P54762 (EPHB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
ELK
EPH tyrosine kinase 2
EPH-like kinase 6
Short name=EK6
Short name=hEK6
Neuronally-expressed EPH-related tyrosine kinase
Short name=NET
Tyrosine-protein kinase receptor EPH-2

Gene names

Name:	EPHB1
Synonyms:	ELK, EPHT2, HEK6, NET

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 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.2 Ref.9 Ref.11 Ref.12 Ref.13
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. Interacts with PICK1 By similarity. Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion By similarity. 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.2 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Cell membrane; Single-pass type I membrane protein. Early endosome membrane. Cell projection › dendrite By similarity Ref.13.
Tissue specificity	Preferentially expressed in brain.
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. Ref.7 Ref.11 Ref.13 Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation. Ref.13
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.
Sequence caution	The sequence AAB94627.1 differs from that shown. Reason: wrong intron-exon boundaries. The sequence AAB94628.1 differs from that shown. Reason: wrong intron-exon boundaries. The sequence AAD02031.1 differs from that shown. Reason: Chimeric cDNA.

Ontologies

Keywords
Biological process	Cell adhesion Neurogenesis
Cellular component	Cell membrane Cell projection Endosome Membrane
Coding sequence diversity	Polymorphism
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from direct assay Ref.9. Source: UniProtKB camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara cell chemotaxis Inferred from direct assay Ref.12. Source: UniProtKB cell-substrate adhesion Inferred from direct assay Ref.2. Source: UniProtKB central nervous system projection neuron axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB dendritic spine morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB detection of temperature stimulus involved in sensory perception of pain Inferred from sequence or structural similarity. Source: UniProtKB establishment of cell polarity Inferred from sequence or structural similarity. Source: UniProtKB neural precursor cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB optic nerve morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of synapse assembly Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.13. Source: UniProtKB regulation of ERK1 and ERK2 cascade Inferred from direct assay Ref.12Ref.13. Source: UniProtKB regulation of JNK cascade Inferred from direct assay Ref.2. Source: UniProtKB retinal ganglion cell axon guidance Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome membrane Inferred from direct assay Ref.13. Source: UniProtKB integral to plasma membrane Inferred from direct assay Ref.13. Source: UniProtKB membrane raft Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW axon guidance receptor activity Inferred from electronic annotation. Source: Compara transmembrane-ephrin receptor activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB10	Q13322	2	EBI-80252,EBI-80275
GRB2	P62993	2	EBI-80252,EBI-401755
GRB7	Q14451	4	EBI-80252,EBI-970191

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.6

Chain

18 – 984

967

Ephrin type-B receptor 1

PRO_0000016824

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 Probable

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

Natural variant

18

1

M → V. Ref.16
Corresponds to variant rs55650774 [ dbSNP | Ensembl ].

VAR_042165

Natural variant

87

1

T → S.
Corresponds to variant rs1042794 [ dbSNP | Ensembl ].

VAR_011801

Natural variant

152

1

G → R.
Corresponds to variant rs1042793 [ dbSNP | Ensembl ].

VAR_011802

Natural variant

367

1

R → G.
Corresponds to variant rs1042789 [ dbSNP | Ensembl ].

VAR_011803

Natural variant

387

1

T → M. Ref.16
Corresponds to variant rs56396912 [ dbSNP | Ensembl ].

VAR_042166

Natural variant

485

1

R → S.
Corresponds to variant rs1042788 [ dbSNP | Ensembl ].

VAR_011804

Natural variant

707

1

S → T in an ovarian undifferentiated carcinoma sample; somatic mutation. Ref.16

VAR_042167

Natural variant

719

1

I → V in a gastric adenocarcinoma sample; somatic mutation. Ref.16

VAR_042168

Natural variant

743

1

R → Q in a gastric adenocarcinoma sample; somatic mutation. Ref.16

VAR_042169

Natural variant

847

1

M → T.
Corresponds to variant rs1042785 [ dbSNP | Ensembl ].

VAR_011805

Natural variant

912

1

A → T. Ref.16
Corresponds to variant rs56345346 [ dbSNP | Ensembl ].

VAR_042170

Natural variant

973

1

R → W. Ref.2
Corresponds to variant rs1042784 [ dbSNP | Ensembl ].

VAR_058479

Natural variant

981

1

T → M. Ref.16
Corresponds to variant rs56186270 [ dbSNP | Ensembl ].

VAR_042171

Experimental info

Mutagenesis

594

1

Y → F: Loss of interaction with NCK1. Ref.2

Mutagenesis

600

1

Y → F: Loss of interaction with SHC1 and SRC. Ref.12

Mutagenesis

651

1

K → R: Kinase-dead mutant. Unable to autophosphorylate, to interact with SH2 domain-containing interactors, to activate the MAPK/ERK and JUN signaling cascades. Not ubiquitinated by CBL. Ref.2 Ref.13

Mutagenesis

778

1

Y → F: Loss of interaction with SHC1. Ref.12

Mutagenesis

928

1

Y → F: Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation. Disrupts interaction with GRB7 and ACP1. Ref.7 Ref.9 Ref.11

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

752

1

V → L in AAI11745. Ref.5

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

881

1

M → I in BAF83897. Ref.3

Sequence conflict

903

1

L → H in BAF83897. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

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.

.

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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)
	P54762 [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

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CELL ADHESION, FUNCTION IN JUN CASCADE ACTIVATION, INTERACTION WITH NCK1, MUTAGENESIS OF TYR-594 AND LYS-651, VARIANT TRP-973. Tissue: Kidney.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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].
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-32.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB2 AND GRB10, MUTAGENESIS OF TYR-928, PHOSPHORYLATION AT TYR-928.
[8]	"Unified nomenclature for Eph family receptors and their ligands, the ephrins." Eph nomenclature committee Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[9]	"Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses." Stein E., Lane A.A., Cerretti D.P., Schoecklmann H.O., Schroff A.D., Van Etten R.L., Daniel T.O. Genes Dev. 12:667-678(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL ADHESION, INTERACTION WITH ACP1, MUTAGENESIS OF TYR-928.
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPHB6.
[11]	"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, FUNCTION, PHOSPHORYLATION AT TYR-928, MUTAGENESIS OF TYR-928.
[12]	"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: FUNCTION IN CELL MIGRATION, FUNCTION IN ERK CASCADE ACTIVATION, INTERACTION WITH GRB2; SHC1 AND SRC, MUTAGENESIS OF TYR-600 AND TYR-778.
[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: FUNCTION IN ERK CASCADE ACTIVATION, UBIQUITINATION BY CBL, INTERACTION WITH CBL, MUTAGENESIS OF LYS-651, AUTOPHOSPHORYLATION, IDENTIFICATION OF EFNB1 AS LIGAND, SUBCELLULAR LOCATION.
[14]	"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.
[15]	"Solution structures of the FN3 domain of human ephrin type-B receptor 1." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 434-528.
[16]	"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] [Europe PMC] [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

EMBL
GenBank
DDBJ

L40636 mRNA. Translation: AAB08520.1.
AF037331 mRNA. Translation: AAD02030.1.
AF037332 mRNA. Translation: AAD02031.1. Sequence problems.
AF037333 mRNA. Translation: AAB94627.1. Sequence problems.
AF037334 mRNA. Translation: AAB94628.1. Sequence problems.
AK291208 mRNA. Translation: BAF83897.1.
AC016931 Genomic DNA. No translation available.
AC016951 Genomic DNA. No translation available.
AC063918 Genomic DNA. No translation available.
AC073244 Genomic DNA. No translation available.
AC092969 Genomic DNA. No translation available.
BC111744 mRNA. Translation: AAI11745.1.

IPI

IPI00008315.

RefSeq

NP_004432.1. NM_004441.4.

UniGene

Hs.116092.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P54762.

ModBase

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Protein-protein interaction databases

IntAct

P54762. 6 interactions.

STRING

9606.ENSP00000381097.

PTM databases

PhosphoSite

P54762.

Polymorphism databases

DMDM

1706663.

Proteomic databases

PaxDb

P54762.

PRIDE

P54762.

Protocols and materials databases

DNASU

2047.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398015; ENSP00000381097; ENSG00000154928.

GeneID

2047.

KEGG

hsa:2047.

UCSC

uc003eqt.3. human.

Organism-specific databases

CTD

2047.

GeneCards

GC03P134316.

HGNC

HGNC:3392. EPHB1.

MIM

600600. gene.

neXtProt

NX_P54762.

PharmGKB

PA27824.

GenAtlas

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Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233856.

HOVERGEN

HBG062180.

InParanoid

P54762.

KO

K05110.

OMA

ELGWTAN.

OrthoDB

EOG4W9J35.

PhylomeDB

P54762.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

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.

Genevestigator

P54762.

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.
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.
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

BindingDB

P54762.

ChEMBL

CHEMBL5072.

EvolutionaryTrace

P54762.

GenomeRNAi

2047.

NextBio

8321.

PMAP-CutDB

P54762.

SOURCE

Search...

Entry information

Entry name

EPHB1_HUMAN

Accession

Primary (citable) accession number: P54762
Secondary accession number(s): A8K593 , O43569, O95142, O95143, Q0VG87

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 143 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.