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Reviewed, UniProtKB/Swiss-Prot P54753 (EPHB3_HUMAN)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ephrin type-B receptor 3
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor HEK-2
    Tyrosine-protein kinase TYRO6
Gene names
Name: EPHB3
Synonyms: ETK2, HEK2, TYRO6
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length998 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Receptor for members of the ephrin-B family. Binds to ephrin-B1 and -B2.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 998965Ephrin type-B receptor 3
PRO_0000016831

Regions

Topological domain34 – 559526Extracellular Potential
Transmembrane560 – 58021 Potential
Topological domain581 – 998418Cytoplasmic Potential
Domain340 – 443104Fibronectin type-III 1
Domain453 – 54492Fibronectin type-III 2
Domain633 – 896264Protein kinase
Domain925 – 98965SAM
Nucleotide binding639 – 6479ATP By similarity
Motif996 – 9983PDZ-binding Potential
Compositional bias199 – 336138Cys-rich

Sites

Active site7581Proton acceptor By similarity
Binding site6651ATP By similarity

Amino acid modifications

Modified residue6001Phosphotyrosine Ref.3
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential

Natural variations

Natural variant1681R → L in a lung small cell carcinoma sample; somatic mutation. Ref.4
VAR_042176
Natural variant4401R → C Ref.4
VAR_042177
Natural variant5791I → V Ref.4
VAR_042178
Natural variant6011I → L Ref.4
VAR_042179
Natural variant7241R → W in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.4
VAR_042180

Experimental info

Sequence conflict3671G → V in CAA53021. Ref.1
Sequence conflict406 – 4083TER → SEP in CAA53021. Ref.1
Sequence conflict4121I → T in CAA53021. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54753-1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 9B65A4EF58B27407

FASTA998110,330
        10         20         30         40         50         60 
MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS ELAWTSHPES 

        70         80         90        100        110        120 
GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR DVQRVYVELK FTVRDCNSIP 

       130        140        150        160        170        180 
NIPGSCKETF NLFYYEADSD VASASSPFWM ENPYVKVDTI APDESFSRLD AGRVNTKVRS 

       190        200        210        220        230        240 
FGPLSKAGFY LAFQDQGACM SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT 

       250        260        270        280        290        300 
CIPNAVEVSV PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP 

       310        320        330        340        350        360 
CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV NETSLILEWS 

       370        380        390        400        410        420 
EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP RQLGLTERRV HISHLLAHTR 

       430        440        450        460        470        480 
YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ AAPSEVPTLR LHSSSGSSLT LSWAPPERPN 

       490        500        510        520        530        540 
GVILDYEMKY FEKSEGIAST VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF 

       550        560        570        580        590        600 
ETTSERGSGA QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY 

       610        620        630        640        650        660 
IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG RLKQPGRREV 

       670        680        690        700        710        720 
FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV VTKSRPVMIL TEFMENCALD 

       730        740        750        760        770        780 
SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS 

       790        800        810        820        830        840 
RFLEDDPSDP TYTSSLGGKI PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW 

       850        860        870        880        890        900 
DMSNQDVINA VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA 

       910        920        930        940        950        960 
SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG FASFDLVAQM 

       970        980        990 
TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV 

« Hide

References

« Hide 'large scale' references
[1]"PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2."
Boehme B., Holtrich U., Wolf G., Luzius H., Grzeschik K.-H., Strebhardt K., Ruebsamen-Waigmann H.
Oncogene 8:2857-2862(1993) [PubMed: 8397371] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[3]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-600, MASS SPECTROMETRY.
[4]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-168; CYS-440; VAL-579; LEU-601 AND TRP-724.
+Additional computationally mapped references.

Cross-references

Sequence databases

X75208 mRNA. Translation: CAA53021.1.
BC052968 mRNA. Translation: AAH52968.1.
IPIIPI00289329.
PIRS37627.
RefSeqNP_004434.2.
UniGeneHs.2913

3D structure databases

HSSPHSSP built from PDB template 1JPA based on UniProtKB P54763.
SMRP54753. Positions 38-212, 606-903, 920-996.
ModBaseSearch...

PTM databases

PhosphoSiteP54753.

Proteomic databases

PRIDEP54753.

Genome annotation databases

EnsemblENSG00000182580. Homo sapiens. [Contig view]
GeneID2049.
KEGGhsa:2049.

Organism-specific databases

GeneCardsGC03P185762.
H-InvDBHIX0024492.
HGNCHGNC:3394. EPHB3.
HPAHPA007698.
HPA008184.
MIM601839. gene.
PharmGKBPA27826.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP54753.
HOVERGENP54753.
OMAP54753. FASFDLV.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBephbfwdpathway. EPHB forward signaling.
ephrinb_ephbpathway. EphrinB-EPHB pathway.

Gene expression databases

ArrayExpressP54753.
BgeeP54753.
CleanExHS_EPHB3.
GermOnlineENSG00000182580. Homo sapiens.

Family and domain databases

InterProIPR001090. Ephrin_rcpt_lig-bd.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR003962. FnIII_subd.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM_type.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016257. TyrPK_ephrin_receptor.
IPR001426. YKase_receptorV_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00014. FNTYPEIII.
PR00109. TYRKINASE.
ProDomPD001495. Ephrin_receptor. 1 hit.
PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50853. 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 Resources

NextBio8331.
SOURCESearch...

Entry information

Entry nameEPHB3_HUMAN
AccessionPrimary (citable) accession number: P54753
Secondary accession number(s): Q7Z740
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 27, 2005
Last modified: June 16, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents