Description

UniProt is a resource of information on protein sequences and function.
Manual curation of high quality experimental protein data from the literature
describes the role of a protein, and regions or sites of interest such as functional
domains, binding and enzyme active sites, sequence structure, post-translational
modifications and variants associated with disease.

In order to support the genomics community in the interpretation and exploitation of
the human genome, UniProt provides an up-to-date mapping between specific genomic
sequence coordinates and the corresponding protein sequence annotations.

Methods

Human protein sequences in the UniProt Knowledgebase (UniProtKB) have been mapped
to the human reference genome assembly (GRCh38) via the Ensembl resource. For each
protein sequence in UniProtKB the corresponding peptide, transcript and genomic
coordinates in Ensembl are identified. These mappings are updated for each UniProt
release and specific tracks are provided for each UniProt sequence annotation
type e.g. binding site.

Display Conventions and Configuration

Track naming convention

Each track name consists of a unique proteome identifier followed by the species
NCBI taxonomy identifier and the specific UniProt sequence annotation name.
For example, for human the UniProt unique proteome identifier is UP000005640
and the NCBI taxonomy identifier is 9606.

The list of sequence annotation names and their descriptions are provided below.

UP000005640_9606_proteome

The proteome is the set of proteins thought to be expressed by the organism.
UniProt proteomes include both manually reviewed (UniProtKB/Swiss-Prot)
and unreviewed (UniProtKB/TrEMBL) entries.

UP000005640_9606_site

Any interesting single amino acid site on the sequence.

UP000005640_9606_binding

Binding site for any chemical group (co-enzyme, prosthetic group, etc).

UP000005640_9606_ca_bind.bb

Position(s) of calcium binding region(s) within the protein.

UP000005640_9606_carbohyd.bb

Covalently attached glycan group(s).

UP000005640_9606_chain

Extent of a polypeptide chain in the mature protein.

UP000005640_9606_coiled

Positions of regions of coiled coil within the protein.

UP000005640_9606_crosslnk

Residues participating in covalent linkage(s) between proteins.

UP000005640_9606_disulfide

Cysteine residues participating in disulfide bonds.

UP000005640_9606_dna_bind

Position and type of a DNA-binding domain.

UP000005640_9606_domain

Position and type of each modular protein domain.

UP000005640_9606_intramem

Extent of a region located in a membrane without crossing it.

UP000005640_9606_lipid

Covalently attached lipid group(s).

UP000005640_9606_metal

Binding site for a metal ion.

UP000005640_9606_modres

Modified residues excluding lipids, glycans and protein cross-links.

UP000005640_9606_motif

Short (up to 20 amino acids) sequence motif of biological interest.

UP000005640_9606_np_bind

Nucleotide phosphate binding region.

UP000005640_9606_peptide

Extent of an active peptide in the mature protein.

UP000005640_9606_region

Region of interest in the sequence.

UP000005640_9606_repeat

Positions of repeated sequence motifs or repeated domains.

UP000005640_9606_signal

Sequence targeting proteins to the secretory pathway or periplasmic space.

UP000005640_9606_site

Any interesting single amino acid site on the sequence.

UP000005640_9606_topodomain

Location of non-membrane regions of membrane-spanning proteins.

UP000005640_9606_transit

Extent of a transit peptide for organelle targeting.

UP000005640_9606_transmem

Extent of a membrane-spanning region.

UP000005640_9606_variants

A natural variant in the protein.

UP000005640_9606_zn_fing

Position(s) and type(s) of zinc fingers within the protein.


Credits

UniProt is a collaboration between the EMBL-European Bioinformatics Institute (EMBL-EBI),
the SIB Swiss Institute of Bioinformatics and the Protein Information Resource (PIR).

UniProt is mainly supported by the National Institutes of Health (NIH) grant U41HG007822.
Additional support for the EMBL-EBI's involvement in UniProt comes from European Molecular Biology Laboratory (EMBL),
the British Heart Foundation (BHF) (RG/13/5/30112), the Parkinson's Disease United Kingdom (PDUK) GO grant G-1307,
and the NIH GO grant U41HG02273. UniProt activities at the SIB are additionally supported by the Swiss Federal
Government through the State Secretariat for Education, Research and Innovation SERI. PIR's UniProt activities
are also supported by the NIH grants R01GM080646, G08LM010720, and P20GM103446, and the National Science Foundation
(NSF) grant DBI-1062520.

help@uniprot.org

References

https://academic.oup.com/nar/article/47/D1/D506/5160987
and
https://onlinelibrary.wiley.com/doi/full/10.1002/humu.23738