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UniProtKB - Q5F3T9 (UGDH_CHICK)

Entry version 115 (29 Sep 2021)
Sequence version 1 (15 Mar 2005)
Previous versions | rss
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Protein

UDP-glucose 6-dehydrogenase

Gene

UGDH

Organism
Gallus gallus (Chicken)
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 transcript 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

Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (By similarity).

Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity).

By similarity

<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 <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

UDP-alpha-D-xylose (UDX) acts as a feedback inhibitor. It binds at the same site as the substrate, but functions as allosteric inhibitor by triggering a conformation change that disrupts the active hexameric ring structure and gives rise to an inactive, horseshoe-shaped hexamer.By similarity

<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: UDP-alpha-D-glucuronate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose.By similarity This subpathway is part of the pathway UDP-alpha-D-glucuronate biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose, the pathway UDP-alpha-D-glucuronate biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei36NADBy similarity1
Binding sitei41NADBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei161Proton donor/acceptorBy similarity1
Binding sitei165NADBy similarity1
Active sitei220Proton donor/acceptorBy similarity1
Binding sitei260SubstrateBy similarity1
Active sitei276NucleophileBy similarity1
Binding sitei346NADBy similarity1
Binding sitei442SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi11 – 16NADBy similarity6
Nucleotide bindingi89 – 93NADBy similarity5
Nucleotide bindingi130 – 132NADBy similarity3
Nucleotide bindingi276 – 279NADBy similarity4

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAllosteric enzyme, Oxidoreductase
Biological processCarbohydrate metabolism
LigandNAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-GGA-173599, Formation of the active cofactor, UDP-glucuronate

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

More...UniPathwayi		UPA00038;UER00491

<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:
UDP-glucose 6-dehydrogenase (EC:1.1.1.22By similarity)
Short name:
UDP-Glc dehydrogenase
Short name:
UDP-GlcDH
Short name:
UDPGDH
<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:UGDH
ORF Names:RCJMB04_7d7
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 4

<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

<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_00003174781 – 494UDP-glucose 6-dehydrogenaseAdd BLAST494

Proteomic databases

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

More...PaxDbi		Q5F3T9

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSGALG00000014320, Expressed in liver and 13 other tissues

<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

Homohexamer.

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9031.ENSGALP00000023101

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...SMRi		Q5F3T9

Database of comparative protein structure models

More...ModBasei		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

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>Regioni88 – 110DisorderedBy similarityAdd BLAST23
Regioni129 – 135Allosteric switch regionBy similarity7
Regioni161 – 165Substrate bindingBy similarity5
Regioni220 – 224Substrate bindingBy similarity5
Regioni267 – 273Substrate bindingBy similarity7
Regioni321 – 325Important for formation of active hexamer structureBy similarity5
Regioni338 – 339Substrate bindingBy similarity2
Regioni466 – 494DisorderedBy similarityAdd BLAST29

<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

The protein goes through several conformation states during the reaction cycle, giving rise to hysteresis. In the initial state, the ligand-free protein is in an inactive conformation (E*). Substrate binding triggers a change to the active conformation (E). UDP-xylose binding triggers the transition to a distinct, inhibited conformation. The presence of an intrinsically disordered C-terminus promotes a more dynamic protein structure and favors a conformation with high affinity for UPD-xylose.By similarity
The allosteric switch region moves by about 5 Angstroms when UDP-xylose is bound, and occupies part of the UDP-glucose binding site. At the same time it promotes domain movements that disrupt the active hexameric ring structure and lead to the formation of a horseshoe-shaped, inactive hexamer.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

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2666, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000015355

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_023810_7_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q5F3T9

Identification of Orthologs from Complete Genome Data

More...OMAi		CLNLPEV

Database of Orthologous Groups

More...OrthoDBi		915490at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q5F3T9

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR036291, NAD(P)-bd_dom_sf
IPR017476, UDP-Glc/GDP-Man
IPR014027, UDP-Glc/GDP-Man_DH_C
IPR036220, UDP-Glc/GDP-Man_DH_C_sf
IPR014026, UDP-Glc/GDP-Man_DH_dimer
IPR001732, UDP-Glc/GDP-Man_DH_N
IPR028356, UDPglc_DH_euk

The PANTHER Classification System

More...PANTHERi		PTHR11374, PTHR11374, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00984, UDPG_MGDP_dh, 1 hit
PF03720, UDPG_MGDP_dh_C, 1 hit
PF03721, UDPG_MGDP_dh_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF500133, UDPglc_DH_euk, 1 hit
PIRSF000124, UDPglc_GDPman_dh, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00984, UDPG_MGDP_dh_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit
SSF52413, SSF52413, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03026, NDP-sugDHase, 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.

Q5F3T9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFEIKKICCI GAGYVGGPTC SVIAQMCPKI QVTVVDVNEA RINAWNSDTL 
        60         70         80         90        100
PIYEPGLKEV VESCRGRNLF FSTSIDDAIR EADLVFISVN TPTKTYGMGK 
       110        120        130        140        150
GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP 
       160        170        180        190        200
NLDLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDDSPEGQK AVRALCAVYE 
       210        220        230        240        250
HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE 
       260        270        280        290        300
VARAIGTDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW 
       310        320        330        340        350
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS 
       360        370        380        390        400
IYISKYLMDE GAKLHIYDPK VPKEQIILDL SHPGVSEDNQ VSRLVTISQD 
       410        420        430        440        450
PYEACDGAHA LVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDDLHN 
       460        470        480        490 
ELQVIGFQIE TIGKKVSAKR IPFASSCEIP KFSLQDPPVK KPRV
Length:494
Mass (Da):55,064
Last modified:March 15, 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:iB5D9F2590D366122
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
AJ851561 mRNA Translation: CAH65195.1

NCBI Reference Sequences

More...RefSeqi		NP_001012599.1, NM_001012581.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSGALT00000090339; ENSGALP00000060119; ENSGALG00000041993

Database of genes from NCBI RefSeq genomes

More...GeneIDi		422792

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		gga:422792

<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
AJ851561 mRNA Translation: CAH65195.1
RefSeqiNP_001012599.1, NM_001012581.1

3D structure databases

SMRiQ5F3T9
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000023101

Proteomic databases

PaxDbiQ5F3T9

Genome annotation databases

EnsembliENSGALT00000090339; ENSGALP00000060119; ENSGALG00000041993
GeneIDi422792
KEGGigga:422792

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7358

Phylogenomic databases

eggNOGiKOG2666, Eukaryota
GeneTreeiENSGT00390000015355
HOGENOMiCLU_023810_7_2_1
InParanoidiQ5F3T9
OMAiCLNLPEV
OrthoDBi915490at2759
PhylomeDBiQ5F3T9

Enzyme and pathway databases

UniPathwayiUPA00038;UER00491
ReactomeiR-GGA-173599, Formation of the active cofactor, UDP-glucuronate

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q5F3T9

Gene expression databases

BgeeiENSGALG00000014320, Expressed in liver and 13 other tissues

Family and domain databases

InterProiView protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR036291, NAD(P)-bd_dom_sf
IPR017476, UDP-Glc/GDP-Man
IPR014027, UDP-Glc/GDP-Man_DH_C
IPR036220, UDP-Glc/GDP-Man_DH_C_sf
IPR014026, UDP-Glc/GDP-Man_DH_dimer
IPR001732, UDP-Glc/GDP-Man_DH_N
IPR028356, UDPglc_DH_euk
PANTHERiPTHR11374, PTHR11374, 1 hit
PfamiView protein in Pfam
PF00984, UDPG_MGDP_dh, 1 hit
PF03720, UDPG_MGDP_dh_C, 1 hit
PF03721, UDPG_MGDP_dh_N, 1 hit
PIRSFiPIRSF500133, UDPglc_DH_euk, 1 hit
PIRSF000124, UDPglc_GDPman_dh, 1 hit
SMARTiView protein in SMART
SM00984, UDPG_MGDP_dh_C, 1 hit
SUPFAMiSSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit
SSF52413, SSF52413, 1 hit
TIGRFAMsiTIGR03026, NDP-sugDHase, 1 hit

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 nameiUGDH_CHICK
<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: Q5F3T9
<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: February 5, 2008
Last sequence update: March 15, 2005
Last modified: September 29, 2021
This is version 115 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 programChordata 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

Reference proteome

Documents

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