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UniProtKB - P09759 (EPHB1_RAT)

Entry version 209 (29 Sep 2021)
Sequence version 2 (01 Dec 1992)
Previous versions | rss
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Protein

Ephrin type-B receptor 1

Gene

Ephb1

Organism
Rattus norvegicus (Rat)
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

Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively (By similarity).

Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei651ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei744Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi625 – 633ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processCell adhesion, Neurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.1, 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-2682334, EPH-Ephrin signaling
R-RNO-3928662, EPHB-mediated forward signaling
R-RNO-3928664, Ephrin signaling
R-RNO-3928665, EPH-ephrin mediated repulsion of cells

<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:
Ephrin type-B receptor 1 (EC:2.7.10.1)
Alternative name(s):
ELK
Tyrosine-protein kinase receptor EPH-2
<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:Ephb1
Synonyms:Elk, Epth2
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 8

Organism-specific databases

Rat genome database

More...RGDi		2556, Ephb1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 540ExtracellularSequence analysisAdd BLAST523
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei541 – 563HelicalSequence analysisAdd BLAST23
Topological domaini564 – 984CytoplasmicSequence analysisAdd BLAST421

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

<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

Chemistry databases

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1830

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001682518 – 984Ephrin type-B receptor 1Add BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi334N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi426N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi480N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei600PhosphotyrosineBy similarity1
Modified residuei928Phosphotyrosine; by autocatalysisBy 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

Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL (By similarity).By similarity
Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P09759

PRoteomics IDEntifications database

More...PRIDEi		P09759

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P09759, 3 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P09759

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

More...PhosphoSitePlusi		P09759

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P09759

<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

Restricted to brain and testes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000007865, Expressed in brain and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P09759, RN

<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

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses.

Interacts with EPHB6; transphosphorylates EPHB6 to form an active signaling complex.

Interacts with PICK1.

Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion. The ligand-activated form interacts (through Tyr-928) with GRB7 and GRB10 (via SH2 domains). The ligand-activated form interacts (residues within the catalytic domain) with GRB2 (via SH2 domain).

Interacts with GRB2, SHC1 and SRC; activates the MAPK/ERK cascade to regulate cell migration.

Interacts with CBL; regulates receptor degradation through ubiquitination.

Interacts with ACP1 (By similarity).

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		246515, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P09759

Database of interacting proteins

More...DIPi		DIP-138N

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000010634

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

3D structure databases

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

More...SMRi		P09759

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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>Domaini19 – 201Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini322 – 432Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini433 – 528Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini619 – 882Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini911 – 975SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi982 – 984PDZ-bindingSequence analysis3

<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 protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0196, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155297

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_141_4_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09759

Identification of Orthologs from Complete Genome Data

More...OMAi		MACKACP

Database of Orthologous Groups

More...OrthoDBi		933071at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09759

TreeFam database of animal gene trees

More...TreeFami		TF315608

Family and domain databases

Conserved Domains Database

More...CDDi		cd10476, EphR_LBD_B1, 1 hit
cd00063, FN3, 2 hits
cd09551, SAM_EPH-B1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.150.50, 1 hit
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027936, Eph_TM
IPR034231, EphB1_rcpt_lig-bd
IPR042819, EphB1_SAM
IPR001090, Ephrin_rcpt_lig-bd_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001660, SAM
IPR013761, SAM/pointed_sf
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
IPR016257, Tyr_kinase_ephrin_rcpt
IPR001426, Tyr_kinase_rcpt_V_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14575, EphA2_TM, 1 hit
PF01404, Ephrin_lbd, 1 hit
PF00041, fn3, 2 hits
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF00536, SAM_1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000666, TyrPK_ephrin_receptor, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00109, TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00615, EPH_lbd, 1 hit
SM00060, FN3, 2 hits
SM00454, SAM, 1 hit
SM00219, TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47769, SSF47769, 1 hit
SSF49265, SSF49265, 1 hit
SSF49785, SSF49785, 1 hit
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01186, EGF_2, 1 hit
PS51550, EPH_LBD, 1 hit
PS50853, FN3, 2 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit
PS00790, RECEPTOR_TYR_KIN_V_1, 1 hit
PS00791, RECEPTOR_TYR_KIN_V_2, 1 hit
PS50105, SAM_DOMAIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P09759-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE 
        60         70         80         90        100
NLNTIRTYQV CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP 
       110        120        130        140        150
NVPGSCKETF NLYYYETDSV IATKKSAFWS EAPYLKVDTI AADESFSQVD 
       160        170        180        190        200
FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY GACMSLLSVR VFFKKCPSIV 
       210        220        230        240        250
QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC NGDGEWMVPI 
       260        270        280        290        300
GRCTCKAGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI 
       310        320        330        340        350
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG 
       360        370        380        390        400
RDDVTYNIIC KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT 
       410        420        430        440        450
PYTFDIQAIN GVSSKSPFPP QHVSVNITTN QAAPSTVPIM HQVSATMRSI 
       460        470        480        490        500
TLSWPQPEQP NGIILDYEIR YYEKEHNEFN SSMARSQTNT ARIDGLRPGM 
       510        520        530        540        550
VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP LIAGSAAAGV 
       560        570        580        590        600
VFVVSLVAIS IVCSRKRAYS KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 
       610        620        630        640        650
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI 
       660        670        680        690        700
KTLKAGYSEK QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM 
       710        720        730        740        750
ENGALDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLSEMNY VHRDLAARNI 
       760        770        780        790        800
LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS SLGGKIPVRW TAPEAIAYRK 
       810        820        830        840        850
FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD YRLPPPMDCP 
       860        870        880        890        900
AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 
       910        920        930        940        950
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED 
       960        970        980 
LLRIGVTLAG HQKKILSSIH SMRVQMNQSP SVMA
Length:984
Mass (Da):109,883
Last modified:December 1, 1992 - 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:i521EAC240D8FB91A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M59814 mRNA No translation available.
X13411 mRNA Translation: CAA31777.1

Protein sequence database of the Protein Information Resource

More...PIRi		A39753

NCBI Reference Sequences

More...RefSeqi		NP_001097998.1, NM_001104528.1
XP_017450939.1, XM_017595450.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000010634; ENSRNOP00000010634; ENSRNOG00000007865

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24338

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24338

UCSC genome browser

More...UCSCi		RGD:2556, rat

<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
M59814 mRNA No translation available.
X13411 mRNA Translation: CAA31777.1
PIRiA39753
RefSeqiNP_001097998.1, NM_001104528.1
XP_017450939.1, XM_017595450.1

3D structure databases

SMRiP09759
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi246515, 2 interactors
CORUMiP09759
DIPiDIP-138N
STRINGi10116.ENSRNOP00000010634

Chemistry databases

GuidetoPHARMACOLOGYi1830

PTM databases

GlyGeniP09759, 3 sites
iPTMnetiP09759
PhosphoSitePlusiP09759
SwissPalmiP09759

Proteomic databases

PaxDbiP09759
PRIDEiP09759

Genome annotation databases

EnsembliENSRNOT00000010634; ENSRNOP00000010634; ENSRNOG00000007865
GeneIDi24338
KEGGirno:24338
UCSCiRGD:2556, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2047
RGDi2556, Ephb1

Phylogenomic databases

eggNOGiKOG0196, Eukaryota
GeneTreeiENSGT00940000155297
HOGENOMiCLU_000288_141_4_1
InParanoidiP09759
OMAiMACKACP
OrthoDBi933071at2759
PhylomeDBiP09759
TreeFamiTF315608

Enzyme and pathway databases

BRENDAi2.7.10.1, 5301
ReactomeiR-RNO-2682334, EPH-Ephrin signaling
R-RNO-3928662, EPHB-mediated forward signaling
R-RNO-3928664, Ephrin signaling
R-RNO-3928665, EPH-ephrin mediated repulsion of cells

Miscellaneous databases

Protein Ontology

More...PROi		PR:P09759

Gene expression databases

BgeeiENSRNOG00000007865, Expressed in brain and 21 other tissues
GenevisibleiP09759, RN

Family and domain databases

CDDicd10476, EphR_LBD_B1, 1 hit
cd00063, FN3, 2 hits
cd09551, SAM_EPH-B1, 1 hit
Gene3Di1.10.150.50, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR027936, Eph_TM
IPR034231, EphB1_rcpt_lig-bd
IPR042819, EphB1_SAM
IPR001090, Ephrin_rcpt_lig-bd_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001660, SAM
IPR013761, SAM/pointed_sf
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
IPR016257, Tyr_kinase_ephrin_rcpt
IPR001426, Tyr_kinase_rcpt_V_CS
PfamiView protein in Pfam
PF14575, EphA2_TM, 1 hit
PF01404, Ephrin_lbd, 1 hit
PF00041, fn3, 2 hits
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF00536, SAM_1, 1 hit
PIRSFiPIRSF000666, TyrPK_ephrin_receptor, 1 hit
PRINTSiPR00109, TYRKINASE
SMARTiView protein in SMART
SM00615, EPH_lbd, 1 hit
SM00060, FN3, 2 hits
SM00454, SAM, 1 hit
SM00219, TyrKc, 1 hit
SUPFAMiSSF47769, SSF47769, 1 hit
SSF49265, SSF49265, 1 hit
SSF49785, SSF49785, 1 hit
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS01186, EGF_2, 1 hit
PS51550, EPH_LBD, 1 hit
PS50853, FN3, 2 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit
PS00790, RECEPTOR_TYR_KIN_V_1, 1 hit
PS00791, RECEPTOR_TYR_KIN_V_2, 1 hit
PS50105, SAM_DOMAIN, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPHB1_RAT
<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: P09759
<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 1, 1989
Last sequence update: December 1, 1992
Last modified: September 29, 2021
This is version 209 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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