Schema for Precurs. Proteins - UniProt Precursor Proteins (before cleavage into protein products)
  Database: wuhCor1    Primary Table: unipCov2FullSeq Data last updated: 2021-03-22
Big Bed File Download: /gbdb/wuhCor1/uniprot/
Item Count: 16
The data is stored in the binary BigBed format.

Format description: Browser extensible data (12 fields), eight fields for bigGenePred support, plus extra fields (dbName-pmids, not used by all UniProt subtracks) with UniProt-specific information
chromNC_045512v2Chromosome (or contig, scaffold, etc.)
chromStart265Start position in chromosome
chromEnd21552End position in chromosome
nameP0DTD1-1Name of item
score1000Score from 0-1000
strand++ or -
thickStart265Start of where display should be thick (start codon)
thickEnd21552End of where display should be thick (stop codon)
reserved12,12,120Used as itemRgb as of 2004-11-22
blockCount2Number of blocks
blockSizes13200,8085Comma separated list of block sizes
chromStarts0,13202Start positions relative to chromStart
name2Alternative/human readable name
cdsStartStatcmplStatus of CDS start annotation (none, unknown, incomplete, or complete)
cdsEndStatcmplStatus of CDS end annotation (none, unknown, incomplete, or complete)
exonFrames0,0Exon frame {0,1,2}, or -1 if no frame for exon
typeswissprotTranscript type
geneNamePrimary identifier for gene
geneName2Alternative/human-readable gene name
geneTypeGene type
accP0DTD1UniProt main accession
uniprotNameR1AB_SARS2UniProt main record name
statusManually reviewed (Swiss-Prot)UniProt status
accListP0DTD1UniProt all accessions
isoIdsUniProt isoform accessions
protFullNamesReplicase polyprotein 1abUniProt protein name
protShortNamespp1abUniProt protein short name
protAltFullNamesORF1ab polyproteinUniProt alternative names
protAltShortNamesUniProt alternative short names
geneNameDuplrepUniProt gene name
geneSynonymsORF1a-1bUniProt gene synonyms
  • Molecule 'Replicase polyprotein 1ab': Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.
  • Molecule 'Host translation inhibitor nsp1': Inhibits host translation by interacting with binds to the host 40S subunit in ribosomal complexes, including the 43S pre-initiation complex and the non-translating 80S ribosome (PubMed:32680882,PubMed:32908316). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:32680882,PubMed:32908316). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:32680882,PubMed:32979938). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316). By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity).
  • Molecule 'Non-structural protein 2': May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.
  • Molecule 'Non-structural protein 3': Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (By similarity). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Prevents also host NF-kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803). Cleaves preferentially ISG15 from substrates in vitro (PubMed:32726803). Can play a role in host ADP-ribosylation by binding ADP-ribose (PubMed:32578982).
  • Molecule 'Non-structural protein 4': Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
  • Molecule '3C-like proteinase': Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481).
  • Molecule 'Non-structural protein 6': Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic (By similarity). Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (By similarity). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938).
  • Molecule 'Non-structural protein 7': Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity).
  • Molecule 'Non-structural protein 8': Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity).
  • Molecule 'Non-structural protein 9': May participate in viral replication by acting as a ssRNA-binding protein.
  • Molecule 'Non-structural protein 10': Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.
  • Molecule 'RNA-directed RNA polymerase': Responsible for replication and transcription of the viral RNA genome.
  • Molecule 'Helicase': Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium (By similarity). Binds to host TBK1 and inhibits TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938).
  • Molecule 'Proofreading exoribonuclease': Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.
  • Molecule 'Uridylate-specific endoribonuclease': Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
  • Molecule '2'-O-methyltransferase': Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.
UniProt function
hgncSymHGNC Gene Symbol
refSeqNC_045512.2RefSeq IDs
refSeqProtYP_009724389.1RefSeq Protein IDs
entrezGene43740578NCBI Entrez Gene
ensGeneEnsembl Gene IDs
ensTransEnsembl Transcript IDs
ensProtEnsembl Protein IDs

Sample Rows
NC_045512v226521552P0DTD1-11000+2652155212,12,120213200,80850,13202cmplcmpl0,0swissprotP0DTD1R1AB_SARS2Manually reviewed (Swiss-Prot)P0DTD1Replicase polyprotein 1abpp1abORF1ab polyproteinrepORF1a-1bMolecule 'Replicase polyprotein 1ab': Multifunctional protein involved in the transcription and replication of viral RNA ...NC_045512.2YP_009724389.143740578
NC_045512v22156225381P0DTC21000+215622538112,12,120138190cmplcmpl0swissprotP0DTC2SPIKE_SARS2Manually reviewed (Swiss-Prot)P0DTC2Spike glycoproteinS glycoproteinE2; Peplomer proteinSORF2Molecule 'Spike protein S1': attaches the virion to the cell membrane by interacting with host receptor, initiating the ...NC_045512.2YP_009724390.143740568
NC_045512v22539226217P0DTC31000+253922621712,12,12018250cmplcmpl0swissprotP0DTC3AP3A_SARS2Manually reviewed (Swiss-Prot)P0DTC3ORF3a proteinORF3aAccessory protein 3a; Protein 3a; Protein U274; Protein X1ORF3aPlays a role in virus egress via lysosomal trafficking (PubMed:33157038, PubMed:33422265). Forms homotetrameric ion chan ...NC_045512.2YP_009724391.143740569
NC_045512v22545625579P0DTG11000+254562557912,12,12011230cmplcmpl0swissprotP0DTG1ORF3C_SARS2Manually reviewed (Swiss-Prot)P0DTG1ORF3c proteinORF3cORF3h proteinORF3hMay play a role in host modulation.
NC_045512v22552325694P0DTG01000+255232569412,12,12011710cmplcmpl0swissprotP0DTG0ORF3D_SARS2Manually reviewed (Swiss-Prot)P0DTG0ORF3d proteinORF3d proteinMay play a role in host modulation.
NC_045512v22624426469P0DTC41000+262442646912,12,12012250cmplcmpl0swissprotP0DTC4VEMP_SARS2Manually reviewed (Swiss-Prot)P0DTC4Envelope small membrane proteinE; sM proteinEORF4Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes formi ...NC_045512.2YP_009724392.143740570
NC_045512v22652227188P0DTC51000+265222718812,12,12016660cmplcmpl0swissprotP0DTC5VME1_SARS2Manually reviewed (Swiss-Prot)P0DTC5Membrane proteinME1 glycoprotein; Matrix glycoprotein; Membrane glycoproteinORFMComponent of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with ...NC_045512.2YP_009724393.143740571
NC_045512v22720127384P0DTC61000+272012738412,12,12011830cmplcmpl0swissprotP0DTC6NS6_SARS2Manually reviewed (Swiss-Prot)P0DTC6ORF6 proteinORF6Accessory protein 6; Non-structural protein 6; Protein X3ns6ORF6Disrupts cell nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane. ...NC_045512.2YP_009724394.143740572
NC_045512v22739327756P0DTC71000+273932775612,12,12013630cmplcmpl0swissprotP0DTC7NS7A_SARS2Manually reviewed (Swiss-Prot)P0DTC7ORF7a proteinORF7aAccessory protein 7a; Protein U122; Protein X4ORF7aPlays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. Acts by binding to BST2 thereby int ...NC_045512.2YP_009724395.143740573
NC_045512v22775527884P0DTD81000+277552788412,12,12011290cmplcmpl0swissprotP0DTD8NS7B_SARS2Manually reviewed (Swiss-Prot)P0DTD8ORF7b proteinORF7bAccessory protein 7bORF7bNC_045512.2YP_009725318.143740574

Precurs. Proteins (unipCov2FullSeq) Track Description


This track shows protein sequence annotations from the UniProt/SwissProt database, mapped to genomic coordinates. The data has been curated from scientific publications by the UniProt/SwissProt staff. The annotations are spread over multiple tracks, 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

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.


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. 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 -chrom=NC_045512v2 -start=0 -end=29903 stdout

Please refer to our mailing list archives for questions or our Data Access FAQ for more information.


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 Phil Berman, UCSC. Thanks to UniProt for making all data available for download.


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