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Protein

Ephrin type-B receptor 1-B

Gene

ephb1-b

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 (By similarity).By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei569ATPPROSITE-ProRule annotation1
Active sitei662Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi543 – 551ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processCell adhesion, Neurogenesis
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

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

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini‹1 – 459ExtracellularSequence analysisAdd BLAST›459
Transmembranei460 – 480HelicalSequence analysisAdd BLAST21
Topological domaini481 – 902CytoplasmicSequence analysisAdd BLAST422

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000160275‹1 – 902Ephrin type-B receptor 1-BAdd BLAST›902

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi252N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi344N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi398N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ91736.

Expressioni

Tissue specificityi

Expressed in the embryo in the brain and spinal cord and in the first and fourth visceral arches. Most abundant in adult brain, with lower levels in eye, heart, ovary, oviduct, lung and pharynx.

Developmental stagei

Expressed during early 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

ProteinModelPortaliQ91736.
SMRiQ91736.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 119Eph LBDPROSITE-ProRule annotationAdd BLAST119
Domaini240 – 350Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini351 – 448Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST98
Domaini537 – 800Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini829 – 893SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi900 – 902PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi101 – 237Cys-richAdd BLAST137

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG062180.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiView protein in InterPro
IPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR036116. FN3_sf.
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.
PfamiView protein in Pfam
PF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiView protein in SMART
SM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiView protein in PROSITE
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.

Sequencei

Sequence statusi: Fragment.

Q91736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
HRVYVEMRFT VRDCSSLPNV PGSCKETFNL YYYETDSNID NKISTFWNES
60 70 80 90 100
PYLKVDTIAA DESFSQVDFG GRLMKVNTEV RSFGPLTRSG FYLAFQDYGA
110 120 130 140 150
CMSLLSVRVF FKKCPSVVQN FAVFPETMTG AESTSLVIAR GTCIPNAEEV
160 170 180 190 200
DVPIKLYCNG DGEWMVPIGK CTCKAGYEPE NHVVCKACPA AMFKANQGMG
210 220 230 240 250
ICAQCPANSR STSEASPICI CRNGYYRADF DTPEAPCTSV PSGPRNVISI
260 270 280 290 300
VNETAITLEW HPPRETGGRD DVNYNIICKK CQSDRRGCSH CDDNVDFVPR
310 320 330 340 350
QLGLTDTRVF ISNLWVHTPY TFEIQAVNGV TNKSPFPPQH VSVNITTNQA
360 370 380 390 400
APSSVPIMHQ VKATMKSITL SWPQPEQPNG IILDYEIRYY EKDHHEFNSS
410 420 430 440 450
LARSQTNTAS IEGLRPGVVY VVQVRARTVA GYGKFSSKMC FQTLTEEDYK
460 470 480 490 500
SELREQLPLI AGSAAAGVVF IVSLVAISIV CSRKRTYSKE AVYSDKLQHY
510 520 530 540 550
STGRGSPGMK IYIDPFTYED PNEAVREFAK EIDVSFVKIE EVIGAGEFGE
560 570 580 590 600
VYKGRLKLPS KREISVAIKT LKAGYSEKQR RDFLSEASIM GQFDHPNIIR
610 620 630 640 650
LEGVVTKSRP VMIITEFMEN GALDSFLRQN DGQFTVIQLV GMLRGIAAGM
660 670 680 690 700
KYLSEMNYVH RDLAARNILV NSNLVCKVSD FGLSRYLQDD TSDPTYTSSL
710 720 730 740 750
GGKIPVRWTA PEAIRYRKFT SASDVWSYGI VMWEVMSYGE RPYWDMSNQD
760 770 780 790 800
VINAIEQDYR LPPPMDCPAA LHQLMLDCWQ KDRNSRPRFG EIVNTLDKMI
810 820 830 840 850
RNPASLKTVA TIPAVPSQPL LDRSIPDISA FTSVDDWLSA IKMGQYRDNF
860 870 880 890 900
LSSGFTSLHV VAQMTSEDLL RIGITLAGHQ KKILNSIQSM RVQISQSPTS

IA
Length:902
Mass (Da):100,851
Last modified:November 1, 1996 - v1
Checksum:iCCB9ABF7D39273CA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43621 mRNA. Translation: AAA93527.1.
UniGeneiXl.1028.

Similar proteinsi

Entry informationi

Entry nameiEPB1B_XENLA
AccessioniPrimary (citable) accession number: Q91736
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: October 25, 2017
This is version 133 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families