Q8CBF3 (EPHB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ephrin type-B receptor 1
EC=2.7.10.1

Gene names

Name:

Ephb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	984 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 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. Beside 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. Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	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. Interacts with EPHB6; transphosphorylates EPHB6 to form an active signaling complex By similarity. 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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.13
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Early endosome membrane By similarity. Cell projection › dendrite Ref.8.
Tissue specificity	Expressed in neural stem and progenitor cells in the dentate gyrus. Ref.10
Developmental stage	Expressed in growth cones of ventrotemporal (uncrossed) retinal ganglion cells that give rise to ipsilateral projections (at protein level). Ref.9 Ref.11
Post-translational modification	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. Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation. Ref.13
Disruption phenotype	Mice development is apparently normal. However, they display a dramatic reduction of ipsilateral retinal projection. Mice do not develop neuropathic algesia and physical dependence to morphine. Ref.9 Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 1 Eph LBD (Eph ligand-binding) domain. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Cell adhesion Neurogenesis
Cellular component	Cell membrane Cell projection Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB camera-type eye morphogenesis Inferred from mutant phenotype Ref.9. Source: MGI cell chemotaxis Inferred from mutant phenotype Ref.10. Source: UniProtKB cell-substrate adhesion Inferred from sequence or structural similarity. Source: UniProtKB central nervous system projection neuron axonogenesis Inferred from direct assay Ref.9. Source: MGI dendritic spine morphogenesis Inferred from mutant phenotype Ref.8. Source: UniProtKB detection of temperature stimulus involved in sensory perception of pain Inferred from mutant phenotype Ref.12. Source: UniProtKB establishment of cell polarity Inferred from mutant phenotype Ref.10. Source: UniProtKB neural precursor cell proliferation Inferred from mutant phenotype Ref.10. Source: UniProtKB optic nerve morphogenesis Inferred from mutant phenotype Ref.9. Source: MGI positive regulation of synapse assembly Inferred from mutant phenotype Ref.8. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB regulation of JNK cascade Inferred from sequence or structural similarity. Source: UniProtKB retinal ganglion cell axon guidance Inferred from direct assay Ref.9. Source: MGI
Cellular_component	axon Inferred from direct assay PubMed 16701205. Source: MGI dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB membrane raft Inferred from direct assay PubMed 15502157. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW axon guidance receptor activity Inferred from direct assay PubMed 11532925. Source: MGI transmembrane-ephrin receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8CBF3-1)

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: Q8CBF3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     588-628: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 984	967	Ephrin type-B receptor 1		PRO_0000260317
Regions
	Topological domain	18 – 540	523	Extracellular Potential
	Transmembrane	541 – 563	23	Helical; Potential
	Topological domain	564 – 984	421	Cytoplasmic Potential
	Domain	19 – 201	183	Eph LBD
	Domain	323 – 424	102	Fibronectin type-III 1
	Domain	430 – 525	96	Fibronectin type-III 2
	Domain	619 – 882	264	Protein kinase
	Domain	911 – 975	65	SAM
	Nucleotide binding	625 – 633	9	ATP By similarity
	Motif	982 – 984	3	PDZ-binding Potential
	Compositional bias	183 – 319	137	Cys-rich
Sites
	Active site	744	1	Proton acceptor By similarity
	Binding site	651	1	ATP By similarity
Amino acid modifications
	Modified residue	928	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	334	1	N-linked (GlcNAc...) Potential
	Glycosylation	426	1	N-linked (GlcNAc...) Potential
	Glycosylation	480	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	588 – 628	41	Missing in isoform 2.		VSP_021595
Experimental info
	Sequence conflict	72	1	L → Q in BAE22386. Ref.1
	Sequence conflict	187	1	L → P in BAE22386. Ref.1
	Sequence conflict	194	1	K → I in AAH57301. Ref.3
	Sequence conflict	641	1	P → Q in BAC29348. Ref.1
	Sequence conflict	678	1	P → R in AAH57301. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: E967019C82AA400A	FASTA	984	109,881
	10 20 30 40 50 60 MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV 70 80 90 100 110 120 CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV 130 140 150 160 170 180 IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY 190 200 210 220 230 240 GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC 250 260 270 280 290 300 NGDGEWMVPI GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI 310 320 330 340 350 360 CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC 370 380 390 400 410 420 KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP 430 440 450 460 470 480 QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN 490 500 510 520 530 540 SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP 550 560 570 580 590 600 LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAAYSDKLQ HYSTGRGSPG MKIYIDPFTY 610 620 630 640 650 660 EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK 670 680 690 700 710 720 QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ 730 740 750 760 770 780 LVGMLRGIAA GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS 790 800 810 820 830 840 SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD 850 860 870 880 890 900 YRLPPPMDCP AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 910 920 930 940 950 960 PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED LLRIGVTLAG 970 980 HQKKILSSIH SMRVQMNQSP SVMA
	Isoform 2 [UniParc]. Checksum: EF28BF1D7FE097C9	FASTA	943	105,294
	10 20 30 40 50 60 MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV 70 80 90 100 110 120 CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV 130 140 150 160 170 180 IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY 190 200 210 220 230 240 GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC 250 260 270 280 290 300 NGDGEWMVPI GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI 310 320 330 340 350 360 CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC 370 380 390 400 410 420 KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP 430 440 450 460 470 480 QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN 490 500 510 520 530 540 SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP 550 560 570 580 590 600 LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAAYSDKLQ HYSTGRGEFG EVYKGRLKLP 610 620 630 640 650 660 GKREIYVAIK TLKAGYSEKQ RRDFLSEASI MGQFDHPNII RLEGVVTKSR PVMIITEFME 670 680 690 700 710 720 NGALDSFLRQ NDGQFTVIQL VGMLRGIAAG MKYLSEMNYV HRDLAARNIL VNSNLVCKVS 730 740 750 760 770 780 DFGLSRYLQD DTSDPTYTSS LGGKIPVRWT APEAIAYRKF TSASDVWSYG IVMWEVMSFG 790 800 810 820 830 840 ERPYWDMSNQ DVINAIEQDY RLPPPMDCPA ALHQLMLDCW QKDRNSRPRF AEIVNTLDKM 850 860 870 880 890 900 IRNPASLKTV ATITAVPSQP LLDRSIPDFT AFTTVDDWLS AIKMVQYRDS FLTAGFTSLQ 910 920 930 940 LVTQMTSEDL LRIGVTLAGH QKKILSSIHS MRVQMNQSPS VMA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Cerebellum and Olfactory bulb.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[4]	"Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase." Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O. J. Biol. Chem. 273:1303-1308(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCK1. Tissue: Kidney.
[5]	"PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands." Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D. Neuron 21:1453-1463(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PICK1.
[6]	"EphB1 associates with Grb7 and regulates cell migration." Han D.C., Shen T.L., Miao H., Wang B., Guan J.L. J. Biol. Chem. 277:45655-45661(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB7.
[7]	"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis." Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U. J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB2; SHC1 AND SRC.
[8]	"Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus." Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M. J. Cell Biol. 163:1313-1326(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY SYNAPSE FORMATION, SUBCELLULAR LOCATION.
[9]	"Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm." Williams S.E., Mann F., Erskine L., Sakurai T., Wei S., Rossi D.J., Gale N.W., Holt C.E., Mason C.A., Henkemeyer M. Neuron 39:919-935(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN RETINAL GLANGLION CELL AXON GUIDANCE, DEVELOPMENTAL STAGE.
[10]	"EphB receptors regulate stem/progenitor cell proliferation, migration, and polarity during hippocampal neurogenesis." Chumley M.J., Catchpole T., Silvany R.E., Kernie S.G., Henkemeyer M. J. Neurosci. 27:13481-13490(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEUROGENESIS, IDENTIFICATION OF EFNB3 AS LIGAND, TISSUE SPECIFICITY.
[11]	"Zic2 regulates retinal ganglion cell axon avoidance of ephrinB2 through inducing expression of the guidance receptor EphB1." Lee R., Petros T.J., Mason C.A. J. Neurosci. 28:5910-5919(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[12]	"Targeted mutation of EphB1 receptor prevents development of neuropathic hyperalgesia and physical dependence on morphine in mice." Han Y., Song X.S., Liu W.T., Henkemeyer M., Song X.J. Mol. Pain 4:60-60(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[13]	"Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway." Fasen K., Cerretti D.P., Huynh-Do U. Traffic 9:251-266(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY CBL, INTERACTION WITH CBL.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK036148 mRNA. Translation: BAC29320.1. AK036211 mRNA. Translation: BAC29348.1. AK135018 mRNA. Translation: BAE22386.1. CT025594 , AC109247, AC132684, AC156635 Genomic DNA. Translation: CAM23741.1. BC057301 mRNA. Translation: AAH57301.1.
IPI	IPI00228309. IPI00808241.
RefSeq	NP_001161768.1. NM_001168296.1. NP_775623.3. NM_173447.3.
UniGene	Mm.22897.
3D structure databases
HSSP	HSSP built from PDB template 1JPA based on UniProtKB P54763.
ProteinModelPortal	Q8CBF3.
SMR	Q8CBF3. Positions 18-528, 595-984.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CBF3. 1 interaction.
STRING	10090.ENSMUSP00000035129.
PTM databases
PhosphoSite	Q8CBF3.
Proteomic databases
PaxDb	Q8CBF3.
PRIDE	Q8CBF3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537. ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537.
GeneID	270190.
KEGG	mmu:270190.
UCSC	uc012gzg.1. mouse.
Organism-specific databases
CTD	2047.
MGI	MGI:1096337. Ephb1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104274.
HOGENOM	HOG000233856.
HOVERGEN	HBG062180.
InParanoid	Q8CBF3.
KO	K05110.
OMA	ELGWTAN.
OrthoDB	EOG4W9J35.
Gene expression databases
ArrayExpress	Q8CBF3.
Bgee	Q8CBF3.
CleanEx	MM_EPHB1.
Genevestigator	Q8CBF3.
GermOnline	ENSMUSG00000032537. Mus musculus.
Family and domain databases
Gene3D	1.10.150.50. 1 hit. 2.60.40.10. 2 hits.
InterPro	IPR001090. Ephrin_rcpt_lig-bd_dom. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR009030. Growth_fac_rcpt. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM/pointed. IPR021129. SAM_type1. 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. [Graphical view]
Pfam	PF01404. Ephrin_lbd. 1 hit. PF00041. fn3. 2 hits. PF07714. Pkinase_Tyr. 1 hit. PF00536. SAM_1. 1 hit. [Graphical view]
PIRSF	PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF57184. Grow_fac_recept. 1 hit. SSF56112. Kinase_like. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS01186. EGF_2. 1 hit. Uncertain. 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. [Graphical view]
ProtoNet	Search...
Other
NextBio	393293.
SOURCE	Search...

Entry information

Entry name

EPHB1_MOUSE

Accession

Primary (citable) accession number: Q8CBF3
Secondary accession number(s): B1B1C2 , Q3UY27, Q6PG23, Q8CBE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program