Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P29323

- EPHB2_HUMAN

UniProt

P29323 - EPHB2_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 5 (27 Sep 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: IntAct
    4. protein tyrosine kinase activity Source: UniProtKB
    5. 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

    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.
    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

    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

    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

    ArrayExpressiP29323.
    BgeeiP29323.
    CleanExiHS_EPHB2.
    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. 18 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 – 255
    Helixi26 – 283
    Beta strandi36 – 394
    Beta strandi44 – 496
    Beta strandi55 – 617
    Beta strandi66 – 683
    Beta strandi71 – 744
    Beta strandi84 – 9411
    Helixi97 – 993
    Beta strandi111 – 12010
    Beta strandi130 – 1323
    Beta strandi135 – 1417
    Beta strandi148 – 1525
    Beta strandi155 – 16612
    Beta strandi171 – 18313
    Beta strandi185 – 19410
    Helixi618 – 6203
    Beta strandi621 – 6266
    Beta strandi635 – 6406
    Beta strandi648 – 6558
    Helixi661 – 67414
    Beta strandi685 – 6895
    Beta strandi691 – 70010
    Helixi707 – 7126
    Turni713 – 7164
    Helixi720 – 73920
    Helixi749 – 7513
    Beta strandi752 – 7543
    Beta strandi760 – 7623
    Helixi790 – 7923
    Helixi795 – 8006
    Helixi805 – 82016
    Turni826 – 8294
    Helixi832 – 8409
    Helixi853 – 86210
    Helixi873 – 88513
    Helixi887 – 8904
    Helixi918 – 9247
    Helixi928 – 9303
    Helixi931 – 9366
    Helixi942 – 9454
    Helixi950 – 9556
    Helixi961 – 98222

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 18-531, 575-985.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29323.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei544 – 56421HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MALRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD     50
    ENMNTIRTYQ VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI 100
    PSVPGSCKET FNLYYYEADF DSATKTFPNW MENPWVKVDT IAADESFSQV 150
    DLGGRVMKIN TEVRSFGPVS RSGFYLAFQD YGGCMSLIAV RVFYRKCPRI 200
    IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY CNGDGEWLVP 250
    IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA 300
    TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS 350
    GGREDLVYNI ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA 400
    HTQYTFEIQA VNGVTDQSPF SPQFASVNIT TNQAAPSAVS IMHQVSRTVD 450
    SITLSWSQPD QPNGVILDYE LQYYEKELSE YNATAIKSPT NTVTVQGLKA 500
    GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIQEK LPLIIGSSAA 550
    GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF 600
    TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV 650
    AIKTLKSGYT EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE 700
    FMENGSLDSF LRQNDGQFTV IQLVGMLRGI AAGMKYLADM NYVHRDLAAR 750
    NILVNSNLVC KVSDFGLSRF LEDDTSDPTY TSALGGKIPI RWTAPEAIQY 800
    RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE QDYRLPPPMD 850
    CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI 900
    NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM 950
    EDILRVGVTL AGHQKKILNS IQVMRAQMNQ IQSVEGQPLA RRPRATGRTK 1000
    RCQPRDVTKK TCNSNDGKKK GMGKKKTDPG RGREIQGIFF KEDSHKESND 1050
    CSCGG 1055
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 18-531, 575-985.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108362. 18 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.
    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.
    SignaLinki P29323.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi P29323.
    Bgeei P29323.
    CleanExi HS_EPHB2.
    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

    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: October 1, 2014
    This is version 182 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