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Entry version 8 (02 Jun 2021)
Sequence version 1 (22 Apr 2020)
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Protein

Spike glycoprotein

Gene

S

Organism
Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32221306, PubMed:32075877, PubMed:32155444).

Binding to host NRP1 and NRP2 via C-terminal polybasic sequence enhances virion entry into host cell (PubMed:33082294, PubMed:33082293).

This interaction may explain virus tropism of human olfactory epithelium cells, which express high level of NRP1 and NRP2 but low level of ACE2 (PubMed:33082293).

The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270).

Uses human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651).

Can be alternatively processed by host furin (PubMed:32362314).

Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.

1 PublicationUniRule annotation8 Publications

mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.

UniRule annotation

Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.

UniRule annotation

May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity.

By similarity

Miscellaneous

Variant D614G has become the most prevalent circulating sequence in the global pandemic since april 2020 (PubMed:32697968). The mutation is associated with higher viral loads produced in cell culture and animal models (PubMed:32697968, PubMed:33106671, PubMed:33184236). It would not change pathogenicity nor neutralization properties vs vaccination (PubMed:33184236). May be prevalent because the mutation increases virus transmission in human population (PubMed:33106671).3 Publications

Caution

Asn-17, Asn-603, Asn-1134, Asn-1158, and Asn-1173 are non glycosylated when S1 or S2 are expressed individually in HEK293 cells.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processFusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host tetherin by virus, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virulence, Virus entry into host cell

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-9694322, Virion Assembly and Release
R-HSA-9694548, Maturation of spike protein
R-HSA-9694614, Attachment and Entry
R-HSA-9694635, Translation of structural proteins

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0DTC2

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P0DTC2

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Spike glycoproteinUniRule annotation
Short name:
S glycoproteinUniRule annotation
Alternative name(s):
E2UniRule annotation
Peplomer proteinUniRule annotation
Cleaved into the following 3 chains:
Spike protein S1UniRule annotation
Spike protein S2UniRule annotation
Spike protein S2'UniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SUniRule annotation
ORF Names:2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSevere acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri2697049 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesNidoviralesCornidovirineaeCoronaviridaeOrthocoronavirinaeBetacoronavirusSarbecovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000464024 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini13 – 1213ExtracellularUniRule annotationAdd BLAST1201
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1214 – 1234HelicalUniRule annotationAdd BLAST21
Topological domaini1235 – 1273CytoplasmicUniRule annotationAdd BLAST39

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi234N → Q: Increased resistance to neutralizing antibodies. 1 Publication1
Mutagenesisi331N → Q: Reduced viral infectivity. 1 Publication1
Mutagenesisi343N → Q: Reduced viral infectivity. 1 Publication1
Mutagenesisi452L → R: Increased resistance to neutralizing antibodies. 1 Publication1
Mutagenesisi475A → V: Increased resistance to neutralizing antibodies. 1 Publication1
Mutagenesisi483V → A: Increased resistance to neutralizing antibodies. 1 Publication1
Mutagenesisi490F → L: Increased resistance to neutralizing antibodies and human covalescent sera neutralization. 1 Publication1
Mutagenesisi493Q → N: Reduced host ACE2-binding affinity in vitro. 1 Publication1
Mutagenesisi493Q → Y: Reduced host ACE2-binding affinity in vitro. 1 Publication1
Mutagenesisi501N → T: Reduced host ACE2-binding affinity in vitro. 1 Publication1
Mutagenesisi519H → P: Increased resistance to human covalescent sera neutralization. 1 Publication1
Mutagenesisi614D → G: Increase of pseudotyped VSV particle production ex vivo. Increase of viral load in hamster upper respiratory tract. Produces more infectious particles when cultured in primary human epithelial cells; increases replication and transmissibility in hamsters and ferrets. 3 Publications1
Mutagenesisi679 – 684NSPRRA → IL: About 50% stronger entry efficiency in Vero E6 cells while 30% weaker entry efficiency in hACE2-expressing BHK cells. 1 Publication6
Mutagenesisi681 – 684PRRA → RRRK: Optimized cleavage by host furin. 1 Publication4
Mutagenesisi682 – 684Missing : Complete loss of cleavage by host furin. 1 Publication3

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB15691, Anti-SARS-CoV-2 REGN-COV2
DB15718, Bamlanivimab
DB15941, Casirivimab
DB15897, Etesevimab
DB15940, Imdevimab

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 12UniRule annotationAdd BLAST12
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000044964613 – 1273Spike glycoproteinAdd BLAST1261
ChainiPRO_000044964713 – 685Spike protein S1UniRule annotationAdd BLAST673
ChainiPRO_0000449648686 – 1273Spike protein S2UniRule annotationAdd BLAST588
ChainiPRO_0000449649816 – 1273Spike protein S2'UniRule annotationAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi15 ↔ 136PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi17N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation2 Publications1
Glycosylationi61N-linked (GlcNAc...) (hybrid) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi74N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi122N-linked (GlcNAc...) (hybrid) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi131 ↔ 166PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi149N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi165N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi234N-linked (GlcNAc...) (high mannose) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi282N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi291 ↔ 301PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi323O-linked (GalNAc) threonine; by host1 Publication1
Glycosylationi325O-linked (HexNAc...) serine; by host1 Publication1
Glycosylationi331N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi336 ↔ 361PROSITE-ProRule annotation2 Publications
Glycosylationi343N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi379 ↔ 432PROSITE-ProRule annotation2 Publications
Disulfide bondi391 ↔ 525PROSITE-ProRule annotationCombined sources4 Publications
Disulfide bondi480 ↔ 4881 Publication
Disulfide bondi538 ↔ 590Combined sources1 Publication
Glycosylationi603N-linked (GlcNAc...) (hybrid) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi616N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi617 ↔ 649Combined sources1 Publication
Glycosylationi657N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi662 ↔ 671Combined sources1 Publication
Glycosylationi709N-linked (GlcNAc...) (high mannose) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi717N-linked (GlcNAc...) (hybrid) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi738 ↔ 760Combined sources1 Publication
Disulfide bondi743 ↔ 749Combined sources1 Publication
Glycosylationi801N-linked (GlcNAc...) (hybrid) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi840 ↔ 851UniRule annotation
Disulfide bondi1032 ↔ 1043Combined sources1 Publication
Glycosylationi1074N-linked (GlcNAc...) (hybrid) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi1082 ↔ 1126Combined sources1 Publication
Glycosylationi1098N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi1134N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi1158N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation2 Publications1
Glycosylationi1173N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation2 Publications1
Glycosylationi1194N-linked (GlcNAc...) (complex) asparagine; by hostUniRule annotation3 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.UniRule annotation
Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host CTSL, TMPRSS2 or furin to yield the mature S1 and S2 proteins (PubMed:32155444). CTSL cleavage would occur in endosomes (PubMed:32221306, PubMed:33465165). TMPRSS2 cleavage would occur at the cell surface, allowing the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). In addition, a second cleavage results in the release of a fusion peptide upon viral binding to the host cell receptor (By similarity). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165).UniRule annotation4 Publications
Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32366695, PubMed:32363391, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei685 – 686Cleavage; by TMPRSS2 or furinUniRule annotation2 Publications2
Sitei815 – 816Cleavage; by hostUniRule annotation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2838, 153 N-Linked glycans (18 sites), 4 O-Linked glycans (2 sites)
2839, 66 N-Linked glycans (20 sites)
2840, 109 N-Linked glycans (22 sites)
2951, 2 O-Linked glycans (6 sites)
2952, 2 O-Linked glycans (18 sites)
2953, 2 O-Linked glycans (13 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P0DTC2, 24 sites, 172 N-linked glycans (22 sites), 4 O-linked glycans (2 sites)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer; each monomer consists of a S1 and a S2 subunit (PubMed:32075877, PubMed:32155444, PubMed:32245784). The resulting peplomers protrude from the virus surface as spikes (PubMed:32979942).

Interacts with ORF3a protein and ORF7a protein (By similarity) (PubMed:32075877, PubMed:32155444, PubMed:32245784, PubMed:32979942). There are an average of 26 +/-15 spike trimers at the surface of virion particles (PubMed:32979942).

UniRule annotation4 Publications

Binds to host ACE2 (PubMed:32221306, PubMed:33607086, PubMed:32075877, PubMed:32132184, PubMed:32155444, PubMed:32225175, PubMed:32225176). RBD also interacts with the N-linked glycan on Asn90 of ACE2 (PubMed:33607086). Cleavage of S generates a polybasic C-terminal sequence on S1 that binds to host Neuropilin-1 (NRP1) and Neuropilin-2 (NRP2) receptors (PubMed:33082294, PubMed:33082293).

Interacts with host integrin alpha-5/beta-1 (ITGA5:ITGB1) and with ACE2 in complex with integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:33102950). May interact via cytoplasmic c-terminus with M protein (PubMed:33229438).

11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4383848, 633 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-5682, SARS-CoV-2 Spike protein complex

Protein interaction database and analysis system

More...
IntActi
P0DTC2, 48 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

More...
SASBDBi
P0DTC2

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0DTC2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini13 – 303BetaCoV S1-NTDPROSITE-ProRule annotationAdd BLAST291
Domaini334 – 527BetaCoV S1-CTDPROSITE-ProRule annotation1 PublicationAdd BLAST194

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni319 – 541Receptor-binding domain (RBD)1 PublicationAdd BLAST223
Regioni403 – 405Integrin-binding motif;1 Publication3
Regioni437 – 508Receptor-binding motif; binding to human ACE2By similarityAdd BLAST72
Regioni816 – 837Fusion peptide 1UniRule annotationAdd BLAST22
Regioni835 – 855Fusion peptide 2UniRule annotationAdd BLAST21
Regioni920 – 970Heptad repeat 1UniRule annotationAdd BLAST51
Regioni1163 – 1202Heptad repeat 2UniRule annotationAdd BLAST40

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili949 – 993UniRule annotationAdd BLAST45
Coiled coili1176 – 1203UniRule annotationAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1269 – 1273KxHxxUniRule annotation5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The KxHxx motif seems to function as an ER retrieval and binds COPI in vitro.By similarity
Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function cooperatively and have a membrane-ordering effect on lipid headgroups and shallow hydrophobic regions of target bilayers. They are considered as two domains of an extended, bipartite FP. The membrane-ordering activity is calcium-dependent and also dependent on correct folding, which is maintained by an internal disulfide bond in FP2.UniRule annotation

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the betacoronaviruses spike protein family.UniRule annotation

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd21480, SARS-CoV-2_Spike_S1_RBD, 1 hit
cd21624, SARS-CoV-like_Spike_S1_NTD, 1 hit

Database of protein disorder

More...
DisProti
DP02772

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.5.790, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_04099, BETA_CORONA_SPIKE, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032500, bCoV_S1_N
IPR042578, BETA_CORONA_SPIKE
IPR043607, CoV_S1_C
IPR043473, S2_sf_CoV
IPR027400, S_HR2_CoV
IPR036326, Spike_rcpt-bd_sf_CoV
IPR044341, Spike_S1_N_SARS-CoV-like
IPR018548, Spike_S1_RBD_bCoV
IPR044366, Spike_S1_RBD_SARS-CoV-2
IPR002552, Spike_S2_CoV

Pfam protein domain database

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Pfami
View protein in Pfam
PF16451, bCoV_S1_N, 1 hit
PF09408, bCoV_S1_RBD, 1 hit
PF19209, CoV_S1_C, 1 hit
PF01601, CoV_S2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF111474, SSF111474, 2 hits
SSF143587, SSF143587, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51921, BCOV_S1_CTD, 1 hit
PS51922, BCOV_S1_NTD, 1 hit
PS51923, COV_S2_HR1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0DTC2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFVFLVLLPL VSSQCVNLTT RTQLPPAYTN SFTRGVYYPD KVFRSSVLHS
60 70 80 90 100
TQDLFLPFFS NVTWFHAIHV SGTNGTKRFD NPVLPFNDGV YFASTEKSNI
110 120 130 140 150
IRGWIFGTTL DSKTQSLLIV NNATNVVIKV CEFQFCNDPF LGVYYHKNNK
160 170 180 190 200
SWMESEFRVY SSANNCTFEY VSQPFLMDLE GKQGNFKNLR EFVFKNIDGY
210 220 230 240 250
FKIYSKHTPI NLVRDLPQGF SALEPLVDLP IGINITRFQT LLALHRSYLT
260 270 280 290 300
PGDSSSGWTA GAAAYYVGYL QPRTFLLKYN ENGTITDAVD CALDPLSETK
310 320 330 340 350
CTLKSFTVEK GIYQTSNFRV QPTESIVRFP NITNLCPFGE VFNATRFASV
360 370 380 390 400
YAWNRKRISN CVADYSVLYN SASFSTFKCY GVSPTKLNDL CFTNVYADSF
410 420 430 440 450
VIRGDEVRQI APGQTGKIAD YNYKLPDDFT GCVIAWNSNN LDSKVGGNYN
460 470 480 490 500
YLYRLFRKSN LKPFERDIST EIYQAGSTPC NGVEGFNCYF PLQSYGFQPT
510 520 530 540 550
NGVGYQPYRV VVLSFELLHA PATVCGPKKS TNLVKNKCVN FNFNGLTGTG
560 570 580 590 600
VLTESNKKFL PFQQFGRDIA DTTDAVRDPQ TLEILDITPC SFGGVSVITP
610 620 630 640 650
GTNTSNQVAV LYQDVNCTEV PVAIHADQLT PTWRVYSTGS NVFQTRAGCL
660 670 680 690 700
IGAEHVNNSY ECDIPIGAGI CASYQTQTNS PRRARSVASQ SIIAYTMSLG
710 720 730 740 750
AENSVAYSNN SIAIPTNFTI SVTTEILPVS MTKTSVDCTM YICGDSTECS
760 770 780 790 800
NLLLQYGSFC TQLNRALTGI AVEQDKNTQE VFAQVKQIYK TPPIKDFGGF
810 820 830 840 850
NFSQILPDPS KPSKRSFIED LLFNKVTLAD AGFIKQYGDC LGDIAARDLI
860 870 880 890 900
CAQKFNGLTV LPPLLTDEMI AQYTSALLAG TITSGWTFGA GAALQIPFAM
910 920 930 940 950
QMAYRFNGIG VTQNVLYENQ KLIANQFNSA IGKIQDSLSS TASALGKLQD
960 970 980 990 1000
VVNQNAQALN TLVKQLSSNF GAISSVLNDI LSRLDKVEAE VQIDRLITGR
1010 1020 1030 1040 1050
LQSLQTYVTQ QLIRAAEIRA SANLAATKMS ECVLGQSKRV DFCGKGYHLM
1060 1070 1080 1090 1100
SFPQSAPHGV VFLHVTYVPA QEKNFTTAPA ICHDGKAHFP REGVFVSNGT
1110 1120 1130 1140 1150
HWFVTQRNFY EPQIITTDNT FVSGNCDVVI GIVNNTVYDP LQPELDSFKE
1160 1170 1180 1190 1200
ELDKYFKNHT SPDVDLGDIS GINASVVNIQ KEIDRLNEVA KNLNESLIDL
1210 1220 1230 1240 1250
QELGKYEQYI KWPWYIWLGF IAGLIAIVMV TIMLCCMTSC CSCLKGCCSC
1260 1270
GSCCKFDEDD SEPVLKGVKL HYT
Length:1,273
Mass (Da):141,178
Last modified:April 22, 2020 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB17BE6D9F1C4EA34
GO

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Variant B.1.1.7 belongs to a lineage isolated first in United Kingdom (Dec 2020). It is also called Variant Of Concern (VOC) 202012/01, Variant Under Investigation (VUI) 202012/01, 501Y.V1 or 20B/501Y.V1.1 Publication
Variant 501Y.V2 belongs to a lineage first isolated in South Africa (Dec 2020) is also called B 1.351.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti5L → F in strain: B.1.526. Curated1
Natural varianti13S → I in strain: B.1.429. Curated1
Natural varianti18L → F in strain: B.1.351, P1, 19B/501Y. Curated1
Natural varianti20T → N in strain: P1. Curated1
Natural varianti26P → S in strain: P1. Curated1
Natural varianti52Q → R in strain: B.1.525. Curated1
Natural varianti69 – 70Missing in strain: B.1.1.7, 19B/501T. Curated2
Natural varianti80D → A in strain: B.1.351. 1 Publication1
Natural varianti95T → I in strain: B.1.526, B.1.1.318. Curated1
Natural varianti102R → I in strain: A23.1. Curated1
Natural varianti138D → Y in strain: P1. Curated1
Natural varianti144Missing in strain: B.1.1.7, B.1.1.318. Curated1
Natural varianti152W → C Frequently in strain B.1.429. Curated1
Natural varianti157F → L in strain: A23.1. Curated1
Natural varianti190R → S in strain: P1. Curated1
Natural varianti215D → G in strain: B.1.351. 1 Publication1
Natural varianti222A → V in strain: 20A.EU1. Curated1
Natural varianti253D → G in strain: B.1.526. Curated1
Natural varianti417K → N in strain: B.1.351, P1; May enhance affinity to human ACE2 receptor. 1 Publication1
Natural varianti417K → T in strain: P1. Curated1
Natural varianti452L → R in strain: B.1.429, 19B/501Y. Curated1
Natural varianti477S → N in strain: 20A.EU2, B.1.526. Curated1
Natural varianti484E → K in strain: B.1.351, B.1.525, B.1.526, B.1.1.318, P1, P2; May enhance affinity to human ACE2 receptor. Curated1
Natural varianti501N → T in strain: 19B/501T. Curated1
Natural varianti501N → Y in strain: B.1.1.7, B.1.351, P1,19B/501Y; May enhance affinity to human ACE2 receptor. Curated1 Publication1
Natural varianti570A → D in strain: B.1.1.7. 1 Publication1
Natural varianti613Q → H in strain: A23.1. Curated1
Natural varianti614D → G in strain B.1.1.7, B.1.351, B.1.429, B.1.526, B.1.1.318, P1, P2, 20A.EU1, 20A.EU2; common variant; binds to hACE2 more efficiently; produces more infectious particles when cultured in primary human epithelial cells; does not significantly shift SARS-CoV-2 neutralization properties. Curated1
Natural varianti653A → V in strain: 19B/501Y. Curated1
Natural varianti655H → Y in strain: P1, 19B/501T, 19B/501Y. Curated1
Natural varianti677Q → H in strain: B.1.525. Curated1
Natural varianti681P → H in strain: B.1.1.7, B.1.1.318, A23.1. 1 Publication1
Natural varianti701A → V in strain: B.1.351, B.1.526. Curated1
Natural varianti716T → I in strain: B.1.1.7. 1 Publication1
Natural varianti796D → H in strain: B.1.1.318. Curated1
Natural varianti796D → Y in strain: 19B/501Y. Curated1
Natural varianti888F → L in strain: B.1.525. Curated1
Natural varianti982S → A in strain: B.1.1.7. 1 Publication1
Natural varianti1027T → I in strain: P1. Curated1
Natural varianti1118D → H in strain: B.1.1.7. 1 Publication1
Natural varianti1176V → F in strain: P1, P2. Curated1
Natural varianti1219G → V in strain: 19B/501Y. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
MN908947 Genomic RNA Translation: QHD43416.1

NCBI Reference Sequences

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RefSeqi
YP_009724390.1, NC_045512.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
43740568

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:43740568

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MN908947 Genomic RNA Translation: QHD43416.1
RefSeqiYP_009724390.1, NC_045512.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6LVNX-ray2.47A/B/C/D1168-1203[»]
6LXTX-ray2.90A/B/C/D/E/F910-988[»]
A/B/C/D/E/F1162-1206[»]
6LZGX-ray2.50B319-527[»]
6M0JX-ray2.45E319-541[»]
6M17electron microscopy2.90E/F319-541[»]
6M1VX-ray1.50A917-966[»]
6VSBelectron microscopy3.46A/B/C1-1208[»]
6VW1X-ray2.68E/F455-518[»]
6VXXelectron microscopy2.80A/B/C14-1211[»]
6VYBelectron microscopy3.20A/B/C14-1211[»]
6W41X-ray3.08C319-541[»]
6WPSelectron microscopy3.10A/B/E11-1211[»]
6WPTelectron microscopy3.70A/B/C11-1211[»]
6X29electron microscopy2.70A/B/C16-1208[»]
6X2Aelectron microscopy3.30A/B/C16-1208[»]
6X2Belectron microscopy3.60A/B/C16-1208[»]
6X2Celectron microscopy3.20A/B/C16-1208[»]
6X6Pelectron microscopy3.22A/B/C15-1208[»]
6X79electron microscopy2.90A/B/C14-1211[»]
6XC2X-ray3.11A/Z319-541[»]
6XC3X-ray2.70C319-541[»]
6XC4X-ray2.34A/Z319-541[»]
6XC7X-ray2.88A319-541[»]
6XCMelectron microscopy3.42A/B/C1-1213[»]
6XCNelectron microscopy3.66A/C/E1-1213[»]
6XDGelectron microscopy3.90E319-541[»]
6XE1X-ray2.75E319-591[»]
6XEYelectron microscopy3.25A/B/C1-1208[»]
6XF5electron microscopy3.45A/B/C14-1208[»]
6XF6electron microscopy4.00A/B/C14-1208[»]
6XKLelectron microscopy3.21A/B/C1-1208[»]
6XKPX-ray2.72A/B319-541[»]
6XKQX-ray2.55A319-541[»]
6XLUelectron microscopy2.40A/B/C14-1208[»]
6XM0electron microscopy2.70A/B/C14-1208[»]
6XM3electron microscopy2.90A/B/C14-1208[»]
6XM4electron microscopy2.90A/B/C14-1208[»]
6XM5electron microscopy3.10A/B/C14-1208[»]
6XR8electron microscopy2.90A/B/C1-1273[»]
6XRAelectron microscopy3.00A/B/C1-1273[»]
6XS6electron microscopy3.70A/B/C1-1213[»]
6YLAX-ray2.42A/E330-532[»]
6YM0X-ray4.36E330-532[»]
6YORelectron microscopy3.30A/E330-532[»]
6YZ5X-ray1.80E330-532[»]
6YZ7X-ray3.30AAA/EEE330-532[»]
6Z2MX-ray2.71A/E332-528[»]
6Z43electron microscopy3.30A/B/C1-1208[»]
6Z97electron microscopy3.40A/B/C1-1208[»]
6ZB4electron microscopy3.03A/B/C1-1213[»]
6ZB5electron microscopy2.85A/B/C1-1213[»]
6ZBPX-ray1.85EEE330-532[»]
6ZCZX-ray2.65E333-528[»]
6ZDGelectron microscopy4.70A/D/E333-526[»]
6ZDHelectron microscopy3.70A/B/C1-1208[»]
6ZERX-ray3.80A/D/E330-532[»]
6ZFOelectron microscopy4.40A/E333-526[»]
6ZGEelectron microscopy2.60A/B/C1-1208[»]
6ZGGelectron microscopy3.80A/B/C1-1208[»]
6ZGIelectron microscopy2.90A/B/C1-1208[»]
6ZH9X-ray3.31EEE332-528[»]
6ZHDelectron microscopy3.70A/B/C1-1208[»]
6ZLRX-ray3.10AAA/DDD/EEE319-541[»]
6ZOWelectron microscopy3.00A/B/C/a1-1273[»]
6ZOXelectron microscopy3.00A/B/C14-1211[»]
6ZOYelectron microscopy3.10A/B/C14-1211[»]
6ZOZelectron microscopy3.50A/B/C14-1211[»]
6ZP0electron microscopy3.00A/B/C14-1211[»]
6ZP1electron microscopy3.30A/B/C14-1211[»]
6ZP2electron microscopy3.10A/B/C14-1211[»]
6ZP5electron microscopy3.10A/B/C1-1273[»]
6ZP7electron microscopy3.30A/B/C1-1273[»]
6ZWVelectron microscopy3.50A/B/C1-1273[»]
6ZXNelectron microscopy2.93A/B/C1-1208[»]
7A25electron microscopy3.06A/B/C1-1146[»]
7A29electron microscopy2.94A/B/C1-1208[»]
7A4Nelectron microscopy2.75A/B/C1-1208[»]
7A5Relectron microscopy3.70A/B1-1208[»]
7A5Selectron microscopy3.90A/B1-1208[»]
7A91electron microscopy3.60A1-685[»]
7A92electron microscopy4.20A1-676[»]
7A93electron microscopy5.90A/B/C1-1208[»]
7A94electron microscopy3.90A/B/C1-1208[»]
7A95electron microscopy4.30A/B/C1-1208[»]
7A96electron microscopy4.80A/B/C1-1208[»]
7A97electron microscopy4.40A/B/C1-1208[»]
7A98electron microscopy5.40A/B/C1-1208[»]
7AD1electron microscopy2.92A/B/C1-1208[»]
7B17electron microscopy4.01A334-528[»]
7BEHX-ray2.30E333-528[»]
7BEIX-ray2.30E333-528[»]
7BEJX-ray2.42E333-528[»]
7BEKX-ray2.04E333-528[»]
7BELX-ray2.53R/X333-528[»]
7BEMX-ray2.52E333-528[»]
7BENX-ray2.50C/E333-528[»]
7BEOX-ray3.19R/X333-528[»]
7BEPX-ray2.61C/E333-528[»]
7BWJX-ray2.85E319-529[»]
7BYRelectron microscopy3.84A/B/C1-1208[»]
7BZ5X-ray1.84A319-541[»]
7C01X-ray2.88A/B319-541[»]
7C2Lelectron microscopy3.10A/B/C1-1273[»]
7C8Delectron microscopy3.00B333-527[»]
7C8JX-ray3.18B333-527[»]
7C8VX-ray2.15B330-531[»]
7C8WX-ray2.77B330-531[»]
7CABelectron microscopy3.52A/B/C1-1208[»]
7CACelectron microscopy3.55A/B/C1-1208[»]
7CAHelectron microscopy3.90A334-527[»]
7CAIelectron microscopy3.49A/B/C1-1208[»]
7CAKelectron microscopy3.58A/B/C1-1208[»]
7CANX-ray2.94B330-531[»]
7CDIX-ray2.96E319-529[»]
7CDJX-ray3.40E319-529[»]
7CH4X-ray3.15R319-541[»]
7CH5X-ray2.70R319-541[»]
7CHBX-ray2.40R319-541[»]
7CHCX-ray2.71R319-541[»]
7CHEX-ray3.42R319-541[»]
7CHFX-ray2.67R319-541[»]
7CHHelectron microscopy3.49A/B/C1-1208[»]
7CJFX-ray2.11C334-527[»]
7CM4X-ray2.71A319-536[»]
7CN9electron microscopy4.70A/B/C14-1140[»]
7CT5electron microscopy4.00A/B/C1-1273[»]
7CWLelectron microscopy3.80A/B/C1-1273[»]
7CWMelectron microscopy3.60A/B/C1-1273[»]
7CWNelectron microscopy3.20A/B/C1-1273[»]
7CWOelectron microscopy3.90A1-1273[»]
7CWSelectron microscopy3.40O/Q/R14-1147[»]
7CWUelectron microscopy3.50A/B/C1-1273[»]
7D2ZX-ray1.97B330-531[»]
7D30X-ray2.10B330-531[»]
7DCCelectron microscopy4.30E/I/K1-1208[»]
7DCXelectron microscopy5.90C/D/K1-1208[»]
7DD2electron microscopy5.60C/D/K1-1208[»]
7DD8electron microscopy7.50C/D/E1-1208[»]
7DDDelectron microscopy3.00A/B/C1-1208[»]
7DDNelectron microscopy6.30A/B/C1-1208[»]
7DF3electron microscopy2.70A/B/C1-1208[»]
7DF4electron microscopy3.80B/C/D1-1208[»]
7DK3electron microscopy6.00A/B/C1-1208[»]
7DK4electron microscopy3.80A/B/C1-1208[»]
7DK5electron microscopy13.50A/B/C1-1208[»]
7DK6electron microscopy4.30A/B/C1-1208[»]
7DK7electron microscopy9.70A/B/C1-1208[»]
7DMUX-ray3.20B/D319-531[»]
7DPMX-ray3.30C/F/I/L319-541[»]
7JJCX-ray2.36E/F/G/H679-685[»]
7JJIelectron microscopy3.60A/B/C1-1273[»]
7JJJelectron microscopy4.50A/B/C/D/E/F1-1273[»]
7JMOX-ray2.36A319-541[»]
7JMPX-ray1.71A319-541[»]
7JMWX-ray2.89A319-541[»]
7JV2electron microscopy3.50A14-1211[»]
7JV4electron microscopy3.40A/B/C14-1211[»]
7JV6electron microscopy3.00A/B/E14-1211[»]
7JVAelectron microscopy3.60A14-1211[»]
7JVBX-ray3.29A/B319-541[»]
7JVCelectron microscopy3.30A/B/E14-1211[»]
7JW0electron microscopy4.30A/B/E14-1211[»]
7JWBelectron microscopy6.00A/B/C1-1208[»]
7JWYelectron microscopy2.50A/B/C14-1208[»]
7JX3X-ray2.65R328-531[»]
7JZLelectron microscopy2.70A/B/C1-1208[»]
7JZMelectron microscopy3.50B1-1208[»]
7JZNelectron microscopy3.10A/B/C1-1208[»]
7JZUelectron microscopy3.10B1-1208[»]
7K43electron microscopy2.60A/B/E14-1211[»]
7K45electron microscopy3.70B1-1208[»]
7K4Nelectron microscopy3.30A/B/E1-1208[»]
7K8MX-ray3.20E331-517[»]
7K8Selectron microscopy3.40A/B/C1-1213[»]
7K8Telectron microscopy3.40A/B/C1-1213[»]
7K8Uelectron microscopy3.80A/B/C1-1213[»]
7K8Velectron microscopy3.80A/B/C1-1213[»]
7K8Welectron microscopy3.60A/B/G1-1213[»]
7K8Xelectron microscopy3.90A/B/C1-1213[»]
7K8Yelectron microscopy4.40B/D/E1-1213[»]
7K8Zelectron microscopy3.50A/B/C1-1213[»]
7K90electron microscopy3.24A/B/C1-1208[»]
7K9ZX-ray2.95E319-541[»]
7KDGelectron microscopy3.01A/B/C1-1208[»]
7KDHelectron microscopy3.33A/B/C1-1208[»]
7KDIelectron microscopy3.26A/B/C1-1208[»]
7KDJelectron microscopy3.49A/B/C1-1208[»]
7KDKelectron microscopy2.80A/B/C1-1208[»]
7KDLelectron microscopy2.96A/B/C1-1208[»]
7KE4electron microscopy3.21A/B/C1-1208[»]
7KE6electron microscopy3.10A/B/C1-1208[»]
7KE7electron microscopy3.32A/B/C1-1208[»]
7KE8electron microscopy3.26A/B/C1-1208[»]
7KE9electron microscopy3.08A/B/C1-1208[»]
7KEAelectron microscopy3.33A/B/C1-1208[»]
7KEBelectron microscopy3.48A/B/C1-1208[»]
7KECelectron microscopy3.84A/B/C1-1208[»]
7KGJX-ray2.30A333-528[»]
7KGKX-ray2.60A333-527[»]
7KJ2electron microscopy3.60A/B/C14-1208[»]
7KJ3electron microscopy3.70A/B/C14-1208[»]
7KJ4electron microscopy3.40A/B/C14-1208[»]
7KJ5electron microscopy3.60A/B/C14-1208[»]
7KKKelectron microscopy3.03A/C/E1-1208[»]
7KKLelectron microscopy2.85A/C/D1-1208[»]
7KL9electron microscopy4.10A/B/C1-1208[»]
7KLGX-ray3.20A/B328-528[»]
7KLHX-ray3.00A/B328-528[»]
7KLWX-ray2.60A334-527[»]
7KMBelectron microscopy3.39G16-1208[»]
7KMGX-ray2.16C/F329-527[»]
7KMHX-ray1.72C329-527[»]
7KMIX-ray1.73C329-527[»]
7KMKelectron microscopy4.20A/B/C1-1211[»]
7KMLelectron microscopy3.80A/B/C1-1211[»]
7KMSelectron microscopy3.64A/B/C1-1208[»]
7KMZelectron microscopy3.62A/B/C1-1208[»]
7KN5X-ray1.87A/B319-541[»]
7KN6X-ray2.55A319-541[»]
7KN7X-ray2.73A319-541[»]
7KNBelectron microscopy3.93A/B/C1-1208[»]
7KNEelectron microscopy3.85A/B/C1-1208[»]
7KNHelectron microscopy3.74A/B/C1-1208[»]
7KNIelectron microscopy3.91A/B/C1-1208[»]
7KS9electron microscopy4.75A/B/C1-1208[»]
7KSGelectron microscopy3.33A/B/C1-1208[»]
7KXJelectron microscopy6.40A/B/C1-1211[»]
7KXKelectron microscopy5.00A/B/C1-1211[»]
7KZBX-ray2.83C333-528[»]
7L02electron microscopy3.20A/B/C27-1147[»]
7L06electron microscopy3.30A/B/C27-1147[»]
7L09electron microscopy3.10A/B/C27-1147[»]
7L0NX-ray2.78R/S328-531[»]
7L2CX-ray3.65A/B1-334[»]
7L3Nelectron microscopy3.27A/B/C13-1208[»]
7L5BX-ray3.18A319-537[»]
7L7Felectron microscopy3.24E/F323-528[»]
7L7Kelectron microscopy3.29A/B/C1-1273[»]
7LCNelectron microscopy3.35A/C/K27-1147[»]
7LD1electron microscopy3.40A/B/C27-1147[»]
7LOPX-ray2.25A/Z319-541[»]
7ND3electron microscopy3.70A/B/C1-1208[»]
7ND4electron microscopy3.60A/B/C1-1208[»]
7ND5electron microscopy3.40A/B/C1-1208[»]
7ND6electron microscopy7.30A/B/C1-1208[»]
7ND7electron microscopy3.60A/B/C1-1208[»]
7ND8electron microscopy3.50A/B/C1-1208[»]
7ND9electron microscopy2.80A/B/C1-1208[»]
7NDAelectron microscopy3.30A/B/C1-1208[»]
7NDBelectron microscopy4.60A/B/C1-1208[»]
7NDCelectron microscopy4.10A/B/C1-1208[»]
7NDDelectron microscopy4.20A/B/C1-1208[»]
7NEHX-ray1.77E333-528[»]
SASBDBiP0DTC2
SMRiP0DTC2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4383848, 633 interactors
ComplexPortaliCPX-5682, SARS-CoV-2 Spike protein complex
IntActiP0DTC2, 48 interactors

Chemistry databases

DrugBankiDB15691, Anti-SARS-CoV-2 REGN-COV2
DB15718, Bamlanivimab
DB15941, Casirivimab
DB15897, Etesevimab
DB15940, Imdevimab

PTM databases

GlyConnecti2838, 153 N-Linked glycans (18 sites), 4 O-Linked glycans (2 sites)
2839, 66 N-Linked glycans (20 sites)
2840, 109 N-Linked glycans (22 sites)
2951, 2 O-Linked glycans (6 sites)
2952, 2 O-Linked glycans (18 sites)
2953, 2 O-Linked glycans (13 sites)
GlyGeniP0DTC2, 24 sites, 172 N-linked glycans (22 sites), 4 O-linked glycans (2 sites)

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P0DTC2, 662 sequenced antibodies

The DNASU plasmid repository

More...
DNASUi
43740568

Genome annotation databases

GeneIDi43740568
KEGGivg:43740568

Enzyme and pathway databases

ReactomeiR-HSA-9694322, Virion Assembly and Release
R-HSA-9694548, Maturation of spike protein
R-HSA-9694614, Attachment and Entry
R-HSA-9694635, Translation of structural proteins
SABIO-RKiP0DTC2
SIGNORiP0DTC2

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0DTC2

Family and domain databases

CDDicd21480, SARS-CoV-2_Spike_S1_RBD, 1 hit
cd21624, SARS-CoV-like_Spike_S1_NTD, 1 hit
DisProtiDP02772
Gene3Di1.20.5.790, 1 hit
HAMAPiMF_04099, BETA_CORONA_SPIKE, 1 hit
InterProiView protein in InterPro
IPR032500, bCoV_S1_N
IPR042578, BETA_CORONA_SPIKE
IPR043607, CoV_S1_C
IPR043473, S2_sf_CoV
IPR027400, S_HR2_CoV
IPR036326, Spike_rcpt-bd_sf_CoV
IPR044341, Spike_S1_N_SARS-CoV-like
IPR018548, Spike_S1_RBD_bCoV
IPR044366, Spike_S1_RBD_SARS-CoV-2
IPR002552, Spike_S2_CoV
PfamiView protein in Pfam
PF16451, bCoV_S1_N, 1 hit
PF09408, bCoV_S1_RBD, 1 hit
PF19209, CoV_S1_C, 1 hit
PF01601, CoV_S2, 1 hit
SUPFAMiSSF111474, SSF111474, 2 hits
SSF143587, SSF143587, 1 hit
PROSITEiView protein in PROSITE
PS51921, BCOV_S1_CTD, 1 hit
PS51922, BCOV_S1_NTD, 1 hit
PS51923, COV_S2_HR1, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSPIKE_SARS2
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0DTC2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 22, 2020
Last sequence update: April 22, 2020
Last modified: June 2, 2021
This is version 8 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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