Reviewed, UniProtKB/Swiss-Prot P54762 (EPHB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ephrin type-B receptor 1
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor EPH-2
      Short name=NET
    HEK6
    ELK

Gene names

Name:	EPHB1
Synonyms:	EPHT2, NET

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 for members of the ephrin-B family. Binds to ephrin-B1, -B2 and -B3. May be involved in cell-cell interactions in the nervous system.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	The ligand-activated form interacts with GRB2, GRB10 and NCK through their respective SH2 domains. The GRB10 SH2 domain binds EPHB1 through Tyr-928, while GRB2 binds residues within the catalytic domain. Interacts with EPHB6. The NCK SH2 domain binds EPHB1 through Tyr-594. Interacts with PRKCABP By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Preferentially expressed in brain.
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 Polymorphism
Domain	Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nervous system development Ref.1 Traceable author statement. Source: ProtInc protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor activity Inferred from electronic annotation. Source: InterPro protein binding Ref.4 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB10	Q13322	1	EBI-80252,EBI-80275
GRB2	P62993	1	EBI-80252,EBI-401755

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P54762-1)

Also known as: EPHB1A;

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: P54762-2)

Also known as: EPH1B1B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MALDYLLLLLLASAVAAMEETLMDTRT → METRERKKSRAEFGTR

Isoform 3 (identifier: P54762-3)

Also known as: EPHB1C;

The sequence of this isoform differs from the canonical sequence as follows:
     642-682: Missing.

Isoform 4 (identifier: P54762-4)

Also known as: EPHB1D;

The sequence of this isoform differs from the canonical sequence as follows:
     617-984: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.3

Chain

18 – 984

967

Ephrin type-B receptor 1

PRO_0000016824

Regions

Topological domain

18 – 540

523

Extracellular Potential

Transmembrane

541 – 563

23

Potential

Topological domain

564 – 984

421

Cytoplasmic Potential

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 Ref.4

Modified residue

968

1

Phosphoserine Ref.6

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

1 – 27

27

MALDY…MDTRT → METRERKKSRAEFGTR in isoform 2.

VSP_003013

Alternative sequence

617 – 984

368

Missing in isoform 4.

VSP_003014

Alternative sequence

642 – 682

41

Missing in isoform 3.

VSP_003015

Natural variant

18

1

M → V Ref.8

VAR_042165

Natural variant

87

1

T → S: dbSNP rs1042794.

VAR_011801

Natural variant

152

1

G → R: dbSNP rs1042793.

VAR_011802

Natural variant

367

1

R → G: dbSNP rs1042789.

VAR_011803

Natural variant

387

1

T → M Ref.8

VAR_042166

Natural variant

485

1

R → S: dbSNP rs1042788.

VAR_011804

Natural variant

707

1

S → T in an ovarian undifferentiated carcinoma sample; somatic mutation. Ref.8

VAR_042167

Natural variant

719

1

I → V in a gastric adenocarcinoma sample; somatic mutation. Ref.8

VAR_042168

Natural variant

743

1

R → Q in a gastric adenocarcinoma sample; somatic mutation. Ref.8

VAR_042169

Natural variant

847

1

M → T: dbSNP rs1042785.

VAR_011805

Natural variant

912

1

A → T Ref.8

VAR_042170

Natural variant

981

1

T → M Ref.8

VAR_042171

Experimental info

Mutagenesis

928

1

Y → F: Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation. Ref.4

Sequence conflict

12

1

A → E in AAD02030. Ref.2

Sequence conflict

12

1

A → E in AAB94627. Ref.2

Sequence conflict

12

1

A → E in AAB94628. Ref.2

Sequence conflict

185

1

S → I in AAD02030. Ref.2

Sequence conflict

185

1

S → I in AAD02031. Ref.2

Sequence conflict

185

1

S → I in AAB94627. Ref.2

Sequence conflict

185

1

S → I in AAB94628. Ref.2

Sequence conflict

274

1

T → R in AAD02030. Ref.2

Sequence conflict

274

1

T → R in AAD02031. Ref.2

Sequence conflict

274

1

T → R in AAB94627. Ref.2

Sequence conflict

274

1

T → R in AAB94628. Ref.2

Sequence conflict

336

1

T → S in AAD02030. Ref.2

Sequence conflict

336

1

T → S in AAD02031. Ref.2

Sequence conflict

336

1

T → S in AAB94627. Ref.2

Sequence conflict

336

1

T → S in AAB94628. Ref.2

Sequence conflict

813

1

V → H in AAD02030. Ref.2

Sequence conflict

813

1

V → H in AAB94627. Ref.2

Sequence conflict

819

1

S → Y in AAD02030. Ref.2

Sequence conflict

819

1

S → Y in AAB94627. Ref.2

Sequence conflict

973

1

R → W in AAD02030. Ref.2

Sequence conflict

973

1

R → W in AAD02031. Ref.2

Sequence conflict

973

1

R → W in AAB94627. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

984

Helix Strand Turn

Details...

Beta strand

441 – 445

5

Beta strand

447 – 453

7

Beta strand

464 – 473

10

Beta strand

482 – 495

14

Beta strand

501 – 512

12

Beta strand

514 – 517

4

Beta strand

521 – 524

4

Helix

916 – 921

6

Turn

922 – 924

3

Helix

926 – 928

3

Helix

929 – 935

7

Helix

940 – 943

4

Helix

948 – 954

7

Helix

959 – 975

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (EPHB1A) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8044160E24E93A92	FASTA	984	109,885
	10 20 30 40 50 60 MALDYLLLLL 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 SRSPAEASPI 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 KEAVYSDKLQ 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 GMKYLAEMNY 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 LLRIGITLAG 970 980 HQKKILNSIH SMRVQISQSP TAMA
	Isoform 2 (EPH1B1B). Checksum: AD6BBC76C9487EC9	FASTA	973	108,898
	10 20 30 40 50 60 METRERKKSR AEFGTRATAE LGWTANPASG WEEVSGYDEN LNTIRTYQVC NVFEPNQNNW 70 80 90 100 110 120 LLTTFINRRG AHRIYTEMRF TVRDCSSLPN VPGSCKETFN LYYYETDSVI ATKKSAFWSE 130 140 150 160 170 180 APYLKVDTIA ADESFSQVDF GGRLMKVNTE VRSFGPLTRN GFYLAFQDYG ACMSLLSVRV 190 200 210 220 230 240 FFKKCPSIVQ NFAVFPETMT GAESTSLVIA RGTCIPNAEE VDVPIKLYCN GDGEWMVPIG 250 260 270 280 290 300 RCTCKPGYEP ENSVACKACP AGTFKASQEA EGCSHCPSNS RSPAEASPIC TCRTGYYRAD 310 320 330 340 350 360 FDPPEVACTS VPSGPRNVIS IVNETSIILE WHPPRETGGR DDVTYNIICK KCRADRRSCS 370 380 390 400 410 420 RCDDNVEFVP RQLGLTECRV SISSLWAHTP YTFDIQAING VSSKSPFPPQ HVSVNITTNQ 430 440 450 460 470 480 AAPSTVPIMH QVSATMRSIT LSWPQPEQPN GIILDYEIRY YEKEHNEFNS SMARSQTNTA 490 500 510 520 530 540 RIDGLRPGMV YVVQVRARTV AGYGKFSGKM CFQTLTDDDY KSELREQLPL IAGSAAAGVV 550 560 570 580 590 600 FVVSLVAISI VCSRKRAYSK EAVYSDKLQH YSTGRGSPGM KIYIDPFTYE DPNEAVREFA 610 620 630 640 650 660 KEIDVSFVKI EEVIGAGEFG EVYKGRLKLP GKREIYVAIK TLKAGYSEKQ RRDFLSEASI 670 680 690 700 710 720 MGQFDHPNII RLEGVVTKSR PVMIITEFME NGALDSFLRQ NDGQFTVIQL VGMLRGIAAG 730 740 750 760 770 780 MKYLAEMNYV HRDLAARNIL VNSNLVCKVS DFGLSRYLQD DTSDPTYTSS LGGKIPVRWT 790 800 810 820 830 840 APEAIAYRKF TSASDVWSYG IVMWEVMSFG ERPYWDMSNQ DVINAIEQDY RLPPPMDCPA 850 860 870 880 890 900 ALHQLMLDCW QKDRNSRPRF AEIVNTLDKM IRNPASLKTV ATITAVPSQP LLDRSIPDFT 910 920 930 940 950 960 AFTTVDDWLS AIKMVQYRDS FLTAGFTSLQ LVTQMTSEDL LRIGITLAGH QKKILNSIHS 970 MRVQISQSPT AMA
	Isoform 3 (EPHB1C). Checksum: 153B7903D9A7D48C	FASTA	943	105,136
	10 20 30 40 50 60 MALDYLLLLL 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 SRSPAEASPI 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 KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 610 620 630 640 650 660 EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PLEGVVTKSR PVMIITEFME 670 680 690 700 710 720 NGALDSFLRQ NDGQFTVIQL VGMLRGIAAG MKYLAEMNYV 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 LRIGITLAGH QKKILNSIHS MRVQISQSPT AMA
	Isoform 4 (EPHB1D). Checksum: 681E7EBB892759E7	FASTA	616	68,432
	10 20 30 40 50 60 MALDYLLLLL 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 SRSPAEASPI 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 KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 610 EDPNEAVREF AKEIDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, molecular characterization, and chromosomal localization of NET(EPHT2), a human EPH-related receptor protein-tyrosine kinase gene preferentially expressed in brain." Tang X.X., Biegel J.A., Nycum L.M., Yoshioka A., Brodeur G.M., Pleasure D.E., Ikegaki N. Genomics 29:426-437(1995) [PubMed: 8666391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain.
[2]	Stein E., Schoecklmann H.O., Daniel T.O. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). Tissue: Kidney.
[3]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-32.
[4]	"Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells." Stein E., Cerretti D.P., Daniel T.O. J. Biol. Chem. 271:23588-23593(1996) [PubMed: 8798570] [Abstract] Cited for: INTERACTION WITH GRB2 AND GRB10, MUTAGENESIS OF TYR-928, PHOSPHORYLATION AT TYR-928.
[5]	"The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1." Freywald A., Sharfe N., Roifman C.M. J. Biol. Chem. 277:3823-3828(2002) [PubMed: 11713248] [Abstract] Cited for: INTERACTION WITH EPHB6.
[6]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, MASS SPECTROMETRY.
[7]	"Solution structure of the C-terminal SAM-domain of mouse ephrin type-B receptor 1 precursor (EC 2.7.1.112)." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 899-984.
[8]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-18; MET-387; THR-707; VAL-719; GLN-743; THR-912 AND MET-981.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L40636 mRNA. Translation: AAB08520.1.
AF037331 mRNA. Translation: AAD02030.1.
AF037332 mRNA. Translation: AAD02031.1.
AF037333 mRNA. Translation: AAB94627.1.
AF037334 mRNA. Translation: AAB94628.1.

IPI

IPI00008315.
IPI00219244.
IPI00219245.
IPI00334334.

RefSeq

NP_004432.1.

UniGene

Hs.116092

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DJS	NMR	-	A	434-528	[»]
2EAO	NMR	-	A	899-984	[»]

SMR

P54762. Positions 18-197, 592-889.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54762. 7 interactions.

PTM databases

PhosphoSite

P54762.

Proteomic databases

PRIDE

P54762.

Genome annotation databases

Ensembl

ENSG00000154928. Homo sapiens. [Contig view]

GeneID

2047.

KEGG

hsa:2047.

UCSC

uc003eqt.1. human.

Organism-specific databases

GeneCards

GC03P135996.

H-InvDB

HIX0021414.
HIX0043235.

HGNC

HGNC:3392. EPHB1.

MIM

600600. gene.

PharmGKB

PA27824.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P54762.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Pathway_Interaction_DB

ephbfwdpathway. EPHB forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
ephrinb_ephbpathway. EphrinB-EPHB pathway.

Gene expression databases

ArrayExpress

P54762.

Bgee

P54762.

CleanEx

HS_EPHB1.

Family and domain databases

InterPro

IPR013032. EGF-like_reg_CS.
IPR001090. Ephrin_rcpt_lig-bd.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR003962. FnIII_subd.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM_type.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016257. TyrPK_ephrin_receptor.
IPR001426. YKase_receptorV_CS.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.

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

PR00014. FNTYPEIII.
PR00109. TYRKINASE.

ProDom

PD001495. Ephrin_receptor. 1 hit.
PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS01186. EGF_2. 1 hit. Uncertain.
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 Resources

NextBio

8321.

PMAP-CutDB

P54762.

SOURCE

Search...

Entry information

Entry name

EPHB1_HUMAN

Accession

Primary (citable) accession number: P54762
Secondary accession number(s): O43569, O95142, O95143

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	July 7, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)