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Protein

Ephrin type-B receptor 1

Gene

EPHB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. In addition to 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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei651 – 6511ATPCurated
Active sitei744 – 7441Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi625 – 6339ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • axon guidance Source: UniProtKB
  • camera-type eye morphogenesis Source: Ensembl
  • cell chemotaxis Source: UniProtKB
  • cell-substrate adhesion Source: UniProtKB
  • central nervous system projection neuron axonogenesis Source: UniProtKB
  • dendritic spine development Source: UniProtKB
  • dendritic spine morphogenesis Source: UniProtKB
  • detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
  • ephrin receptor signaling pathway Source: UniProtKB
  • establishment of cell polarity Source: UniProtKB
  • neural precursor cell proliferation Source: UniProtKB
  • neurogenesis Source: UniProtKB
  • optic nerve morphogenesis Source: Ensembl
  • positive regulation of synapse assembly Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of JNK cascade Source: UniProtKB
  • regulation of neuron death Source: UniProtKB
  • 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.
ReactomeiREACT_263952. EPHB-mediated forward signaling.
REACT_264047. Ephrin signaling.
REACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3392. EPHB1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 540523ExtracellularSequence AnalysisAdd
BLAST
Transmembranei541 – 56323HelicalSequence AnalysisAdd
BLAST
Topological domaini564 – 984421CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axon Source: Ensembl
  • cytosol Source: Reactome
  • dendrite Source: UniProtKB-SubCell
  • early endosome membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • integral component of plasma membrane Source: UniProtKB
  • membrane raft Source: Ensembl
  • plasma membrane Source: Reactome
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.

Polymorphism and mutation databases

BioMutaiEPHB1.
DMDMi1706663.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis
Modified residuei594 – 5941PhosphotyrosineBy similarity
Modified residuei600 – 6001PhosphotyrosineBy similarity
Modified residuei778 – 7781PhosphotyrosineBy similarity
Modified residuei928 – 9281Phosphotyrosine; by autocatalysisBy 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

BgeeiP54762.
CleanExiHS_EPHB1.
ExpressionAtlasiP54762. baseline and differential.
GenevisibleiP54762. HS.

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.By similarity7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108361. 13 interactions.
IntActiP54762. 8 interactions.
MINTiMINT-1519362.
STRINGi9606.ENSP00000381097.

Structurei

Secondary structure

1
984
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi441 – 4455Combined sources
Beta strandi447 – 4537Combined sources
Beta strandi464 – 47310Combined sources
Beta strandi482 – 49514Combined sources
Beta strandi501 – 51212Combined sources
Beta strandi514 – 5174Combined sources
Beta strandi521 – 5244Combined sources
Helixi616 – 6183Combined sources
Beta strandi619 – 6268Combined sources
Beta strandi633 – 6386Combined sources
Beta strandi646 – 6527Combined sources
Helixi659 – 67214Combined sources
Beta strandi683 – 6875Combined sources
Beta strandi689 – 6924Combined sources
Beta strandi694 – 6985Combined sources
Helixi705 – 7106Combined sources
Turni711 – 7144Combined sources
Helixi718 – 73720Combined sources
Helixi747 – 7493Combined sources
Beta strandi750 – 7523Combined sources
Beta strandi758 – 7603Combined sources
Helixi793 – 7986Combined sources
Helixi803 – 81816Combined sources
Turni824 – 8274Combined sources
Helixi830 – 8389Combined sources
Helixi851 – 86010Combined sources
Helixi865 – 8673Combined sources
Helixi871 – 88313Combined sources
Helixi885 – 8884Combined sources
Beta strandi889 – 8913Combined sources
Helixi916 – 9216Combined sources
Turni922 – 9243Combined sources
Helixi926 – 9283Combined sources
Helixi929 – 9357Combined sources
Helixi940 – 9434Combined sources
Helixi948 – 9547Combined sources
Helixi959 – 97517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 572-894, 900-984.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54762.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 201183Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini322 – 432111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini433 – 52896Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini619 – 882264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini911 – 97565SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi982 – 9843PDZ-bindingSequence Analysis

Compositional bias

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

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
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. FN3_dom.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P54762-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALDYLLLLL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE
60 70 80 90 100
NLNTIRTYQV CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP
110 120 130 140 150
NVPGSCKETF NLYYYETDSV IATKKSAFWS EAPYLKVDTI AADESFSQVD
160 170 180 190 200
FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY GACMSLLSVR VFFKKCPSIV
210 220 230 240 250
QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC NGDGEWMVPI
260 270 280 290 300
GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPAEASPI
310 320 330 340 350
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG
360 370 380 390 400
RDDVTYNIIC KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT
410 420 430 440 450
PYTFDIQAIN GVSSKSPFPP QHVSVNITTN QAAPSTVPIM HQVSATMRSI
460 470 480 490 500
TLSWPQPEQP NGIILDYEIR YYEKEHNEFN SSMARSQTNT ARIDGLRPGM
510 520 530 540 550
VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP LIAGSAAAGV
560 570 580 590 600
VFVVSLVAIS IVCSRKRAYS KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY
610 620 630 640 650
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI
660 670 680 690 700
KTLKAGYSEK QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM
710 720 730 740 750
ENGALDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLAEMNY VHRDLAARNI
760 770 780 790 800
LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS SLGGKIPVRW TAPEAIAYRK
810 820 830 840 850
FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD YRLPPPMDCP
860 870 880 890 900
AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ
910 920 930 940 950
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED
960 970 980
LLRIGITLAG HQKKILNSIH SMRVQISQSP TAMA
Length:984
Mass (Da):109,885
Last modified:October 1, 1996 - v1
Checksum:i8044160E24E93A92
GO
Isoform 2 (identifier: P54762-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-439: Missing.

Note: No experimental confirmation available.
Show »
Length:545
Mass (Da):61,401
Checksum:i2BC8548F9403B5C2
GO
Isoform 3 (identifier: P54762-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-242: VNTEVRSFGP...DVPIKLYCNG → LALQGHSRPA...LQGRQVGGMM
     243-984: Missing.

Show »
Length:242
Mass (Da):26,906
Checksum:iF89C739C1AB3F92E
GO

Sequence cautioni

The sequence AAB94627.1 differs from that shown.wrong intron-exon boundaries.Curated
The sequence AAB94628.1 differs from that shown.wrong intron-exon boundaries.Curated
The sequence AAD02031.1 differs from that shown.Chimeric cDNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → E in AAD02030 (PubMed:9430661).Curated
Sequence conflicti12 – 121A → E in AAB94627 (PubMed:9430661).Curated
Sequence conflicti12 – 121A → E in AAB94628 (PubMed:9430661).Curated
Sequence conflicti185 – 1851S → I in AAD02030 (PubMed:9430661).Curated
Sequence conflicti185 – 1851S → I in AAD02031 (PubMed:9430661).Curated
Sequence conflicti185 – 1851S → I in AAB94627 (PubMed:9430661).Curated
Sequence conflicti185 – 1851S → I in AAB94628 (PubMed:9430661).Curated
Sequence conflicti274 – 2741T → R in AAD02030 (PubMed:9430661).Curated
Sequence conflicti274 – 2741T → R in AAD02031 (PubMed:9430661).Curated
Sequence conflicti274 – 2741T → R in AAB94627 (PubMed:9430661).Curated
Sequence conflicti274 – 2741T → R in AAB94628 (PubMed:9430661).Curated
Sequence conflicti336 – 3361T → S in AAD02030 (PubMed:9430661).Curated
Sequence conflicti336 – 3361T → S in AAD02031 (PubMed:9430661).Curated
Sequence conflicti336 – 3361T → S in AAB94627 (PubMed:9430661).Curated
Sequence conflicti336 – 3361T → S in AAB94628 (PubMed:9430661).Curated
Sequence conflicti752 – 7521V → L in AAI11745 (PubMed:15489334).Curated
Sequence conflicti813 – 8131V → H in AAD02030 (PubMed:9430661).Curated
Sequence conflicti813 – 8131V → H in AAB94627 (PubMed:9430661).Curated
Sequence conflicti819 – 8191S → Y in AAD02030 (PubMed:9430661).Curated
Sequence conflicti819 – 8191S → Y in AAB94627 (PubMed:9430661).Curated
Sequence conflicti881 – 8811M → I in BAF83897 (PubMed:14702039).Curated
Sequence conflicti903 – 9031L → H in BAF83897 (PubMed:14702039).Curated

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 439439Missing in isoform 2. 1 PublicationVSP_056017Add
BLAST
Alternative sequencei158 – 24285VNTEV…LYCNG → LALQGHSRPARKLKAAPTAP PTAAPLQRRLPSAPVGPVIT ERTLTLQKWHALASHQVPAM LSPSSMRRPSFWSGTLQGRQ VGGMM in isoform 3. 1 PublicationVSP_056018Add
BLAST
Alternative sequencei243 – 984742Missing in isoform 3. 1 PublicationVSP_056019Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
EU826607 mRNA. Translation: ACF47643.1.
AK095305 mRNA. Translation: BAG53024.1.
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. [P54762-1]
RefSeqiNP_004432.1. NM_004441.4. [P54762-1]
UniGeneiHs.116092.

Genome annotation databases

EnsembliENST00000398015; ENSP00000381097; ENSG00000154928. [P54762-1]
ENST00000493838; ENSP00000419574; ENSG00000154928. [P54762-5]
GeneIDi2047.
KEGGihsa:2047.
UCSCiuc003eqt.3. human. [P54762-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
EU826607 mRNA. Translation: ACF47643.1.
AK095305 mRNA. Translation: BAG53024.1.
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. [P54762-1]
RefSeqiNP_004432.1. NM_004441.4. [P54762-1]
UniGeneiHs.116092.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 572-894, 900-984.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108361. 13 interactions.
IntActiP54762. 8 interactions.
MINTiMINT-1519362.
STRINGi9606.ENSP00000381097.

Chemistry

BindingDBiP54762.
ChEMBLiCHEMBL2363043.
GuidetoPHARMACOLOGYi1830.

PTM databases

PhosphoSiteiP54762.

Polymorphism and mutation databases

BioMutaiEPHB1.
DMDMi1706663.

Proteomic databases

MaxQBiP54762.
PaxDbiP54762.
PRIDEiP54762.

Protocols and materials databases

DNASUi2047.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398015; ENSP00000381097; ENSG00000154928. [P54762-1]
ENST00000493838; ENSP00000419574; ENSG00000154928. [P54762-5]
GeneIDi2047.
KEGGihsa:2047.
UCSCiuc003eqt.3. human. [P54762-1]

Organism-specific databases

CTDi2047.
GeneCardsiGC03P134316.
HGNCiHGNC:3392. EPHB1.
MIMi600600. gene.
neXtProtiNX_P54762.
PharmGKBiPA27824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54762.
KOiK05110.
OMAiTLMDTRT.
OrthoDBiEOG7VTDM6.
PhylomeDBiP54762.
TreeFamiTF315608.

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_263952. EPHB-mediated forward signaling.
REACT_264047. Ephrin signaling.
REACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54762.

Miscellaneous databases

ChiTaRSiEPHB1. human.
EvolutionaryTraceiP54762.
GeneWikiiEPH_receptor_B1.
GenomeRNAii2047.
NextBioi35469877.
PMAP-CutDBP54762.
PROiP54762.
SOURCEiSearch...

Gene expression databases

BgeeiP54762.
CleanExiHS_EPHB1.
ExpressionAtlasiP54762. baseline and differential.
GenevisibleiP54762. HS.

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. FN3_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    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] (ISOFORM 1), 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. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
    Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
    Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING.
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Tongue.
  5. "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].
  6. "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] (ISOFORM 1).
  7. "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.
  8. "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.
  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. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  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.
    , 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
, B3KTB2, B5A969, O43569, O95142, O95143, Q0VG87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 166 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.