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P54760

- EPHB4_HUMAN

UniProt

P54760 - EPHB4_HUMAN

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Protein

Ephrin type-B receptor 4

Gene

EPHB4

Organism
Homo sapiens (Human)
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. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis.2 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 sitei647 – 6471ATPPROSITE-ProRule annotation
Active sitei740 – 7401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi621 – 6299ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor activity Source: UniProtKB
  3. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. cell adhesion Source: UniProtKB
  3. cell migration involved in sprouting angiogenesis Source: UniProtKB
  4. ephrin receptor signaling pathway Source: UniProtKB
  5. heart morphogenesis Source: UniProtKB
  6. peptidyl-tyrosine phosphorylation Source: GOC
  7. protein autophosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_228085. EPHB-mediated forward signaling.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.
SignaLinkiP54760.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 4 (EC:2.7.10.1)
Alternative name(s):
Hepatoma transmembrane kinase
Tyrosine-protein kinase TYRO11
Gene namesi
Name:EPHB4
Synonyms:HTK, MYK1, TYRO11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:3395. EPHB4.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 539524ExtracellularSequence AnalysisAdd
BLAST
Transmembranei540 – 56021HelicalSequence AnalysisAdd
BLAST
Topological domaini561 – 987427CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951L → R: Reduces binding affinity for EFNB2. 1 Publication

Organism-specific databases

PharmGKBiPA27827.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 987972Ephrin type-B receptor 4PRO_0000016834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 ↔ 184
Disulfide bondi97 ↔ 107
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
Modified residuei911 – 9111Phosphoserine2 Publications
Modified residuei976 – 9761Phosphothreonine3 Publications
Modified residuei987 – 9871Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated; autophosphorylation is stimulated by EFNB2.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP54760.
PaxDbiP54760.
PRIDEiP54760.

2D gel databases

DOSAC-COBS-2DPAGEP54760.

PTM databases

PhosphoSiteiP54760.

Expressioni

Tissue specificityi

Abundantly expressed in placenta but also detected in kidney, liver, lung, pancreas, skeletal muscle and heart. Expressed in primitive and myeloid, but not lymphoid, hematopoietic cells. Also observed in cell lines derived from liver, breast, colon, lung, melanocyte and cervix.1 Publication

Developmental stagei

Expressed in fetal heart, lung, liver and to a lower extent in brain. Not expressed in adult brain.1 Publication

Gene expression databases

BgeeiP54760.
CleanExiHS_EPHB4.
ExpressionAtlasiP54760. baseline and differential.
GenevestigatoriP54760.

Organism-specific databases

HPAiCAB013537.

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

Protein-protein interaction databases

BioGridi108364. 8 interactions.
IntActiP54760. 3 interactions.
STRINGi9606.ENSP00000350896.

Structurei

Secondary structure

1
987
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 226Combined sources
Helixi23 – 253Combined sources
Beta strandi33 – 364Combined sources
Beta strandi43 – 486Combined sources
Beta strandi54 – 618Combined sources
Beta strandi63 – 653Combined sources
Beta strandi70 – 745Combined sources
Beta strandi84 – 9512Combined sources
Helixi97 – 993Combined sources
Beta strandi109 – 12113Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi171 – 18212Combined sources
Beta strandi184 – 19613Combined sources
Beta strandi441 – 4466Combined sources
Beta strandi449 – 4535Combined sources
Beta strandi460 – 4623Combined sources
Beta strandi466 – 4738Combined sources
Turni479 – 4813Combined sources
Beta strandi482 – 49615Combined sources
Beta strandi503 – 5108Combined sources
Helixi612 – 6143Combined sources
Beta strandi615 – 6239Combined sources
Beta strandi625 – 63410Combined sources
Beta strandi637 – 6393Combined sources
Beta strandi642 – 6498Combined sources
Helixi655 – 66814Combined sources
Beta strandi679 – 6835Combined sources
Beta strandi685 – 69410Combined sources
Helixi701 – 7077Combined sources
Turni708 – 7103Combined sources
Helixi714 – 73320Combined sources
Helixi743 – 7453Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi754 – 7563Combined sources
Helixi765 – 7673Combined sources
Helixi784 – 7863Combined sources
Helixi789 – 7946Combined sources
Helixi799 – 81416Combined sources
Turni815 – 8173Combined sources
Turni820 – 8234Combined sources
Helixi826 – 8349Combined sources
Helixi847 – 85610Combined sources
Helixi861 – 8633Combined sources
Helixi867 – 87913Combined sources
Helixi881 – 8855Combined sources
Helixi912 – 9187Combined sources
Helixi922 – 9243Combined sources
Helixi925 – 9306Combined sources
Helixi936 – 9394Combined sources
Helixi944 – 9507Combined sources
Helixi955 – 96511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BBAX-ray1.65A17-196[»]
2E7HNMR-A434-529[»]
2HLEX-ray2.05A17-196[»]
2QKQX-ray2.10A/B896-977[»]
2VWUX-ray2.00A598-887[»]
2VWVX-ray1.90A598-899[»]
2VWWX-ray1.90A598-899[»]
2VWXX-ray1.65A598-899[»]
2VWYX-ray1.65A598-899[»]
2VWZX-ray1.65A598-899[»]
2VX0X-ray2.10A598-899[»]
2VX1X-ray1.65A598-899[»]
2X9FX-ray1.75A598-899[»]
2XVDX-ray1.70A598-899[»]
2YN8X-ray2.11A/B598-892[»]
3ZEWX-ray2.50A/B598-892[»]
4AW5X-ray2.33A605-890[»]
4BB4X-ray1.65A598-899[»]
ProteinModelPortaliP54760.
SMRiP54760. Positions 15-529, 608-973.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54760.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 202186Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini323 – 432110Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 52994Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini615 – 899285Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini907 – 97165SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi985 – 9873PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi184 – 320137Cys-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.
InParanoidiP54760.
KOiK05113.
OMAiTVFYFES.
PhylomeDBiP54760.
TreeFamiTF315608.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
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.
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. 2 hits.
PF07699. GCC2_GCC3. 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.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54760-1) [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
MELRVLLCWA SLAAALEETL LNTKLETADL KWVTFPQVDG QWEELSGLDE
60 70 80 90 100
EQHSVRTYEV CDVQRAPGQA HWLRTGWVPR RGAVHVYATL RFTMLECLSL
110 120 130 140 150
PRAGRSCKET FTVFYYESDA DTATALTPAW MENPYIKVDT VAAEHLTRKR
160 170 180 190 200
PGAEATGKVN VKTLRLGPLS KAGFYLAFQD QGACMALLSL HLFYKKCAQL
210 220 230 240 250
TVNLTRFPET VPRELVVPVA GSCVVDAVPA PGPSPSLYCR EDGQWAEQPV
260 270 280 290 300
TGCSCAPGFE AAEGNTKCRA CAQGTFKPLS GEGSCQPCPA NSHSNTIGSA
310 320 330 340 350
VCQCRVGYFR ARTDPRGAPC TTPPSAPRSV VSRLNGSSLH LEWSAPLESG
360 370 380 390 400
GREDLTYALR CRECRPGGSC APCGGDLTFD PGPRDLVEPW VVVRGLRPDF
410 420 430 440 450
TYTFEVTALN GVSSLATGPV PFEPVNVTTD REVPPAVSDI RVTRSSPSSL
460 470 480 490 500
SLAWAVPRAP SGAVLDYEVK YHEKGAEGPS SVRFLKTSEN RAELRGLKRG
510 520 530 540 550
ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SEGWREQLAL IAGTAVVGVV
560 570 580 590 600
LVLVVIVVAV LCLRKQSNGR EAEYSDKHGQ YLIGHGTKVY IDPFTYEDPN
610 620 630 640 650
EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK
660 670 680 690 700
GGYTERQRRE FLSEASIMGQ FEHPNIIRLE GVVTNSMPVM ILTEFMENGA
710 720 730 740 750
LDSFLRLNDG QFTVIQLVGM LRGIASGMRY LAEMSYVHRD LAARNILVNS
760 770 780 790 800
NLVCKVSDFG LSRFLEENSS DPTYTSSLGG KIPIRWTAPE AIAFRKFTSA
810 820 830 840 850
SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP PPPDCPTSLH
860 870 880 890 900
QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD
910 920 930 940 950
QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFELVS QISAEDLLRI
960 970 980
GVTLAGHQKK ILASVQHMKS QAKPGTPGGT GGPAPQY
Length:987
Mass (Da):108,270
Last modified:October 18, 2001 - v2
Checksum:i11A004622F194706
GO
Isoform 2 (identifier: P54760-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     507-516: VRARSEAGYG → RARAGGSSWP
     517-987: Missing.

Show »
Length:516
Mass (Da):55,975
Checksum:i076696B61467596C
GO
Isoform 3 (identifier: P54760-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     270-306: ACAQGTFKPLSGEGSCQPCPANSHSNTIGSAVCQCRV → GRRGSQQRAVPEDVRKPGRAAGAEAGSQLPGAGTGAL
     307-987: Missing.

Show »
Length:306
Mass (Da):33,342
Checksum:iAAAB50A132494B86
GO
Isoform 4 (identifier: P54760-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     406-414: VTALNGVSS → YLLQCLTSG
     415-987: Missing.

Show »
Length:414
Mass (Da):45,195
Checksum:iA9596D1E38B18785
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621D → E in AAA20598. (PubMed:8188704)Curated
Sequence conflicti308 – 3081Y → D in AAA20598. (PubMed:8188704)Curated
Sequence conflicti464 – 4641V → W in AAA20598. (PubMed:8188704)Curated
Sequence conflicti926 – 9272ES → AR in AAA20598. (PubMed:8188704)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671P → L.1 Publication
Corresponds to variant rs34653459 [ dbSNP | Ensembl ].
VAR_042181
Natural varianti113 – 1131V → I.1 Publication
Corresponds to variant rs55866373 [ dbSNP | Ensembl ].
VAR_042182
Natural varianti162 – 1621K → R.1 Publication
Corresponds to variant rs17854760 [ dbSNP | Ensembl ].
VAR_071163
Natural varianti346 – 3461P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042183
Natural varianti371 – 3711A → V.1 Publication
Corresponds to variant rs55720981 [ dbSNP | Ensembl ].
VAR_042184
Natural varianti576 – 5761D → E.1 Publication
Corresponds to variant rs36050247 [ dbSNP | Ensembl ].
VAR_042185
Natural varianti678 – 6781R → H.1 Publication
Corresponds to variant rs55692440 [ dbSNP | Ensembl ].
VAR_042186
Natural varianti882 – 8821A → T.1 Publication
Corresponds to variant rs34918225 [ dbSNP | Ensembl ].
VAR_042187
Natural varianti889 – 8891R → W in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042188
Natural varianti890 – 8901E → D.1 Publication
Corresponds to variant rs35638378 [ dbSNP | Ensembl ].
VAR_042189

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei270 – 30637ACAQG…CQCRV → GRRGSQQRAVPEDVRKPGRA AGAEAGSQLPGAGTGAL in isoform 3. 1 PublicationVSP_056020Add
BLAST
Alternative sequencei307 – 987681Missing in isoform 3. 1 PublicationVSP_056021Add
BLAST
Alternative sequencei406 – 4149VTALNGVSS → YLLQCLTSG in isoform 4. 1 PublicationVSP_056022
Alternative sequencei415 – 987573Missing in isoform 4. 1 PublicationVSP_056023Add
BLAST
Alternative sequencei507 – 51610VRARSEAGYG → RARAGGSSWP in isoform 2. 1 PublicationVSP_056024
Alternative sequencei517 – 987471Missing in isoform 2. 1 PublicationVSP_056025Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07695 mRNA. Translation: AAA20598.1.
AF312032 Genomic DNA. Translation: AAK21010.1.
EU826608 mRNA. Translation: ACF47644.1.
EU826609 mRNA. Translation: ACF47645.1.
EU826610 mRNA. Translation: ACF47646.1.
BC004264 mRNA. Translation: AAH04264.1.
BC052804 mRNA. Translation: AAH52804.1.
CCDSiCCDS5706.1. [P54760-1]
PIRiA54092.
RefSeqiNP_004435.3. NM_004444.4. [P54760-1]
UniGeneiHs.437008.

Genome annotation databases

EnsembliENST00000358173; ENSP00000350896; ENSG00000196411. [P54760-1]
ENST00000616502; ENSP00000482702; ENSG00000196411. [P54760-3]
GeneIDi2050.
KEGGihsa:2050.
UCSCiuc003uwm.1. human. [P54760-1]

Polymorphism databases

DMDMi19860819.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07695 mRNA. Translation: AAA20598.1 .
AF312032 Genomic DNA. Translation: AAK21010.1 .
EU826608 mRNA. Translation: ACF47644.1 .
EU826609 mRNA. Translation: ACF47645.1 .
EU826610 mRNA. Translation: ACF47646.1 .
BC004264 mRNA. Translation: AAH04264.1 .
BC052804 mRNA. Translation: AAH52804.1 .
CCDSi CCDS5706.1. [P54760-1 ]
PIRi A54092.
RefSeqi NP_004435.3. NM_004444.4. [P54760-1 ]
UniGenei Hs.437008.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BBA X-ray 1.65 A 17-196 [» ]
2E7H NMR - A 434-529 [» ]
2HLE X-ray 2.05 A 17-196 [» ]
2QKQ X-ray 2.10 A/B 896-977 [» ]
2VWU X-ray 2.00 A 598-887 [» ]
2VWV X-ray 1.90 A 598-899 [» ]
2VWW X-ray 1.90 A 598-899 [» ]
2VWX X-ray 1.65 A 598-899 [» ]
2VWY X-ray 1.65 A 598-899 [» ]
2VWZ X-ray 1.65 A 598-899 [» ]
2VX0 X-ray 2.10 A 598-899 [» ]
2VX1 X-ray 1.65 A 598-899 [» ]
2X9F X-ray 1.75 A 598-899 [» ]
2XVD X-ray 1.70 A 598-899 [» ]
2YN8 X-ray 2.11 A/B 598-892 [» ]
3ZEW X-ray 2.50 A/B 598-892 [» ]
4AW5 X-ray 2.33 A 605-890 [» ]
4BB4 X-ray 1.65 A 598-899 [» ]
ProteinModelPortali P54760.
SMRi P54760. Positions 15-529, 608-973.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108364. 8 interactions.
IntActi P54760. 3 interactions.
STRINGi 9606.ENSP00000350896.

Chemistry

BindingDBi P54760.
ChEMBLi CHEMBL5147.
GuidetoPHARMACOLOGYi 1833.

PTM databases

PhosphoSitei P54760.

Polymorphism databases

DMDMi 19860819.

2D gel databases

DOSAC-COBS-2DPAGE P54760.

Proteomic databases

MaxQBi P54760.
PaxDbi P54760.
PRIDEi P54760.

Protocols and materials databases

DNASUi 2050.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358173 ; ENSP00000350896 ; ENSG00000196411 . [P54760-1 ]
ENST00000616502 ; ENSP00000482702 ; ENSG00000196411 . [P54760-3 ]
GeneIDi 2050.
KEGGi hsa:2050.
UCSCi uc003uwm.1. human. [P54760-1 ]

Organism-specific databases

CTDi 2050.
GeneCardsi GC07M100402.
H-InvDB HIX0025312.
HGNCi HGNC:3395. EPHB4.
HPAi CAB013537.
MIMi 600011. gene.
neXtProti NX_P54760.
PharmGKBi PA27827.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P54760.
KOi K05113.
OMAi TVFYFES.
PhylomeDBi P54760.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_228085. EPHB-mediated forward signaling.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.
SignaLinki P54760.

Miscellaneous databases

ChiTaRSi EPHB4. human.
EvolutionaryTracei P54760.
GeneWikii EPH_receptor_B4.
GenomeRNAii 2050.
NextBioi 35477787.
PROi P54760.
SOURCEi Search...

Gene expression databases

Bgeei P54760.
CleanExi HS_EPHB4.
ExpressionAtlasi P54760. baseline and differential.
Genevestigatori P54760.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
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.
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 ]
Pfami PF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
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. "Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily."
    Bennett B.D., Wang Z., Kuang W.J., Wang A., Groopman J.E., Goeddel D.V., Scadden D.T.
    J. Biol. Chem. 269:14211-14218(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
    Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
    Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
    Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
    Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), ALTERNATIVE SPLICING.
  4. "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), VARIANT ARG-162.
    Tissue: Ovary and Pancreas.
  5. "Unified nomenclature for Eph family receptors and their ligands, the ephrins."
    Eph nomenclature committee
    Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  6. "Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells."
    Fueller T., Korff T., Kilian A., Dandekar G., Augustin H.G.
    J. Cell Sci. 116:2461-2470(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL ADHESION, FUNCTION IN CELL MIGRATION.
  7. "EphB4 controls blood vascular morphogenesis during postnatal angiogenesis."
    Erber R., Eichelsbacher U., Powajbo V., Korn T., Djonov V., Lin J., Hammes H.P., Grobholz R., Ullrich A., Vajkoczy P.
    EMBO J. 25:628-641(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN POSTNATAL AND TUMOR ANGIOGENESIS.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-976, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-976, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; THR-976 AND TYR-987, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structural and biophysical characterization of the EphB4*ephrinB2 protein-protein interaction and receptor specificity."
    Chrencik J.E., Brooun A., Kraus M.L., Recht M.I., Kolatkar A.R., Han G.W., Seifert J.M., Widmer H., Auer M., Kuhn P.
    J. Biol. Chem. 281:28185-28192(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 17-196 IN COMPLEX WITH EFNB2, MUTAGENESIS OF LEU-95, DISULFIDE BOND.
  14. "Structure and thermodynamic characterization of the EphB4/Ephrin-B2 antagonist peptide complex reveals the determinants for receptor specificity."
    Chrencik J.E., Brooun A., Recht M.I., Kraus M.L., Koolpe M., Kolatkar A.R., Bruce R.H., Martiny-Baron G., Widmer H., Pasquale E.B., Kuhn P.
    Structure 14:321-330(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 17-196 IN COMPLEX WITH ANTAGONISTIC PEPTIDE, DISULFIDE BOND.
  15. "Solution structure of the second FN3 domain from human ephrin type-B receptor 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 434-529.
  16. "Patterns of somatic mutation in human cancer genomes."
    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.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-67; ILE-113; LEU-346; VAL-371; GLU-576; HIS-678; THR-882; TRP-889 AND ASP-890.

Entry informationi

Entry nameiEPHB4_HUMAN
AccessioniPrimary (citable) accession number: P54760
Secondary accession number(s): B5A970
, B5A971, B5A972, Q7Z635, Q9BTA5, Q9BXP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: November 26, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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