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Entry version 177 (11 Dec 2019)
Sequence version 2 (27 Jul 2011)
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Protein

Epidermal growth factor receptor kinase substrate 8

Gene

Eps8

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

Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.9 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 functionActin-binding

<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:
Epidermal growth factor receptor kinase substrate 8
<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:Eps8
<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 6

Organism-specific databases

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

More...
MGIi
MGI:104684 Eps8

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

<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

No visible phenotype. Defects in PDGF-induced membrane ruffling due to defects in Ras to Rac signals. Dendritic cells are impaired in directional and chemotactic migration and are delayed in reaching the draining lymph node in vivo after inflammatory challenge. Mice show short stereocilia.3 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>Mutagenesisi624S → A: Does not detach from actin following BDNF treatment; when associated with A-628. 1 Publication1
Mutagenesisi624S → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-628. 1 Publication1
Mutagenesisi628T → A: Does not detach from actin following BDNF treatment; when associated with A-624. 1 Publication1
Mutagenesisi628T → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-624. 1 Publication1
Mutagenesisi689V → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. 1 Publication1
Mutagenesisi693L → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. 1 Publication1
Mutagenesisi706R → A: Impairs both actin capping and bundling activities. 1 Publication1
Mutagenesisi708F → A: Impairs both actin capping and bundling activities. 1 Publication1

<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_00000869951 – 821Epidermal growth factor receptor kinase substrate 8Add BLAST821

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 residuei58PhosphoserineBy similarity1
Modified residuei223PhosphothreonineBy similarity1
Modified residuei317PhosphothreonineCombined sources1
Modified residuei475PhosphoserineBy similarity1
Modified residuei624Phosphoserine; by MAPK1 Publication1
Modified residuei628Phosphothreonine; by MAPK1 Publication1
Modified residuei658PhosphoserineCombined sources1
Modified residuei661PhosphoserineCombined sources1
Modified residuei684PhosphoserineCombined sources1
Modified residuei810PhosphoserineCombined sources1
Modified residuei814PhosphoserineCombined sources1

<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

Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during G2 phase, leading to its transient degradation and subsequent cell shape changes required to allow mitotic progression. Reappears at the midzone of dividing cells.1 Publication
Phosphorylation at Ser-624 and Thr-628 by MAPK following BDNF treatment promotes removal from actin and filopodia formation. Phosphorylated by several receptor tyrosine kinases.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q08509

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q08509

MaxQB - The MaxQuant DataBase

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MaxQBi
Q08509

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

More...
PaxDbi
Q08509

PeptideAtlas

More...
PeptideAtlasi
Q08509

PRoteomics IDEntifications database

More...
PRIDEi
Q08509

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q08509

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

More...
PhosphoSitePlusi
Q08509

<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 neuronal cell body and neurites, and prominently enriched in the axonal growth cone (PubMed:19564905). Expressed at the tips of cochlear hair cells stereocilia (PubMed:23918390).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000015766 Expressed in 311 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q08509 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q08509 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.

Part of a complex consisting of ABI1, EPS8 and SOS1.

Interacts with BAIAP2.

Interacts with SHB and LANCL1.

Interacts with EGFR; mediates EPS8 phosphorylation.

Interacts with MYO15A and WHRN.

8 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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199491, 8 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q08509

Database of interacting proteins

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DIPi
DIP-32858N

Protein interaction database and analysis system

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IntActi
Q08509, 11 interactors

Molecular INTeraction database

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MINTi
Q08509

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000052776

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q08509 protein

<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

1821
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q08509

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q08509

<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>Domaini69 – 129PH; first partAdd BLAST61
Domaini381 – 414PH; second partAdd BLAST34
Domaini530 – 589SH3PROSITE-ProRule annotationAdd BLAST60

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>Regioni648 – 821Effector regionAdd BLAST174
Regioni679 – 697Amphipathic helixAdd BLAST19
Regioni717 – 737Helix bundle 1Add BLAST21
Regioni751 – 756Helix bundle 26
Regioni761 – 766Helix bundle 36
Regioni765 – 784Helix bundle 4Add BLAST20

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 biasi210 – 213Poly-Pro4
Compositional biasi322 – 325Poly-Pro4
Compositional biasi421 – 440Pro-richAdd BLAST20
Compositional biasi620 – 650Pro-richAdd BLAST31
Compositional biasi658 – 663Poly-Ser6

<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 effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity (PubMed:11524436). It mediates both barbed-end actin capping and actin bundling activities (PubMed:20532239). The capping activity is mediated by an amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers, while the bundling activity is mediated by a compact 4 helix bundle, which contacts 3 actin subunits along the filament (PubMed:20532239).2 Publications
The SH3 domain mediates interaction with SHB.By similarity

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

Belongs to the EPS8 family.Curated

Keywords - Domaini

SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3557 Eukaryota
ENOG410XT9R LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156403

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000060324

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q08509

KEGG Orthology (KO)

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KOi
K17277

Identification of Orthologs from Complete Genome Data

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OMAi
SETSQYH

Database of Orthologous Groups

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OrthoDBi
218804at2759

TreeFam database of animal gene trees

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TreeFami
TF313069

Family and domain databases

Conserved Domains Database

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CDDi
cd01210 PTB_EPS8, 1 hit
cd11764 SH3_Eps8, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.150.50, 1 hit
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR030222 EPS8
IPR039801 EPS8-like
IPR033928 EPS8_PTB
IPR035462 Eps8_SH3
IPR011993 PH-like_dom_sf
IPR013625 PTB
IPR006020 PTB/PI_dom
IPR013761 SAM/pointed_sf
IPR041418 SAM_3
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain

The PANTHER Classification System

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PANTHERi
PTHR12287 PTHR12287, 1 hit
PTHR12287:SF21 PTHR12287:SF21, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08416 PTB, 1 hit
PF18016 SAM_3, 1 hit
PF00018 SH3_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00462 PTB, 1 hit
SM00326 SH3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50044 SSF50044, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50002 SH3, 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 5 potential isoforms that are computationally mapped.Show allAlign All

Q08509-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNGHMSNRSS GYGVYPSQLN GYGSSPPYSQ MDREHSSRTS AKALYEQRKN
60 70 80 90 100
YARDSVSSVS DVSQYRVEHL TTFVLDRKDA MITVEDGIRK LKLLDAKGKV
110 120 130 140 150
WTQDMILQVD DRAVSLIDLE SKNELENFPL NTISHCQAVV HACSYDSILA
160 170 180 190 200
LVCKEPTQSK PDLHLFQCDE VKANLISEDI ESAISDSKGG KQKRRPEALR
210 220 230 240 250
MIAKADPGIP PPPRAPAPVP PGTVTQVDVR SRVAAWSAWA ADQGDFEKPR
260 270 280 290 300
QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR
310 320 330 340 350
KKSKKSKRKG PGEGVLTLRA KPPPPDEFVD CFQKFKHGFN LLAKLKSHIQ
360 370 380 390 400
NPSASDLVHF LFTPLNMVVQ ATGGPELASS VLSPLLTKDT VDFLNYTATA
410 420 430 440 450
EERKLWMSLG DSWVKVRAEW PKEQFIPPYV PRFRNGWEPP MLNFMGAPTE
460 470 480 490 500
QDMYQLAESV ANAEHQRKQD SKRLSTEHSN VSDYPPADGY AYSSSMYHRG
510 520 530 540 550
PHADHGEAAM PFKSTPNHQV DRNYDAVKTQ PKKYAKSKYD FVARNSSELS
560 570 580 590 600
VMKDDVLEIL DDRRQWWKVR NASGDSGFVP NNILDIMRTP ESGVGRADPP
610 620 630 640 650
YTHTIQKQRT EYGLRSADTP SAPSPPPTPA PVPVPLPPSV PAPVSVPKVP
660 670 680 690 700
ANVTRQNSSS SDSGGSIVRD SQRYKQLPVD RRKSQMEEVQ DELFQRLTIG
710 720 730 740 750
RSAAQRKFHV PRQNVPVINI TYDSSPEEVK TWLQSKGFNP VTVNSLGVLN
760 770 780 790 800
GAQLFSLNKD ELRSVCPEGA RVFNQITVQK AALEDSNGSS ELQEIMRRRQ
810 820
EKISAAASDS GVESFDEGSS H
Length:821
Mass (Da):91,737
Last modified:July 27, 2011 - v2
<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:i50F691FAC3EF1304
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z7F4D3Z7F4_MOUSE
Epidermal growth factor receptor ki...
Eps8
189Annotation 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>
D3Z5I5D3Z5I5_MOUSE
Epidermal growth factor receptor ki...
Eps8
329Annotation 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>
Q3UGL1Q3UGL1_MOUSE
Epidermal growth factor receptor ki...
Eps8
587Annotation 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>
A0A0N4SVD8A0A0N4SVD8_MOUSE
Epidermal growth factor receptor ki...
Eps8
38Annotation 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>
D3YXC3D3YXC3_MOUSE
Epidermal growth factor receptor ki...
Eps8
14Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti652N → D in AAA16358 (PubMed:8404850).Curated1
Sequence conflicti652N → D in AAH16890 (PubMed:15489334).Curated1

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
L21671 mRNA Translation: AAA16358.1
AK149683 mRNA Translation: BAE29023.1
AK166156 mRNA Translation: BAE38601.1
BC016890 mRNA Translation: AAH16890.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS20665.1

Protein sequence database of the Protein Information Resource

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PIRi
S39983

NCBI Reference Sequences

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RefSeqi
NP_001258516.1, NM_001271587.1
NP_001258517.1, NM_001271588.1
NP_001258518.1, NM_001271589.1
NP_001258524.1, NM_001271595.1
NP_031971.2, NM_007945.3
XP_011239506.1, XM_011241204.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766
ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766
ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766

Database of genes from NCBI RefSeq genomes

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GeneIDi
13860

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13860

UCSC genome browser

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UCSCi
uc009emz.2 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
L21671 mRNA Translation: AAA16358.1
AK149683 mRNA Translation: BAE29023.1
AK166156 mRNA Translation: BAE38601.1
BC016890 mRNA Translation: AAH16890.1
CCDSiCCDS20665.1
PIRiS39983
RefSeqiNP_001258516.1, NM_001271587.1
NP_001258517.1, NM_001271588.1
NP_001258518.1, NM_001271589.1
NP_001258524.1, NM_001271595.1
NP_031971.2, NM_007945.3
XP_011239506.1, XM_011241204.2

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
1AOJX-ray2.50A/B532-591[»]
1I07X-ray1.80A/B532-591[»]
1I0CX-ray2.00A/B532-591[»]
SMRiQ08509
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi199491, 8 interactors
CORUMiQ08509
DIPiDIP-32858N
IntActiQ08509, 11 interactors
MINTiQ08509
STRINGi10090.ENSMUSP00000052776

PTM databases

iPTMnetiQ08509
PhosphoSitePlusiQ08509

Proteomic databases

EPDiQ08509
jPOSTiQ08509
MaxQBiQ08509
PaxDbiQ08509
PeptideAtlasiQ08509
PRIDEiQ08509

Genome annotation databases

EnsembliENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766
ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766
ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766
GeneIDi13860
KEGGimmu:13860
UCSCiuc009emz.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2059
MGIiMGI:104684 Eps8

Phylogenomic databases

eggNOGiKOG3557 Eukaryota
ENOG410XT9R LUCA
GeneTreeiENSGT00940000156403
HOGENOMiHOG000060324
InParanoidiQ08509
KOiK17277
OMAiSETSQYH
OrthoDBi218804at2759
TreeFamiTF313069

Miscellaneous databases

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

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ChiTaRSi
Eps8 mouse
EvolutionaryTraceiQ08509

Protein Ontology

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PROi
PR:Q08509
RNActiQ08509 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000015766 Expressed in 311 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ08509 baseline and differential
GenevisibleiQ08509 MM

Family and domain databases

CDDicd01210 PTB_EPS8, 1 hit
cd11764 SH3_Eps8, 1 hit
Gene3Di1.10.150.50, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR030222 EPS8
IPR039801 EPS8-like
IPR033928 EPS8_PTB
IPR035462 Eps8_SH3
IPR011993 PH-like_dom_sf
IPR013625 PTB
IPR006020 PTB/PI_dom
IPR013761 SAM/pointed_sf
IPR041418 SAM_3
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PANTHERiPTHR12287 PTHR12287, 1 hit
PTHR12287:SF21 PTHR12287:SF21, 1 hit
PfamiView protein in Pfam
PF08416 PTB, 1 hit
PF18016 SAM_3, 1 hit
PF00018 SH3_1, 1 hit
SMARTiView protein in SMART
SM00462 PTB, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS50002 SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

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 nameiEPS8_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: Q08509
Secondary accession number(s): Q3TM41
<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: November 1, 1997
Last sequence update: July 27, 2011
Last modified: December 11, 2019
This is version 177 of the entry and version 2 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, Reference proteome

Documents

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