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P29323

- EPHB2_HUMAN

UniProt

P29323 - EPHB2_HUMAN

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Protein

Ephrin type-B receptor 2

Gene

EPHB2

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. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor.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 sitei653 – 6531ATPPROSITE-ProRule annotation
Active sitei746 – 7461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi627 – 6359ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. axonal fasciculation Source: UniProtKB
  3. axon guidance Source: UniProtKB
  4. camera-type eye morphogenesis Source: Ensembl
  5. central nervous system projection neuron axonogenesis Source: Ensembl
  6. commissural neuron axon guidance Source: UniProtKB
  7. corpus callosum development Source: UniProtKB
  8. dendritic spine development Source: UniProtKB
  9. dendritic spine morphogenesis Source: UniProtKB
  10. ephrin receptor signaling pathway Source: UniProtKB
  11. inner ear morphogenesis Source: UniProtKB
  12. learning Source: Ensembl
  13. negative regulation of axonogenesis Source: Ensembl
  14. nervous system development Source: UniProtKB
  15. optic nerve morphogenesis Source: Ensembl
  16. palate development Source: UniProtKB
  17. peptidyl-tyrosine phosphorylation Source: UniProtKB
  18. phosphorylation Source: UniProtKB
  19. positive regulation of long-term neuronal synaptic plasticity Source: Ensembl
  20. positive regulation of synapse assembly Source: UniProtKB
  21. regulation of body fluid levels Source: UniProtKB
  22. retinal ganglion cell axon guidance Source: Ensembl
  23. urogenital system development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_22205. L1CAM interactions.
REACT_228085. EPHB-mediated forward signaling.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.
SignaLinkiP29323.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 2 (EC:2.7.10.1)
Alternative name(s):
Developmentally-regulated Eph-related tyrosine kinase
ELK-related tyrosine kinase
EPH tyrosine kinase 3
EPH-like kinase 5
Short name:
EK5
Short name:
hEK5
Renal carcinoma antigen NY-REN-47
Tyrosine-protein kinase TYRO5
Tyrosine-protein kinase receptor EPH-3
Gene namesi
Name:EPHB2
Synonyms:DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3393. EPHB2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 543525ExtracellularSequence AnalysisAdd
BLAST
Transmembranei544 – 56421HelicalSequence AnalysisAdd
BLAST
Topological domaini565 – 1055491CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
  4. neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Involvement in diseasei

Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.2 Publications
Note: The gene represented in this entry may be involved in disease pathogenesis. EPHB2 mutations have been found in a prostate cancer cell line derived from a brain metastasis.

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi176807. phenotype.
603688. phenotype.
Orphaneti1331. Familial prostate cancer.
PharmGKBiPA27825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 10551037Ephrin type-B receptor 2PRO_0000016827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 1841 Publication
Disulfide bondi97 ↔ 1071 Publication
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP29323.
PaxDbiP29323.
PRIDEiP29323.

PTM databases

PhosphoSiteiP29323.

Expressioni

Tissue specificityi

Brain, heart, lung, kidney, placenta, pancreas, liver and skeletal muscle. Preferentially expressed in fetal brain.

Gene expression databases

BgeeiP29323.
CleanExiHS_EPHB2.
ExpressionAtlasiP29323. baseline and differential.
GenevestigatoriP29323.

Organism-specific databases

HPAiCAB013647.

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 (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) (By similarity). Interacts with ARHGEF15; mediates ARHGEF15 phosphorylation, ubiquitination and degradation by the proteasome. Interacts with AQP1; involved in endolymph production in the inner ear.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NUP153P497902EBI-1059294,EBI-286779

Protein-protein interaction databases

BioGridi108362. 19 interactions.
DIPiDIP-1162N.
IntActiP29323. 3 interactions.
MINTiMINT-5005955.
STRINGi9606.ENSP00000363763.

Structurei

Secondary structure

1
1055
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 255Combined sources
Helixi26 – 283Combined sources
Beta strandi36 – 394Combined sources
Beta strandi44 – 496Combined sources
Beta strandi55 – 617Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 744Combined sources
Beta strandi84 – 9411Combined sources
Helixi97 – 993Combined sources
Beta strandi111 – 12010Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi135 – 1417Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi155 – 16612Combined sources
Beta strandi171 – 18313Combined sources
Beta strandi185 – 19410Combined sources
Helixi618 – 6203Combined sources
Beta strandi621 – 6266Combined sources
Beta strandi635 – 6406Combined sources
Beta strandi648 – 6558Combined sources
Helixi661 – 67414Combined sources
Beta strandi685 – 6895Combined sources
Beta strandi691 – 70010Combined sources
Helixi707 – 7126Combined sources
Turni713 – 7164Combined sources
Helixi720 – 73920Combined sources
Helixi749 – 7513Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi760 – 7623Combined sources
Helixi790 – 7923Combined sources
Helixi795 – 8006Combined sources
Helixi805 – 82016Combined sources
Turni826 – 8294Combined sources
Helixi832 – 8409Combined sources
Helixi853 – 86210Combined sources
Helixi873 – 88513Combined sources
Helixi887 – 8904Combined sources
Helixi918 – 9247Combined sources
Helixi928 – 9303Combined sources
Helixi931 – 9366Combined sources
Helixi942 – 9454Combined sources
Helixi950 – 9556Combined sources
Helixi961 – 98222Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4FX-ray1.95A/B/C/D/E/F/G/H908-985[»]
1F0MX-ray2.20A908-985[»]
2QBXX-ray2.30A/B20-196[»]
3ZFMX-ray2.27A604-898[»]
ProteinModelPortaliP29323.
SMRiP29323. Positions 20-531, 577-985.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 202183Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini324 – 434111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini435 – 53096Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini621 – 884264Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini913 – 97765SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi984 – 9863PDZ-binding (in isoform 2)Sequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi184 – 324141Cys-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.
InParanoidiP29323.
KOiK05111.
OMAiIVCNRRR.
OrthoDBiEOG7VTDM6.
PhylomeDBiP29323.
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.
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.
PROSITEiPS51550. 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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P29323-1) [UniParc]FASTAAdd to Basket

Also known as: EPHB2v, Long

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
MALRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD
60 70 80 90 100
ENMNTIRTYQ VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI
110 120 130 140 150
PSVPGSCKET FNLYYYEADF DSATKTFPNW MENPWVKVDT IAADESFSQV
160 170 180 190 200
DLGGRVMKIN TEVRSFGPVS RSGFYLAFQD YGGCMSLIAV RVFYRKCPRI
210 220 230 240 250
IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY CNGDGEWLVP
260 270 280 290 300
IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA
310 320 330 340 350
TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS
360 370 380 390 400
GGREDLVYNI ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA
410 420 430 440 450
HTQYTFEIQA VNGVTDQSPF SPQFASVNIT TNQAAPSAVS IMHQVSRTVD
460 470 480 490 500
SITLSWSQPD QPNGVILDYE LQYYEKELSE YNATAIKSPT NTVTVQGLKA
510 520 530 540 550
GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIQEK LPLIIGSSAA
560 570 580 590 600
GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF
610 620 630 640 650
TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV
660 670 680 690 700
AIKTLKSGYT EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE
710 720 730 740 750
FMENGSLDSF LRQNDGQFTV IQLVGMLRGI AAGMKYLADM NYVHRDLAAR
760 770 780 790 800
NILVNSNLVC KVSDFGLSRF LEDDTSDPTY TSALGGKIPI RWTAPEAIQY
810 820 830 840 850
RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE QDYRLPPPMD
860 870 880 890 900
CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI
910 920 930 940 950
NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM
960 970 980 990 1000
EDILRVGVTL AGHQKKILNS IQVMRAQMNQ IQSVEGQPLA RRPRATGRTK
1010 1020 1030 1040 1050
RCQPRDVTKK TCNSNDGKKK GMGKKKTDPG RGREIQGIFF KEDSHKESND

CSCGG
Length:1,055
Mass (Da):117,493
Last modified:September 27, 2005 - v5
Checksum:i4F8BFEDC45986483
GO
Isoform 2 (identifier: P29323-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     986-986: G → V
     987-1055: Missing.

Note: Contains a phosphoserine at position 983.

Show »
Length:986
Mass (Da):109,874
Checksum:i4B9B532A48B754A6
GO
Isoform 3 (identifier: P29323-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     568-568: R → RR
     986-986: G → V
     987-1055: Missing.

Note: No experimental confirmation available. Contains a phosphoserine at position 984.

Show »
Length:987
Mass (Da):110,030
Checksum:iEF6DA7A63D894E47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2020MALRR…LAAVE → MWVPVLALPVCTYA in BAA06506. (PubMed:8033077)CuratedAdd
BLAST
Sequence conflicti154 – 1541G → D in BAA06506. (PubMed:8033077)Curated
Sequence conflicti476 – 4761K → KQ in BAA06506. (PubMed:8033077)Curated
Sequence conflicti495 – 4962Missing in AAA74244. (PubMed:7898931)Curated
Sequence conflicti532 – 5321E → D in BAA06506. (PubMed:8033077)Curated
Sequence conflicti589 – 5891M → I in AAA74244. (PubMed:7898931)Curated
Sequence conflicti671 – 6711A → R in BAA03537. (PubMed:7688222)Curated
Sequence conflicti788 – 7881I → F in AAA74244. (PubMed:7898931)Curated
Sequence conflicti853 – 8531S → A in BAA06506. (PubMed:8033077)Curated
Sequence conflicti853 – 8531S → A in BAA07073. (PubMed:7601466)Curated
Sequence conflicti853 – 8531S → A in BAA03537. (PubMed:7688222)Curated
Sequence conflicti923 – 9231E → K in BAA06506. (PubMed:8033077)Curated
Sequence conflicti923 – 9231E → K in BAA07073. (PubMed:7601466)Curated
Sequence conflicti923 – 9231E → K in BAA03537. (PubMed:7688222)Curated
Sequence conflicti958 – 9581V → L in AAA99310. (PubMed:8589679)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991R → H in prostate cancer. 1 Publication
VAR_032853
Natural varianti279 – 2791A → S in prostate cancer. 3 Publications
Corresponds to variant rs35882952 [ dbSNP | Ensembl ].
VAR_032854
Natural varianti289 – 2891C → G.1 Publication
VAR_042172
Natural varianti361 – 3611I → V.1 Publication
Corresponds to variant rs56180036 [ dbSNP | Ensembl ].
VAR_042173
Natural varianti650 – 6501V → A in prostate cancer. 1 Publication
Corresponds to variant rs142173175 [ dbSNP | Ensembl ].
VAR_032855
Natural varianti678 – 6781D → N.1 Publication
Corresponds to variant rs28936395 [ dbSNP | Ensembl ].
VAR_042174
Natural varianti679 – 6791H → N in prostate cancer. 1 Publication
VAR_032856
Natural varianti844 – 8441R → W.1 Publication
Corresponds to variant rs55826626 [ dbSNP | Ensembl ].
VAR_042175
Natural varianti883 – 8831M → V in prostate cancer. 1 Publication
VAR_032857
Natural varianti909 – 9091I → M in prostate cancer. 1 Publication
VAR_032858

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei568 – 5681R → RR in isoform 3. 1 PublicationVSP_015713
Alternative sequencei986 – 9861G → V in isoform 2 and isoform 3. 5 PublicationsVSP_003016
Alternative sequencei987 – 105569Missing in isoform 2 and isoform 3. 5 PublicationsVSP_003017Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31661 mRNA. Translation: BAA06506.1.
L41939 mRNA. Translation: AAA99310.1.
AF025304 mRNA. Translation: AAB94602.1.
AL035704, AL158086, AL512444 Genomic DNA. Translation: CAI22645.1.
AL035704, AL158086, AL512444 Genomic DNA. Translation: CAI22646.1.
AL035704, AL158086, AL512444 Genomic DNA. Translation: CAI22647.2.
AL158086, AL035704, AL512444 Genomic DNA. Translation: CAI22897.1.
AL158086, AL512444, AL035704 Genomic DNA. Translation: CAI22898.1.
AL158086, AL035704, AL512444 Genomic DNA. Translation: CAI22899.2.
AL512444, AL035704, AL158086 Genomic DNA. Translation: CAI16428.1.
AL512444, AL035704, AL158086 Genomic DNA. Translation: CAI16429.1.
AL512444, AL035704, AL158086 Genomic DNA. Translation: CAI16430.2.
L36643 mRNA. Translation: AAA74244.1.
D37827 mRNA. Translation: BAA07073.1.
D14717 mRNA. Translation: BAA03537.1.
X59292 Genomic DNA. Translation: CAA41981.1.
CCDSiCCDS229.2. [P29323-2]
CCDS230.1. [P29323-3]
PIRiA57174.
I78842.
RefSeqiNP_004433.2. NM_004442.6. [P29323-3]
NP_059145.2. NM_017449.3. [P29323-2]
UniGeneiHs.523329.

Genome annotation databases

EnsembliENST00000374630; ENSP00000363761; ENSG00000133216. [P29323-2]
ENST00000374632; ENSP00000363763; ENSG00000133216. [P29323-3]
ENST00000400191; ENSP00000383053; ENSG00000133216. [P29323-1]
GeneIDi2048.
KEGGihsa:2048.
UCSCiuc001bge.3. human. [P29323-3]
uc001bgf.3. human. [P29323-2]
uc009vqj.1. human. [P29323-1]

Polymorphism databases

DMDMi76803654.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31661 mRNA. Translation: BAA06506.1 .
L41939 mRNA. Translation: AAA99310.1 .
AF025304 mRNA. Translation: AAB94602.1 .
AL035704 , AL158086 , AL512444 Genomic DNA. Translation: CAI22645.1 .
AL035704 , AL158086 , AL512444 Genomic DNA. Translation: CAI22646.1 .
AL035704 , AL158086 , AL512444 Genomic DNA. Translation: CAI22647.2 .
AL158086 , AL035704 , AL512444 Genomic DNA. Translation: CAI22897.1 .
AL158086 , AL512444 , AL035704 Genomic DNA. Translation: CAI22898.1 .
AL158086 , AL035704 , AL512444 Genomic DNA. Translation: CAI22899.2 .
AL512444 , AL035704 , AL158086 Genomic DNA. Translation: CAI16428.1 .
AL512444 , AL035704 , AL158086 Genomic DNA. Translation: CAI16429.1 .
AL512444 , AL035704 , AL158086 Genomic DNA. Translation: CAI16430.2 .
L36643 mRNA. Translation: AAA74244.1 .
D37827 mRNA. Translation: BAA07073.1 .
D14717 mRNA. Translation: BAA03537.1 .
X59292 Genomic DNA. Translation: CAA41981.1 .
CCDSi CCDS229.2. [P29323-2 ]
CCDS230.1. [P29323-3 ]
PIRi A57174.
I78842.
RefSeqi NP_004433.2. NM_004442.6. [P29323-3 ]
NP_059145.2. NM_017449.3. [P29323-2 ]
UniGenei Hs.523329.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B4F X-ray 1.95 A/B/C/D/E/F/G/H 908-985 [» ]
1F0M X-ray 2.20 A 908-985 [» ]
2QBX X-ray 2.30 A/B 20-196 [» ]
3ZFM X-ray 2.27 A 604-898 [» ]
ProteinModelPortali P29323.
SMRi P29323. Positions 20-531, 577-985.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108362. 19 interactions.
DIPi DIP-1162N.
IntActi P29323. 3 interactions.
MINTi MINT-5005955.
STRINGi 9606.ENSP00000363763.

Chemistry

BindingDBi P29323.
ChEMBLi CHEMBL3290.
GuidetoPHARMACOLOGYi 1831.

PTM databases

PhosphoSitei P29323.

Polymorphism databases

DMDMi 76803654.

Proteomic databases

MaxQBi P29323.
PaxDbi P29323.
PRIDEi P29323.

Protocols and materials databases

DNASUi 2048.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374630 ; ENSP00000363761 ; ENSG00000133216 . [P29323-2 ]
ENST00000374632 ; ENSP00000363763 ; ENSG00000133216 . [P29323-3 ]
ENST00000400191 ; ENSP00000383053 ; ENSG00000133216 . [P29323-1 ]
GeneIDi 2048.
KEGGi hsa:2048.
UCSCi uc001bge.3. human. [P29323-3 ]
uc001bgf.3. human. [P29323-2 ]
uc009vqj.1. human. [P29323-1 ]

Organism-specific databases

CTDi 2048.
GeneCardsi GC01P023037.
H-InvDB HIX0028518.
HGNCi HGNC:3393. EPHB2.
HPAi CAB013647.
MIMi 176807. phenotype.
600997. gene.
603688. phenotype.
neXtProti NX_P29323.
Orphaneti 1331. Familial prostate cancer.
PharmGKBi PA27825.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P29323.
KOi K05111.
OMAi IVCNRRR.
OrthoDBi EOG7VTDM6.
PhylomeDBi P29323.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_22205. L1CAM interactions.
REACT_228085. EPHB-mediated forward signaling.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.
SignaLinki P29323.

Miscellaneous databases

ChiTaRSi EPHB2. human.
EvolutionaryTracei P29323.
GeneWikii EPH_receptor_B2.
GenomeRNAii 2048.
NextBioi 8325.
PROi P29323.
SOURCEi Search...

Gene expression databases

Bgeei P29323.
CleanExi HS_EPHB2.
ExpressionAtlasi P29323. baseline and differential.
Genevestigatori P29323.

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.
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 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. "Overexpression of ERK, an EPH family receptor protein tyrosine kinase, in various human tumors."
    Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y.Y., Naito Y., Yamada K., Sugimura H., Kino I.
    Cancer Res. 54:3645-3650(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Molecular characterization and chromosomal localization of DRT (EPHT3): a developmentally regulated human protein-tyrosine kinase gene of the EPH family."
    Ikegaki N., Tang X.X., Liu X.-G., Biegel J.A., Allen C., Yoshioka A., Sulman E.P., Brodeur G.M., Pleasure D.E.
    Hum. Mol. Genet. 4:2033-2045(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Fetal brain.
  3. "A variant transcript encoding an isoform of the human protein tyrosine kinase EPHB2 is generated by alternative splicing and alternative use of polyadenylation signals."
    Tang X.X., Pleasure D.E., Brodeur G.M., Ikegaki N.
    Oncogene 17:521-526(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases."
    Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R., Welcher A.A.
    Oncogene 10:897-905(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-986 (ISOFORM 2).
    Tissue: Brain.
  6. "Identification of the human ERK gene as a putative receptor tyrosine kinase and its chromosomal localization to 1p36.1: a comparative mapping of human, mouse, and rat chromosomes."
    Saito T., Seki N., Matsuda Y., Kitahara M., Murata M., Kanda N., Nomura N., Yamamoto T., Hori T.-A.
    Genomics 26:382-384(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-986 (ISOFORM 2).
    Tissue: Fetal brain.
  7. "Identification of protein-tyrosine kinase genes preferentially expressed in embryo stomach and gastric cancer."
    Iwase T., Tanaka M., Suzuki M., Naito Y., Sugimura H., Kino I.
    Biochem. Biophys. Res. Commun. 194:698-705(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 640-986 (ISOFORM 2).
    Tissue: Gastric carcinoma.
  8. "eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases."
    Chan J., Watt V.M.
    Oncogene 6:1057-1061(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-712.
  9. "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.
  10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Oligomeric structure of the human EphB2 receptor SAM domain."
    Thanos C.D., Goodwill K.E., Bowie J.U.
    Science 283:833-836(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 910-986 (ISOFORM SHORT).
  14. "Three-dimensional structure of the EphB2 receptor in complex with an antagonistic peptide reveals a novel mode of inhibition."
    Chrencik J.E., Brooun A., Recht M.I., Nicola G., Davis L.K., Abagyan R., Widmer H., Pasquale E.B., Kuhn P.
    J. Biol. Chem. 282:36505-36513(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-195 OF HOMODIMER IN COMPLEX WITH ANTAGONISTIC PEPTIDE, DISULFIDE BOND.
  15. Cited for: VARIANTS PROSTATE CANCER HIS-199; SER-279; ASN-679 AND MET-909, FUNCTION AS A TUMOR SUPPRESSOR.
  16. Cited for: VARIANTS PROSTATE CANCER SER-279; ALA-650 AND VAL-883.
  17. "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] SER-279; GLY-289; VAL-361; ASN-678 AND TRP-844.

Entry informationi

Entry nameiEPHB2_HUMAN
AccessioniPrimary (citable) accession number: P29323
Secondary accession number(s): O43477
, Q5T0U6, Q5T0U7, Q5T0U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 27, 2005
Last modified: November 26, 2014
This is version 184 of the entry and version 5 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 1
    Human chromosome 1: 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

Dasty 3