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P54762 (EPHB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length984 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. 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 projectiondendrite 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 processCell adhesion
Neurogenesis
   Cellular componentCell membrane
Cell projection
Endosome
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay Ref.9. Source: UniProtKB

axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

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 development

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

ephrin receptor signaling pathway

Inferred from direct assay Ref.12Ref.13. 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

neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

optic nerve morphogenesis

Inferred from electronic annotation. Source: Ensembl

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_componentaxon

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome membrane

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

membrane raft

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

transmembrane-ephrin receptor activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.6
Chain18 – 984967Ephrin type-B receptor 1
PRO_0000016824

Regions

Topological domain18 – 540523Extracellular Potential
Transmembrane541 – 56323Helical; Potential
Topological domain564 – 984421Cytoplasmic Potential
Domain19 – 201183Eph LBD
Domain322 – 432111Fibronectin type-III 1
Domain433 – 52896Fibronectin type-III 2
Domain619 – 882264Protein kinase
Domain911 – 97565SAM
Nucleotide binding625 – 6339ATP By similarity
Motif982 – 9843PDZ-binding Potential
Compositional bias183 – 319137Cys-rich

Sites

Active site7441Proton acceptor By similarity
Binding site6511ATP Probable

Amino acid modifications

Modified residue9281Phosphotyrosine; by autocatalysis By similarity
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential

Natural variations

Natural variant181M → V. Ref.16
Corresponds to variant rs55650774 [ dbSNP | Ensembl ].
VAR_042165
Natural variant871T → S.
Corresponds to variant rs1042794 [ dbSNP | Ensembl ].
VAR_011801
Natural variant1521G → R.
Corresponds to variant rs1042793 [ dbSNP | Ensembl ].
VAR_011802
Natural variant3671R → G.
Corresponds to variant rs1042789 [ dbSNP | Ensembl ].
VAR_011803
Natural variant3871T → M. Ref.16
Corresponds to variant rs56396912 [ dbSNP | Ensembl ].
VAR_042166
Natural variant4851R → S.
Corresponds to variant rs1042788 [ dbSNP | Ensembl ].
VAR_011804
Natural variant7071S → T in an ovarian undifferentiated carcinoma sample; somatic mutation. Ref.16
VAR_042167
Natural variant7191I → V in a gastric adenocarcinoma sample; somatic mutation. Ref.16
VAR_042168
Natural variant7431R → Q in a gastric adenocarcinoma sample; somatic mutation. Ref.16
VAR_042169
Natural variant8471M → T.
Corresponds to variant rs1042785 [ dbSNP | Ensembl ].
VAR_011805
Natural variant9121A → T. Ref.16
Corresponds to variant rs56345346 [ dbSNP | Ensembl ].
VAR_042170
Natural variant9731R → W. Ref.2
Corresponds to variant rs1042784 [ dbSNP | Ensembl ].
VAR_058479
Natural variant9811T → M. Ref.16
Corresponds to variant rs56186270 [ dbSNP | Ensembl ].
VAR_042171

Experimental info

Mutagenesis5941Y → F: Loss of interaction with NCK1. Ref.2
Mutagenesis6001Y → F: Loss of interaction with SHC1 and SRC. Ref.12
Mutagenesis6511K → 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
Mutagenesis7781Y → F: Loss of interaction with SHC1. Ref.12
Mutagenesis9281Y → 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 conflict121A → E in AAD02030. Ref.2
Sequence conflict121A → E in AAB94627. Ref.2
Sequence conflict121A → E in AAB94628. Ref.2
Sequence conflict1851S → I in AAD02030. Ref.2
Sequence conflict1851S → I in AAD02031. Ref.2
Sequence conflict1851S → I in AAB94627. Ref.2
Sequence conflict1851S → I in AAB94628. Ref.2
Sequence conflict2741T → R in AAD02030. Ref.2
Sequence conflict2741T → R in AAD02031. Ref.2
Sequence conflict2741T → R in AAB94627. Ref.2
Sequence conflict2741T → R in AAB94628. Ref.2
Sequence conflict3361T → S in AAD02030. Ref.2
Sequence conflict3361T → S in AAD02031. Ref.2
Sequence conflict3361T → S in AAB94627. Ref.2
Sequence conflict3361T → S in AAB94628. Ref.2
Sequence conflict7521V → L in AAI11745. Ref.5
Sequence conflict8131V → H in AAD02030. Ref.2
Sequence conflict8131V → H in AAB94627. Ref.2
Sequence conflict8191S → Y in AAD02030. Ref.2
Sequence conflict8191S → Y in AAB94627. Ref.2
Sequence conflict8811M → I in BAF83897. Ref.3
Sequence conflict9031L → H in BAF83897. Ref.3

Secondary structure

..................................................................... 984
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54762 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8044160E24E93A92

FASTA984109,885
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. 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] 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.
RefSeqNP_004432.1. NM_004441.4.
UniGeneHs.116092.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJSNMR-A434-528[»]
2EAONMR-A899-984[»]
3ZFXX-ray2.50A/B/C/D/E/F/G/H/I602-896[»]
ProteinModelPortalP54762.
SMRP54762. Positions 17-528, 579-894, 900-984.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108361. 12 interactions.
IntActP54762. 8 interactions.
MINTMINT-1519362.
STRING9606.ENSP00000381097.

Chemistry

BindingDBP54762.
ChEMBLCHEMBL2363043.
GuidetoPHARMACOLOGY1830.

PTM databases

PhosphoSiteP54762.

Polymorphism databases

DMDM1706663.

Proteomic databases

PaxDbP54762.
PRIDEP54762.

Protocols and materials databases

DNASU2047.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398015; ENSP00000381097; ENSG00000154928.
GeneID2047.
KEGGhsa:2047.
UCSCuc003eqt.3. human.

Organism-specific databases

CTD2047.
GeneCardsGC03P134316.
HGNCHGNC:3392. EPHB1.
MIM600600. gene.
neXtProtNX_P54762.
PharmGKBPA27824.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP54762.
KOK05110.
OMANSVACKA.
OrthoDBEOG7VTDM6.
PhylomeDBP54762.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP54762.

Gene expression databases

ArrayExpressP54762.
BgeeP54762.
CleanExHS_EPHB1.
GenevestigatorP54762.

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.
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.
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

EvolutionaryTraceP54762.
GeneWikiEPH_receptor_B1.
GenomeRNAi2047.
NextBio8321.
PMAP-CutDBP54762.
PROP54762.
SOURCESearch...

Entry information

Entry nameEPHB1_HUMAN
AccessionPrimary (citable) accession number: P54762
Secondary accession number(s): A8K593 expand/collapse secondary AC list , O43569, O95142, O95143, Q0VG87
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 153 of the entry and version 1 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 3

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