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Protein

Urease

Gene
N/A
Organism
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
Status
Reviewed-Annotation score:

Annotation score:4 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

Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism.By similarity

<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 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

Ni cationBy similarityNote: Binds 2 nickel ions per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).
Proteins known to be involved in this subpathway in this organism are:
  1. Urease, Urease
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism.

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 bindingi407Nickel 1; via tele nitrogen1
Metal bindingi409Nickel 1; via tele nitrogen1
Metal bindingi490Nickel 1; via carbamate group1
Metal bindingi490Nickel 2; via carbamate group1
<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 sitei492SubstrateBy similarity1
Metal bindingi519Nickel 2; via pros nitrogen1
Metal bindingi545Nickel 2; via tele nitrogen1
<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 sitei593Proton donorBy similarity1
Metal bindingi633Nickel 11

<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 functionHydrolase
LigandMetal-binding, Nickel

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.5 1091

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P07374

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

More...
UniPathwayi
UPA00258;UER00370

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M38.982

<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:
Urease (EC:3.5.1.5)
Alternative name(s):
Urea amidohydrolase
<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>OrganismiCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
<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 identifieri3823 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeCanavalia

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4161

<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_00000675241 – 840UreaseAdd BLAST840

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 residuei490N6-carboxylysine1 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

Carbamylation allows a single lysine to coordinate two nickel ions.1 Publication

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P07374

<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

Homohexamer.By similarity

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P07374

<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

1840
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
P07374

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

More...
SMRi
P07374

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
P07374

<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>Domaini402 – 840UreaseAdd BLAST439

<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

In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00375 Urease_alpha, 1 hit
cd00407 Urease_beta, 1 hit
cd00390 Urease_gamma, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.150.10, 1 hit
2.30.40.10, 1 hit
3.30.280.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01953 Urease_alpha, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006680 Amidohydro-rel
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR008221 Urease
IPR011612 Urease_alpha_N_dom
IPR017950 Urease_AS
IPR005848 Urease_asu
IPR017951 Urease_asu_c
IPR002019 Urease_beta
IPR036461 Urease_betasu_sf
IPR002026 Urease_gamma/gamma-beta_su
IPR036463 Urease_gamma_sf
IPR029754 Urease_Ni-bd

The PANTHER Classification System

More...
PANTHERi
PTHR43440 PTHR43440, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01979 Amidohydro_1, 1 hit
PF00449 Urease_alpha, 1 hit
PF00699 Urease_beta, 1 hit
PF00547 Urease_gamma, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001222 Urease, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01752 UREASE

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD002319 Urease_gamma_reg, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51278 SSF51278, 1 hit
SSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit
SSF54111 SSF54111, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01792 urease_alph, 1 hit
TIGR00192 urease_beta, 1 hit
TIGR00193 urease_gam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 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.

P07374-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLSPREVEK LGLHNAGYLA QKRLARGVRL NYTEAVALIA SQIMEYARDG
60 70 80 90 100
EKTVAQLMCL GQHLLGRRQV LPAVPHLLNA VQVEATFPDG TKLVTVHDPI
110 120 130 140 150
SRENGELQEA LFGSLLPVPS LDKFAETKED NRIPGEILCE DECLTLNIGR
160 170 180 190 200
KAVILKVTSK GDRPIQVGSH YHFIEVNPYL TFDRRKAYGM RLNIAAGTAV
210 220 230 240 250
RFEPGDCKSV TLVSIEGNKV IRGGNAIADG PVNETNLEAA MHAVRSKGFG
260 270 280 290 300
HEEEKDASEG FTKEDPNCPF NTFIHRKEYA NKYGPTTGDK IRLGDTNLLA
310 320 330 340 350
EIEKDYALYG DECVFGGGKV IRDGMGQSCG HPPAISLDTV ITNAVIIDYT
360 370 380 390 400
GIIKADIGIK DGLIASIGKA GNPDIMNGVF SNMIIGANTE VIAGEGLIVT
410 420 430 440 450
AGAIDCHVHY ICPQLVYEAI SSGITTLVGG GTGPAAGTRA TTCTPSPTQM
460 470 480 490 500
RLMLQSTDDL PLNFGFTGKG SSSKPDELHE IIKAGAMGLK LHEDWGSTPA
510 520 530 540 550
AIDNCLTIAE HHDIQINIHT DTLNEAGFVE HSIAAFKGRT IHTYHSEGAG
560 570 580 590 600
GGHAPDIIKV CGIKNVLPSS TNPTRPLTSN TIDEHLDMLM VCHHLDREIP
610 620 630 640 650
EDLAFAHSRI RKKTIAAEDV LNDIGAISII SSDSQAMGRV GEVISRTWQT
660 670 680 690 700
ADKMKAQTGP LKCDSSDNDN FRIRRYIAKY TINPAIANGF SQYVGSVEVG
710 720 730 740 750
KLADLVMWKP SFFGTKPEMV IKGGMVAWAD IGDPNASIPT PEPVKMRPMY
760 770 780 790 800
GTLGKAGGAL SIAFVSKAAL DQRVNVLYGL NKRVEAVSNV RKLTKLDMKL
810 820 830 840
NDALPEITVD PESYTVKADG KLLCVSEATT VPLSRNYFLF
Length:840
Mass (Da):90,748
Last modified:February 1, 1994 - 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:i1407E4ECCF00727F
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 conflicti247K → R AA sequence (PubMed:3402446).Curated1
Sequence conflicti247K → R AA sequence (Ref. 3) Curated1
Sequence conflicti258S → P AA sequence (PubMed:3402446).Curated1
Sequence conflicti258S → P AA sequence (Ref. 3) Curated1
Sequence conflicti269P → S AA sequence (PubMed:3402446).Curated1
Sequence conflicti269P → S AA sequence (Ref. 3) Curated1
Sequence conflicti459D → Y in AAA83831 (PubMed:1721034).Curated1
Sequence conflicti653K → P in AAA83831 (PubMed:1721034).Curated1

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
M65260 mRNA Translation: AAA83831.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC1396 URJB

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65260 mRNA Translation: AAA83831.1
PIRiJC1396 URJB

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
3LA4X-ray2.05A1-840[»]
4GOAX-ray2.20A1-840[»]
4GY7X-ray1.49A1-840[»]
4H9MX-ray1.52A1-840[»]
ProteinModelPortaliP07374
SMRiP07374
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP07374
ChEMBLiCHEMBL4161

Protein family/group databases

MEROPSiM38.982

Proteomic databases

PRIDEiP07374

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00258;UER00370

BRENDAi3.5.1.5 1091
SABIO-RKiP07374

Miscellaneous databases

EvolutionaryTraceiP07374

Family and domain databases

CDDicd00375 Urease_alpha, 1 hit
cd00407 Urease_beta, 1 hit
cd00390 Urease_gamma, 1 hit
Gene3Di2.10.150.10, 1 hit
2.30.40.10, 1 hit
3.30.280.10, 1 hit
HAMAPiMF_01953 Urease_alpha, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR008221 Urease
IPR011612 Urease_alpha_N_dom
IPR017950 Urease_AS
IPR005848 Urease_asu
IPR017951 Urease_asu_c
IPR002019 Urease_beta
IPR036461 Urease_betasu_sf
IPR002026 Urease_gamma/gamma-beta_su
IPR036463 Urease_gamma_sf
IPR029754 Urease_Ni-bd
PANTHERiPTHR43440 PTHR43440, 1 hit
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
PF00449 Urease_alpha, 1 hit
PF00699 Urease_beta, 1 hit
PF00547 Urease_gamma, 1 hit
PIRSFiPIRSF001222 Urease, 1 hit
PRINTSiPR01752 UREASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002319 Urease_gamma_reg, 1 hit
SUPFAMiSSF51278 SSF51278, 1 hit
SSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit
SSF54111 SSF54111, 1 hit
TIGRFAMsiTIGR01792 urease_alph, 1 hit
TIGR00192 urease_beta, 1 hit
TIGR00193 urease_gam, 1 hit
PROSITEiView protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 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 nameiUREA_CANEN
<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: P07374
<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 1, 1988
Last sequence update: February 1, 1994
Last modified: December 5, 2018
This is version 130 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

3D-structure, Direct protein sequencing

Documents

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