Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 111 (13 Feb 2019)
Sequence version 1 (27 Sep 2005)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Zinc/cadmium/lead-transporting P-type ATPase

Gene

zntA

Organism
Shigella sonnei (strain Ss046)
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

Confers resistance to zinc, cadmium and lead. Couples the hydrolysis of ATP with the export of zinc, cadmium or lead.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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi58Zinc 1By similarity1
Metal bindingi59Zinc 1By similarity1
Metal bindingi62Zinc 1By similarity1
Metal bindingi392Zinc 2By similarity1
Metal bindingi394Zinc 2By similarity1
<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 sitei4364-aspartylphosphate intermediate1 Publication1
Metal bindingi436Magnesium1 Publication1
Metal bindingi438Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi628Magnesium1 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>Sitei693Important for metal transport1 Publication1
Metal bindingi714Zinc 2By similarity1 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

<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, Translocase
Biological processIon transport, Transport, Zinc transport
LigandATP-binding, Cadmium, Lead, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SSON300269:G1GL2-4465-MONOMER

<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:
Zinc/cadmium/lead-transporting P-type ATPaseCurated (EC:3.6.3.3By similarity, EC:7.2.2.-By similarity, EC:7.2.2.121 Publication)
Alternative name(s):
Zn(2+)/Cd(2+)/Pb(2+) export ATPaseCurated
<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:zntA1 Publication
Ordered Locus Names:SSON_3707Imported
<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>OrganismiShigella sonnei (strain Ss046)
<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 identifieri300269 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
<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
  • UP000002529 <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 provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 124CytoplasmicCuratedAdd BLAST124
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Topological domaini146PeriplasmicCurated1
Transmembranei147 – 167HelicalSequence analysisAdd BLAST21
Topological domaini168 – 179CytoplasmicCuratedAdd BLAST12
Transmembranei180 – 197HelicalSequence analysisAdd BLAST18
Topological domaini198 – 202PeriplasmicCurated5
Transmembranei203 – 222HelicalSequence analysisAdd BLAST20
Topological domaini223 – 356CytoplasmicCuratedAdd BLAST134
Transmembranei357 – 377HelicalSequence analysisAdd BLAST21
Topological domaini378 – 383PeriplasmicCurated6
Transmembranei384 – 404HelicalSequence analysisAdd BLAST21
Topological domaini405 – 685CytoplasmicCuratedAdd BLAST281
Transmembranei686 – 702HelicalSequence analysisAdd BLAST17
Topological domaini703 – 707PeriplasmicCurated5
Transmembranei708 – 729HelicalSequence analysisAdd BLAST22
Topological domaini730 – 732CytoplasmicBy similarity3

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, 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>Mutagenesisi187M → A: No change in ATPase activity and in zinc binding. 1 Publication1
Mutagenesisi202E → A: Lack of ATPase activity and decrease in zinc binding. 1 Publication1
Mutagenesisi202E → D: Lack of ATPase activity. 1 Publication1
Mutagenesisi202E → Q: Strong decrease in ATPase activity. 1 Publication1
Mutagenesisi210F → A: Decrease in ATPase activity and slight decrease in zinc binding. 1 Publication1
Mutagenesisi214E → A or Q: Decrease in ATPase activity. 1 Publication1
Mutagenesisi354Y → A or F: Decrease in ATPase activity. 1 Publication1
Mutagenesisi436D → N: Lack of ATPase activity. 1 Publication1
Mutagenesisi693K → A: Lack of ATPase activity but does not affect zinc binding. 1 Publication1
Mutagenesisi693K → R: Lack of ATPase activity. 1 Publication1
Mutagenesisi714D → E: Strong decrease in ATPase activity. 1 Publication1
Mutagenesisi714D → N: Lack of ATPase activity and strong decrease in zinc binding. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004393561 – 732Zinc/cadmium/lead-transporting P-type ATPaseAdd BLAST732

Keywords - PTMi

Phosphoprotein

<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

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
4UMVX-ray3.20A1-732[»]
4UMWX-ray2.71A1-732[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q3YW59

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

More...
SMRi
Q3YW59

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>Domaini49 – 113HMAPROSITE-ProRule annotationAdd BLAST65

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

Has two high-affinity metal-binding sites, one in the N-terminal region and another in the transmembrane region. Both sites are able to access and bind metal ion independently of each other. The N-terminal metal-binding site is not strictly necessary for activity and metal selectivity, but is needed for maximal activity and may be involved in regulation. The metal-binding site in the transmembrane region is essential for activity of the pump.By similarity

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000250399

KEGG Orthology (KO)

More...
KOi
K01534

Identification of Orthologs from Complete Genome Data

More...
OMAi
WLPWIYK

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00371 HMA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR017969 Heavy-metal-associated_CS
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
IPR027256 P-typ_ATPase_IB
IPR001757 P_typ_ATPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00403 HMA, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00120 HATPASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55008 SSF55008, 1 hit
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01525 ATPase-IB_hvy, 1 hit
TIGR01494 ATPase_P-type, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 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.

Q3YW59-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSSPT LSENVSGTRY
60 70 80 90 100
SWKVSGMDCA ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV
110 120 130 140 150
ESAVQKAGYS LRDEQAADEP QASRLKENLP LITLIVMMAI SWGLEQFNHP
160 170 180 190 200
FGQLAFIATT LVGLYPIARQ ALRLIKSGSY FAIETLMSVA AIGALFIGAT
210 220 230 240 250
AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT RLRNGEREEV
260 270 280 290 300
AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD
310 320 330 340 350
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF
360 370 380 390 400
SRIYTPAIMA VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST
410 420 430 440 450
PAAITSGLAA AARRGALIKG GAALEQLGRV TQVAFDKTGT LTVGKPRVTA
460 470 480 490 500
IHPATGISES ELLTLAAAVE QGATHPLAQA IVREAQVAEL AIPTAESQRA
510 520 530 540 550
LVGSGIEAQV NGERVLICAA GKHPADAFAG LINELESAGQ TVVLVVRNDD
560 570 580 590 600
VLGIIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE
610 620 630 640 650
FKAGLLPEDK VKAVTKLNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD
660 670 680 690 700
VALETADAAL THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT
710 720 730
LLGMTGLWLA VLADTGATVL VTANALRLLR RR
Length:732
Mass (Da):76,767
Last modified:September 27, 2005 - 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:i115E513DD79413EA
GO

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
CP000038 Genomic DNA Translation: AAZ90253.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAZ90253; AAZ90253; SSON_3707

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssn:SSON_3707

<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
CP000038 Genomic DNA Translation: AAZ90253.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UMVX-ray3.20A1-732[»]
4UMWX-ray2.71A1-732[»]
ProteinModelPortaliQ3YW59
SMRiQ3YW59
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ90253; AAZ90253; SSON_3707
KEGGissn:SSON_3707

Phylogenomic databases

HOGENOMiHOG000250399
KOiK01534
OMAiWLPWIYK

Enzyme and pathway databases

BioCyciSSON300269:G1GL2-4465-MONOMER

Family and domain databases

CDDicd00371 HMA, 1 hit
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR017969 Heavy-metal-associated_CS
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
IPR027256 P-typ_ATPase_IB
IPR001757 P_typ_ATPase
PfamiView protein in Pfam
PF00403 HMA, 1 hit
PRINTSiPR00120 HATPASE
SUPFAMiSSF55008 SSF55008, 1 hit
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit
TIGRFAMsiTIGR01525 ATPase-IB_hvy, 1 hit
TIGR01494 ATPase_P-type, 1 hit
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 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 nameiZNTA_SHISS
<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: Q3YW59
<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: April 12, 2017
Last sequence update: September 27, 2005
Last modified: February 13, 2019
This is version 111 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again