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Entry version 108 (16 Oct 2019)
Sequence version 1 (05 Jul 2004)
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Protein

Transcription factor SPEECHLESS

Gene

SPCH

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

Transcription factor acting as an integration node for stomata and brassinosteroid (BR) signaling pathways to control stomatal initiation and development (PubMed:22466366, PubMed:28507175). Activates transcription when in the presence of SCRM/ICE1 (PubMed:28507175). Functions as a dimer with SCRM or SCRM2 during stomatal initiation (PubMed:18641265). Required for the initiation, the spacing and the formation of stomata, by promoting the first asymmetric cell divisions (PubMed:25843888, PubMed:25680231, PubMed:19008449). Together with FMA and MUTE, modulates the stomata formation. Involved in the regulation of growth reduction under osmotic stress (e.g. mannitol), associated with a quick decrease of meristemoid mother cells (MMCs) number lower stomatal index and density (PubMed:25381317).9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Negatively regulated through phosphorylation by the MAPK module (PubMed:19008449). Activity is constrained by polarized BASL in stomatal lineage ground cells (SLGCs) undergoing ACD (PubMed:27746029).2 Publications

<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 functionActivator, Developmental protein, DNA-binding
Biological processTranscription, Transcription regulation

<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:
Transcription factor SPEECHLESS1 Publication
Alternative name(s):
Basic helix-loop-helix protein 982 Publications
Short name:
AtbHLH982 Publications
Short name:
bHLH 982 Publications
Transcription factor EN 191 Publication
bHLH transcription factor bHLH0982 Publications
<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:SPCH1 Publication
Synonyms:BHLH982 Publications, EN191 Publication
Ordered Locus Names:At5g53210Imported
ORF Names:MFH8.15Imported
<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 5

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT5G53210

The Arabidopsis Information Resource

More...
TAIRi
locus:2154197 AT5G53210

<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

Nucleus

<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

Stomatal defects in cotyledons and hypocotyls.2 Publications

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>Mutagenesisi38S → A: Extra divisions outside the stomatal cell lineage and reduced phosphorylation by ASK7; when associated with A-44. 2 Publications1
Mutagenesisi44T → A: Extra divisions outside the stomatal cell lineage and reduced phosphorylation by ASK7; when associated with A-38. 2 Publications1
Mutagenesisi65S → A: Extra divisions outside the stomatal cell lineage and reduced phosphorylation by ASK7. 1 Publication1
Mutagenesisi104 – 112HVTVERNRR → PVTVPRNRP: Plants are fertile and have a normal growth, but they form few stomata, some of them clustered, in cotyledons and leaves, and lack stomata in hypocotyls. 1 Publication9
Mutagenesisi111R → W in spch-5; normal growth, but extremely low number of sometimes clustered stomata in leaves and stomata free hypocotyls due to decreased ability to initiate and amplify lineages, defects in asymmetric cell fate allocation, and misorientation of asymmetric division planes. These phenotypes are partly rescued by brassinosteroids (BRs) by rescuing the expression of a set of target genes. 1 Publication1
Mutagenesisi171 – 264Missing in delta-93; impaired MPK3/MPK6 mediated phosphorylation and large clusters of stomata in leaves epidermis. 1 PublicationAdd BLAST94
Mutagenesisi171 – 220Missing in delta-49; reduced MPK3/MPK6 mediated phosphorylation and excessive numbers of asymmetric cell divisions in leaves epidermis leading to the creation of cells with meristemoid morphology, but fails to produce stomata. 1 PublicationAdd BLAST50
Mutagenesisi186S → A: Strong reduction of CDKA-1-mediated phosphorylation. Unable to rescue stomatal defects in disrupted mutants. Triggers excess physically asymmetric divisions but not stomata formation. 1 Publication1
Mutagenesisi186S → D: Phosphomimetic, presence of stomatal clusters and increased stomatal density, can complement stomatal production defects associated with inactive CDKA-1. 1 Publication1
Mutagenesisi193S → A: Unable to rescue disruption phenotype. Ectopic stomata formation and increased accumulation; when associated with A-211, A-214, A-219 and A-255. Ectopic asymmetric cell divisions, but fails to produce stomata, and reduced repression by osmotic stress (e.g. mannitol); when associated with A-211, A-214 and A-219. 1 Publication1
Mutagenesisi211S → A: Ectopic stomata formation and increased accumulation; when associated with A-193, A-214, A-219 and A-255. Ectopic asymmetric cell divisions, but fails to produce stomata, and reduced repression by osmotic stress (e.g. mannitol); when associated with A-193, A-214 and A-219. 1 Publication1
Mutagenesisi214T → A: Ectopic stomata formation and increased accumulation; when associated with A-193, A-211, A-219 and A-255. Ectopic asymmetric cell divisions, but fails to produce stomata, and reduced repression by osmotic stress (e.g. mannitol); when associated with A-193, A-211 and A-219. 1 Publication1
Mutagenesisi219S → A: Ectopic stomata formation and increased accumulation; when associated with A-193, A-211, A-214 and A-255. Ectopic asymmetric cell divisions, but fails to produce stomata, and reduced repression by osmotic stress (e.g. mannitol); when associated with A-193, A-211 and A-214. 1 Publication1
Mutagenesisi237 – 267Missing in delta-31; reduced MPK3/MPK6 mediated phosphorylation and excessive numbers of asymmetric cell divisions in leaves epidermis leading to the creation of cells with meristemoid morphology. 1 PublicationAdd BLAST31
Mutagenesisi255S → A: Ectopic stomata formation and increased accumulation; when associated with A-193, A-211, A-214 and A-219. 1 Publication1
Mutagenesisi290V → M in spch-2; reduced stomatal index. 1 Publication1
Mutagenesisi358 – 364Missing in spch-1; no stomata. 1 Publication7

<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_00003588561 – 364Transcription factor SPEECHLESSAdd BLAST364

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 residuei38Phosphoserine; by ASK71 Publication1
Modified residuei40Phosphothreonine; by ASK71 Publication1
Modified residuei43Phosphoserine; by ASK71 Publication1
Modified residuei44Phosphothreonine; by ASK71 Publication1
Modified residuei65Phosphoserine; by ASK71 Publication1
Modified residuei171Phosphoserine; by ASK71 Publication1
Modified residuei177Phosphoserine; by ASK7, MPK3 and MPK61 Publication1 Publication1
Modified residuei181Phosphoserine; by ASK71 Publication1
Modified residuei186Phosphoserine; by CDKA-1, ASK7, MPK3 and MPK61 Publication2 Publications1
Modified residuei193Phosphoserine; by MPK3 and MPK61 Publication1
Modified residuei211Phosphoserine; by MPK3 and MPK61 Publication1
Modified residuei214Phosphothreonine; by ASK7, MPK3 and MPK62 Publications1
Modified residuei219Phosphoserine; by ASK7, MPK3 and MPK62 Publications1

<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

Phosphorylated by ASK7/BIN2 and ASK3/SK12; this post-translational modification inhibits activity and limit epidermal cell proliferation (PubMed:30429609, PubMed:22466366). Phosphorylation by MPK3 and MPK6 leads to the inhibition of stomatal fate and to degradation (PubMed:25843888, PubMed:19008449). Stabilized by CDKA-1-mediated phosphorylation at Ser-186 which promotes stomatal development (PubMed:25680231).5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

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PaxDbi
Q700C7

PRoteomics IDEntifications database

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PRIDEi
Q700C7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q700C7

<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 developing leaf epidermis (PubMed:17183265). Reduced accumulation in the stomatal lineage ground cells (SLGCs) where BASL is polarized in the cell cortex (PubMed:27746029). Observed in small cells of non-protruding hypocotyl cell files and of developing cotyledon epidermis (PubMed:22466366). Restricted to meristemoids (stomatal precursor cell) in leaves epidermis, mostly in dividing cells of non-protruding cell files (PubMed:25680231, PubMed:18641265, PubMed:19008449).6 Publications

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

First observed in a subset of undifferentiated epidermal cells, often by pair of neighboring cells. Later confined to small epidermal cells, including cells that have recently divided next to stomatal lineage cells. Also expressed in stomatal lineage cells, fading out progressively during meristemoid determination.3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Repressed by brassinazole (BRZ), thus leading to a reduced number of stomata in hypocotyls (PubMed:25680231). Inhibited by low relative humidity (LRH) via epigenetic CG methylation, thus leading to a reduced stomatal index (PubMed:22442411). Repressed by YDA (at protein level) (PubMed:19008449). Post-transcriptional decrease of protein level in response to osmotic stress (e.g. mannitol), through the action of a mitogen-activated protein kinase (MAPK) cascade; this repression is reversed by the MAPK kinase inhibitor PD98059 (PubMed:25381317).4 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q700C7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q700C7 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

<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

Homodimer (Probable). Forms dimers with SCRM and SCRM2 (PubMed:18641265, PubMed:28507175). May interact with CDKA-1 (PubMed:25680231).

Curated3 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
20647, 2 interactors

Database of interacting proteins

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DIPi
DIP-61849N

Protein interaction database and analysis system

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IntActi
Q700C7, 1 interactor

STRING: functional protein association networks

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STRINGi
3702.AT5G53210.1

<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

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SMRi
Q700C7

Database of comparative protein structure models

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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

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>Domaini99 – 150bHLHPROSITE-ProRule annotationAdd BLAST52

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>Regioni99 – 112Basic motifPROSITE-ProRule annotationAdd BLAST14
Regioni113 – 150Helix-loop-helix motifPROSITE-ProRule annotationAdd BLAST38

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi78 – 84Poly-GluSequence analysis7
Compositional biasi172 – 256Pro-richPROSITE-ProRule annotationAdd BLAST85
Compositional biasi198 – 204His-richPROSITE-ProRule annotation7
Compositional biasi238 – 272Ser-richPROSITE-ProRule annotationAdd BLAST35

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJ4X Eukaryota
ENOG410ZJF9 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000238962

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q700C7

KEGG Orthology (KO)

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KOi
K20558

Identification of Orthologs from Complete Genome Data

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OMAi
DDTMVHS

Database of Orthologous Groups

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OrthoDBi
1208483at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q700C7

Family and domain databases

Conserved Domains Database

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CDDi
cd00083 HLH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.280.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00010 HLH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00353 HLH, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47459 SSF47459, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50888 BHLH, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q700C7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQEIIPDFLE ECEFVDTSLA GDDLFAILES LEGAGEISPT AASTPKDGTT
60 70 80 90 100
SSKELVKDQD YENSSPKRKK QRLETRKEED EEEEDGDGEA EEDNKQDGQQ
110 120 130 140 150
KMSHVTVERN RRKQMNEHLT VLRSLMPCFY VKRGDQASII GGVVEYISEL
160 170 180 190 200
QQVLQSLEAK KQRKTYAEVL SPRVVPSPRP SPPVLSPRKP PLSPRINHHQ
210 220 230 240 250
IHHHLLLPPI SPRTPQPTSP YRAIPPQLPL IPQPPLRSYS SLASCSSLGD
260 270 280 290 300
PPPYSPASSS SSPSVSSNHE SSVINELVAN SKSALADVEV KFSGANVLLK
310 320 330 340 350
TVSHKIPGQV MKIIAALEDL ALEILQVNIN TVDETMLNSF TIKIGIECQL
360
SAEELAQQIQ QTFC
Length:364
Mass (Da):40,169
Last modified:July 5, 2004 - 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:i3946B847B6D4371C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1P8BE01A0A1P8BE01_ARATH
Basic helix-loop-helix (BHLH) DNA-b...
SPCH MFH8.15, SPEECHLESS, At5g53210
351Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAB09783 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
DQ868373 mRNA Translation: ABI26170.1
AB013388 Genomic DNA Translation: BAB09783.1 Sequence problems.
CP002688 Genomic DNA Translation: AED96323.1
AJ630498 mRNA Translation: CAG25871.1
AY568670 mRNA Translation: AAS79560.1

NCBI Reference Sequences

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RefSeqi
NP_200133.2, NM_124700.3

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT5G53210.1; AT5G53210.1; AT5G53210

Database of genes from NCBI RefSeq genomes

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GeneIDi
835402

Gramene; a comparative resource for plants

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Gramenei
AT5G53210.1; AT5G53210.1; AT5G53210

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT5G53210

<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
DQ868373 mRNA Translation: ABI26170.1
AB013388 Genomic DNA Translation: BAB09783.1 Sequence problems.
CP002688 Genomic DNA Translation: AED96323.1
AJ630498 mRNA Translation: CAG25871.1
AY568670 mRNA Translation: AAS79560.1
RefSeqiNP_200133.2, NM_124700.3

3D structure databases

SMRiQ700C7
ModBaseiSearch...

Protein-protein interaction databases

BioGridi20647, 2 interactors
DIPiDIP-61849N
IntActiQ700C7, 1 interactor
STRINGi3702.AT5G53210.1

PTM databases

iPTMnetiQ700C7

Proteomic databases

PaxDbiQ700C7
PRIDEiQ700C7

Genome annotation databases

EnsemblPlantsiAT5G53210.1; AT5G53210.1; AT5G53210
GeneIDi835402
GrameneiAT5G53210.1; AT5G53210.1; AT5G53210
KEGGiath:AT5G53210

Organism-specific databases

AraportiAT5G53210
TAIRilocus:2154197 AT5G53210

Phylogenomic databases

eggNOGiENOG410IJ4X Eukaryota
ENOG410ZJF9 LUCA
HOGENOMiHOG000238962
InParanoidiQ700C7
KOiK20558
OMAiDDTMVHS
OrthoDBi1208483at2759
PhylomeDBiQ700C7

Miscellaneous databases

Protein Ontology

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PROi
PR:Q700C7

Gene expression databases

ExpressionAtlasiQ700C7 baseline and differential
GenevisibleiQ700C7 AT

Family and domain databases

CDDicd00083 HLH, 1 hit
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
PfamiView protein in Pfam
PF00010 HLH, 1 hit
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SUPFAMiSSF47459 SSF47459, 1 hit
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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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 nameiSPCH_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: Q700C7
Secondary accession number(s): Q9FK20
<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: December 16, 2008
Last sequence update: July 5, 2004
Last modified: October 16, 2019
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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