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Protein

Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1

Gene

glgE1

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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

Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.1 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 regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Is competitively inhibited by alpha-, beta- and gamma-cyclodextrins (cyclic maltooligosaccharides), unlike GlgE from M.tuberculosis.1 Publication

<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=1.5 mM for maltohexaose (in the presence of 5 mM M1P)1 Publication
  2. KM=0.30 mM for alpha-maltose 1-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.0 with maltohexaose as acceptor substrate.1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius with maltohexaose as acceptor substrate.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei264Maltose 1-phosphate1 Publication1
    Binding sitei324Maltose 1-phosphate1 Publication1
    Binding sitei359Maltose 1-phosphate1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei394Nucleophile1 Publication1
    Binding sitei395Maltose 1-phosphate1 Publication1
    Active sitei423Proton donor1 Publication1
    <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>Sitei480Transition state stabilizer1 Publication1

    <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

    Molecular functionGlycosyltransferase, Transferase
    Biological processCarbohydrate metabolism

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH13 Glycoside Hydrolase Family 13

    <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:
    Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 (EC:2.4.99.161 Publication)
    Short name:
    GMPMT 1
    Alternative name(s):
    (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase 1
    <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:glgE1
    Synonyms:pep1, pep1A, pep1I
    Ordered Locus Names:SCO5443
    ORF Names:SC6A11.19c
    <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>OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    <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 identifieri100226 [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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    <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
    • UP000001973 <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

    <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_00000543491 – 675Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1Add BLAST675

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9L1K2

    <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.1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    100226.SCO5443

    <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

    1675
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9L1K2

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

    More...
    SMRi
    Q9L1K2

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q9L1K2

    <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

    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>Regioni534 – 535Maltose 1-phosphate binding1 Publication2

    <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 glycosyl hydrolase 13 family. GlgE subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105EP6 Bacteria
    COG0366 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000239230

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9L1K2

    KEGG Orthology (KO)

    More...
    KOi
    K16147

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RDLHFHH

    Database of Orthologous Groups

    More...
    OrthoDBi
    POG091H0A4R

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9L1K2

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.60.40.10, 1 hit
    2.60.40.1180, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02124 GlgE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR026585 GlgE
    IPR021828 GlgE_dom_N/S
    IPR006047 Glyco_hydro_13_cat_dom
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF
    IPR013783 Ig-like_fold

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10357:SF137 PTHR10357:SF137, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF11896 DUF3416, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00642 Aamy, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 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.

    Q9L1K2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPATHHSSAT SAERPTVVGR IPVLDVRPVV QRGRRPAKAV TGESFEVSAT
    60 70 80 90 100
    VFREGHDAVG ANVVLRDPRG RPGPWTPMRE LAPGTDRWGA TVTAGETGTW
    110 120 130 140 150
    SYTVEAWGDP VTTWRHHARI KIPAGLDTDL VLEEGARLYE RAAADVPGRE
    160 170 180 190 200
    DRRELLAAVD ALRDESRPAA SRLAAALTPQ VDAVLARHPL RDLVTSSDPL
    210 220 230 240 250
    PLLVERERAL YGAWYEFFPR SEGTPHTPHG TFRTAARRLP AIAAMGFDVV
    260 270 280 290 300
    YLPPIHPIGT THRKGRNNTL SATGDDVGVP WAIGSPEGGH DSIHPALGTL
    310 320 330 340 350
    DDFDHFVTEA GKLGLEIALD FALQCSPDHP WVHKHPEWFH HRPDGTIAHA
    360 370 380 390 400
    ENPPKKYQDI YPIAFDADPD GLATETVRIL RHWMDHGVRI FRVDNPHTKP
    410 420 430 440 450
    VAFWERVIAD INGTDPDVIF LAEAFTRPAM MATLAQIGFQ QSYTYFTWRN
    460 470 480 490 500
    TKQELTEYLT ELSGEAASYM RPNFFANTPD ILHAYLQHGG RPAFEVRAVL
    510 520 530 540 550
    AATLSPTWGI YSGYELCENT PLREGSEEYL DSEKYQLKPR DWTRAAREGT
    560 570 580 590 600
    TIAPLVTRLN TIRRENPALR QLRDLHFHPT DKEEVIAYSK RQGSNTVLVV
    610 620 630 640 650
    VNLDPRHTQE ATVSLDMPQL GLDWHESVPV RDELTGETYH WGRANYVRLE
    660 670
    PGRTPAHVCT VLRPSHPQIG GSHTT
    Length:675
    Mass (Da):75,290
    Last modified:October 1, 2000 - 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:iC23DBCFF23AD42D6
    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 conflicti218F → W in CAA04600 (PubMed:10821190).Curated1
    Sequence conflicti450 – 451NT → LR in CAA04600 (PubMed:10821190).Curated2

    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
    AJ001205 Genomic DNA Translation: CAA04600.1
    AL939123 Genomic DNA Translation: CAB72419.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_629581.1, NC_003888.3
    WP_011030248.1, NC_003888.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB72419; CAB72419; CAB72419

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1100883

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sco:SCO5443

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|100226.15.peg.5524

    <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
    AJ001205 Genomic DNA Translation: CAA04600.1
    AL939123 Genomic DNA Translation: CAB72419.1
    RefSeqiNP_629581.1, NC_003888.3
    WP_011030248.1, NC_003888.3

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZSSX-ray1.80A/B/C/D1-675[»]
    3ZSTX-ray2.30A/B1-675[»]
    3ZT5X-ray2.09A/B/C/D1-675[»]
    3ZT6X-ray2.19A/B/C/D1-675[»]
    3ZT7X-ray2.50A/B/C/D1-675[»]
    4CN1X-ray2.55A/B1-675[»]
    4CN4X-ray2.40A/B1-675[»]
    4CN6X-ray2.29A/B1-675[»]
    4U2YX-ray2.48A/B1-675[»]
    4U2ZX-ray2.26A/B1-675[»]
    4U31X-ray1.85A/B1-675[»]
    5CVSX-ray2.30A/B1-675[»]
    5LGVX-ray2.50A/B1-675[»]
    5LGWX-ray1.95A/B1-675[»]
    5VSJX-ray2.46A/B1-663[»]
    5VT4X-ray3.21A/B/C/D1-663[»]
    ProteinModelPortaliQ9L1K2
    SMRiQ9L1K2
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO5443

    Protein family/group databases

    CAZyiGH13 Glycoside Hydrolase Family 13

    Proteomic databases

    PRIDEiQ9L1K2

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB72419; CAB72419; CAB72419
    GeneIDi1100883
    KEGGisco:SCO5443
    PATRICifig|100226.15.peg.5524

    Phylogenomic databases

    eggNOGiENOG4105EP6 Bacteria
    COG0366 LUCA
    HOGENOMiHOG000239230
    InParanoidiQ9L1K2
    KOiK16147
    OMAiRDLHFHH
    OrthoDBiPOG091H0A4R
    PhylomeDBiQ9L1K2

    Miscellaneous databases

    EvolutionaryTraceiQ9L1K2

    Family and domain databases

    Gene3Di2.60.40.10, 1 hit
    2.60.40.1180, 1 hit
    HAMAPiMF_02124 GlgE, 1 hit
    InterProiView protein in InterPro
    IPR026585 GlgE
    IPR021828 GlgE_dom_N/S
    IPR006047 Glyco_hydro_13_cat_dom
    IPR013780 Glyco_hydro_b
    IPR017853 Glycoside_hydrolase_SF
    IPR013783 Ig-like_fold
    PANTHERiPTHR10357:SF137 PTHR10357:SF137, 1 hit
    PfamiView protein in Pfam
    PF11896 DUF3416, 1 hit
    SMARTiView protein in SMART
    SM00642 Aamy, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    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 nameiGLGE1_STRCO
    <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: Q9L1K2
    Secondary accession number(s): O54202
    <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: July 3, 2003
    Last sequence update: October 1, 2000
    Last modified: December 5, 2018
    This is version 118 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 programProkaryotic 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, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
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