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P29323 (EPHB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 177. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-B receptor 2

EC=2.7.10.1
Alternative name(s):
Developmentally-regulated Eph-related tyrosine kinase
ELK-related tyrosine kinase
EPH tyrosine kinase 3
EPH-like kinase 5
Short name=EK5
Short name=hEK5
Renal carcinoma antigen NY-REN-47
Tyrosine-protein kinase TYRO5
Tyrosine-protein kinase receptor EPH-3
Gene names
Name:EPHB2
Synonyms:DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1055 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. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. Beside axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. Ref.15

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 (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) By similarity. Interacts with ARHGEF15; mediates ARHGEF15 phosphorylation, ubiquitination and degradation by the proteasome. Interacts with AQP1; involved in endolymph production in the inner ear.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell projectionaxon By similarity. Cell projectiondendrite By similarity.

Tissue specificity

Brain, heart, lung, kidney, placenta, pancreas, liver and skeletal muscle. Preferentially expressed in fetal brain.

Involvement in disease

Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
Note: The gene represented in this entry may be involved in disease pathogenesis. EPHB2 mutations have been found in a prostate cancer cell line derived from a brain metastasis.

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 processNeurogenesis
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   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

axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

axonal fasciculation

Inferred from sequence or structural similarity. Source: UniProtKB

camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

central nervous system projection neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

commissural neuron axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

corpus callosum development

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine development

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

inner ear morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

learning

Inferred from electronic annotation. Source: Ensembl

negative regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

nervous system development

Traceable author statement Ref.2. Source: UniProtKB

optic nerve morphogenesis

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

positive regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of body fluid levels

Inferred from sequence or structural similarity. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from electronic annotation. Source: Ensembl

urogenital system development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance receptor activity

Inferred from electronic annotation. Source: Ensembl

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane-ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NUP153P497902EBI-1059294,EBI-286779

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29323-1)

Also known as: EPHB2v; Long;

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: P29323-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     986-986: G → V
     987-1055: Missing.
Note: Contains a phosphoserine at position 983.
Isoform 3 (identifier: P29323-3)

The sequence of this isoform differs from the canonical sequence as follows:
     568-568: R → RR
     986-986: G → V
     987-1055: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 984.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 10551037Ephrin type-B receptor 2
PRO_0000016827

Regions

Topological domain19 – 543525Extracellular Potential
Transmembrane544 – 56421Helical; Potential
Topological domain565 – 1055491Cytoplasmic Potential
Domain20 – 202183Eph LBD
Domain324 – 434111Fibronectin type-III 1
Domain435 – 53096Fibronectin type-III 2
Domain621 – 884264Protein kinase
Domain913 – 97765SAM
Nucleotide binding627 – 6359ATP By similarity
Motif984 – 9863PDZ-binding (in isoform 2) Potential
Compositional bias184 – 324141Cys-rich

Sites

Active site7461Proton acceptor By similarity
Binding site6531ATP By similarity

Amino acid modifications

Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 184 Ref.14
Disulfide bond97 ↔ 107 Ref.14

Natural variations

Alternative sequence5681R → RR in isoform 3.
VSP_015713
Alternative sequence9861G → V in isoform 2 and isoform 3.
VSP_003016
Alternative sequence987 – 105569Missing in isoform 2 and isoform 3.
VSP_003017
Natural variant1991R → H in prostate cancer. Ref.15
VAR_032853
Natural variant2791A → S in prostate cancer. Ref.15 Ref.16 Ref.17
Corresponds to variant rs35882952 [ dbSNP | Ensembl ].
VAR_032854
Natural variant2891C → G. Ref.17
VAR_042172
Natural variant3611I → V. Ref.17
Corresponds to variant rs56180036 [ dbSNP | Ensembl ].
VAR_042173
Natural variant6501V → A in prostate cancer. Ref.16
Corresponds to variant rs142173175 [ dbSNP | Ensembl ].
VAR_032855
Natural variant6781D → N. Ref.17
Corresponds to variant rs28936395 [ dbSNP | Ensembl ].
VAR_042174
Natural variant6791H → N in prostate cancer. Ref.15
VAR_032856
Natural variant8441R → W. Ref.17
Corresponds to variant rs55826626 [ dbSNP | Ensembl ].
VAR_042175
Natural variant8831M → V in prostate cancer. Ref.16
VAR_032857
Natural variant9091I → M in prostate cancer. Ref.15
VAR_032858

Experimental info

Sequence conflict1 – 2020MALRR…LAAVE → MWVPVLALPVCTYA in BAA06506. Ref.1
Sequence conflict1541G → D in BAA06506. Ref.1
Sequence conflict4761K → KQ in BAA06506. Ref.1
Sequence conflict495 – 4962Missing in AAA74244. Ref.5
Sequence conflict5321E → D in BAA06506. Ref.1
Sequence conflict5891M → I in AAA74244. Ref.5
Sequence conflict6711A → R in BAA03537. Ref.7
Sequence conflict7881I → F in AAA74244. Ref.5
Sequence conflict8531S → A in BAA06506. Ref.1
Sequence conflict8531S → A in BAA07073. Ref.6
Sequence conflict8531S → A in BAA03537. Ref.7
Sequence conflict9231E → K in BAA06506. Ref.1
Sequence conflict9231E → K in BAA07073. Ref.6
Sequence conflict9231E → K in BAA03537. Ref.7
Sequence conflict9581V → L in AAA99310. Ref.2

Secondary structure

.................................................................................. 1055
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (EPHB2v) (Long) [UniParc].

Last modified September 27, 2005. Version 5.
Checksum: 4F8BFEDC45986483

FASTA1,055117,493
        10         20         30         40         50         60 
MALRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD ENMNTIRTYQ 

        70         80         90        100        110        120 
VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI PSVPGSCKET FNLYYYEADF 

       130        140        150        160        170        180 
DSATKTFPNW MENPWVKVDT IAADESFSQV DLGGRVMKIN TEVRSFGPVS RSGFYLAFQD 

       190        200        210        220        230        240 
YGGCMSLIAV RVFYRKCPRI IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY 

       250        260        270        280        290        300 
CNGDGEWLVP IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA 

       310        320        330        340        350        360 
TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS GGREDLVYNI 

       370        380        390        400        410        420 
ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA HTQYTFEIQA VNGVTDQSPF 

       430        440        450        460        470        480 
SPQFASVNIT TNQAAPSAVS IMHQVSRTVD SITLSWSQPD QPNGVILDYE LQYYEKELSE 

       490        500        510        520        530        540 
YNATAIKSPT NTVTVQGLKA GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIQEK 

       550        560        570        580        590        600 
LPLIIGSSAA GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF 

       610        620        630        640        650        660 
TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV AIKTLKSGYT 

       670        680        690        700        710        720 
EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE FMENGSLDSF LRQNDGQFTV 

       730        740        750        760        770        780 
IQLVGMLRGI AAGMKYLADM NYVHRDLAAR NILVNSNLVC KVSDFGLSRF LEDDTSDPTY 

       790        800        810        820        830        840 
TSALGGKIPI RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE 

       850        860        870        880        890        900 
QDYRLPPPMD CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI 

       910        920        930        940        950        960 
NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM EDILRVGVTL 

       970        980        990       1000       1010       1020 
AGHQKKILNS IQVMRAQMNQ IQSVEGQPLA RRPRATGRTK RCQPRDVTKK TCNSNDGKKK 

      1030       1040       1050 
GMGKKKTDPG RGREIQGIFF KEDSHKESND CSCGG 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 4B9B532A48B754A6
Show »

FASTA986109,874
Isoform 3 [UniParc].

Checksum: EF6DA7A63D894E47
Show »

FASTA987110,030

References

« Hide 'large scale' references
[1]"Overexpression of ERK, an EPH family receptor protein tyrosine kinase, in various human tumors."
Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y.Y., Naito Y., Yamada K., Sugimura H., Kino I.
Cancer Res. 54:3645-3650(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Molecular characterization and chromosomal localization of DRT (EPHT3): a developmentally regulated human protein-tyrosine kinase gene of the EPH family."
Ikegaki N., Tang X.X., Liu X.-G., Biegel J.A., Allen C., Yoshioka A., Sulman E.P., Brodeur G.M., Pleasure D.E.
Hum. Mol. Genet. 4:2033-2045(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fetal brain.
[3]"A variant transcript encoding an isoform of the human protein tyrosine kinase EPHB2 is generated by alternative splicing and alternative use of polyadenylation signals."
Tang X.X., Pleasure D.E., Brodeur G.M., Ikegaki N.
Oncogene 17:521-526(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases."
Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R., Welcher A.A.
Oncogene 10:897-905(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-986 (ISOFORM 2).
Tissue: Brain.
[6]"Identification of the human ERK gene as a putative receptor tyrosine kinase and its chromosomal localization to 1p36.1: a comparative mapping of human, mouse, and rat chromosomes."
Saito T., Seki N., Matsuda Y., Kitahara M., Murata M., Kanda N., Nomura N., Yamamoto T., Hori T.-A.
Genomics 26:382-384(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-986 (ISOFORM 2).
Tissue: Fetal brain.
[7]"Identification of protein-tyrosine kinase genes preferentially expressed in embryo stomach and gastric cancer."
Iwase T., Tanaka M., Suzuki M., Naito Y., Sugimura H., Kino I.
Biochem. Biophys. Res. Commun. 194:698-705(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 640-986 (ISOFORM 2).
Tissue: Gastric carcinoma.
[8]"eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases."
Chan J., Watt V.M.
Oncogene 6:1057-1061(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-712.
[9]"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.
[10]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-983 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Oligomeric structure of the human EphB2 receptor SAM domain."
Thanos C.D., Goodwill K.E., Bowie J.U.
Science 283:833-836(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 910-986 (ISOFORM SHORT).
[14]"Three-dimensional structure of the EphB2 receptor in complex with an antagonistic peptide reveals a novel mode of inhibition."
Chrencik J.E., Brooun A., Recht M.I., Nicola G., Davis L.K., Abagyan R., Widmer H., Pasquale E.B., Kuhn P.
J. Biol. Chem. 282:36505-36513(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-195 OF HOMODIMER IN COMPLEX WITH ANTAGONISTIC PEPTIDE, DISULFIDE BOND.
[15]"Nonsense-mediated decay microarray analysis identifies mutations of EPHB2 in human prostate cancer."
Huusko P., Ponciano-Jackson D., Wolf M., Kiefer J.A., Azorsa D.O., Tuzmen S., Weaver D., Robbins C., Moses T., Allinen M., Hautaniemi S., Chen Y., Elkahloun A., Basik M., Bova G.S., Bubendorf L., Lugli A., Sauter G. expand/collapse author list , Schleutker J., Ozcelik H., Elowe S., Pawson T., Trent J.M., Carpten J.D., Kallioniemi O.-P., Mousses S.
Nat. Genet. 36:979-983(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER HIS-199; SER-279; ASN-679 AND MET-909, FUNCTION AS A TUMOR SUPPRESSOR.
[16]"A common nonsense mutation in EphB2 is associated with prostate cancer risk in African American men with a positive family history."
Kittles R.A., Baffoe-Bonnie A.B., Moses T.Y., Robbins C.M., Ahaghotu C., Huusko P., Pettaway C., Vijayakumar S., Bennett J., Hoke G., Mason T., Weinrich S., Trent J.M., Collins F.S., Mousses S., Bailey-Wilson J., Furbert-Harris P., Dunston G., Powell I.J., Carpten J.D.
J. Med. Genet. 43:507-511(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER SER-279; ALA-650 AND VAL-883.
[17]"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] SER-279; GLY-289; VAL-361; ASN-678 AND TRP-844.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31661 mRNA. Translation: BAA06506.1.
L41939 mRNA. Translation: AAA99310.1.
AF025304 mRNA. Translation: AAB94602.1.
AL035704, AL158086, AL512444 Genomic DNA. Translation: CAI22645.1.
AL035704, AL158086, AL512444 Genomic DNA. Translation: CAI22646.1.
AL035704, AL158086, AL512444 Genomic DNA. Translation: CAI22647.2.
AL158086, AL035704, AL512444 Genomic DNA. Translation: CAI22897.1.
AL158086, AL512444, AL035704 Genomic DNA. Translation: CAI22898.1.
AL158086, AL035704, AL512444 Genomic DNA. Translation: CAI22899.2.
AL512444, AL035704, AL158086 Genomic DNA. Translation: CAI16428.1.
AL512444, AL035704, AL158086 Genomic DNA. Translation: CAI16429.1.
AL512444, AL035704, AL158086 Genomic DNA. Translation: CAI16430.2.
L36643 mRNA. Translation: AAA74244.1.
D37827 mRNA. Translation: BAA07073.1.
D14717 mRNA. Translation: BAA03537.1.
X59292 Genomic DNA. Translation: CAA41981.1.
PIRA57174.
I78842.
RefSeqNP_004433.2. NM_004442.6.
NP_059145.2. NM_017449.3.
UniGeneHs.523329.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4FX-ray1.95A/B/C/D/E/F/G/H910-985[»]
1F0MX-ray2.20A910-985[»]
2QBXX-ray2.30A/B20-196[»]
3ZFMX-ray2.27A604-898[»]
ProteinModelPortalP29323.
SMRP29323. Positions 18-531, 575-985.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108362. 18 interactions.
DIPDIP-1162N.
IntActP29323. 3 interactions.
MINTMINT-5005955.
STRING9606.ENSP00000363763.

Chemistry

BindingDBP29323.
ChEMBLCHEMBL3290.
GuidetoPHARMACOLOGY1831.

PTM databases

PhosphoSiteP29323.

Polymorphism databases

DMDM76803654.

Proteomic databases

PaxDbP29323.
PRIDEP29323.

Protocols and materials databases

DNASU2048.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374630; ENSP00000363761; ENSG00000133216. [P29323-2]
ENST00000374632; ENSP00000363763; ENSG00000133216. [P29323-3]
ENST00000400191; ENSP00000383053; ENSG00000133216. [P29323-1]
GeneID2048.
KEGGhsa:2048.
UCSCuc001bge.3. human. [P29323-3]
uc001bgf.3. human. [P29323-2]
uc009vqj.1. human. [P29323-1]

Organism-specific databases

CTD2048.
GeneCardsGC01P023037.
H-InvDBHIX0028518.
HGNCHGNC:3393. EPHB2.
HPACAB013647.
MIM176807. phenotype.
600997. gene.
603688. phenotype.
neXtProtNX_P29323.
Orphanet1331. Familial prostate cancer.
PharmGKBPA27825.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP29323.
KOK05111.
OMAIVCNRRR.
OrthoDBEOG7VTDM6.
PhylomeDBP29323.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111045. Developmental Biology.
SignaLinkP29323.

Gene expression databases

ArrayExpressP29323.
BgeeP29323.
CleanExHS_EPHB2.
GenevestigatorP29323.

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.
PROSITEPS51550. 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

ChiTaRSEPHB2. human.
EvolutionaryTraceP29323.
GeneWikiEPH_receptor_B2.
GenomeRNAi2048.
NextBio8325.
PROP29323.
SOURCESearch...

Entry information

Entry nameEPHB2_HUMAN
AccessionPrimary (citable) accession number: P29323
Secondary accession number(s): O43477 expand/collapse secondary AC list , Q5T0U6, Q5T0U7, Q5T0U8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 177 of the entry and version 5 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 1

Human chromosome 1: entries, gene names and cross-references to MIM