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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)DescriptionActionsGraphical viewLength
Binding sitei651ATPCurated1
Active sitei744Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi625 – 633ATPPROSITE-ProRule annotation9

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
  • immunological synapse formation Source: Ensembl
  • 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

BioCyciZFISH:HS14544-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54762.
SIGNORiP54762.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Topological domaini18 – 540ExtracellularSequence analysisAdd BLAST523
Transmembranei541 – 563HelicalSequence analysisAdd BLAST23
Topological domaini564 – 984CytoplasmicSequence analysisAdd BLAST421

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
  • filopodium tip Source: Ensembl
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi594Y → F: Loss of interaction with NCK1. 1 Publication1
Mutagenesisi600Y → F: Loss of interaction with SHC1 and SRC. 1 Publication1
Mutagenesisi651K → 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 Publications1
Mutagenesisi778Y → F: Loss of interaction with SHC1. 1 Publication1
Mutagenesisi928Y → F: Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation. Disrupts interaction with GRB7 and ACP1. 3 Publications1

Organism-specific databases

DisGeNETi2047.
OpenTargetsiENSG00000154928.
PharmGKBiPA27824.

Chemistry databases

ChEMBLiCHEMBL5072.
GuidetoPHARMACOLOGYi1830.

Polymorphism and mutation databases

BioMutaiEPHB1.
DMDMi1706663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000001682418 – 984Ephrin type-B receptor 1Add BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Glycosylationi426N-linked (GlcNAc...)Sequence analysis1
Glycosylationi480N-linked (GlcNAc...)Sequence analysis1
Modified residuei600PhosphotyrosineBy similarity1
Modified residuei928Phosphotyrosine; by autocatalysisBy similarity1

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

EPDiP54762.
MaxQBiP54762.
PaxDbiP54762.
PeptideAtlasiP54762.
PRIDEiP54762.

PTM databases

iPTMnetiP54762.
PhosphoSitePlusiP54762.

Miscellaneous databases

PMAP-CutDBP54762.

Expressioni

Tissue specificityi

Preferentially expressed in brain.

Gene expression databases

BgeeiENSG00000154928.
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 interactors.
IntActiP54762. 8 interactors.
MINTiMINT-1519362.
STRINGi9606.ENSP00000381097.

Chemistry databases

BindingDBiP54762.

Structurei

Secondary structure

1984
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi441 – 445Combined sources5
Beta strandi447 – 453Combined sources7
Beta strandi464 – 473Combined sources10
Beta strandi482 – 495Combined sources14
Beta strandi501 – 512Combined sources12
Beta strandi514 – 517Combined sources4
Beta strandi521 – 524Combined sources4
Helixi616 – 618Combined sources3
Beta strandi619 – 626Combined sources8
Beta strandi633 – 638Combined sources6
Beta strandi646 – 652Combined sources7
Helixi659 – 672Combined sources14
Beta strandi683 – 687Combined sources5
Beta strandi689 – 692Combined sources4
Beta strandi694 – 698Combined sources5
Helixi705 – 710Combined sources6
Turni711 – 714Combined sources4
Helixi718 – 737Combined sources20
Helixi747 – 749Combined sources3
Beta strandi750 – 752Combined sources3
Beta strandi758 – 760Combined sources3
Helixi793 – 798Combined sources6
Helixi803 – 818Combined sources16
Turni824 – 827Combined sources4
Helixi830 – 838Combined sources9
Helixi851 – 860Combined sources10
Helixi865 – 867Combined sources3
Helixi871 – 883Combined sources13
Helixi885 – 888Combined sources4
Beta strandi889 – 891Combined sources3
Helixi916 – 921Combined sources6
Turni922 – 924Combined sources3
Helixi926 – 928Combined sources3
Helixi929 – 935Combined sources7
Helixi940 – 943Combined sources4
Helixi948 – 954Combined sources7
Helixi959 – 975Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJSNMR-A434-528[»]
2EAONMR-A899-984[»]
3ZFXX-ray2.50A/B/C/D/E/F/G/H/I602-896[»]
ProteinModelPortaliP54762.
SMRiP54762.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54762.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 201Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini322 – 432Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini433 – 528Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini619 – 882Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini911 – 975SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi982 – 984PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi183 – 319Cys-richAdd BLAST137

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

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54762.
KOiK05110.
OMAiKDHAEIN.
OrthoDBiEOG091G00W0.
PhylomeDBiP54762.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
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.
SM01411. Ephrin_rec_like. 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 differs from that shown. wrong intron-exon boundaries.Curated
The sequence AAB94628 differs from that shown. wrong intron-exon boundaries.Curated
The sequence AAD02031 differs from that shown. Chimeric cDNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12A → E in AAD02030 (PubMed:9430661).Curated1
Sequence conflicti12A → E in AAB94627 (PubMed:9430661).Curated1
Sequence conflicti12A → E in AAB94628 (PubMed:9430661).Curated1
Sequence conflicti185S → I in AAD02030 (PubMed:9430661).Curated1
Sequence conflicti185S → I in AAD02031 (PubMed:9430661).Curated1
Sequence conflicti185S → I in AAB94627 (PubMed:9430661).Curated1
Sequence conflicti185S → I in AAB94628 (PubMed:9430661).Curated1
Sequence conflicti274T → R in AAD02030 (PubMed:9430661).Curated1
Sequence conflicti274T → R in AAD02031 (PubMed:9430661).Curated1
Sequence conflicti274T → R in AAB94627 (PubMed:9430661).Curated1
Sequence conflicti274T → R in AAB94628 (PubMed:9430661).Curated1
Sequence conflicti336T → S in AAD02030 (PubMed:9430661).Curated1
Sequence conflicti336T → S in AAD02031 (PubMed:9430661).Curated1
Sequence conflicti336T → S in AAB94627 (PubMed:9430661).Curated1
Sequence conflicti336T → S in AAB94628 (PubMed:9430661).Curated1
Sequence conflicti752V → L in AAI11745 (PubMed:15489334).Curated1
Sequence conflicti813V → H in AAD02030 (PubMed:9430661).Curated1
Sequence conflicti813V → H in AAB94627 (PubMed:9430661).Curated1
Sequence conflicti819S → Y in AAD02030 (PubMed:9430661).Curated1
Sequence conflicti819S → Y in AAB94627 (PubMed:9430661).Curated1
Sequence conflicti881M → I in BAF83897 (PubMed:14702039).Curated1
Sequence conflicti903L → H in BAF83897 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04216518M → V.1 PublicationCorresponds to variant rs55650774dbSNPEnsembl.1
Natural variantiVAR_01180187T → S.Corresponds to variant rs1042794dbSNPEnsembl.1
Natural variantiVAR_011802152G → R.Corresponds to variant rs1042793dbSNPEnsembl.1
Natural variantiVAR_011803367R → G.Corresponds to variant rs1042789dbSNPEnsembl.1
Natural variantiVAR_042166387T → M.1 PublicationCorresponds to variant rs56396912dbSNPEnsembl.1
Natural variantiVAR_011804485R → S.Corresponds to variant rs1042788dbSNPEnsembl.1
Natural variantiVAR_042167707S → T in an ovarian undifferentiated carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042168719I → V in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042169743R → Q in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_011805847M → T.Corresponds to variant rs1042785dbSNPEnsembl.1
Natural variantiVAR_042170912A → T.1 PublicationCorresponds to variant rs56345346dbSNPEnsembl.1
Natural variantiVAR_058479973R → W.1 PublicationCorresponds to variant rs1042784dbSNPEnsembl.1
Natural variantiVAR_042171981T → M.1 PublicationCorresponds to variant rs56186270dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0560171 – 439Missing in isoform 2. 1 PublicationAdd BLAST439
Alternative sequenceiVSP_056018158 – 242VNTEV…LYCNG → LALQGHSRPARKLKAAPTAP PTAAPLQRRLPSAPVGPVIT ERTLTLQKWHALASHQVPAM LSPSSMRRPSFWSGTLQGRQ VGGMM in isoform 3. 1 PublicationAdd BLAST85
Alternative sequenceiVSP_056019243 – 984Missing in isoform 3. 1 PublicationAdd BLAST742

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.4. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DJSNMR-A434-528[»]
2EAONMR-A899-984[»]
3ZFXX-ray2.50A/B/C/D/E/F/G/H/I602-896[»]
ProteinModelPortaliP54762.
SMRiP54762.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP54762.
ChEMBLiCHEMBL5072.
GuidetoPHARMACOLOGYi1830.

PTM databases

iPTMnetiP54762.
PhosphoSitePlusiP54762.

Polymorphism and mutation databases

BioMutaiEPHB1.
DMDMi1706663.

Proteomic databases

EPDiP54762.
MaxQBiP54762.
PaxDbiP54762.
PeptideAtlasiP54762.
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.4. human. [P54762-1]

Organism-specific databases

CTDi2047.
DisGeNETi2047.
GeneCardsiEPHB1.
HGNCiHGNC:3392. EPHB1.
MIMi600600. gene.
neXtProtiNX_P54762.
OpenTargetsiENSG00000154928.
PharmGKBiPA27824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54762.
KOiK05110.
OMAiKDHAEIN.
OrthoDBiEOG091G00W0.
PhylomeDBiP54762.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS14544-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54762.
SIGNORiP54762.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000154928.
CleanExiHS_EPHB1.
ExpressionAtlasiP54762. baseline and differential.
GenevisibleiP54762. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
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.
SM01411. Ephrin_rec_like. 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...

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: November 30, 2016
This is version 180 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

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 one 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.