[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Fetal brain; DOI=10.1006/geno.1995.9985; PubMed=8666391 [NCBI, ExPASy, EBI, Israel, Japan] Tang X.X., Biegel J.A., Nycum L.M., Yoshioka A., Brodeur G.M., Pleasure D.E., Ikegaki N.; "cDNA cloning, molecular characterization, and chromosomal localization of NET(EPHT2), a human EPH-related receptor protein-tyrosine kinase gene preferentially expressed in brain."; Genomics 29:426-437(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). TISSUE=Kidney; Stein E., Schoecklmann H.O., Daniel T.O.; Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 18-32. DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Henzel W.J.; "Signal peptide prediction based on analysis of experimentally verified cleavage sites."; Protein Sci. 13:2819-2824(2004).
[4]	INTERACTION WITH GRB2 AND GRB10. DOI=10.1074/jbc.271.38.23588; PubMed=8798570 [NCBI, ExPASy, EBI, Israel, Japan] Stein E., Cerretti D.P., Daniel T.O.; "Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells."; J. Biol. Chem. 271:23588-23593(1996).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Anal. Sci. 24:161-166(2008).
[6]	STRUCTURE BY NMR OF 899-984. RIKEN structural genomics initiative (RSGI); "Solution structure of the C-terminal SAM-domain of mouse ephrin type-B receptor 1 precursor (EC 2.7.1.112)."; Submitted (JUL-2007) to the PDB data bank.
[7]	VARIANTS [LARGE SCALE ANALYSIS] VAL-18; MET-387; THR-707; VAL-719; GLN-743; THR-912 AND MET-981. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; "Patterns of somatic mutation in human cancer genomes."; Nature 446:153-158(2007).

Comments

FUNCTION: Receptor for members of the ephrin-B family. Binds to ephrin-B1, -B2 and -B3. May be involved in cell-cell interactions in the nervous system.
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SUBUNIT: The ligand-activated form interacts with GRB2, GRB10 and NCK through their respective SH2 domains. The GRB10 SH2 domain binds EPHB1 through Tyr-928, while GRB2 binds residues within the catalytic domain. The NCK SH2 domain binds EPHB1 through Tyr-594. Interacts with PRKCABP (By similarity).
INTERACTION:
Q13322:GRB10; NbExp=1; IntAct=EBI-80252, EBI-80275;
P62993:GRB2; NbExp=1; IntAct=EBI-80252, EBI-401755;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	EPHB1A
Isoform ID	P54762-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	EPH1B1B
Isoform ID	P54762-2
Features which should be applied to build the isoform sequence: VSP_003013.

Name	3
Synonyms	EPHB1C
Isoform ID	P54762-3
Features which should be applied to build the isoform sequence: VSP_003015.

Name	4
Synonyms	EPHB1D
Isoform ID	P54762-4
Features which should be applied to build the isoform sequence: VSP_003014.

TISSUE SPECIFICITY: Preferentially expressed in brain.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.
SIMILARITY: Contains 2 fibronectin type-III domains.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L40636; AAB08520.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF037331; AAD02030.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF037332; AAD02031.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF037333; AAB94627.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF037334; AAB94628.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_004432.1; -.

UniGene

Hs.116092

3D structure databases

PDB

2EAO; NMR; -; A=899-984.

[ExPASy / RCSB / EBI]

PDBsum

2EAO; -.

SMR

P54762; 18-197, 592-889.

ModBase

P54762.

Protein-protein interaction databases

IntAct

P54762; -.

PTM databases

PhosphoSite

P54762; -.

Organism-specific databases

H-InvDB

HIX0021414; -.
HIX0043235; -.

HGNC:3392; EPHB1.

600600; gene. [NCBI / EBI]

PharmGKB

PA27824; -.

GeneCards

P54762.

Gene expression databases

ArrayExpress

P54762; -.

CleanEx

HS_EPHB1; -.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004714;	Molecular function: transmembrane receptor protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0007399;	Biological process: nervous system development (traceable author statement from ProtInc).
GO:0007165;	Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR013032; EGF_like_reg_CS.
IPR001090; Eph_rcpt_lig_bd.
IPR008957; Fibronectin_typ-III-like_fold.
IPR003961; FN_III.
IPR003962; FnIII_subd.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR001660; SAM.
IPR013761; SAM_type.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
IPR016257; TyrPK_ephrin_receptor.
IPR001426; YKase_receptorV_CS.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.30; FN_III-like; 2.
G3DSA:1.10.150.50; SAM_type; 1.

Pfam

PF01404; Ephrin_lbd; 1.
PF00041; fn3; 2.
PF07714; Pkinase_Tyr; 1.
PF00536; SAM_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000666; TyrPK_ephrin_receptor; 1.

PRINTS

PR00014; FNTYPEIII.
PR00109; TYRKINASE.

ProDom

PD001495; Ephrin_receptor; 1.
PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00615; EPH_lbd; 1.
SM00060; FN3; 2.
SM00454; SAM; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS01186; EGF_2; UNKNOWN_1.
PS50853; FN3; 2.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PS50105; SAM_DOMAIN; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSG00000154928; Homo sapiens. [Contig view]

GeneID

2047; -.

KEGG

hsa:2047; -.

Phylogenomic databases

HOVERGEN

P54762; -.

Other

P54762; -.

8321; -.

EPHB1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; ATP-binding; Direct protein sequencing; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`
`CHAIN`	`18 984`	`967`	`Ephrin type-B receptor 1.`	`PRO_0000016824`
`TOPO_DOM`	`18 540`	`523`	`Extracellular (Potential).`
`TRANSMEM`	`541 563`	`23`	`Potential.`
`TOPO_DOM`	`564 984`	`421`	`Cytoplasmic (Potential).`
`DOMAIN`	`323 424`	`102`	`Fibronectin type-III 1.`
`DOMAIN`	`430 525`	`96`	`Fibronectin type-III 2.`
`DOMAIN`	`619 882`	`264`	`Protein kinase.`
`DOMAIN`	`911 975`	`65`	`SAM.`
`NP_BIND`	`625 633`	`9`	`ATP (By similarity).`
`MOTIF`	`982 984`	`3`	`PDZ-binding (Potential).`
`COMPBIAS`	`183 319`	`137`	`Cys-rich.`
`ACT_SITE`	`744 744`		`Proton acceptor (By similarity).`
`BINDING`	`651 651`		`ATP (By similarity).`
`MOD_RES`	`594 594`		`Phosphotyrosine; by autocatalysis.`
`MOD_RES`	`600 600`		`Phosphotyrosine; by autocatalysis (Potential).`
`MOD_RES`	`778 778`		`Phosphotyrosine; by autocatalysis (Potential).`
`MOD_RES`	`928 928`		`Phosphotyrosine; by autocatalysis.`
`MOD_RES`	`968 968`		`Phosphoserine.`
`CARBOHYD`	`334 334`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`426 426`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`480 480`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`1 27`		`MALDYLLLLLLASAVAAMEETLMDTRT -> METRERKKSRAEFGTR (in isoform 2).`	`VSP_003013`
`VAR_SEQ`	`617 984`		`Missing (in isoform 4).`	`VSP_003014`
`VAR_SEQ`	`642 682`		`Missing (in isoform 3).`	`VSP_003015`
`VARIANT`	`18 18`	`1`	`M -> V.`	`VAR_042165`
`VARIANT`	`87 87`	`1`	`T -> S (in dbSNP:rs1042794 [NCBI]).`	`VAR_011801`
`VARIANT`	`152 152`	`1`	`G -> R (in dbSNP:rs1042793 [NCBI]).`	`VAR_011802`
`VARIANT`	`367 367`	`1`	`R -> G (in dbSNP:rs1042789 [NCBI]).`	`VAR_011803`
`VARIANT`	`387 387`	`1`	`T -> M.`	`VAR_042166`
`VARIANT`	`485 485`	`1`	`R -> S (in dbSNP:rs1042788 [NCBI]).`	`VAR_011804`
`VARIANT`	`707 707`	`1`	`S -> T (in an ovarian undifferentiated carcinoma sample; somatic mutation).`	`VAR_042167 [3D]`
`VARIANT`	`719 719`	`1`	`I -> V (in a gastric adenocarcinoma sample; somatic mutation).`	`VAR_042168 [3D]`
`VARIANT`	`743 743`	`1`	`R -> Q (in a gastric adenocarcinoma sample; somatic mutation).`	`VAR_042169 [3D]`
`VARIANT`	`847 847`	`1`	`M -> T (in dbSNP:rs1042785 [NCBI]).`	`VAR_011805 [3D]`
`VARIANT`	`912 912`	`1`	`A -> T.`	`VAR_042170`
`VARIANT`	`981 981`	`1`	`T -> M.`	`VAR_042171`
`CONFLICT`	`12 12`		`A -> E (in Ref. 2; AAD02030/AAB94627/AAB94628).`
`CONFLICT`	`185 185`		`S -> I (in Ref. 2; AAD02030/AAD02031/AAB94627/AAB94628).`
`CONFLICT`	`274 274`		`T -> R (in Ref. 2; AAD02030/AAD02031/AAB94627/AAB94628).`
`CONFLICT`	`336 336`		`T -> S (in Ref. 2; AAD02030/AAD02031/AAB94627/AAB94628).`
`CONFLICT`	`813 813`		`V -> H (in Ref. 2; AAD02030/AAB94627).`
`CONFLICT`	`819 819`		`S -> Y (in Ref. 2; AAD02030/AAB94627).`
`CONFLICT`	`973 973`		`R -> W (in Ref. 2; AAD02030/AAD02031/AAB94627).`
`STRAND`	`441 445`	`5`
`STRAND`	`447 453`	`7`
`STRAND`	`464 473`	`10`
`STRAND`	`482 495`	`14`
`STRAND`	`501 512`	`12`
`STRAND`	`514 517`	`4`
`STRAND`	`521 524`	`4`
`HELIX`	`916 921`	`6`
`TURN`	`922 924`	`3`
`HELIX`	`926 928`	`3`
`HELIX`	`929 935`	`7`
`HELIX`	`940 943`	`4`
`HELIX`	`948 954`	`7`
`HELIX`	`959 975`	`17`

Sequence information

Length: 984 AA [This is the length of the unprocessed precursor]

Molecular weight: 109885 Da [This is the MW of the unprocessed precursor]

CRC64: 8044160E24E93A92 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALDYLLLLL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV 

        70         80         90        100        110        120 
CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV 

       130        140        150        160        170        180 
IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY 

       190        200        210        220        230        240 
GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC 

       250        260        270        280        290        300 
NGDGEWMVPI GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPAEASPI 

       310        320        330        340        350        360 
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC 

       370        380        390        400        410        420 
KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP 

       430        440        450        460        470        480 
QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN 

       490        500        510        520        530        540 
SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP 

       550        560        570        580        590        600 
LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 

       610        620        630        640        650        660 
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK 

       670        680        690        700        710        720 
QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ 

       730        740        750        760        770        780 
LVGMLRGIAA GMKYLAEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS 

       790        800        810        820        830        840 
SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD 

       850        860        870        880        890        900 
YRLPPPMDCP AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 

       910        920        930        940        950        960 
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED LLRIGITLAG 

       970        980 
HQKKILNSIH SMRVQISQSP TAMA

P54762 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools