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P54762

- EPHB1_HUMAN

UniProt

P54762 - EPHB1_HUMAN

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Protein
Ephrin type-B receptor 1
Gene
EPHB1, ELK, EPHT2, HEK6, NET
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei651 – 6511ATP Inferred
Active sitei744 – 7441Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi625 – 6339ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. axon guidance receptor activity Source: Ensembl
  3. protein binding Source: UniProtKB
  4. transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. axon guidance Source: UniProtKB
  3. camera-type eye morphogenesis Source: Ensembl
  4. cell chemotaxis Source: UniProtKB
  5. cell-substrate adhesion Source: UniProtKB
  6. central nervous system projection neuron axonogenesis Source: UniProtKB
  7. dendritic spine development Source: UniProtKB
  8. dendritic spine morphogenesis Source: UniProtKB
  9. detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
  10. ephrin receptor signaling pathway Source: UniProtKB
  11. establishment of cell polarity Source: UniProtKB
  12. neural precursor cell proliferation Source: UniProtKB
  13. neurogenesis Source: UniProtKB
  14. optic nerve morphogenesis Source: Ensembl
  15. positive regulation of synapse assembly Source: UniProtKB
  16. protein autophosphorylation Source: UniProtKB
  17. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  18. regulation of JNK cascade Source: UniProtKB
  19. retinal ganglion cell axon guidance Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiP54762.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EPHB1
Synonyms:ELK, EPHT2, HEK6, NET
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3392. EPHB1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Early endosome membrane. Cell projectiondendrite By similarity 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 540523Extracellular Reviewed prediction
Add
BLAST
Transmembranei541 – 56323Helical; Reviewed prediction
Add
BLAST
Topological domaini564 – 984421Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. dendrite Source: UniProtKB-SubCell
  3. early endosome membrane Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. integral component of plasma membrane Source: UniProtKB
  6. membrane raft Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi594 – 5941Y → F: Loss of interaction with NCK1. 1 Publication
Mutagenesisi600 – 6001Y → F: Loss of interaction with SHC1 and SRC. 1 Publication
Mutagenesisi651 – 6511K → 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. 2 Publications
Mutagenesisi778 – 7781Y → F: Loss of interaction with SHC1. 1 Publication
Mutagenesisi928 – 9281Y → F: Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation. Disrupts interaction with GRB7 and ACP1. 3 Publications

Organism-specific databases

PharmGKBiPA27824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 Publication
Add
BLAST
Chaini18 – 984967Ephrin type-B receptor 1
PRO_0000016824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi334 – 3341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi426 – 4261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi480 – 4801N-linked (GlcNAc...) Reviewed prediction
Modified residuei928 – 9281Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

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.3 Publications
Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP54762.
PaxDbiP54762.
PRIDEiP54762.

PTM databases

PhosphoSiteiP54762.

Miscellaneous databases

PMAP-CutDBP54762.

Expressioni

Tissue specificityi

Preferentially expressed in brain.

Gene expression databases

ArrayExpressiP54762.
BgeeiP54762.
CleanExiHS_EPHB1.
GenevestigatoriP54762.

Interactioni

Subunit structurei

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 ACP1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB10Q133222EBI-80252,EBI-80275
GRB2P629932EBI-80252,EBI-401755
GRB7Q144514EBI-80252,EBI-970191

Protein-protein interaction databases

BioGridi108361. 12 interactions.
IntActiP54762. 8 interactions.
MINTiMINT-1519362.
STRINGi9606.ENSP00000381097.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi441 – 4455
Beta strandi447 – 4537
Beta strandi464 – 47310
Beta strandi482 – 49514
Beta strandi501 – 51212
Beta strandi514 – 5174
Beta strandi521 – 5244
Helixi616 – 6183
Beta strandi619 – 6268
Beta strandi633 – 6386
Beta strandi646 – 6527
Helixi659 – 67214
Beta strandi683 – 6875
Beta strandi689 – 6924
Beta strandi694 – 6985
Helixi705 – 7106
Turni711 – 7144
Helixi718 – 73720
Helixi747 – 7493
Beta strandi750 – 7523
Beta strandi758 – 7603
Helixi793 – 7986
Helixi803 – 81816
Turni824 – 8274
Helixi830 – 8389
Helixi851 – 86010
Helixi865 – 8673
Helixi871 – 88313
Helixi885 – 8884
Beta strandi889 – 8913
Helixi916 – 9216
Turni922 – 9243
Helixi926 – 9283
Helixi929 – 9357
Helixi940 – 9434
Helixi948 – 9547
Helixi959 – 97517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJSNMR-A434-528[»]
2EAONMR-A899-984[»]
3ZFXX-ray2.50A/B/C/D/E/F/G/H/I602-896[»]
ProteinModelPortaliP54762.
SMRiP54762. Positions 17-528, 592-984.

Miscellaneous databases

EvolutionaryTraceiP54762.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 201183Eph LBD
Add
BLAST
Domaini322 – 432111Fibronectin type-III 1
Add
BLAST
Domaini433 – 52896Fibronectin type-III 2
Add
BLAST
Domaini619 – 882264Protein kinase
Add
BLAST
Domaini911 – 97565SAM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi982 – 9843PDZ-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi183 – 319137Cys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54762.
KOiK05110.
OMAiTLMDTRT.
OrthoDBiEOG7VTDM6.
PhylomeDBiP54762.
TreeFamiTF315608.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. 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]
PfamiPF14575. 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]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS01186. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54762-1 [UniParc]FASTAAdd to Basket

« Hide

MALDYLLLLL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE    50
NLNTIRTYQV CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP 100
NVPGSCKETF NLYYYETDSV IATKKSAFWS EAPYLKVDTI AADESFSQVD 150
FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY GACMSLLSVR VFFKKCPSIV 200
QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC NGDGEWMVPI 250
GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPAEASPI 300
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG 350
RDDVTYNIIC KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT 400
PYTFDIQAIN GVSSKSPFPP QHVSVNITTN QAAPSTVPIM HQVSATMRSI 450
TLSWPQPEQP NGIILDYEIR YYEKEHNEFN SSMARSQTNT ARIDGLRPGM 500
VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP LIAGSAAAGV 550
VFVVSLVAIS IVCSRKRAYS KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 600
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI 650
KTLKAGYSEK QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM 700
ENGALDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLAEMNY VHRDLAARNI 750
LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS SLGGKIPVRW TAPEAIAYRK 800
FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD YRLPPPMDCP 850
AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 900
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED 950
LLRIGITLAG HQKKILNSIH SMRVQISQSP TAMA 984
Length:984
Mass (Da):109,885
Last modified:October 1, 1996 - v1
Checksum:i8044160E24E93A92
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181M → V.1 Publication
Corresponds to variant rs55650774 [ dbSNP | Ensembl ].
VAR_042165
Natural varianti87 – 871T → S.
Corresponds to variant rs1042794 [ dbSNP | Ensembl ].
VAR_011801
Natural varianti152 – 1521G → R.
Corresponds to variant rs1042793 [ dbSNP | Ensembl ].
VAR_011802
Natural varianti367 – 3671R → G.
Corresponds to variant rs1042789 [ dbSNP | Ensembl ].
VAR_011803
Natural varianti387 – 3871T → M.1 Publication
Corresponds to variant rs56396912 [ dbSNP | Ensembl ].
VAR_042166
Natural varianti485 – 4851R → S.
Corresponds to variant rs1042788 [ dbSNP | Ensembl ].
VAR_011804
Natural varianti707 – 7071S → T in an ovarian undifferentiated carcinoma sample; somatic mutation. 1 Publication
VAR_042167
Natural varianti719 – 7191I → V in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042168
Natural varianti743 – 7431R → Q in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042169
Natural varianti847 – 8471M → T.
Corresponds to variant rs1042785 [ dbSNP | Ensembl ].
VAR_011805
Natural varianti912 – 9121A → T.1 Publication
Corresponds to variant rs56345346 [ dbSNP | Ensembl ].
VAR_042170
Natural varianti973 – 9731R → W.1 Publication
Corresponds to variant rs1042784 [ dbSNP | Ensembl ].
VAR_058479
Natural varianti981 – 9811T → M.1 Publication
Corresponds to variant rs56186270 [ dbSNP | Ensembl ].
VAR_042171

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → E in AAD02030. 1 Publication
Sequence conflicti12 – 121A → E in AAB94627. 1 Publication
Sequence conflicti12 – 121A → E in AAB94628. 1 Publication
Sequence conflicti185 – 1851S → I in AAD02030. 1 Publication
Sequence conflicti185 – 1851S → I in AAD02031. 1 Publication
Sequence conflicti185 – 1851S → I in AAB94627. 1 Publication
Sequence conflicti185 – 1851S → I in AAB94628. 1 Publication
Sequence conflicti274 – 2741T → R in AAD02030. 1 Publication
Sequence conflicti274 – 2741T → R in AAD02031. 1 Publication
Sequence conflicti274 – 2741T → R in AAB94627. 1 Publication
Sequence conflicti274 – 2741T → R in AAB94628. 1 Publication
Sequence conflicti336 – 3361T → S in AAD02030. 1 Publication
Sequence conflicti336 – 3361T → S in AAD02031. 1 Publication
Sequence conflicti336 – 3361T → S in AAB94627. 1 Publication
Sequence conflicti336 – 3361T → S in AAB94628. 1 Publication
Sequence conflicti752 – 7521V → L in AAI11745. 1 Publication
Sequence conflicti813 – 8131V → H in AAD02030. 1 Publication
Sequence conflicti813 – 8131V → H in AAB94627. 1 Publication
Sequence conflicti819 – 8191S → Y in AAD02030. 1 Publication
Sequence conflicti819 – 8191S → Y in AAB94627. 1 Publication
Sequence conflicti881 – 8811M → I in BAF83897. 1 Publication
Sequence conflicti903 – 9031L → H in BAF83897. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS46921.1.
RefSeqiNP_004432.1. NM_004441.4.
UniGeneiHs.116092.

Genome annotation databases

EnsembliENST00000398015; ENSP00000381097; ENSG00000154928.
GeneIDi2047.
KEGGihsa:2047.
UCSCiuc003eqt.3. human.

Polymorphism databases

DMDMi1706663.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS46921.1.
RefSeqi NP_004432.1. NM_004441.4.
UniGenei Hs.116092.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DJS NMR - A 434-528 [» ]
2EAO NMR - A 899-984 [» ]
3ZFX X-ray 2.50 A/B/C/D/E/F/G/H/I 602-896 [» ]
ProteinModelPortali P54762.
SMRi P54762. Positions 17-528, 592-984.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108361. 12 interactions.
IntActi P54762. 8 interactions.
MINTi MINT-1519362.
STRINGi 9606.ENSP00000381097.

Chemistry

BindingDBi P54762.
ChEMBLi CHEMBL2363043.
GuidetoPHARMACOLOGYi 1830.

PTM databases

PhosphoSitei P54762.

Polymorphism databases

DMDMi 1706663.

Proteomic databases

MaxQBi P54762.
PaxDbi P54762.
PRIDEi P54762.

Protocols and materials databases

DNASUi 2047.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398015 ; ENSP00000381097 ; ENSG00000154928 .
GeneIDi 2047.
KEGGi hsa:2047.
UCSCi uc003eqt.3. human.

Organism-specific databases

CTDi 2047.
GeneCardsi GC03P134316.
HGNCi HGNC:3392. EPHB1.
MIMi 600600. gene.
neXtProti NX_P54762.
PharmGKBi PA27824.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P54762.
KOi K05110.
OMAi TLMDTRT.
OrthoDBi EOG7VTDM6.
PhylomeDBi P54762.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P54762.

Miscellaneous databases

EvolutionaryTracei P54762.
GeneWikii EPH_receptor_B1.
GenomeRNAii 2047.
NextBioi 8321.
PMAP-CutDB P54762.
PROi P54762.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54762.
Bgeei P54762.
CleanExi HS_EPHB1.
Genevestigatori P54762.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProi IPR027936. 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 ]
Pfami PF14575. 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 ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS01186. 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.
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Publicationsi

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  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.
    , 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.
    , 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.
    , 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.

Entry informationi

Entry nameiEPHB1_HUMAN
AccessioniPrimary (citable) accession number: P54762
Secondary accession number(s): A8K593
, O43569, O95142, O95143, Q0VG87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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