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P54760 (EPHB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length987 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processAngiogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from direct assay Ref.5. Source: UniProtKB

cell migration involved in sprouting angiogenesis

Inferred from direct assay Ref.5. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from direct assay Ref.5. Source: UniProtKB

heart morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.1. Source: GOC

protein autophosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentintegral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ephrin receptor activity

Inferred from direct assay Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 987972Ephrin type-B receptor 4
PRO_0000016834

Regions

Topological domain16 – 539524Extracellular Potential
Transmembrane540 – 56021Helical; Potential
Topological domain561 – 987427Cytoplasmic Potential
Domain17 – 202186Eph LBD
Domain323 – 432110Fibronectin type-III 1
Domain436 – 52994Fibronectin type-III 2
Domain615 – 899285Protein kinase
Domain907 – 97165SAM
Nucleotide binding621 – 6299ATP By similarity
Motif985 – 9873PDZ-binding Potential
Compositional bias184 – 320137Cys-rich

Sites

Active site7401Proton acceptor By similarity
Binding site6471ATP By similarity

Amino acid modifications

Modified residue9111Phosphoserine Ref.7 Ref.10
Modified residue9761Phosphothreonine Ref.7 Ref.8 Ref.10
Modified residue9871Phosphotyrosine Ref.10
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 184 Ref.12 Ref.13
Disulfide bond97 ↔ 107 Ref.12 Ref.13

Natural variations

Natural variant671P → L. Ref.15
Corresponds to variant rs34653459 [ dbSNP | Ensembl ].
VAR_042181
Natural variant1131V → I. Ref.15
Corresponds to variant rs55866373 [ dbSNP | Ensembl ].
VAR_042182
Natural variant3461P → L in a metastatic melanoma sample; somatic mutation. Ref.15
VAR_042183
Natural variant3711A → V. Ref.15
Corresponds to variant rs55720981 [ dbSNP | Ensembl ].
VAR_042184
Natural variant5761D → E. Ref.15
Corresponds to variant rs36050247 [ dbSNP | Ensembl ].
VAR_042185
Natural variant6781R → H. Ref.15
Corresponds to variant rs55692440 [ dbSNP | Ensembl ].
VAR_042186
Natural variant8821A → T. Ref.15
Corresponds to variant rs34918225 [ dbSNP | Ensembl ].
VAR_042187
Natural variant8891R → W in a gastric adenocarcinoma sample; somatic mutation. Ref.15
VAR_042188
Natural variant8901E → D. Ref.15
Corresponds to variant rs35638378 [ dbSNP | Ensembl ].
VAR_042189

Experimental info

Mutagenesis951L → R: Reduces binding affinity for EFNB2. Ref.12
Sequence conflict621D → E in AAA20598. Ref.1
Sequence conflict3081Y → D in AAA20598. Ref.1
Sequence conflict4641V → W in AAA20598. Ref.1
Sequence conflict926 – 9272ES → AR in AAA20598. Ref.1

Secondary structure

.................................................................................................... 987
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54760 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 11A004622F194706

FASTA987108,270
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"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.
[13]"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.
[14]"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.
[15]"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. expand/collapse author list , 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.
CCDSCCDS5706.1.
PIRA54092.
RefSeqNP_004435.3. NM_004444.4.
UniGeneHs.437008.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BBAX-ray1.65A17-196[»]
2E7HNMR-A434-529[»]
2HLEX-ray2.05A17-196[»]
2QKQX-ray2.10A/B896-977[»]
2VWUX-ray2.00A598-887[»]
2VWVX-ray1.90A598-899[»]
2VWWX-ray1.90A598-899[»]
2VWXX-ray1.65A598-899[»]
2VWYX-ray1.65A598-899[»]
2VWZX-ray1.65A598-899[»]
2VX0X-ray2.10A598-899[»]
2VX1X-ray1.65A598-899[»]
2X9FX-ray1.75A598-899[»]
2XVDX-ray1.70A598-899[»]
2YN8X-ray2.11A/B598-892[»]
3ZEWX-ray2.50A/B598-892[»]
4AW5X-ray2.33A605-890[»]
4BB4X-ray1.65A598-899[»]
ProteinModelPortalP54760.
SMRP54760. Positions 15-529, 608-973.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108364. 4 interactions.
IntActP54760. 2 interactions.
STRING9606.ENSP00000350896.

Chemistry

BindingDBP54760.
ChEMBLCHEMBL5147.
GuidetoPHARMACOLOGY1833.

PTM databases

PhosphoSiteP54760.

Polymorphism databases

DMDM19860819.

2D gel databases

DOSAC-COBS-2DPAGEP54760.

Proteomic databases

MaxQBP54760.
PaxDbP54760.
PRIDEP54760.

Protocols and materials databases

DNASU2050.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358173; ENSP00000350896; ENSG00000196411.
GeneID2050.
KEGGhsa:2050.
UCSCuc003uwm.1. human.

Organism-specific databases

CTD2050.
GeneCardsGC07M100402.
H-InvDBHIX0025312.
HGNCHGNC:3395. EPHB4.
HPACAB013537.
MIM600011. gene.
neXtProtNX_P54760.
PharmGKBPA27827.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP54760.
KOK05113.
OMATVFYFES.
PhylomeDBP54760.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP54760.

Gene expression databases

ArrayExpressP54760.
BgeeP54760.
CleanExHS_EPHB4.
GenevestigatorP54760.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamPF14575. EphA2_TM. 1 hit.
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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS01186. EGF_2. 1 hit.
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]
ProtoNetSearch...

Other

ChiTaRSEPHB4. human.
EvolutionaryTraceP54760.
GeneWikiEPH_receptor_B4.
GenomeRNAi2050.
NextBio8335.
PROP54760.
SOURCESearch...

Entry information

Entry nameEPHB4_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM