Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8CBF3

- EPHB1_MOUSE

UniProt

Q8CBF3 - EPHB1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ephrin type-B receptor 1

Gene

Ephb1

Organism
Mus musculus (Mouse)
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. 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.4 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 – 6511ATPPROSITE-ProRule annotation
Active sitei744 – 7441Proton acceptorPROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. axon guidance receptor activity Source: MGI
  3. transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. axon guidance Source: MGI
  3. camera-type eye morphogenesis Source: MGI
  4. cell chemotaxis Source: UniProtKB
  5. cell-substrate adhesion Source: UniProtKB
  6. central nervous system projection neuron axonogenesis Source: MGI
  7. cranial nerve development Source: MGI
  8. dendritic spine development Source: UniProtKB
  9. dendritic spine morphogenesis Source: UniProtKB
  10. detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
  11. ephrin receptor signaling pathway Source: UniProtKB
  12. establishment of cell polarity Source: UniProtKB
  13. neural precursor cell proliferation Source: UniProtKB
  14. neurogenesis Source: UniProtKB
  15. optic nerve morphogenesis Source: MGI
  16. positive regulation of synapse assembly Source: UniProtKB
  17. protein autophosphorylation Source: UniProtKB
  18. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  19. regulation of JNK cascade Source: UniProtKB
  20. retinal ganglion cell axon guidance Source: MGI
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

ReactomeiREACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 1 (EC:2.7.10.1)
Gene namesi
Name:Ephb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1096337. Ephb1.

Subcellular locationi

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

Topology

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

GO - Cellular componenti

  1. axon Source: MGI
  2. cytoplasm Source: MGI
  3. early endosome membrane Source: UniProtKB
  4. extracellular vesicular exosome Source: Ensembl
  5. integral component of plasma membrane Source: UniProtKB
  6. membrane Source: MGI
  7. membrane raft Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice development is apparently normal. However, they display a dramatic reduction of ipsilateral retinal projection. Mice do not develop neuropathic algesia and physical dependence to morphine.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 984967Ephrin type-B receptor 1PRO_0000260317Add
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 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 (By similarity).By similarity
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

MaxQBiQ8CBF3.
PaxDbiQ8CBF3.
PRIDEiQ8CBF3.

PTM databases

PhosphoSiteiQ8CBF3.

Expressioni

Tissue specificityi

Expressed in neural stem and progenitor cells in the dentate gyrus.1 Publication

Developmental stagei

Expressed in growth cones of ventrotemporal (uncrossed) retinal ganglion cells that give rise to ipsilateral projections (at protein level).2 Publications

Gene expression databases

BgeeiQ8CBF3.
CleanExiMM_EPHB1.
ExpressionAtlasiQ8CBF3. baseline and differential.
GenevestigatoriQ8CBF3.

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 (By similarity). Interacts with PICK1. Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion. 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 similarity5 Publications

Protein-protein interaction databases

BioGridi234781. 3 interactions.
IntActiQ8CBF3. 1 interaction.
STRINGi10090.ENSMUSP00000035129.

Structurei

3D structure databases

ProteinModelPortaliQ8CBF3.
SMRiQ8CBF3. Positions 17-528, 611-984.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ8CBF3.
KOiK05110.
OMAiTLMDTRT.
OrthoDBiEOG7VTDM6.
PhylomeDBiQ8CBF3.
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. 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.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CBF3-1) [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
MALDCLLLFL 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 SRSPSEASPI
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 KEAAYSDKLQ 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 GMKYLSEMNY 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
LLRIGVTLAG HQKKILSSIH SMRVQMNQSP SVMA
Length:984
Mass (Da):109,881
Last modified:March 1, 2003 - v1
Checksum:iE967019C82AA400A
GO
Isoform 2 (identifier: Q8CBF3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     588-628: Missing.

Show »
Length:943
Mass (Da):105,294
Checksum:iEF28BF1D7FE097C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721L → Q in BAE22386. (PubMed:16141072)Curated
Sequence conflicti187 – 1871L → P in BAE22386. (PubMed:16141072)Curated
Sequence conflicti194 – 1941K → I in AAH57301. (PubMed:15489334)Curated
Sequence conflicti641 – 6411P → Q in BAC29348. (PubMed:16141072)Curated
Sequence conflicti678 – 6781P → R in AAH57301. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei588 – 62841Missing in isoform 2. 1 PublicationVSP_021595Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036148 mRNA. Translation: BAC29320.1.
AK036211 mRNA. Translation: BAC29348.1.
AK135018 mRNA. Translation: BAE22386.1.
CT025594
, AC109247, AC132684, AC156635 Genomic DNA. Translation: CAM23741.1.
BC057301 mRNA. Translation: AAH57301.1.
CCDSiCCDS40742.1. [Q8CBF3-1]
CCDS52901.1. [Q8CBF3-2]
RefSeqiNP_001161768.1. NM_001168296.1. [Q8CBF3-2]
NP_775623.3. NM_173447.3. [Q8CBF3-1]
UniGeneiMm.22897.

Genome annotation databases

EnsembliENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537. [Q8CBF3-1]
ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537. [Q8CBF3-2]
GeneIDi270190.
KEGGimmu:270190.
UCSCiuc009rfn.2. mouse. [Q8CBF3-1]
uc012gzg.1. mouse. [Q8CBF3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036148 mRNA. Translation: BAC29320.1 .
AK036211 mRNA. Translation: BAC29348.1 .
AK135018 mRNA. Translation: BAE22386.1 .
CT025594
, AC109247 , AC132684 , AC156635 Genomic DNA. Translation: CAM23741.1 .
BC057301 mRNA. Translation: AAH57301.1 .
CCDSi CCDS40742.1. [Q8CBF3-1 ]
CCDS52901.1. [Q8CBF3-2 ]
RefSeqi NP_001161768.1. NM_001168296.1. [Q8CBF3-2 ]
NP_775623.3. NM_173447.3. [Q8CBF3-1 ]
UniGenei Mm.22897.

3D structure databases

ProteinModelPortali Q8CBF3.
SMRi Q8CBF3. Positions 17-528, 611-984.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 234781. 3 interactions.
IntActi Q8CBF3. 1 interaction.
STRINGi 10090.ENSMUSP00000035129.

PTM databases

PhosphoSitei Q8CBF3.

Proteomic databases

MaxQBi Q8CBF3.
PaxDbi Q8CBF3.
PRIDEi Q8CBF3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035129 ; ENSMUSP00000035129 ; ENSMUSG00000032537 . [Q8CBF3-1 ]
ENSMUST00000085169 ; ENSMUSP00000082261 ; ENSMUSG00000032537 . [Q8CBF3-2 ]
GeneIDi 270190.
KEGGi mmu:270190.
UCSCi uc009rfn.2. mouse. [Q8CBF3-1 ]
uc012gzg.1. mouse. [Q8CBF3-2 ]

Organism-specific databases

CTDi 2047.
MGIi MGI:1096337. Ephb1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi Q8CBF3.
KOi K05110.
OMAi TLMDTRT.
OrthoDBi EOG7VTDM6.
PhylomeDBi Q8CBF3.
TreeFami TF315608.

Enzyme and pathway databases

Reactomei REACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.

Miscellaneous databases

ChiTaRSi Ephb1. mouse.
NextBioi 393293.
PROi Q8CBF3.
SOURCEi Search...

Gene expression databases

Bgeei Q8CBF3.
CleanExi MM_EPHB1.
ExpressionAtlasi Q8CBF3. baseline and differential.
Genevestigatori Q8CBF3.

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.
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 ]
Pfami PF14575. 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 ]
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.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Olfactory bulb.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "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: INTERACTION WITH NCK1.
    Tissue: Kidney.
  5. "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands."
    Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.
    Neuron 21:1453-1463(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PICK1.
  6. "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.
  7. "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: INTERACTION WITH GRB2; SHC1 AND SRC.
  8. "Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus."
    Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.
    J. Cell Biol. 163:1313-1326(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY SYNAPSE FORMATION, SUBCELLULAR LOCATION.
  9. "Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm."
    Williams S.E., Mann F., Erskine L., Sakurai T., Wei S., Rossi D.J., Gale N.W., Holt C.E., Mason C.A., Henkemeyer M.
    Neuron 39:919-935(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN RETINAL GLANGLION CELL AXON GUIDANCE, DEVELOPMENTAL STAGE.
  10. "EphB receptors regulate stem/progenitor cell proliferation, migration, and polarity during hippocampal neurogenesis."
    Chumley M.J., Catchpole T., Silvany R.E., Kernie S.G., Henkemeyer M.
    J. Neurosci. 27:13481-13490(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEUROGENESIS, IDENTIFICATION OF EFNB3 AS LIGAND, TISSUE SPECIFICITY.
  11. "Zic2 regulates retinal ganglion cell axon avoidance of ephrinB2 through inducing expression of the guidance receptor EphB1."
    Lee R., Petros T.J., Mason C.A.
    J. Neurosci. 28:5910-5919(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  12. "Targeted mutation of EphB1 receptor prevents development of neuropathic hyperalgesia and physical dependence on morphine in mice."
    Han Y., Song X.S., Liu W.T., Henkemeyer M., Song X.J.
    Mol. Pain 4:60-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "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: UBIQUITINATION BY CBL, INTERACTION WITH CBL.

Entry informationi

Entry nameiEPHB1_MOUSE
AccessioniPrimary (citable) accession number: Q8CBF3
Secondary accession number(s): B1B1C2
, Q3UY27, Q6PG23, Q8CBE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3