P54760 (EPHB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ephrin type-B receptor 4
EC=2.7.10.1

Alternative name(s):
Hepatoma transmembrane kinase
Tyrosine-protein kinase TYRO11

Gene names

Name:	EPHB4
Synonyms:	HTK, MYK1, TYRO11

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	987 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. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis. Ref.5 Ref.6
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.
Subcellular location	Cell membrane; Single-pass type I membrane protein Ref.1.
Tissue specificity	Abundantly expressed in placenta but also detected in kidney, liver, lung, pancreas, skeletal muscle and heart. Expressed in primitive and myeloid, but not lymphoid, hematopoietic cells. Also observed in cell lines derived from liver, breast, colon, lung, melanocyte and cervix. Ref.1
Developmental stage	Expressed in fetal heart, lung, liver and to a lower extent in brain. Not expressed in adult brain. Ref.1
Post-translational modification	Phosphorylated; autophosphorylation is stimulated by EFNB2. Ref.1
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	Angiogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from direct assay Ref.5. Source: UniProtKB cell migration involved in sprouting angiogenesis Inferred from direct assay Ref.5. Source: UniProtKB heart morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cell surface Inferred from direct assay PubMed 12493773. Source: UniProtKB integral to plasma membrane Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Potential

Chain

16 – 987

972

Ephrin type-B receptor 4

PRO_0000016834

Regions

Topological domain

16 – 539

524

Extracellular Potential

Transmembrane

540 – 560

21

Helical; Potential

Topological domain

561 – 987

427

Cytoplasmic Potential

Domain

17 – 202

186

Eph LBD

Domain

323 – 428

106

Fibronectin type-III 1

Domain

434 – 526

93

Fibronectin type-III 2

Domain

615 – 899

285

Protein kinase

Domain

907 – 971

65

SAM

Nucleotide binding

621 – 629

9

ATP By similarity

Motif

985 – 987

3

PDZ-binding Potential

Compositional bias

184 – 320

137

Cys-rich

Sites

Active site

740

1

Proton acceptor By similarity

Binding site

647

1

ATP By similarity

Amino acid modifications

Modified residue

911

1

Phosphoserine Ref.7 Ref.9

Modified residue

976

1

Phosphothreonine Ref.7 Ref.8 Ref.9

Modified residue

987

1

Phosphotyrosine Ref.9

Glycosylation

203

1

N-linked (GlcNAc...) Potential

Glycosylation

335

1

N-linked (GlcNAc...) Potential

Glycosylation

426

1

N-linked (GlcNAc...) Potential

Disulfide bond

61 ↔ 184

Ref.11 Ref.12

Disulfide bond

97 ↔ 107

Ref.11 Ref.12

Natural variations

Natural variant

67

1

P → L. Ref.14
Corresponds to variant rs34653459 [ dbSNP | Ensembl ].

VAR_042181

Natural variant

113

1

V → I. Ref.14
Corresponds to variant rs55866373 [ dbSNP | Ensembl ].

VAR_042182

Natural variant

346

1

P → L in a metastatic melanoma sample; somatic mutation. Ref.14

VAR_042183

Natural variant

371

1

A → V. Ref.14
Corresponds to variant rs55720981 [ dbSNP | Ensembl ].

VAR_042184

Natural variant

576

1

D → E. Ref.14
Corresponds to variant rs36050247 [ dbSNP | Ensembl ].

VAR_042185

Natural variant

678

1

R → H. Ref.14
Corresponds to variant rs55692440 [ dbSNP | Ensembl ].

VAR_042186

Natural variant

882

1

A → T. Ref.14
Corresponds to variant rs34918225 [ dbSNP | Ensembl ].

VAR_042187

Natural variant

889

1

R → W in a gastric adenocarcinoma sample; somatic mutation. Ref.14

VAR_042188

Natural variant

890

1

E → D. Ref.14
Corresponds to variant rs35638378 [ dbSNP | Ensembl ].

VAR_042189

Experimental info

Mutagenesis

95

1

L → R: Reduces binding affinity for EFNB2. Ref.11

Sequence conflict

62

1

D → E in AAA20598. Ref.1

Sequence conflict

308

1

Y → D in AAA20598. Ref.1

Sequence conflict

464

1

V → W in AAA20598. Ref.1

Sequence conflict

926 – 927

2

ES → AR in AAA20598. Ref.1

Secondary structure

1

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987

Helix Strand Turn

Details...

Beta strand

17 – 22

6

Helix

23 – 25

3

Beta strand

33 – 36

4

Beta strand

43 – 48

6

Beta strand

54 – 61

8

Beta strand

63 – 65

3

Beta strand

70 – 74

5

Beta strand

84 – 95

12

Helix

97 – 99

3

Beta strand

109 – 121

13

Beta strand

130 – 132

3

Beta strand

135 – 142

8

Beta strand

147 – 150

4

Turn

151 – 153

3

Beta strand

154 – 156

3

Beta strand

160 – 166

7

Beta strand

171 – 182

12

Beta strand

184 – 196

13

Beta strand

441 – 446

6

Beta strand

449 – 453

5

Beta strand

460 – 462

3

Beta strand

466 – 473

8

Turn

479 – 481

3

Beta strand

482 – 496

15

Beta strand

503 – 510

8

Helix

612 – 614

3

Beta strand

615 – 623

9

Beta strand

625 – 634

10

Beta strand

637 – 639

3

Beta strand

642 – 649

8

Helix

655 – 668

14

Beta strand

679 – 683

5

Beta strand

685 – 694

10

Helix

701 – 707

7

Turn

708 – 710

3

Helix

714 – 733

20

Helix

743 – 745

3

Beta strand

746 – 748

3

Beta strand

754 – 756

3

Helix

765 – 767

3

Helix

784 – 786

3

Helix

789 – 794

6

Helix

799 – 814

16

Turn

815 – 817

3

Turn

820 – 823

4

Helix

826 – 834

9

Helix

847 – 856

10

Helix

861 – 863

3

Helix

867 – 879

13

Helix

881 – 885

5

Helix

912 – 918

7

Helix

922 – 924

3

Helix

925 – 930

6

Helix

936 – 939

4

Helix

944 – 950

7

Helix

955 – 965

11

Sequences

	Sequence		Length	Mass (Da)
	P54760 [UniParc]. Last modified October 18, 2001. Version 2. Checksum: 11A004622F194706	FASTA	987	108,270
	10 20 30 40 50 60 MELRVLLCWA SLAAALEETL LNTKLETADL KWVTFPQVDG QWEELSGLDE EQHSVRTYEV 70 80 90 100 110 120 CDVQRAPGQA HWLRTGWVPR RGAVHVYATL RFTMLECLSL PRAGRSCKET FTVFYYESDA 130 140 150 160 170 180 DTATALTPAW MENPYIKVDT VAAEHLTRKR PGAEATGKVN VKTLRLGPLS KAGFYLAFQD 190 200 210 220 230 240 QGACMALLSL HLFYKKCAQL TVNLTRFPET VPRELVVPVA GSCVVDAVPA PGPSPSLYCR 250 260 270 280 290 300 EDGQWAEQPV TGCSCAPGFE AAEGNTKCRA CAQGTFKPLS GEGSCQPCPA NSHSNTIGSA 310 320 330 340 350 360 VCQCRVGYFR ARTDPRGAPC TTPPSAPRSV VSRLNGSSLH LEWSAPLESG GREDLTYALR 370 380 390 400 410 420 CRECRPGGSC APCGGDLTFD PGPRDLVEPW VVVRGLRPDF TYTFEVTALN GVSSLATGPV 430 440 450 460 470 480 PFEPVNVTTD REVPPAVSDI RVTRSSPSSL SLAWAVPRAP SGAVLDYEVK YHEKGAEGPS 490 500 510 520 530 540 SVRFLKTSEN RAELRGLKRG ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SEGWREQLAL 550 560 570 580 590 600 IAGTAVVGVV LVLVVIVVAV LCLRKQSNGR EAEYSDKHGQ YLIGHGTKVY IDPFTYEDPN 610 620 630 640 650 660 EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK GGYTERQRRE 670 680 690 700 710 720 FLSEASIMGQ FEHPNIIRLE GVVTNSMPVM ILTEFMENGA LDSFLRLNDG QFTVIQLVGM 730 740 750 760 770 780 LRGIASGMRY LAEMSYVHRD LAARNILVNS NLVCKVSDFG LSRFLEENSS DPTYTSSLGG 790 800 810 820 830 840 KIPIRWTAPE AIAFRKFTSA SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP 850 860 870 880 890 900 PPPDCPTSLH QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD 910 920 930 940 950 960 QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFELVS QISAEDLLRI GVTLAGHQKK 970 980 ILASVQHMKS QAKPGTPGGT GGPAPQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily." Bennett B.D., Wang Z., Kuang W.J., Wang A., Groopman J.E., Goeddel D.V., Scadden D.T. J. Biol. Chem. 269:14211-14218(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5." Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F. Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] OF 143-987. Tissue: Pancreas.
[4]	"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.
[5]	"Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells." Fueller T., Korff T., Kilian A., Dandekar G., Augustin H.G. J. Cell Sci. 116:2461-2470(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL ADHESION, FUNCTION IN CELL MIGRATION.
[6]	"EphB4 controls blood vascular morphogenesis during postnatal angiogenesis." Erber R., Eichelsbacher U., Powajbo V., Korn T., Djonov V., Lin J., Hammes H.P., Grobholz R., Ullrich A., Vajkoczy P. EMBO J. 25:628-641(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN POSTNATAL AND TUMOR ANGIOGENESIS.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-976, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-976, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; THR-976 AND TYR-987, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Structural and biophysical characterization of the EphB4*ephrinB2 protein-protein interaction and receptor specificity." Chrencik J.E., Brooun A., Kraus M.L., Recht M.I., Kolatkar A.R., Han G.W., Seifert J.M., Widmer H., Auer M., Kuhn P. J. Biol. Chem. 281:28185-28192(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 17-196 IN COMPLEX WITH EFNB2, MUTAGENESIS OF LEU-95, DISULFIDE BOND.
[12]	"Structure and thermodynamic characterization of the EphB4/Ephrin-B2 antagonist peptide complex reveals the determinants for receptor specificity." Chrencik J.E., Brooun A., Recht M.I., Kraus M.L., Koolpe M., Kolatkar A.R., Bruce R.H., Martiny-Baron G., Widmer H., Pasquale E.B., Kuhn P. Structure 14:321-330(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 17-196 IN COMPLEX WITH ANTAGONISTIC PEPTIDE, DISULFIDE BOND.
[13]	"Solution structure of the second FN3 domain from human ephrin type-B receptor 4." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 434-529.
[14]	"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] LEU-67; ILE-113; LEU-346; VAL-371; GLU-576; HIS-678; THR-882; TRP-889 AND ASP-890.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U07695 mRNA. Translation: AAA20598.1.
AF312032 Genomic DNA. Translation: AAK21010.1.
BC004264 mRNA. Translation: AAH04264.1.

IPI

IPI00289342.

PIR

A54092.

RefSeq

NP_004435.3. NM_004444.4.

UniGene

Hs.437008.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BBA	X-ray	1.65	A	17-196	[»]
2E7H	NMR	-	A	434-529	[»]
2HLE	X-ray	2.05	A	17-196	[»]
2QKQ	X-ray	2.10	A/B	896-977	[»]
2VWU	X-ray	2.00	A	598-887	[»]
2VWV	X-ray	1.90	A	598-899	[»]
2VWW	X-ray	1.90	A	598-899	[»]
2VWX	X-ray	1.65	A	598-899	[»]
2VWY	X-ray	1.65	A	598-899	[»]
2VWZ	X-ray	1.65	A	598-899	[»]
2VX0	X-ray	2.10	A	598-899	[»]
2VX1	X-ray	1.65	A	598-899	[»]
2X9F	X-ray	1.75	A	598-899	[»]
2XVD	X-ray	1.70	A	598-899	[»]
4AW5	X-ray	2.33	A	605-890	[»]
4BB4	X-ray	1.65	A	598-899	[»]

ProteinModelPortal

P54760.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54760. 2 interactions.

STRING

9606.ENSP00000350896.

PTM databases

PhosphoSite

P54760.

Polymorphism databases

DMDM

19860819.

2D gel databases

DOSAC-COBS-2DPAGE

P54760.

Proteomic databases

PaxDb

P54760.

PRIDE

P54760.

Protocols and materials databases

DNASU

2050.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358173; ENSP00000350896; ENSG00000196411.

GeneID

2050.

KEGG

hsa:2050.

UCSC

uc003uwm.1. human.

Organism-specific databases

CTD

2050.

GeneCards

GC07M100402.

H-InvDB

HIX0025312.

HGNC

HGNC:3395. EPHB4.

HPA

CAB013537.

MIM

600011. gene.

neXtProt

NX_P54760.

PharmGKB

PA27827.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233856.

HOVERGEN

HBG062180.

InParanoid

P54760.

KO

K05113.

OMA

CVADAVP.

OrthoDB

EOG408N7B.

PhylomeDB

P54760.

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.

SignaLink

P54760.

Gene expression databases

ArrayExpress

P54760.

Bgee

P54760.

CleanEx

HS_EPHB4.

Genevestigator

P54760.

GermOnline

ENSG00000196411. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
2.60.120.260. 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.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
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.
PF07699. GCC2_GCC3. 1 hit.
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

P54760.

ChEMBL

CHEMBL5147.

ChiTaRS

EPHB4. human.

EvolutionaryTrace

P54760.

GenomeRNAi

2050.

NextBio

8335.

SOURCE

Search...

Entry information

Entry name

EPHB4_HUMAN

Accession

Primary (citable) accession number: P54760
Secondary accession number(s): Q9BTA5, Q9BXP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 18, 2001
Last modified:	May 29, 2013
This is version 150 of the entry and version 2 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.