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Q91571

- EPB1A_XENLA

UniProt

Q91571 - EPB1A_XENLA

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Protein

Ephrin type-B receptor 1-A

Gene

ephb1-a

Organism
Xenopus laevis (African clawed frog)
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. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei652 – 6521ATPPROSITE-ProRule annotation
Active sitei745 – 7451Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi626 – 6349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: UniProtKB
  2. cell chemotaxis Source: UniProtKB
  3. cell-substrate adhesion Source: UniProtKB
  4. dendritic spine development Source: UniProtKB
  5. dendritic spine morphogenesis Source: UniProtKB
  6. ephrin receptor signaling pathway Source: UniProtKB
  7. establishment of cell polarity Source: UniProtKB
  8. positive regulation of synapse assembly Source: UniProtKB
  9. protein autophosphorylation Source: UniProtKB
  10. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  11. regulation of JNK cascade 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. 6726.

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

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. early endosome membrane Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 985966Ephrin type-B receptor 1-APRO_0000016826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis

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.
SMRiQ91571. Positions 20-199, 438-529, 593-890, 901-985.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 542523ExtracellularSequence AnalysisAdd
BLAST
Topological domaini564 – 985422CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei543 – 56321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 203183Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini324 – 434111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini435 – 53298Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini620 – 883264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini912 – 97665SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi983 – 9853PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi185 – 321137Cys-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

HOVERGENiHBG062180.
KOiK05110.

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.
IPR011510. SAM_2.
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.
PF07647. SAM_2. 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.
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 [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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U14164 mRNA. Translation: AAA74888.1 .
PIRi I51672.
RefSeqi NP_001084070.1. NM_001090601.1.
UniGenei Xl.1028.

3D structure databases

ProteinModelPortali Q91571.
SMRi Q91571. Positions 20-199, 438-529, 593-890, 901-985.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 399288.
KEGGi xla:399288.

Organism-specific databases

CTDi 2047.
Xenbasei XB-GENE-865799. ephb1.

Phylogenomic databases

HOVERGENi HBG062180.
KOi K05110.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 6726.

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.
IPR011510. SAM_2.
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.
PF07647. SAM_2. 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.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Expression of an amphibian homolog of the Eph family of receptor tyrosine kinases is developmentally regulated."
    Jones T.L., Karavanova I., Maeno M., Ong R.C., Kung H.-F., Daar I.O.
    Oncogene 10:1111-1117(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells."
    Smith A., Robinson V., Patel K., Wilkinson D.G.
    Curr. Biol. 7:561-570(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TARGETED CELL MIGRATION.

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: October 29, 2014
This is version 124 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

External Data

Dasty 3