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 142 (11 Dec 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1

Gene

RHM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II) (PubMed:14671019, PubMed:17190829, PubMed:19056285). Plays a major role in supplying UDP-rhamnose for flavonol biosynthesis (PubMed:18757557). Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose (By similarity).By similarity4 Publications

Miscellaneous

The increased accumulation of auxin in rol1-2 seedlings appears to be caused by a flavonol-induced modification of auxin transport (PubMed:18567791, PubMed:21502189). In bacteria, TDP-L-rhamnose is formed by the successive action of three different enzymes on TDP-D-glucose. In plants, on the other hand, a single polypeptide probably catalyzes all three reactions that lead to the conversion of UDP-D-glucose to UDP-L-rhamnose.2 Publications

<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

Protein has several cofactor binding sites:

<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: Carbohydrate biosynthesis

This protein is involved in Carbohydrate biosynthesis.Curated
View all proteins of this organism that are known to be involved in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei132SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei133Proton donorBy similarity1
Active sitei134Proton acceptorBy similarity1
Active sitei159Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi13 – 19NADSequence analysis7
Nucleotide bindingi391 – 397NADPBy similarity7

<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 functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processCell wall biogenesis/degradation
LigandNAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT1G78570-MONOMER
MetaCyc:AT1G78570-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:
Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM11 Publication
Alternative name(s):
Protein REPRESSOR OF LRX1 11 Publication
Rhamnose biosynthetic enzyme 1
Short name:
AtRHM1
Including the following 2 domains:
UDP-glucose 4,6-dehydratase1 Publication (EC:4.2.1.761 Publication)
UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase1 Publication (EC:1.1.1.-1 Publication, EC:5.1.3.-1 Publication)
<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:RHM11 Publication
Synonyms:ROL11 Publication
Ordered Locus Names:At1g78570
ORF Names:T30F21.10
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<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
  • UP000006548 <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 1

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT1G78570

The Arabidopsis Information Resource

More...
TAIRi
locus:2202960 AT1G78570

<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

Cytoplasm

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Hyponastic growth, aberrant pavement cell and stomatal morphology in cotyledons, and defective trichome formation.1 Publication

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>Mutagenesisi283R → K in rol1-2; Abolishes dehydratase activity in vitro (PubMed:16766693). Induces aberrant accumulation of flavonols leading to alterations in plant growth and cell shape formation (PubMed:18567791, PubMed:18757557). 3 Publications1

<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_00001832521 – 669Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1Add BLAST669

Proteomic databases

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

More...
PaxDbi
Q9SYM5

PRoteomics IDEntifications database

More...
PRIDEi
Q9SYM5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9SYM5

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in roots, stems, leaves, seedlings, inflorescence tips, and siliques. Detected in the adaxial side of cotyledons, in the emerging leaves and in trichomes. Also detected in the root tip, more precisely in the epidermal cells in the meristematic and elongation zone.5 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9SYM5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9SYM5 AT

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
29412, 4 interactors

Protein interaction database and analysis system

More...
IntActi
Q9SYM5, 2 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT1G78570.1

<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
Q9SYM5

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

<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 dehydratase activity is contained in the N-terminal region while the epimerase and reductase activities are in the C-terminal region.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

In the C-terminal section; belongs to the dTDP-4-dehydrorhamnose reductase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0747 Eukaryota
COG1088 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000167988

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9SYM5

KEGG Orthology (KO)

More...
KOi
K12450

Identification of Orthologs from Complete Genome Data

More...
OMAi
DALVGNH

Database of Orthologous Groups

More...
OrthoDBi
848823at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9SYM5

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05246 dTDP_GD_SDR_e, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
IPR029903 RmlD-like-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
PF04321 RmlD_sub_bind, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01181 dTDP_gluc_dehyt, 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>. 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_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.

Q9SYM5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASYTPKNIL ITGAAGFIAS HVANRLIRSY PDYKIVVLDK LDYCSNLKNL
60 70 80 90 100
NPSKHSPNFK FVKGDIASAD LVNHLLITEG IDTIMHFAAQ THVDNSFGNS
110 120 130 140 150
FEFTKNNIYG THVLLEACKV TGQIRRFIHV STDEVYGETD EDALVGNHEA
160 170 180 190 200
SQLLPTNPYS ATKAGAEMLV MAYGRSYGLP VITTRGNNVY GPNQFPEKLI
210 220 230 240 250
PKFILLAMRG QVLPIHGDGS NVRSYLYCED VAEAFEVVLH KGEVGHVYNI
260 270 280 290 300
GTKKERRVND VAKDICKLFN MDPEANIKFV DNRPFNDQRY FLDDQKLKKL
310 320 330 340 350
GWSERTTWEE GLKKTMDWYT QNPEWWGDVS GALLPHPRML MMPGGRHFDG
360 370 380 390 400
SEDNSLAATL SEKPSQTHMV VPSQRSNGTP QKPSLKFLIY GKTGWIGGLL
410 420 430 440 450
GKICDKQGIA YEYGKGRLED RSSLLQDIQS VKPTHVFNSA GVTGRPNVDW
460 470 480 490 500
CESHKTETIR ANVAGTLTLA DVCREHGLLM MNFATGCIFE YDDKHPEGSG
510 520 530 540 550
IGFKEEDTPN FTGSFYSKTK AMVEELLKEY DNVCTLRVRM PISSDLNNPR
560 570 580 590 600
NFITKISRYN KVVNIPNSMT VLDELLPISI EMAKRNLKGI WNFTNPGVVS
610 620 630 640 650
HNEILEMYRD YINPEFKWAN FTLEEQAKVI VAPRSNNEMD ASKLKKEFPE
660
LLSIKESLIK YAYGPNKKT
Length:669
Mass (Da):75,372
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFB8DF9C864F176D4
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
AC007260 Genomic DNA Translation: AAD30579.1
CP002684 Genomic DNA Translation: AEE36122.1
AY042833 mRNA Translation: AAK68773.1
AY081471 mRNA Translation: AAM10033.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C96814

NCBI Reference Sequences

More...
RefSeqi
NP_177978.1, NM_106504.4

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT1G78570.1; AT1G78570.1; AT1G78570

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
844193

Gramene; a comparative resource for plants

More...
Gramenei
AT1G78570.1; AT1G78570.1; AT1G78570

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G78570

<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
AC007260 Genomic DNA Translation: AAD30579.1
CP002684 Genomic DNA Translation: AEE36122.1
AY042833 mRNA Translation: AAK68773.1
AY081471 mRNA Translation: AAM10033.1
PIRiC96814
RefSeqiNP_177978.1, NM_106504.4

3D structure databases

SMRiQ9SYM5
ModBaseiSearch...

Protein-protein interaction databases

BioGridi29412, 4 interactors
IntActiQ9SYM5, 2 interactors
STRINGi3702.AT1G78570.1

PTM databases

iPTMnetiQ9SYM5

Proteomic databases

PaxDbiQ9SYM5
PRIDEiQ9SYM5

Genome annotation databases

EnsemblPlantsiAT1G78570.1; AT1G78570.1; AT1G78570
GeneIDi844193
GrameneiAT1G78570.1; AT1G78570.1; AT1G78570
KEGGiath:AT1G78570

Organism-specific databases

AraportiAT1G78570
TAIRilocus:2202960 AT1G78570

Phylogenomic databases

eggNOGiKOG0747 Eukaryota
COG1088 LUCA
HOGENOMiHOG000167988
InParanoidiQ9SYM5
KOiK12450
OMAiDALVGNH
OrthoDBi848823at2759
PhylomeDBiQ9SYM5

Enzyme and pathway databases

BioCyciARA:AT1G78570-MONOMER
MetaCyc:AT1G78570-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9SYM5

Gene expression databases

ExpressionAtlasiQ9SYM5 baseline and differential
GenevisibleiQ9SYM5 AT

Family and domain databases

CDDicd05246 dTDP_GD_SDR_e, 1 hit
InterProiView protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
IPR029903 RmlD-like-bd
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
PF04321 RmlD_sub_bind, 1 hit
SUPFAMiSSF51735 SSF51735, 2 hits
TIGRFAMsiTIGR01181 dTDP_gluc_dehyt, 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 nameiRHM1_ARATH
<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: Q9SYM5
<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 26, 2005
Last sequence update: May 1, 2000
Last modified: December 11, 2019
This is version 142 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 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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