catFace Fixed-size glyph; across more than one residue a line joins its ends —
triangle Fixed-size glyph; across more than one residue a line joins its ends MOD_RES
wave Fixed-size glyph; across more than one residue a line joins its ends LIPID
hexagon Fixed-size glyph; across more than one residue a line joins its ends CARBOHYD
pentagon Fixed-size glyph; across more than one residue a line joins its ends NON_STD
circle Fixed-size glyph; across more than one residue a line joins its ends ACT_SITE, VARIANT
arrow Fixed-size glyph; across more than one residue a line joins its ends INIT_MET
doubleBar Fixed-size glyph; across more than one residue a line joins its ends NON_CONS, NON_TER
discontinuosStart Stretches to cover the feature —
discontinuos Stretches to cover the feature —
discontinuosEnd Stretches to cover the feature —
helix Stretches to cover the feature —
strand Stretches to cover the feature —
leftEndedTag Not drawn — shows a question mark —
rightEndedTag Not drawn — shows a question mark —
doubleEndedTag Not drawn — shows a question mark —

This work was supported by the Research Software Maintenance Fund, managed by the Software Sustainability Institute and funded by UKRI grant reference AH/Z000114/1.