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Entry version 137 (07 Apr 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Ephrin type-B receptor 2

Gene

EPHB2

Organism
Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
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 transcript 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. Functions in axon guidance during development. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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 sitei654ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei747Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi628 – 636ATPPROSITE-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

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 functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processNeurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1, 1673

<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%5Fand%5Ftaxonomy%5Fsection">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 2 (EC:2.7.10.1)
Alternative name(s):
EPH-like kinase 5
Short name:
EK5
Short name:
qEK5
Cleaved into the following 2 chains:
EphB2/CTF1By similarity
EphB2/CTF2By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:EPHB2
Synonyms:QEK5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiCoturnix japonica (Japanese quail) (Coturnix coturnix japonica)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri93934 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePerdicinaeCoturnix

<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%5Flocation%5Fsection">'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 domaini20 – 544ExtracellularSequence analysisAdd BLAST525
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei545 – 565HelicalSequence analysisAdd BLAST21
Topological domaini566 – 987CytoplasmicSequence analysisAdd BLAST422

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

<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 – 19Sequence analysisAdd BLAST19
<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_000001683020 – 987Ephrin type-B receptor 2Add BLAST968
ChainiPRO_0000445967537 – 987EphB2/CTF1By similarityAdd BLAST451
ChainiPRO_0000445968563 – 987EphB2/CTF2By similarityAdd BLAST425

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi63 ↔ 185By similarity
Disulfide bondi98 ↔ 108By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi266N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi429N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi478N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi483N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ligand binding induces cleavage by matrix metalloproteinases (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF) and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved by MMPs, producing EphB2/CTF1 which is further cleaved by the PS1/gamma-secretase producing EphB2/CTF2.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei536 – 537Cleavage; by a metalloproteinaseBy similarity2
Sitei562 – 563Cleavage; by gamma-secretase/PS1By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

<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%5Fsection">'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%5Fsection">'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 (By similarity).

By similarity

<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

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q90344

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

More...
SMRi
Q90344

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%5Fand%5Fdomains%5Fsection">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>Domaini21 – 203Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini325 – 435Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini436 – 531Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini622 – 885Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini914 – 978SAMPROSITE-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>Motifi985 – 987PDZ-bindingSequence analysis3

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 biasi185 – 322Cys-richAdd BLAST138

<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

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10477, EphR_LBD_B2, 1 hit
cd00063, FN3, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.50, 1 hit
2.60.120.260, 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
IPR034238, EphB2_rcpt_lig-bd
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
IPR011641, Tyr-kin_ephrin_A/B_rcpt-like
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
PF07699, Ephrin_rec_like, 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
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q90344-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGPLWFCCLP LALLPLLAAV EETLMDSTTA TAELGWMVHP PSGWEEVSGY
60 70 80 90 100
DENMNTIRTY QVCNVFESSQ NNWLRTKYIR RRGAHRIHVE MKFSVRDCSS
110 120 130 140 150
IPNVPGSCKE TFNLYYYESD FDSATKTFPN WMENPWMKVD TIAADERFSQ
160 170 180 190 200
VDLGGRVMKI NTEVRSFGPV SKNGFYLAFQ DYWGCMSLIA VRVFYRKCPR
210 220 230 240 250
VIQNGADFQE TLSGAESTSL VASRGTCINK AEEVDVPIKQ HCNGDGEWLV
260 270 280 290 300
PIGRCMCRPG YESVANGTVC RGCPSGTFKA SQGDEGCVHC PINSRTTSEG
310 320 330 340 350
ATNCVCRNGY YRADADPVDM PCTTIPSAPQ SVISSVNETS LMLEWTPPRD
360 370 380 390 400
SGGREDLVYN IICKSCGSGR GACTRCGDNV QFAPRQLGLT EPRIYISDLL
410 420 430 440 450
AHTQYTFEIQ AVNGVTDQSP FSPQFASVNI TTNQAAPSAV SIMHQVSRTV
460 470 480 490 500
DSITLSWSQP DQPNGVILDY ELQYYEKNLS ELNSTAVKSP TNTVTVQNLK
510 520 530 540 550
AGTIYVFQVR ARTVAGYGRY SGKMYFQTMT EAEYQTSVQE KLPLIIGSSA
560 570 580 590 600
AGLVFLIAVV VIIIVCNRRG FERADSEYTD KLQHYTSGHM TPGMKIYIDP
610 620 630 640 650
FTYEDPNEAV REFAKEIDIS CVKIEQVIGA GEFGEVCSGH LKLPGKREIF
660 670 680 690 700
VAIKTLKSGY TEKQRRDFLS EASIMGQFDH PNVIHLEGVV TKSSPVMIIT
710 720 730 740 750
EFMENGSLDS FLRQNDGQFT VIQLVGMLRG IAAGMKYLAD MNYVHRDLAA
760 770 780 790 800
RNTLVNSNLV CKVSDFGLSR FLEDDTSDPT YTSALGGKIP IRWTAPEAIQ
810 820 830 840 850
YRKFTSASDV WSYGIVMWEV MSYGERPYWD MTNQDVINAI EQDYRLPPPM
860 870 880 890 900
DCPNALHQLM LDCWQKDRNH RPKFGQIVNT LDKMIRNPNS LKAMAPLSSG
910 920 930 940 950
VNLPLLDRTI PDYTSFNTVD EWLDAIKMSQ YKESYASAGF TTFDIVSQMT
960 970 980
VEDILRVGVT LAGHQKKILN SIQVMRAQMN QIQSVEV
Length:987
Mass (Da):110,331
Last modified:November 1, 1996 - 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:i05D6ECC68B718DD7
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
X91737 mRNA Translation: CAA62862.1

<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
X91737 mRNA Translation: CAA62862.1

3D structure databases

BMRBiQ90344
SMRiQ90344
ModBaseiSearch...

Enzyme and pathway databases

BRENDAi2.7.10.1, 1673

Family and domain databases

CDDicd10477, EphR_LBD_B2, 1 hit
cd00063, FN3, 2 hits
Gene3Di1.10.150.50, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR027936, Eph_TM
IPR034238, EphB2_rcpt_lig-bd
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
IPR011641, Tyr-kin_ephrin_A/B_rcpt-like
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
PF07699, Ephrin_rec_like, 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
PS00790, RECEPTOR_TYR_KIN_V_1, 1 hit
PS00791, RECEPTOR_TYR_KIN_V_2, 1 hit
PS50105, SAM_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPHB2_COTJA
<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: Q90344
<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%5Fand%5Fisoforms">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: November 1, 1996
Last modified: April 7, 2021
This is version 137 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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