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Protein

Protein diaphanous homolog 1

Gene

Diaph1

Organism
Mus musculus (Mouse)
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

Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (PubMed:10678165, PubMed:15044801, PubMed:18572016). Required for cytokinesis, and transcriptional activation of the serum response factor (PubMed:10678165, PubMed:15044801, PubMed:18572016). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (PubMed:10678165, PubMed:15044801, PubMed:18572016). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (PubMed:15311282). Has neurite outgrowth promoting activity (PubMed:10678165, PubMed:15044801, PubMed:18572016). Acts in a Rho-dependent manner to recruit PFY1 to the membrane (PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (By similarity). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the control of cell shape (By similarity). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (PubMed:23558171).By similarity6 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

  • actin binding Source: MGI
  • identical protein binding Source: IntAct
  • ion channel binding Source: BHF-UCL
  • profilin binding Source: MGI
  • Rho GTPase binding Source: MGI

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 functionActin-binding
Biological processHearing

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6785631 ERBB2 Regulates Cell Motility
R-MMU-6798695 Neutrophil degranulation

<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:
Protein diaphanous homolog 1
Alternative name(s):
Diaphanous-related formin-1
Short name:
DRF1
p140mDIA
Short name:
mDIA11 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:Diaph1
Synonyms:Diap1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 18

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1194490 Diaph1

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, 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

Knockout mice show normal organization of the cerebral cortex with no significant differences in cortical white matter or callosal thickness (PubMed:24781755). Histological analysis of coronal brain sections at early and postnatal stages shows unilateral ventricular enlargement (PubMed:24781755).1 Publication

<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_00001948941 – 1255Protein diaphanous homolog 1Add BLAST1255

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 residuei1N-acetylmethionineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei751PhosphothreonineBy similarity1
Modified residuei1040N6-acetyllysineBy similarity1
Modified residuei1086N6-acetyllysineBy similarity1
Modified residuei1104PhosphotyrosineCombined sources1
Modified residuei1237PhosphoserineBy similarity1

<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

Phosphorylation at Thr-751 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O08808

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O08808

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O08808

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

More...
PaxDbi
O08808

PRoteomics IDEntifications database

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PRIDEi
O08808

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O08808

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O08808

<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

Widely expressed. In the organ of Corti, it is expressed at the outer and inner hair cell layers. Expression at the inner hair cell layer is restricted to inner pillar cells. Detected in cochlear spiral ganglion neurons (PubMed:27808407).1 Publication

<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

Expressed in the ventricular and subventricular zone progenitor cells of the dorsal and ventral forebrain and the brainstem, at embryonic days E12.5, E14.5, and E17.5. At later embryonic age, it is observed in neurons of the cortex and hippocampus. During postnatal development, expression is detected in the cerebral cortex, basal ganglia, hippocampus, thalamus, and external granular layer of the cerebellum.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000024456 Expressed in 282 organ(s), highest expression level in conjunctival fornix

CleanEx database of gene expression profiles

More...
CleanExi
MM_DIAP1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O08808 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O08808 MM

<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 (PubMed:14992721, PubMed:15864301). Interacts with the GTP-bound form of RHOA (PubMed:9214622). Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC (PubMed:10814512, PubMed:15311282, PubMed:15864301). Interacts with SCAI (PubMed:19350017). Interacts with DCAF7, via FH2 domain (By similarity). Interacts with NCDN (PubMed:18572016). Interacts with OSBPL10, OSBPL2, VIM, TUBB and DYN1 (By similarity).By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199221, 7 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O08808

Database of interacting proteins

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DIPi
DIP-29028N

Protein interaction database and analysis system

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IntActi
O08808, 17 interactors

Molecular INTeraction database

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MINTi
O08808

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000111297

<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

11255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V9DX-ray2.60A/B/C/D826-1163[»]
1Z2CX-ray3.00B/D69-451[»]
2BAPX-ray3.30A/B135-451[»]
C/D1145-1200[»]
2BNXX-ray2.40A/B131-516[»]
2F31X-ray2.10A135-367[»]
B1177-1196[»]
2V8FX-ray1.10C635-655[»]
3EG5X-ray2.70B/D69-451[»]
3O4XX-ray3.20A/B/C/D131-458[»]
E/F/G/H736-1200[»]
3OBVX-ray2.75A/B/C/D131-457[»]
E/F/G/H753-1209[»]
4UWXX-ray1.65A/B135-369[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O08808

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

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SMRi
O08808

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O08808

<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>Domaini75 – 440GBD/FH3PROSITE-ProRule annotationAdd BLAST366
Domaini586 – 747FH1Add BLAST162
Domaini752 – 1154FH2PROSITE-ProRule annotationAdd BLAST403
Domaini1177 – 1205DADPROSITE-ProRule annotationAdd BLAST29

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili460 – 562Sequence analysisAdd BLAST103
Coiled coili1027 – 1179Sequence analysisAdd BLAST153

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 biasi1196 – 1199Arg/Lys-rich (basic)4

<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 DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1924 Eukaryota
ENOG410Y29H LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159910

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000293231

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051357

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O08808

KEGG Orthology (KO)

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KOi
K05740

Database of Orthologous Groups

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OrthoDBi
1204639at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O08808

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR014767 DAD_dom
IPR010465 Drf_DAD
IPR015425 FH2_Formin
IPR010472 FH3_dom
IPR027653 Formin_Diaph1
IPR009408 Formin_homology_1
IPR014768 GBD/FH3_dom
IPR010473 GTPase-bd

The PANTHER Classification System

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PANTHERi
PTHR23213:SF17 PTHR23213:SF17, 2 hits

Pfam protein domain database

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Pfami
View protein in Pfam
PF06345 Drf_DAD, 1 hit
PF06346 Drf_FH1, 1 hit
PF06367 Drf_FH3, 1 hit
PF06371 Drf_GBD, 1 hit
PF02181 FH2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01139 Drf_FH3, 1 hit
SM01140 Drf_GBD, 1 hit
SM00498 FH2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51231 DAD, 1 hit
PS51444 FH2, 1 hit
PS51232 GBD_FH3, 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>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 4 potential isoforms that are computationally mapped.Show allAlign All

O08808-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK
60 70 80 90 100
EKEKPNSAHR NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK
110 120 130 140 150
QQPLREKDIV IKREMVSQYL HTSKAGMNQK ESSRSAMMYI QELRSGLRDM
160 170 180 190 200
HLLSCLESLR VSLNNNPVSW VQTFGAEGLA SLLDILKRLH DEKEETSGNY
210 220 230 240 250
DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD PAVPNMMIDA
260 270 280 290 300
AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA
310 320 330 340 350
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK
360 370 380 390 400
VQLCVFDEQG DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH
410 420 430 440 450
FLSILQHLLL VRNDYEARPQ YYKLIEECVS QIVLHKNGTD PDFKCRHLQI
460 470 480 490 500
DIERLVDQMI DKTKVEKSEA KATELEKKLD SELTARHELQ VEMKKMENDF
510 520 530 540 550
EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA KLSKELEDAK
560 570 580 590 600
NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP
610 620 630 640 650
PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP
660 670 680 690 700
PPLPGATAIP PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP
710 720 730 740 750
PLPGGPGLPP PPPPFPGAPG IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL
760 770 780 790 800
TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF WTKVKEDRFE NNELFAKLTL
810 820 830 840 850
AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA QNLSIFLGSF
860 870 880 890 900
RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL
910 920 930 940 950
AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL
960 970 980 990 1000
RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM
1010 1020 1030 1040 1050
TLLHFLAELC ENDHPEVLKF PDELAHVEKA SRVSAENLQK SLDQMKKQIA
1060 1070 1080 1090 1100
DVERDVQNFP AATDEKDKFV EKMTSFVKDA QEQYNKLRMM HSNMETLYKE
1110 1120 1130 1140 1150
LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE TEEKMRRAKL
1160 1170 1180 1190 1200
AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG
1210 1220 1230 1240 1250
PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL

VGRAS
Length:1,255
Mass (Da):139,343
Last modified:July 1, 1997 - 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:i09404164873CA7C1
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 are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PV41E9PV41_MOUSE
Protein diaphanous homolog 1
Diaph1
1,264Annotation score:

Annotation score:2 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>
F6XC54F6XC54_MOUSE
Protein diaphanous homolog 1
Diaph1
1,220Annotation 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>
D3Z074D3Z074_MOUSE
Protein diaphanous homolog 1
Diaph1
1,220Annotation 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>
E9PXV7E9PXV7_MOUSE
Protein diaphanous homolog 1
Diaph1
1,255Annotation 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>

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

More...
DDBJi
Links Updated
U96963 mRNA Translation: AAC53280.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS57121.1

Protein sequence database of the Protein Information Resource

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PIRi
T31065

NCBI Reference Sequences

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RefSeqi
NP_031884.1, NM_007858.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.195916

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456

Database of genes from NCBI RefSeq genomes

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GeneIDi
13367

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:13367

UCSC genome browser

More...
UCSCi
uc033hgk.1 mouse

<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
U96963 mRNA Translation: AAC53280.1
CCDSiCCDS57121.1
PIRiT31065
RefSeqiNP_031884.1, NM_007858.4
UniGeneiMm.195916

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V9DX-ray2.60A/B/C/D826-1163[»]
1Z2CX-ray3.00B/D69-451[»]
2BAPX-ray3.30A/B135-451[»]
C/D1145-1200[»]
2BNXX-ray2.40A/B131-516[»]
2F31X-ray2.10A135-367[»]
B1177-1196[»]
2V8FX-ray1.10C635-655[»]
3EG5X-ray2.70B/D69-451[»]
3O4XX-ray3.20A/B/C/D131-458[»]
E/F/G/H736-1200[»]
3OBVX-ray2.75A/B/C/D131-457[»]
E/F/G/H753-1209[»]
4UWXX-ray1.65A/B135-369[»]
ProteinModelPortaliO08808
SMRiO08808
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199221, 7 interactors
CORUMiO08808
DIPiDIP-29028N
IntActiO08808, 17 interactors
MINTiO08808
STRINGi10090.ENSMUSP00000111297

PTM databases

iPTMnetiO08808
PhosphoSitePlusiO08808

Proteomic databases

EPDiO08808
jPOSTiO08808
MaxQBiO08808
PaxDbiO08808
PRIDEiO08808

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456
GeneIDi13367
KEGGimmu:13367
UCSCiuc033hgk.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1729
MGIiMGI:1194490 Diaph1

Phylogenomic databases

eggNOGiKOG1924 Eukaryota
ENOG410Y29H LUCA
GeneTreeiENSGT00940000159910
HOGENOMiHOG000293231
HOVERGENiHBG051357
InParanoidiO08808
KOiK05740
OrthoDBi1204639at2759
PhylomeDBiO08808

Enzyme and pathway databases

ReactomeiR-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6785631 ERBB2 Regulates Cell Motility
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Diaph1 mouse
EvolutionaryTraceiO08808

Protein Ontology

More...
PROi
PR:O08808

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000024456 Expressed in 282 organ(s), highest expression level in conjunctival fornix
CleanExiMM_DIAP1
ExpressionAtlasiO08808 baseline and differential
GenevisibleiO08808 MM

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR014767 DAD_dom
IPR010465 Drf_DAD
IPR015425 FH2_Formin
IPR010472 FH3_dom
IPR027653 Formin_Diaph1
IPR009408 Formin_homology_1
IPR014768 GBD/FH3_dom
IPR010473 GTPase-bd
PANTHERiPTHR23213:SF17 PTHR23213:SF17, 2 hits
PfamiView protein in Pfam
PF06345 Drf_DAD, 1 hit
PF06346 Drf_FH1, 1 hit
PF06367 Drf_FH3, 1 hit
PF06371 Drf_GBD, 1 hit
PF02181 FH2, 1 hit
SMARTiView protein in SMART
SM01139 Drf_FH3, 1 hit
SM01140 Drf_GBD, 1 hit
SM00498 FH2, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS51231 DAD, 1 hit
PS51444 FH2, 1 hit
PS51232 GBD_FH3, 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 nameiDIAP1_MOUSE
<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: O08808
<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: July 15, 1999
Last sequence update: July 1, 1997
Last modified: January 16, 2019
This is version 177 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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