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Entry version 103 (11 Dec 2019)
Sequence version 3 (24 Nov 2009)
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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Pisum sativum (Garden pea)
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

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Activated by reductants such as dithiothreitol (DTT), and by thioredoxin in vivo, following exposure to light.2 Publications

<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

Unedited protein has no activity.
    1. Vmax=151 nmol/min/mg enzyme1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: malonyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic (ACCA), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (accD)
    This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi230ZincCurated1
    Metal bindingi233ZincCurated1
    Metal bindingi249ZincCurated1
    Metal bindingi252ZincCurated1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri230 – 252C4-typeUniRule annotationAdd BLAST23

    <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 functionTransferase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00655;UER00711

    <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:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticUniRule annotation (EC:2.1.3.15UniRule annotation)
    Short name:
    ACCase subunit betaUniRule annotation
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule 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:accDUniRule annotation
    Synonyms:ycf11, zfpA
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlastid; Chloroplast
    <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>OrganismiPisum sativum (Garden pea)
    <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 identifieri3888 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeHologaleginaIRL cladeFabeaePisum

    <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 Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Plastid inner 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%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>Mutagenesisi230C → A: Almost complete loss of carboxyltransferase activity in E.coli. 1 Publication1
    Mutagenesisi233C → A: Almost complete loss of carboxyltransferase activity in E.coli. 1 Publication1
    Mutagenesisi249C → A: Almost complete loss of carboxyltransferase activity in E.coli. 1 Publication1
    Mutagenesisi252C → A: Complete loss of carboxyltransferase activity in E.coli. 1 Publication1
    Mutagenesisi442C → A: Loss of redox control, but also considerable loss of carboxyltransferase activity in E.coli. 1 Publication1
    Mutagenesisi466C → A: Retains 50% carboxyltransferase activity in the presence of DTT in E.coli. 1 Publication1

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001997891 – 590Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST590

    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 bondi442Interchain (with C-317 in alpha subunit)1 Publication

    Keywords - PTMi

    Disulfide bond

    <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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Activity was highest in chloroplasts isolated from young, actively dividing leaves.1 Publication

    <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

    Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).

    By similarity

    <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>Domaini226 – 590CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST365

    <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 AccD/PCCB family.UniRule annotation

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri230 – 252C4-typeUniRule annotationAdd BLAST23

    Keywords - Domaini

    Zinc-finger

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01395, AcetylCoA_CT_beta, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR034733, AcCoA_carboxyl
    IPR000438, Acetyl_CoA_COase_Trfase_b_su
    IPR029045, ClpP/crotonase-like_dom_sf
    IPR011762, COA_CT_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01039, Carboxyl_trans, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01070, ACCCTRFRASEB

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52096, SSF52096, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50980, COA_CT_NTER, 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.

    P18823-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MINEDPSSLT DMDNNIDSWK NNSENSSYSH ADSLADVSNI DNLLSDKIFS
    60 70 80 90 100
    IRDSNSNIYD IYYAYDTNDT NITKYKWTNN INRCIESYLR SQICEDIDFN
    110 120 130 140 150
    SDICDKVQRT IIILIRSTND TNDISDTNDI SDTNDTNDTN AIYDPFDISD
    160 170 180 190 200
    TNDTNEIYDP FFILDINDTN DTNDIYGIYD PDDIYETNIK DICERYSEIY
    210 220 230 240 250
    PRNREKSTFV PIDYSDPNCM EKLARLWVQC ETCYGLNFKQ FFRPKMNICE
    260 270 280 290 300
    HCGEHLKMSS SDRIDLLIDR DTWNPMDEDM VSVDPIKFDS IKELGSEEES
    310 320 330 340 350
    SKDRLDEDML SPDPIELDSE EESSKDRVDS EEEKDQSYID RLDSYQEKTG
    360 370 380 390 400
    LPETVQTGTD QREEIHPLFE DIMNQLDLYL QTAKNRVDSE EEKDQSYIDR
    410 420 430 440 450
    LDSYQEKTGL PEAVQTGTGQ LNGIPLALAV MDSEFIAGSM GCVVGEKITR
    460 470 480 490 500
    LIEYATNLLL PLIIVCASGG ARMQEGSLSL MQMAKISSAL YNYQINQKLF
    510 520 530 540 550
    YVAILTSPTT GGVTASFGML GDIIIAEPNA TIAFAGKRVI EQLLNKEVPE
    560 570 580 590
    GSQSADLLFD RGLLDAVVPR HLLKEFLTEL FQFHGFVPLT
    Length:590
    Mass (Da):67,143
    Last modified:November 24, 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:i66EE291425EBEC49
    GO

    <p>This subsection of the 'Sequence' section provides information relevant to all types of RNA editing events (conversion, insertion, deletion of nucleotides) that lead to one or more amino acid changes compared to the translation of the non-edited RNA version.<p><a href='/help/rna_editing' target='_top'>More...</a></p>RNA editingi

    Edited at position 267.2 Publications

    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
    X56315 Genomic DNA Translation: CAA39754.1 Sequence problems.
    X56315 Genomic DNA Translation: CAA39756.1 Sequence problems.
    X56315 Genomic DNA Translation: CAA39755.1 Sequence problems.
    X15268 Genomic DNA Translation: CAA33339.1 Sequence problems.
    X54750 Genomic DNA Translation: CAA38546.1 Sequence problems.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S17920

    NCBI Reference Sequences

    More...
    RefSeqi
    YP_003587558.1, NC_014057.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    9073106

    Keywords - Coding sequence diversityi

    RNA editing

    <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
    X56315 Genomic DNA Translation: CAA39754.1 Sequence problems.
    X56315 Genomic DNA Translation: CAA39756.1 Sequence problems.
    X56315 Genomic DNA Translation: CAA39755.1 Sequence problems.
    X15268 Genomic DNA Translation: CAA33339.1 Sequence problems.
    X54750 Genomic DNA Translation: CAA38546.1 Sequence problems.
    PIRiS17920
    RefSeqiYP_003587558.1, NC_014057.1

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Genome annotation databases

    GeneIDi9073106

    Enzyme and pathway databases

    UniPathwayiUPA00655;UER00711

    Family and domain databases

    HAMAPiMF_01395, AcetylCoA_CT_beta, 1 hit
    InterProiView protein in InterPro
    IPR034733, AcCoA_carboxyl
    IPR000438, Acetyl_CoA_COase_Trfase_b_su
    IPR029045, ClpP/crotonase-like_dom_sf
    IPR011762, COA_CT_N
    PfamiView protein in Pfam
    PF01039, Carboxyl_trans, 1 hit
    PRINTSiPR01070, ACCCTRFRASEB
    SUPFAMiSSF52096, SSF52096, 2 hits
    PROSITEiView protein in PROSITE
    PS50980, COA_CT_NTER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiACCD_PEA
    <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: P18823
    <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: November 1, 1990
    Last sequence update: November 24, 2009
    Last modified: December 11, 2019
    This is version 103 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 programPlant 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

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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