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Protein

Guanylate-binding protein 2

Gene

GBP2

Organism
Homo sapiens (Human)
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

Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (PubMed:8706832). Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=313 µM for GTP1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi45 – 52GTPBy similarity8
    Nucleotide bindingi67 – 69GTPBy similarity3
    Nucleotide bindingi97 – 101GTPBy similarity5

    <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

    • GTPase activity Source: InterPro
    • GTP binding Source: ProtInc
    • protein homodimerization activity Source: UniProtKB

    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

    Molecular functionHydrolase
    LigandGTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-877300 Interferon gamma signaling
    R-HSA-909733 Interferon alpha/beta signaling

    <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_and_taxonomy_section">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:
    Guanylate-binding protein 2 (EC:3.6.5.-1 Publication)
    Alternative name(s):
    GTP-binding protein 2
    Short name:
    GBP-2
    Short name:
    HuGBP-2
    Guanine nucleotide-binding protein 2
    Interferon-induced guanylate-binding protein 2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:GBP2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome 1

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000162645.12

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:4183 GBP2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    600412 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P32456

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane

    <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_and_biotech_section">'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>Mutagenesisi588 – 591Missing : No effect on subcellular location by confocal microscopy, but loss of membrane-association by subcellular fractionation. 1 Publication4

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    2634

    Open Targets

    More...
    OpenTargetsi
    ENSG00000162645

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA28597

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    GBP2

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    226694187

    <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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001909641 – 588Guanylate-binding protein 2Add BLAST588
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000370782589 – 591Removed in mature formBy similarity3

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei588Cysteine methyl esterBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi588S-geranylgeranyl cysteine1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

    Isoprenylation is required for proper subcellular location.1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P32456

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P32456

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P32456

    PeptideAtlas

    More...
    PeptideAtlasi
    P32456

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P32456

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    54878

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P32456

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P32456

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By IFNG/IFN-gamma during macrophage activation, and by TNF and IL1B.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000162645 Expressed in 223 organ(s), highest expression level in tendon of biceps brachii

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_GBP2

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P32456 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB045975
    HPA042682

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer; homodimerization occurs upon GTP-binding and is required for the association with membranous structures. Heterodimer with other family members, including GBP1, GBP3, GBP4 and GBP5.1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-714388,EBI-6863741From Hepatitis C virus genotype 1b (isolate Con1).

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    108904, 46 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P32456, 24 interactors

    Molecular INTeraction database

    More...
    MINTi
    P32456

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000359497

    <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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P32456

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

    More...
    SMRi
    P32456

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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_and_domains_section">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>Domaini35 – 276GB1/RHD3-type GAdd BLAST242

    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>Regioni1 – 309GTPase domain (Globular)By similarityAdd BLAST309

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2037 Eukaryota
    ENOG410XR6Z LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000162297

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000266974

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG001979

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P32456

    KEGG Orthology (KO)

    More...
    KOi
    K20897

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TFVWTLR

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G03P3

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P32456

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF331602

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd16269 GBP_C, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR030386 G_GB1_RHD3_dom
    IPR037684 GBP_C
    IPR003191 Guanylate-bd/ATL_C
    IPR036543 Guanylate-bd_C_sf
    IPR015894 Guanylate-bd_N
    IPR027417 P-loop_NTPase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02263 GBP, 1 hit
    PF02841 GBP_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48340 SSF48340, 1 hit
    SSF52540 SSF52540, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51715 G_GB1_RHD3, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P32456-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAPEINLPGP MSLIDNTKGQ LVVNPEALKI LSAITQPVVV VAIVGLYRTG
    60 70 80 90 100
    KSYLMNKLAG KKNGFSLGST VKSHTKGIWM WCVPHPKKPE HTLVLLDTEG
    110 120 130 140 150
    LGDIEKGDNE NDSWIFALAI LLSSTFVYNS MGTINQQAMD QLHYVTELTD
    160 170 180 190 200
    RIKANSSPGN NSVDDSADFV SFFPAFVWTL RDFTLELEVD GEPITADDYL
    210 220 230 240 250
    ELSLKLRKGT DKKSKSFNDP RLCIRKFFPK RKCFVFDWPA PKKYLAHLEQ
    260 270 280 290 300
    LKEEELNPDF IEQVAEFCSY ILSHSNVKTL SGGIPVNGPR LESLVLTYVN
    310 320 330 340 350
    AISSGDLPCM ENAVLALAQI ENSAAVEKAI AHYEQQMGQK VQLPTETLQE
    360 370 380 390 400
    LLDLHRDSER EAIEVFMKNS FKDVDQMFQR KLGAQLEARR DDFCKQNSKA
    410 420 430 440 450
    SSDCCMALLQ DIFGPLEEDV KQGTFSKPGG YRLFTQKLQE LKNKYYQVPR
    460 470 480 490 500
    KGIQAKEVLK KYLESKEDVA DALLQTDQSL SEKEKAIEVE RIKAESAEAA
    510 520 530 540 550
    KKMLEEIQKK NEEMMEQKEK SYQEHVKQLT EKMERDRAQL MAEQEKTLAL
    560 570 580 590
    KLQEQERLLK EGFENESKRL QKDIWDIQMR SKSLEPICNI L
    Length:591
    Mass (Da):67,209
    Last modified:April 14, 2009 - v3
    <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:iB09B3C2F3C3E1EA2
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti310M → R in AAH73163 (PubMed:15489334).Curated1

    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 variantiVAR_054815281S → P. Corresponds to variant dbSNP:rs2230336Ensembl.1
    Natural variantiVAR_054816285P → A5 PublicationsCorresponds to variant dbSNP:rs1803632Ensembl.1
    Natural variantiVAR_054817303S → G4 PublicationsCorresponds to variant dbSNP:rs2230338Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    M55543 mRNA Translation: AAA67323.1
    AL832451 mRNA Translation: CAD89925.1
    AK314325 mRNA Translation: BAG36973.1
    CR457062 mRNA Translation: CAG33343.1
    AC104459 Genomic DNA No translation available.
    CH471097 Genomic DNA Translation: EAW73146.1
    BC073163 mRNA Translation: AAH73163.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS719.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S70524

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_004111.2, NM_004120.4

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.386567
    Hs.732899
    Hs.734162

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000370466; ENSP00000359497; ENSG00000162645
    ENST00000464839; ENSP00000434282; ENSG00000162645

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2634

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:2634

    UCSC genome browser

    More...
    UCSCi
    uc001dmz.3 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <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
    M55543 mRNA Translation: AAA67323.1
    AL832451 mRNA Translation: CAD89925.1
    AK314325 mRNA Translation: BAG36973.1
    CR457062 mRNA Translation: CAG33343.1
    AC104459 Genomic DNA No translation available.
    CH471097 Genomic DNA Translation: EAW73146.1
    BC073163 mRNA Translation: AAH73163.1
    CCDSiCCDS719.1
    PIRiS70524
    RefSeqiNP_004111.2, NM_004120.4
    UniGeneiHs.386567
    Hs.732899
    Hs.734162

    3D structure databases

    ProteinModelPortaliP32456
    SMRiP32456
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108904, 46 interactors
    IntActiP32456, 24 interactors
    MINTiP32456
    STRINGi9606.ENSP00000359497

    PTM databases

    iPTMnetiP32456
    PhosphoSitePlusiP32456

    Polymorphism and mutation databases

    BioMutaiGBP2
    DMDMi226694187

    Proteomic databases

    EPDiP32456
    MaxQBiP32456
    PaxDbiP32456
    PeptideAtlasiP32456
    PRIDEiP32456
    ProteomicsDBi54878

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000370466; ENSP00000359497; ENSG00000162645
    ENST00000464839; ENSP00000434282; ENSG00000162645
    GeneIDi2634
    KEGGihsa:2634
    UCSCiuc001dmz.3 human

    Organism-specific databases

    Comparative Toxicogenomics Database

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    CTDi
    2634
    DisGeNETi2634
    EuPathDBiHostDB:ENSG00000162645.12

    GeneCards: human genes, protein and diseases

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    GeneCardsi
    GBP2

    H-Invitational Database, human transcriptome db

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    H-InvDBi
    HIX0000764
    HIX0077629
    HGNCiHGNC:4183 GBP2
    HPAiCAB045975
    HPA042682
    MIMi600412 gene
    neXtProtiNX_P32456
    OpenTargetsiENSG00000162645
    PharmGKBiPA28597

    GenAtlas: human gene database

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    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2037 Eukaryota
    ENOG410XR6Z LUCA
    GeneTreeiENSGT00940000162297
    HOGENOMiHOG000266974
    HOVERGENiHBG001979
    InParanoidiP32456
    KOiK20897
    OMAiTFVWTLR
    OrthoDBiEOG091G03P3
    PhylomeDBiP32456
    TreeFamiTF331602

    Enzyme and pathway databases

    ReactomeiR-HSA-877300 Interferon gamma signaling
    R-HSA-909733 Interferon alpha/beta signaling

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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    ChiTaRSi
    GBP2 human

    The Gene Wiki collection of pages on human genes and proteins

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    GeneWikii
    GBP2

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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    GenomeRNAii
    2634

    Protein Ontology

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    PROi
    PR:P32456

    The Stanford Online Universal Resource for Clones and ESTs

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    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000162645 Expressed in 223 organ(s), highest expression level in tendon of biceps brachii
    CleanExiHS_GBP2
    GenevisibleiP32456 HS

    Family and domain databases

    CDDicd16269 GBP_C, 1 hit
    InterProiView protein in InterPro
    IPR030386 G_GB1_RHD3_dom
    IPR037684 GBP_C
    IPR003191 Guanylate-bd/ATL_C
    IPR036543 Guanylate-bd_C_sf
    IPR015894 Guanylate-bd_N
    IPR027417 P-loop_NTPase
    PfamiView protein in Pfam
    PF02263 GBP, 1 hit
    PF02841 GBP_C, 1 hit
    SUPFAMiSSF48340 SSF48340, 1 hit
    SSF52540 SSF52540, 1 hit
    PROSITEiView protein in PROSITE
    PS51715 G_GB1_RHD3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
    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 nameiGBP2_HUMAN
    <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: P32456
    Secondary accession number(s): Q6GPH0, Q6IAU2, Q86TB0
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: April 14, 2009
    Last modified: December 5, 2018
    This is version 164 of the entry and version 3 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 programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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