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Protein

Ephrin type-B receptor 1-A

Gene

ephb1-a

Organism
Xenopus laevis (African clawed frog)
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. May play a role in axon guidance during nervous system development. May also play an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. More generally, may play a role in targeted cell migration and adhesion. Upon activation by ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei652ATPPROSITE-ProRule annotation1
Active sitei745Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi626 – 634ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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. 6725.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 1-A (EC:2.7.10.1)
Alternative name(s):
Tyrosine-protein kinase receptor XEK
Gene namesi
Name:ephb1-a
Synonyms:xek
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865799. ephb1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 542ExtracellularSequence analysisAdd BLAST523
Transmembranei543 – 563HelicalSequence analysisAdd BLAST21
Topological domaini564 – 985CytoplasmicSequence analysisAdd BLAST422

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001682620 – 985Ephrin type-B receptor 1-AAdd BLAST966

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi428N-linked (GlcNAc...)Sequence analysis1
Glycosylationi482N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Phosphorylated. Autophosphorylation is stimulated by ligands (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Expressioni

Developmental stagei

Maternally expressed, it decreases at mid blastula transition and reappears at late neurulation. Expressed at higher levels in the anterior and dorsal regions of embryonic stages 16, 24 and 37. In adult it appears to be ubiquitously expressed with higher expression in brain and ovary. Expression in the brain, brachial arches, trigeminal facial ganglion, and the retina of swimming tadpole stage of development.

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ91571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 203Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini324 – 434Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini435 – 532Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST98
Domaini620 – 883Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini912 – 976SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi983 – 985PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi185 – 321Cys-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

HOVERGENiHBG062180.
KOiK05110.

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. 1 hit.
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.
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.

Q91571-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELNVLLLLL CLSGGQVGAV EETLMDTRTA TAELGWTANP SSGWEEVSGY
60 70 80 90 100
DENLNTIRTY QVCNVFGPKQ NNWLLTTFIP RRGAHRVYVE MRFTVRDCSS
110 120 130 140 150
LPNVPGSCKE TFNLYYYETD SNIENKISTF WNESPYLKVD TIAADESFSQ
160 170 180 190 200
VDFGGRLMKV NTEVRSFGPL TRSGFYLAFQ DYGACMSLLS VRVFFKEMPS
210 220 230 240 250
VVQNLLVFPE TMTGAESTSL VIARGTCIPN AEEVDVPIKL YCNGDGEWMV
260 270 280 290 300
PIGKCTCKAG YEPENHVVCK ACPAAMFKAN QGMGICAQCP ANSRSTSEAS
310 320 330 340 350
PICICRNGYY RADFDTPEAP CTSVPSGPRN VISIVNETAI TLEWHPPRET
360 370 380 390 400
GGRDDVDYNI VCKKCRADRR ACSRCDDNVD FVPRQLGLTD TRVFISNLWA
410 420 430 440 450
HTPYTFETQA VNGVTNKSPF PPQHVSVNIT TNQAAPSSVP IMHQVKATMK
460 470 480 490 500
SITLSWPQQE QPNGIILDYE IRYYEKDHHE FNSSLARSQT NTARRTGGRV
510 520 530 540 550
WMFMSVQVRA RTVAGYGKFS SKCGFQTLTA EDYKSELREQ LPLTGSAAAG
560 570 580 590 600
VVFIVSLVAI SIVCSRKRTY SKEAVYSDKL QHYSTGRGSP GMKIYIDPFT
610 620 630 640 650
YEDPNEAVRE FAKEIDVSFV KIEEVIGAGE FGEVYKGRLK LPSKREISVA
660 670 680 690 700
IKTLKAGYSE KQRRDFLSEA SIMGQFDHPN IIRLEGVVTK SRPVMIITEF
710 720 730 740 750
MENGALDSFL RQNDGQFTVI QLVGMLRGIA AGMKYLSEMN YVHRDLAARN
760 770 780 790 800
ILVNSNLVCK VSDFGLSRYL QDDTSDPTYT SSLGGKIPVR WTAQEAIAYR
810 820 830 840 850
KFTSASDVWS YGIVMWEVMS YGERPYWTMS NQDVINAIEQ DYRLPPPMDC
860 870 880 890 900
PAALHQLMLD CWQKDRNSRP RLAEIVNTLR PMIRNPASLK TVATIPAVPS
910 920 930 940 950
QPLLDRSIPD ISAFTSVDDW LSAIKMGQYR DNFLSSGFTS LQLVAQMTSE
960 970 980
DLLRIGITLA GHQKKILNSI QSMRVQITQS PTSIA
Length:985
Mass (Da):110,104
Last modified:November 1, 1996 - v1
Checksum:iBE72CD1BFF51E623
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14164 mRNA. Translation: AAA74888.1.
PIRiI51672.
RefSeqiNP_001084070.1. NM_001090601.1.
UniGeneiXl.1028.

Genome annotation databases

GeneIDi399288.
KEGGixla:399288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14164 mRNA. Translation: AAA74888.1.
PIRiI51672.
RefSeqiNP_001084070.1. NM_001090601.1.
UniGeneiXl.1028.

3D structure databases

ProteinModelPortaliQ91571.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399288.
KEGGixla:399288.

Organism-specific databases

CTDi2047.
XenbaseiXB-GENE-865799. ephb1.

Phylogenomic databases

HOVERGENiHBG062180.
KOiK05110.

Enzyme and pathway databases

BRENDAi2.7.10.1. 6725.

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. 1 hit.
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.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEPB1A_XENLA
AccessioniPrimary (citable) accession number: Q91571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.