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P29323

- EPHB2_HUMAN

UniProt

P29323 - EPHB2_HUMAN

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Protein
Ephrin type-B receptor 2
Gene
EPHB2, DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5
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. Beside 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei653 – 6531ATP By similarity
Active sitei746 – 7461Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi627 – 6359ATP By similarity

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
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. axon guidance Source: UniProtKB
  3. axonal fasciculation 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.
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 – 543525Extracellular Reviewed prediction
Add
BLAST
Transmembranei544 – 56421Helical; Reviewed prediction
Add
BLAST
Topological domaini565 – 1055491Cytoplasmic Reviewed prediction
Add
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.
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 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 10551037Ephrin type-B receptor 2
PRO_0000016827Add
BLAST

Amino acid modifications

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

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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP29323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 202183Eph LBD
Add
BLAST
Domaini324 – 434111Fibronectin type-III 1
Add
BLAST
Domaini435 – 53096Fibronectin type-III 2
Add
BLAST
Domaini621 – 884264Protein kinase
Add
BLAST
Domaini913 – 97765SAM
Add
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi184 – 324141Cys-rich
Add
BLAST

Sequence similaritiesi

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

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.
VSP_015713
Alternative sequencei986 – 9861G → V in isoform 2 and isoform 3.
VSP_003016
Alternative sequencei987 – 105569Missing in isoform 2 and isoform 3.
VSP_003017Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2020MALRR…LAAVE → MWVPVLALPVCTYA in BAA06506. 1 Publication
Add
BLAST
Sequence conflicti154 – 1541G → D in BAA06506. 1 Publication
Sequence conflicti476 – 4761K → KQ in BAA06506. 1 Publication
Sequence conflicti495 – 4962Missing in AAA74244. 1 Publication
Sequence conflicti532 – 5321E → D in BAA06506. 1 Publication
Sequence conflicti589 – 5891M → I in AAA74244. 1 Publication
Sequence conflicti671 – 6711A → R in BAA03537. 1 Publication
Sequence conflicti788 – 7881I → F in AAA74244. 1 Publication
Sequence conflicti853 – 8531S → A in BAA06506. 1 Publication
Sequence conflicti853 – 8531S → A in BAA07073. 1 Publication
Sequence conflicti853 – 8531S → A in BAA03537. 1 Publication
Sequence conflicti923 – 9231E → K in BAA06506. 1 Publication
Sequence conflicti923 – 9231E → K in BAA07073. 1 Publication
Sequence conflicti923 – 9231E → K in BAA03537. 1 Publication
Sequence conflicti958 – 9581V → L in AAA99310. 1 Publication

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...

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

« 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: September 3, 2014
This is version 181 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

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