Schema for UniProt - UniProt SwissProt/TrEMBL Protein Annotations
  Database: dm6    Primary Table: unipModif Data last updated: 2017-10-10
Big Bed File: /gbdb/dm6/bbi/uniprot/unipModif.bb
Item Count: 6,646
Format description: Browser extensible data (12 fields) plus information about uniProt mutation
fieldexampledescription
chromchr2LChromosome (or contig, scaffold, etc.)
chromStart15729057Start position in chromosome
chromEnd15729060End position in chromosome
namephosName of item
score1000Score from 0-1000
strand-+ or -
thickStart15729057Start of where display should be thick (start codon)
thickEnd15729060End of where display should be thick (stop codon)
reserved200,200,0Used as itemRgb as of 2004-11-22
blockCount1Number of blocks
blockSizes3Comma separated list of block sizes
chromStarts0Start positions relative to chromStart
dbNameManually reviewed (Swiss-Prot)Status
annotationTypemodified residueAnnotation Type
positionamino acid 651 on protein P54733Position
commentsPhosphothreonineComment
uniProtIdP54733UniProt record
pmidsSource articles

Sample Rows
 
chromchromStartchromEndnamescorestrandthickStartthickEndreservedblockCountblockSizeschromStartsdbNameannotationTypepositioncommentsuniProtIdpmids
chr2L1572905715729060phos1000-1572905715729060200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 651 on protein P54733PhosphothreonineP54733
chr2L1573059915730602phos1000-1573059915730602200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 198 on protein P54733PhosphoserineP5473318327897
chr2L1573060815730611phos1000-1573060815730611200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 195 on protein P54733PhosphoserineP5473318327897
chr2L1573061715730620phos1000-1573061715730620200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 192 on protein P54733PhosphoserineP5473318327897
chr2L1573063215730635phos1000-1573063215730635200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 187 on protein P54733PhosphoserineP5473318327897
chr2L1573080615730809phos1000-1573080615730809200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 129 on protein P54733PhosphoserineP5473318327897
chr2L1573763315737636phos1000-1573763315737636200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 117 on protein P54733PhosphoserineP5473318327897
chr2L1573763915737642phos1000-1573763915737642200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 115 on protein P54733PhosphoserineP5473318327897
chr2L1573764215737645phos1000-1573764215737645200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 114 on protein P54733PhosphoserineP5473318327897
chr2L1576766715767670phos1000-1576766715767670200,200,0130Manually reviewed (Swiss-Prot)modified residueamino acid 168 on protein Q9VJN5PhosphoserineQ9VJN518327897

UniProt (uniprot) Track Description
 

Description

This track was produced by the Genome Bioinformatics Group at the UCSC Genomics Institute. It shows protein sequence annotations from the UniProt/SwissProt database, mapped to genomic coordinates. It also shows how the protein sequences in this database map to the genome. The data has been curated from scientific publications by the UniProt/SwissProt staff. The annotations are divided into multiple subtracks, based on their "feature type" in UniProt:

Track Name Description
UCSC Alignment, SwissProt Protein sequences from SwissProt mapped onto the genome. All other tracks are (start,end) annotations mapped using this track.
UCSC Alignment, TrEMBL Protein sequences from TrEMBL mapped onto the genome. All other tracks are (start,end) annotations mapped using this track. This track is hidden by default. To show it, click its checkbox on the track description page.
UniProt Signal Peptides Regions found in proteins destined to be secreted, generally cleaved from mature protein.
UniProt Extracellular Domains Protein domains with the comment "Extracellular".
UniProt Transmembrane Domains Protein domains of the type "Transmembrane".
UniProt Cytoplasmic Domains Protein domains with the comment "Cytoplasmic".
UniProt Polypeptide Chains Polypeptide chain in mature protein after post-processing.
UniProt Domains Protein domains, zinc finger regions and topological domains.
UniProt Disulfide Bonds Disulfide bonds.
UniProt Amino Acid Modifications Glycosylation sites, modified residues and lipid moiety-binding regions.
UniProt Amino Acid Mutations Mutagenesis sites and sequence variants.
UniProt Protein Primary/Secondary Structure Annotations Beta strands, helices, coiled-coil regions and turns.
UniProt Sequence Conflicts Differences between Genbank sequences and the UniProt sequence.
UniProt Repeats Regions of repeated sequence motifs or repeated domains.
UniProt Other Annotations All other annotations

For consistency, the subtrack "UniProt/SwissProt Variants" is a copy of the track "UniProt Variants" in the track group "Phenotype and Literature", or "Variation and Repeats", depending on the assembly.

Display Conventions and Configuration

Genomic locations of UniProt/SwissProt annotations are labeled with a short name for the type of annotation (e.g. "glyco", "disulf bond", "Signal peptide" etc.). A click on them shows the full annotation and provides a link to the UniProt/SwissProt record for more details. TrEMBL annotations are always shown in light blue, except in the Signal Peptides, Extracellular Domains, Transmembrane Domains, and Cytoplamsic domains subtracks.

Mouse over a feature to see the full UniProt annotation comment. For variants, the mouse over will show the full name of the UniProt disease acronym.

The subtracks for domains related to subcellular location are sorted from outside to inside of the cell: Signal peptide, extracellular, transmembrane, and cytoplasmic.

In the "UniProt Modifications" track, lipoification sites are highlighted in dark blue, glycosylation sites in dark green, and phosphorylation in light green.

Duplicate annotations are removed as far as possible: if a TrEMBL annotation has the same genome position and same feature type, comment, disease and mutated amino acids as a SwissProt annotation, it is not shown again. Two annotations mapped through different transcripts but with the same genome coordinates are only shown once.

Methods

UniProt sequences were aligned to UCSC/Gencode transcript sequences first with BLAT, filtered with pslReps (93% query coverage, within top 1% score), lifted to genome positions with pslMap and filtered again. UniProt annotations were obtained from the UniProt XML file. The annotations were then mapped to the genome through the alignment using the pslMap program. This mapping approach draws heavily on the LS-SNP pipeline by Mark Diekhans. For human and mouse, the alignments were filtered by retaining only proteins annotated with a given transcript in the Genome Browser table kgXref. Like all Genome Browser source code, the main script used to build this track can be found on github.

Data Access

The raw data can be explored interactively with the Table Browser, or the Data Integrator. For automated analysis, the genome annotation is stored in a bigBed file that can be downloaded from the download server. The exact filenames can be found in the track configuration file. Annotations can be converted to ASCII text by our tool bigBedToBed which can be compiled from the source code or downloaded as a precompiled binary for your system. Instructions for downloading source code and binaries can be found here. The tool can also be used to obtain only features within a given range, for example:
bigBedToBed http://hgdownload.soe.ucsc.edu/gbdb/dm6/uniprot/unipStruct.bb -chrom=chr6 -start=0 -end=1000000 stdout
This track is updated every month. The MySQL table hgFixed.trackVersion contains the name of the currently available data on the website. Older versions of the data files can be downloaded from the archive folder of our downloads server.
Please refer to our mailing list archives for questions, or our Data Access FAQ for more information.

Credits

This track was created by Maximilian Haeussler at UCSC, with help from Chris Lee, Mark Diekhans and Brian Raney, feedback from the UniProt staff and Alejo Mujica, Regeneron Pharmaceuticals. Thanks to UniProt for making all data available for download.

References

UniProt Consortium. Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res. 2012 Jan;40(Database issue):D71-5. PMID: 22102590; PMC: PMC3245120

Yip YL, Scheib H, Diemand AV, Gattiker A, Famiglietti LM, Gasteiger E, Bairoch A. The Swiss-Prot variant page and the ModSNP database: a resource for sequence and structure information on human protein variants. Hum Mutat. 2004 May;23(5):464-70. PMID: 15108278