Nucleoprotein

<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

<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

• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Biochemical characterization of SARS-CoV-2 nucleocapsid protein."
    Zeng W., Liu G., Ma H., Zhao D., Yang Y., Liu M., Mohammed A., Zhao C., Yang Y., Xie J., Ding C., Ma X., Weng J., Gao Y., He H., Jin T.
    Biochem Biophys Res Commun 527:618-623(2020) [PubMed] [Europe PMC] [Abstract]
  • "Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein."
    Ye Q., West A.M.V., Silletti S., Corbett K.D.
    Protein Sci 29:1890-1901(2020) [PubMed] [Europe PMC] [Abstract]
  • "Virus-Host Interactome and Proteomic Survey Reveal Potential Virulence Factors Influencing SARS-CoV-2 Pathogenesis."
    Li J., Guo M., Tian X., Wang X., Yang X., Wu P., Liu C., Xiao Z., Qu Y., Yin Y., Wang C., Zhang Y., Zhu Z., Liu Z., Peng C., Zhu T., Liang Q.
    Med (N Y) 2:99-112.e7(2021) [PubMed] [Europe PMC] [Abstract]
  • "Liquid-liquid phase separation by SARS-CoV-2 nucleocapsid protein and RNA."
    Chen H., Cui Y., Han X., Hu W., Sun M., Zhang Y., Wang P.H., Song G., Chen W., Lou J.
    Cell Res 30:1143-1145(2020) [PubMed] [Europe PMC] [Abstract]
  • "High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2."
    Zinzula L., Basquin J., Bohn S., Beck F., Klumpe S., Pfeifer G., Nagy I., Bracher A., Hartl F.U., Baumeister W.
    Biochem Biophys Res Commun 538:54-62(2021) [PubMed] [Europe PMC] [Abstract]
  • "Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions."
    Carlson C.R., Asfaha J.B., Ghent C.M., Howard C.J., Hartooni N., Safari M., Frankel A.D., Morgan D.O.
    Mol Cell 80:1092-1103.e4(2020) [PubMed] [Europe PMC] [Abstract]
  • "Genomic RNA Elements Drive Phase Separation of the SARS-CoV-2 Nucleocapsid."
    Iserman C., Roden C.A., Boerneke M.A., Sealfon R.S.G., McLaughlin G.A., Jungreis I., Fritch E.J., Hou Y.J., Ekena J., Weidmann C.A., Theesfeld C.L., Kellis M., Troyanskaya O.G., Baric R.S., Sheahan T.P., Weeks K.M., Gladfelter A.S.
    Mol Cell 80:1078-1091.e6(2020) [PubMed] [Europe PMC] [Abstract]
  • "The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein."
    Lu S., Ye Q., Singh D., Cao Y., Diedrich J.K., Yates J.R., Villa E., Cleveland D.W., Corbett K.D.
    Nat Commun 12:502-502(2021) [PubMed] [Europe PMC] [Abstract]
  • "SARS-CoV-2 nucleocapsid protein phase separates with G3BPs to disassemble stress granules and facilitate viral production."
    Luo L., Li Z., Zhao T., Ju X., Ma P., Jin B., Zhou Y., He S., Huang J., Xu X., Zou Y., Li P., Liang A., Liu J., Chi T., Huang X., Ding Q., Jin Z., Huang C., Zhang Y.
    Sci Bull (Beijing) 66:1194-1204(2021) [PubMed] [Europe PMC] [Abstract]
  • "Structural Insight Into the SARS-CoV-2 Nucleocapsid Protein C-Terminal Domain Reveals a Novel Recognition Mechanism for Viral Transcriptional Regulatory Sequences."
    Yang M., He S., Chen X., Huang Z., Zhou Z., Zhou Z., Chen Q., Chen S., Kang S.
    Front Chem 8:624765-624765(2020) [PubMed] [Europe PMC] [Abstract]
  • "Understanding the phase separation characteristics of nucleocapsid protein provides a new therapeutic opportunity against SARS-CoV-2."
    Zhao D., Xu W., Zhang X., Wang X., Ge Y., Yuan E., Xiong Y., Wu S., Li S., Wu N., Tian T., Feng X., Shu H., Lang P., Li J., Zhu F., Shen X., Li H., Li P., Zeng J.
    Protein Cell 12:734-740(2021) [PubMed] [Europe PMC] [Abstract]
  • "Multivalent binding of the partially disordered SARS-CoV-2 nucleocapsid phosphoprotein dimer to RNA."
    Forsythe H.M., Rodriguez Galvan J., Yu Z., Pinckney S., Reardon P., Cooley R.B., Zhu P., Rolland A.D., Prell J.S., Barbar E.
    Biophys J 120:2890-2901(2021) [PubMed] [Europe PMC] [Abstract]
  • "GCG inhibits SARS-CoV-2 replication by disrupting the liquid phase condensation of its nucleocapsid protein."
    Zhao M., Yu Y., Sun L.M., Xing J.Q., Li T., Zhu Y., Wang M., Yu Y., Xue W., Xia T., Cai H., Han Q.Y., Yin X., Li W.H., Li A.L., Cui J., Yuan Z., Zhang R.

    , Zhou T., Zhang X.M., Li T.
    Nat Commun 12:2114-2114(2021) [PubMed] [Europe PMC] [Abstract]
  • "RNA-induced liquid phase separation of SARS-CoV-2 nucleocapsid protein facilitates NF-kappaB hyper-activation and inflammation."
    Wu Y., Ma L., Cai S., Zhuang Z., Zhao Z., Jin S., Xie W., Zhou L., Zhang L., Zhao J., Cui J.
    Signal Transduct Target Ther 6:167-167(2021) [PubMed] [Europe PMC] [Abstract]
  • "Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids."
    Zhao H., Wu D., Nguyen A., Li Y., Adao R.C., Valkov E., Patterson G.H., Piszczek G., Schuck P.
    iScience 24:102523-102523(2021) [PubMed] [Europe PMC] [Abstract]
  • "Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain."
    Wu C., Qavi A.J., Hachim A., Kavian N., Cole A.R., Moyle A.B., Wagner N.D., Sweeney-Gibbons J., Rohrs H.W., Gross M.L., Peiris J.S.M., Basler C.F., Farnsworth C.W., Valkenburg S.A., Amarasinghe G.K., Leung D.W.
    iScience 24:102681-102681(2021) [PubMed] [Europe PMC] [Abstract]
  • "The Inherent Dynamics and Interaction Sites of the SARS-CoV-2 Nucleocapsid N-Terminal Region."
    Redzic J.S., Lee E., Born A., Issaian A., Henen M.A., Nichols P.J., Blue A., Hansen K.C., D'Alessandro A., Vogeli B., Eisenmesser E.Z.
    J Mol Biol 433:167108-167108(2021) [PubMed] [Europe PMC] [Abstract]
  • "Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV-2 replication."
    Jiang Y., Tong K., Yao R., Zhou Y., Lin H., Du L., Jin Y., Cao L., Tan J., Zhang X.D., Guo D., Pan J.A., Peng X.
    Cell Biosci 11:140-140(2021) [PubMed] [Europe PMC] [Abstract]
  • "Multiple Roles of SARS-CoV-2 N Protein Facilitated by Proteoform-Specific Interactions with RNA, Host Proteins, and Convalescent Antibodies."
    Lutomski C.A., El-Baba T.J., Bolla J.R., Robinson C.V.
    JACS Au 1:1147-1157(2021) [PubMed] [Europe PMC] [Abstract]
• RNA binding Source: UniProtKB-UniRule

GO - Biological processⁱ

• negative regulation of interferon-beta production Source: ComplexPortal <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "The ORF6, ORF8 and nucleocapsid proteins of SARS-CoV-2 inhibit type I interferon signaling pathway."
    Li J.Y., Liao C.H., Wang Q., Tan Y.J., Luo R., Qiu Y., Ge X.Y.
    Virus Res 286:198074-198074(2020) [PubMed] [Europe PMC] [Abstract]
• positive regulation of NLRP3 inflammasome complex assembly Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "SARS-CoV-2 N protein promotes NLRP3 inflammasome activation to induce hyperinflammation."
    Pan P., Shen M., Yu Z., Ge W., Chen K., Tian M., Xiao F., Wang Z., Wang J., Jia Y., Wang W., Wan P., Zhang J., Chen W., Lei Z., Chen X., Luo Z., Zhang Q.

    , Xu M., Li G., Li Y., Wu J.
    Nat. Commun. 12:4664-4664(2021) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH HOST NLRP3, SUBCELLULAR LOCATION.
• viral RNA genome packaging Source: ComplexPortal <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "An in vivo cell-based assay for investigating the specific interaction between the SARS-CoV N-protein and its viral RNA packaging sequence."
    Woo J., Lee E.Y., Lee M., Kim T., Cho Y.E.
    Biochem Biophys Res Commun 520:499-506(2019) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

<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 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

Keywords - Cellular componentⁱ

<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

<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

Amino acid modifications

<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

Keywords - PTMⁱ

<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

<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

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Biochemical characterization of SARS-CoV-2 nucleocapsid protein."
    Zeng W., Liu G., Ma H., Zhao D., Yang Y., Liu M., Mohammed A., Zhao C., Yang Y., Xie J., Ding C., Ma X., Weng J., Gao Y., He H., Jin T.
    Biochem Biophys Res Commun 527:618-623(2020) [PubMed] [Europe PMC] [Abstract]
  • "Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein."
    Ye Q., West A.M.V., Silletti S., Corbett K.D.
    Protein Sci 29:1890-1901(2020) [PubMed] [Europe PMC] [Abstract]
  • "Virus-Host Interactome and Proteomic Survey Reveal Potential Virulence Factors Influencing SARS-CoV-2 Pathogenesis."
    Li J., Guo M., Tian X., Wang X., Yang X., Wu P., Liu C., Xiao Z., Qu Y., Yin Y., Wang C., Zhang Y., Zhu Z., Liu Z., Peng C., Zhu T., Liang Q.
    Med (N Y) 2:99-112.e7(2021) [PubMed] [Europe PMC] [Abstract]
  • "Liquid-liquid phase separation by SARS-CoV-2 nucleocapsid protein and RNA."
    Chen H., Cui Y., Han X., Hu W., Sun M., Zhang Y., Wang P.H., Song G., Chen W., Lou J.
    Cell Res 30:1143-1145(2020) [PubMed] [Europe PMC] [Abstract]
  • "High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2."
    Zinzula L., Basquin J., Bohn S., Beck F., Klumpe S., Pfeifer G., Nagy I., Bracher A., Hartl F.U., Baumeister W.
    Biochem Biophys Res Commun 538:54-62(2021) [PubMed] [Europe PMC] [Abstract]
  • "Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions."
    Carlson C.R., Asfaha J.B., Ghent C.M., Howard C.J., Hartooni N., Safari M., Frankel A.D., Morgan D.O.
    Mol Cell 80:1092-1103.e4(2020) [PubMed] [Europe PMC] [Abstract]
  • "Genomic RNA Elements Drive Phase Separation of the SARS-CoV-2 Nucleocapsid."
    Iserman C., Roden C.A., Boerneke M.A., Sealfon R.S.G., McLaughlin G.A., Jungreis I., Fritch E.J., Hou Y.J., Ekena J., Weidmann C.A., Theesfeld C.L., Kellis M., Troyanskaya O.G., Baric R.S., Sheahan T.P., Weeks K.M., Gladfelter A.S.
    Mol Cell 80:1078-1091.e6(2020) [PubMed] [Europe PMC] [Abstract]
  • "The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein."
    Lu S., Ye Q., Singh D., Cao Y., Diedrich J.K., Yates J.R., Villa E., Cleveland D.W., Corbett K.D.
    Nat Commun 12:502-502(2021) [PubMed] [Europe PMC] [Abstract]
  • "SARS-CoV-2 nucleocapsid protein phase separates with G3BPs to disassemble stress granules and facilitate viral production."
    Luo L., Li Z., Zhao T., Ju X., Ma P., Jin B., Zhou Y., He S., Huang J., Xu X., Zou Y., Li P., Liang A., Liu J., Chi T., Huang X., Ding Q., Jin Z., Huang C., Zhang Y.
    Sci Bull (Beijing) 66:1194-1204(2021) [PubMed] [Europe PMC] [Abstract]
  • "Structural Insight Into the SARS-CoV-2 Nucleocapsid Protein C-Terminal Domain Reveals a Novel Recognition Mechanism for Viral Transcriptional Regulatory Sequences."
    Yang M., He S., Chen X., Huang Z., Zhou Z., Zhou Z., Chen Q., Chen S., Kang S.
    Front Chem 8:624765-624765(2020) [PubMed] [Europe PMC] [Abstract]
  • "Understanding the phase separation characteristics of nucleocapsid protein provides a new therapeutic opportunity against SARS-CoV-2."
    Zhao D., Xu W., Zhang X., Wang X., Ge Y., Yuan E., Xiong Y., Wu S., Li S., Wu N., Tian T., Feng X., Shu H., Lang P., Li J., Zhu F., Shen X., Li H., Li P., Zeng J.
    Protein Cell 12:734-740(2021) [PubMed] [Europe PMC] [Abstract]
  • "Multivalent binding of the partially disordered SARS-CoV-2 nucleocapsid phosphoprotein dimer to RNA."
    Forsythe H.M., Rodriguez Galvan J., Yu Z., Pinckney S., Reardon P., Cooley R.B., Zhu P., Rolland A.D., Prell J.S., Barbar E.
    Biophys J 120:2890-2901(2021) [PubMed] [Europe PMC] [Abstract]
  • "GCG inhibits SARS-CoV-2 replication by disrupting the liquid phase condensation of its nucleocapsid protein."
    Zhao M., Yu Y., Sun L.M., Xing J.Q., Li T., Zhu Y., Wang M., Yu Y., Xue W., Xia T., Cai H., Han Q.Y., Yin X., Li W.H., Li A.L., Cui J., Yuan Z., Zhang R.

    , Zhou T., Zhang X.M., Li T.
    Nat Commun 12:2114-2114(2021) [PubMed] [Europe PMC] [Abstract]
  • "RNA-induced liquid phase separation of SARS-CoV-2 nucleocapsid protein facilitates NF-kappaB hyper-activation and inflammation."
    Wu Y., Ma L., Cai S., Zhuang Z., Zhao Z., Jin S., Xie W., Zhou L., Zhang L., Zhao J., Cui J.
    Signal Transduct Target Ther 6:167-167(2021) [PubMed] [Europe PMC] [Abstract]
  • "Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids."
    Zhao H., Wu D., Nguyen A., Li Y., Adao R.C., Valkov E., Patterson G.H., Piszczek G., Schuck P.
    iScience 24:102523-102523(2021) [PubMed] [Europe PMC] [Abstract]
  • "Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain."
    Wu C., Qavi A.J., Hachim A., Kavian N., Cole A.R., Moyle A.B., Wagner N.D., Sweeney-Gibbons J., Rohrs H.W., Gross M.L., Peiris J.S.M., Basler C.F., Farnsworth C.W., Valkenburg S.A., Amarasinghe G.K., Leung D.W.
    iScience 24:102681-102681(2021) [PubMed] [Europe PMC] [Abstract]
  • "The Inherent Dynamics and Interaction Sites of the SARS-CoV-2 Nucleocapsid N-Terminal Region."
    Redzic J.S., Lee E., Born A., Issaian A., Henen M.A., Nichols P.J., Blue A., Hansen K.C., D'Alessandro A., Vogeli B., Eisenmesser E.Z.
    J Mol Biol 433:167108-167108(2021) [PubMed] [Europe PMC] [Abstract]
  • "Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV-2 replication."
    Jiang Y., Tong K., Yao R., Zhou Y., Lin H., Du L., Jin Y., Cao L., Tan J., Zhang X.D., Guo D., Pan J.A., Peng X.
    Cell Biosci 11:140-140(2021) [PubMed] [Europe PMC] [Abstract]
  • "Multiple Roles of SARS-CoV-2 N Protein Facilitated by Proteoform-Specific Interactions with RNA, Host Proteins, and Convalescent Antibodies."
    Lutomski C.A., El-Baba T.J., Bolla J.R., Robinson C.V.
    JACS Au 1:1147-1157(2021) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<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

3D structure databases

<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

Region

Compositional bias

<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

Family and domain databases

<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.

        10         20         30         40         50
MSDNGPQNQR NAPRITFGGP SDSTGSNQNG ERSGARSKQR RPQGLPNNTA 
        60         70         80         90        100
SWFTALTQHG KEDLKFPRGQ GVPINTNSSP DDQIGYYRRA TRRIRGGDGK 
       110        120        130        140        150
MKDLSPRWYF YYLGTGPEAG LPYGANKDGI IWVATEGALN TPKDHIGTRN 
       160        170        180        190        200
PANNAAIVLQ LPQGTTLPKG FYAEGSRGGS QASSRSSSRS RNSSRNSTPG 
       210        220        230        240        250
SSRGTSPARM AGNGGDAALA LLLLDRLNQL ESKMSGKGQQ QQGQTVTKKS 
       260        270        280        290        300
AAEASKKPRQ KRTATKAYNV TQAFGRRGPE QTQGNFGDQE LIRQGTDYKH 
       310        320        330        340        350
WPQIAQFAPS ASAFFGMSRI GMEVTPSGTW LTYTGAIKLD DKDPNFKDQV 
       360        370        380        390        400
ILLNKHIDAY KTFPPTEPKK DKKKKADETQ ALPQRQKKQQ TVTLLPAADL 
       410 
DDFSKQLQQS MSSADSTQA                                   

<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

Natural variant

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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