Reviewed, UniProtKB/Swiss-Prot P54763 (EPHB2_MOUSE)

Names and origin

Protein names

Recommended name:
    Ephrin type-B receptor 2
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor EPH-3
    Neural kinase
    Nuk receptor tyrosine kinase
    SEK-3

Gene names

Name:	Ephb2
Synonyms:	Epth3, Nuk, Sek3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	994 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Receptor for members of the ephrin-B family. Can function in aspects of retinal ganglion cell axon guidance to the optic disk even lacking its tyrosine kinase domain.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with PRKCABP. The ligand-activated form interacts with multiple proteins, including GTPase-activating protein (RASGAP) through its SH2 domain. Binds RASGAP through the juxtamembrane tyrosines residues By similarity. Interacts with PRKCABP and GRIP1.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in cells of the developing outer retina.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	axon guidance Inferred from direct assay. Source: MGI learning Inferred from mutant phenotype. Source: MGI organ morphogenesis Inferred from mutant phenotype. Source: MGI phosphorylation Ref.4 Inferred from direct assay. Source: UniProtKB positive regulation of long-term neuronal synaptic plasticity Inferred from mutant phenotype. Source: MGI regulation of axonogenesis Inferred from direct assay. Source: MGI transmembrane receptor protein tyrosine kinase signaling pathway Inferred from direct assay. Source: MGI
Cellular component	integral to plasma membrane Traceable author statement. Source: MGI synapse Ref.4 Non-traceable author statement. Source: UniProtKB
Molecular function	axon guidance receptor activity Inferred from direct assay. Source: MGI receptor binding Inferred from direct assay. Source: MGI transmembrane-ephrin receptor activity Traceable author statement. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Efna5	O08543	1	EBI-537711,EBI-1038734
Grb2	Q60631	1	EBI-537711,EBI-1688
Grip1	Q925T6	1	EBI-537711,EBI-537752
Ptk2	P34152	1	EBI-537711,EBI-77070
Src	P05480	1	EBI-537711,EBI-298680

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P54763-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P54763-2)

The sequence of this isoform differs from the canonical sequence as follows:
     576-576: R → RR

Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 994

968

Ephrin type-B receptor 2

Regions

Topological domain

27 – 551

525

Extracellular Potential

Transmembrane

552 – 572

21

Potential

Topological domain

573 – 994

422

Cytoplasmic Potential

Domain

333 – 434

102

Fibronectin type-III 1

Domain

440 – 535

96

Fibronectin type-III 2

Domain

629 – 892

264

Protein kinase

Domain

921 – 985

65

SAM

Nucleotide binding

635 – 643

9

ATP By similarity

Motif

992 – 994

3

PDZ-binding Potential

Compositional bias

192 – 329

138

Cys-rich

Sites

Active site

754

1

Proton acceptor By similarity

Binding site

661

1

ATP By similarity

Amino acid modifications

Modified residue

604

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

610

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

783

1

Phosphothreonine By similarity

Modified residue

788

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

938

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

273

1

N-linked (GlcNAc...) Potential

Glycosylation

344

1

N-linked (GlcNAc...) Potential

Glycosylation

436

1

N-linked (GlcNAc...) Potential

Glycosylation

490

1

N-linked (GlcNAc...) Potential

Disulfide bond

70 ↔ 192

Disulfide bond

105 ↔ 115

Natural variations

Alternative sequence

576

1

R → RR in isoform 2.

Secondary structure

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994

Helix Strand Turn

Details...

Beta strand

28 – 33

6

Helix

34 – 36

3

Beta strand

44 – 47

4

Beta strand

52 – 57

6

Beta strand

63 – 70

8

Beta strand

74 – 76

3

Beta strand

79 – 82

4

Beta strand

92 – 103

12

Helix

105 – 107

3

Beta strand

108 – 110

3

Beta strand

116 – 128

13

Beta strand

133 – 136

4

Turn

140 – 142

3

Beta strand

143 – 150

8

Beta strand

168 – 174

7

Beta strand

179 – 203

25

Helix

607 – 609

3

Beta strand

610 – 612

3

Helix

613 – 620

8

Helix

626 – 628

3

Beta strand

629 – 637

9

Beta strand

639 – 648

10

Beta strand

656 – 662

7

Helix

669 – 682

14

Beta strand

693 – 697

5

Beta strand

699 – 702

4

Beta strand

704 – 708

5

Helix

715 – 720

6

Turn

721 – 724

4

Helix

728 – 747

20

Helix

757 – 759

3

Beta strand

760 – 762

3

Beta strand

768 – 770

3

Helix

798 – 800

3

Helix

803 – 807

5

Helix

813 – 828

16

Turn

834 – 837

4

Helix

840 – 848

9

Helix

861 – 870

10

Turn

875 – 877

3

Helix

881 – 893

13

Helix

895 – 898

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2003. Version 2. Checksum: BC6B9B12A070394C	FASTA	994	110,760
	10 20 30 40 50 60 MGARVPVLPG LDGSFCWLLL LPLLAAVEET LMDSTTATAE LGWMVHPPSG WEEVSGYDEN 70 80 90 100 110 120 MNTIRTYQVC NVFESSQNNW LRTKFIRRRG AHRIHVEMKF SVRDCSSIPS VPGSCKETFN 130 140 150 160 170 180 LYYYEADFDL ATKTFPNWME NPWVKVDTIA ADESFSQVDL GGRVMKINTE VRSFGPVSRN 190 200 210 220 230 240 GFYLAFQDYG GCMSLIAVRV FYRKCPRIIQ NGAIFQETLS GAESTSLVAA RGSCIANAEE 250 260 270 280 290 300 VDVPIKLYCN GDGEWLVPIG RCMCKAGFEA VENGTVCRGC PSGTFKANQG DEACTHCPIN 310 320 330 340 350 360 SRTTSEGATN CVCRNGYYRA DLDPLDMPCT TIPSAPQAVI SSVNETSLML EWTPPRDSGG 370 380 390 400 410 420 REDLVYNIIC KSCGSGRGAC TRCGDNVQYA PRQLGLTEPR IYISDLLAHT QYTFEIQAVN 430 440 450 460 470 480 GVTDQSPFSP QFASVNITTN QAAPSAVSIM HQVSRTVDSI TLSWSQPDQP NGVILDYELQ 490 500 510 520 530 540 YYEKELSEYN ATAIKSPTNT VTVQGLKAGA IYVFQVRART VAGYGRYSGK MYFQTMTEAE 550 560 570 580 590 600 YQTSIKEKLP LIVGSSAAGL VFLIAVVVIA IVCNRRGFER ADSEYTDKLQ HYTSGHMTPG 610 620 630 640 650 660 MKIYIDPFTY EDPNEAVREF AKEIDISCVK IEQVIGAGEF GEVCSGHLKL PGKREIFVAI 670 680 690 700 710 720 KTLKSGYTEK QRRDFLSEAS IMGQFDHPNV IHLEGVVTKS TPVMIITEFM ENGSLDSFLR 730 740 750 760 770 780 QNDGQFTVIQ LVGMLRGIAA GMKYLADMNY VHRDLAARNI LVNSNLVCKV SDFGLSRFLE 790 800 810 820 830 840 DDTSDPTYTS ALGGKIPIRW TAPEAIQYRK FTSASDVWSY GIVMWEVMSY GERPYWDMTN 850 860 870 880 890 900 QDVINAIEQD YRLPPPMDCP SALHQLMLDC WQKDRNHRPK FGQIVNTLDK MIRNPNSLKA 910 920 930 940 950 960 MAPLSSGINL PLLDRTIPDY TSFNTVDEWL EAIKMGQYKE SFANAGFTSF DVVSQMMMED 970 980 990 ILRVGVTLAG HQKKILNSIQ VMRAQMNQIQ SVEV
	Isoform 2 [UniParc]. Checksum: 637A576E0561892A		995	110,916
	10 20 30 40 50 60 MGARVPVLPG LDGSFCWLLL LPLLAAVEET LMDSTTATAE LGWMVHPPSG WEEVSGYDEN 70 80 90 100 110 120 MNTIRTYQVC NVFESSQNNW LRTKFIRRRG AHRIHVEMKF SVRDCSSIPS VPGSCKETFN 130 140 150 160 170 180 LYYYEADFDL ATKTFPNWME NPWVKVDTIA ADESFSQVDL GGRVMKINTE VRSFGPVSRN 190 200 210 220 230 240 GFYLAFQDYG GCMSLIAVRV FYRKCPRIIQ NGAIFQETLS GAESTSLVAA RGSCIANAEE 250 260 270 280 290 300 VDVPIKLYCN GDGEWLVPIG RCMCKAGFEA VENGTVCRGC PSGTFKANQG DEACTHCPIN 310 320 330 340 350 360 SRTTSEGATN CVCRNGYYRA DLDPLDMPCT TIPSAPQAVI SSVNETSLML EWTPPRDSGG 370 380 390 400 410 420 REDLVYNIIC KSCGSGRGAC TRCGDNVQYA PRQLGLTEPR IYISDLLAHT QYTFEIQAVN 430 440 450 460 470 480 GVTDQSPFSP QFASVNITTN QAAPSAVSIM HQVSRTVDSI TLSWSQPDQP NGVILDYELQ 490 500 510 520 530 540 YYEKELSEYN ATAIKSPTNT VTVQGLKAGA IYVFQVRART VAGYGRYSGK MYFQTMTEAE 550 560 570 580 590 600 YQTSIKEKLP LIVGSSAAGL VFLIAVVVIA IVCNRRRGFE RADSEYTDKL QHYTSGHMTP 610 620 630 640 650 660 GMKIYIDPFT YEDPNEAVRE FAKEIDISCV KIEQVIGAGE FGEVCSGHLK LPGKREIFVA 670 680 690 700 710 720 IKTLKSGYTE KQRRDFLSEA SIMGQFDHPN VIHLEGVVTK STPVMIITEF MENGSLDSFL 730 740 750 760 770 780 RQNDGQFTVI QLVGMLRGIA AGMKYLADMN YVHRDLAARN ILVNSNLVCK VSDFGLSRFL 790 800 810 820 830 840 EDDTSDPTYT SALGGKIPIR WTAPEAIQYR KFTSASDVWS YGIVMWEVMS YGERPYWDMT 850 860 870 880 890 900 NQDVINAIEQ DYRLPPPMDC PSALHQLMLD CWQKDRNHRP KFGQIVNTLD KMIRNPNSLK 910 920 930 940 950 960 AMAPLSSGIN LPLLDRTIPD YTSFNTVDEW LEAIKMGQYK ESFANAGFTS FDVVSQMMME 970 980 990 DILRVGVTLA GHQKKILNSI QVMRAQMNQI QSVEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Immunolocalization of the Nuk receptor tyrosine kinase suggests roles in segmental patterning of the brain and axonogenesis." Henkemeyer M., Marengere L.E., McGlade J., Olivier J.P., Conlon R.A., Holmyard D.P., Letwin K., Pawson T. Oncogene 9:1001-1014(1994) [PubMed: 8134103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Several receptor tyrosine kinase genes of the Eph family are segmentally expressed in the developing hindbrain." Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., Wilkinson D.G., Charnay P., Gilardi P. Mech. Dev. 47:3-17(1994) [PubMed: 7947319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 516-994 (ISOFORM 2). Strain: