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P29320

- EPHA3_HUMAN

UniProt

P29320 - EPHA3_HUMAN

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Protein

Ephrin type-A receptor 3

Gene

EPHA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin 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. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.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 – 6531ATP
Active sitei746 – 7461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi628 – 6336ATP
Nucleotide bindingi700 – 7067ATP
Nucleotide bindingi750 – 7512ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GPI-linked ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell migration Source: UniProtKB
  3. cellular response to retinoic acid Source: BHF-UCL
  4. ephrin receptor signaling pathway Source: UniProtKB
  5. fasciculation of motor neuron axon Source: UniProtKB
  6. fasciculation of sensory neuron axon Source: UniProtKB
  7. positive regulation of neuron projection development Source: BHF-UCL
  8. regulation of actin cytoskeleton organization Source: UniProtKB
  9. regulation of epithelial to mesenchymal transition Source: UniProtKB
  10. regulation of focal adhesion assembly Source: UniProtKB
  11. regulation of microtubule cytoskeleton organization Source: UniProtKB
  12. regulation of Rho GTPase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiP29320.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 3 (EC:2.7.10.1)
Alternative name(s):
EPH-like kinase 4
Short name:
EK4
Short name:
hEK4
HEK
Short name:
Human embryo kinase
Tyrosine-protein kinase TYRO4
Tyrosine-protein kinase receptor ETK1
Short name:
Eph-like tyrosine kinase 1
Gene namesi
Name:EPHA3
Synonyms:ETK, ETK1, HEK, TYRO4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3387. EPHA3.

Subcellular locationi

GO - Cellular componenti

  1. early endosome Source: UniProtKB
  2. extracellular region Source: UniProtKB-KW
  3. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Note: The gene represented in this entry may be involved in disease pathogenesis.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331V → E: Loss of EFNA5-binding ability and function. 1 Publication
Mutagenesisi152 – 1521F → L: Loss of EFNA5-binding ability and function. 1 Publication
Mutagenesisi596 – 5961Y → F: 10-fold suppression of kinase activity; when associated with F-602. Full kinase activity; when associated with F-602 and F-742. Full kinase activity; when associated with F-602 and A-768. 1 Publication
Mutagenesisi602 – 6021Y → F: 10-fold suppression of kinase activity; when associated with F-596. Full kinase activity; when associated with F-596 and F-742. Full kinase activity; when associated with F-596 and A-768. 1 Publication
Mutagenesisi742 – 7421Y → F: Full kinase activity; when associated with F-596 and F-602. 1 Publication
Mutagenesisi768 – 7681S → A: Full kinase activity; when associated with F-596 and F-602. 1 Publication

Organism-specific databases

MIMi114500. phenotype.
PharmGKBiPA27819.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 983963Ephrin type-A receptor 3PRO_0000016802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
Modified residuei596 – 5961Phosphotyrosine; by autocatalysis2 Publications
Modified residuei602 – 6021Phosphotyrosine; by autocatalysis2 Publications
Modified residuei701 – 7011Phosphotyrosine; by autocatalysis1 Publication
Modified residuei779 – 7791Phosphotyrosine; by autocatalysis1 Publication
Modified residuei937 – 9371PhosphotyrosineBy similarity

Post-translational modificationi

Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP29320.
PaxDbiP29320.
PRIDEiP29320.

PTM databases

PhosphoSiteiP29320.

Expressioni

Tissue specificityi

Widely expressed. Highest level in placenta.

Gene expression databases

BgeeiP29320.
CleanExiHS_EPHA3.
ExpressionAtlasiP29320. baseline and differential.
GenevestigatoriP29320.

Organism-specific databases

HPAiCAB010462.

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. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling (By similarity). Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation.By similarity5 Publications

Protein-protein interaction databases

BioGridi108356. 18 interactions.
DIPiDIP-40307N.
IntActiP29320. 5 interactions.
MINTiMINT-7145005.
STRINGi9606.ENSP00000337451.

Structurei

Secondary structure

1
983
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni610 – 6123
Helixi618 – 6203
Beta strandi621 – 6299
Beta strandi631 – 64111
Beta strandi647 – 6548
Helixi661 – 67414
Beta strandi685 – 6895
Beta strandi691 – 6944
Beta strandi696 – 7005
Helixi707 – 7126
Turni713 – 7164
Helixi720 – 73920
Helixi749 – 7513
Beta strandi752 – 7543
Beta strandi760 – 7623
Helixi765 – 7673
Helixi788 – 7903
Helixi793 – 7986
Helixi803 – 81816
Turni819 – 8213
Turni824 – 8274
Helixi830 – 8389
Helixi851 – 86010
Helixi865 – 8673
Helixi871 – 88313
Helixi885 – 8895
Beta strandi890 – 8923
Beta strandi898 – 9036

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSFX-ray1.77A577-947[»]
2QO2X-ray1.60A577-947[»]
2QO7X-ray1.60A577-947[»]
2QO9X-ray1.55A577-947[»]
2QOBX-ray1.65A609-947[»]
2QOCX-ray1.25A609-947[»]
2QODX-ray1.15A577-947[»]
2QOFX-ray1.20A577-947[»]
2QOIX-ray1.25A577-947[»]
2QOKX-ray1.20A577-947[»]
2QOLX-ray1.07A577-947[»]
2QONX-ray1.79A577-947[»]
2QOOX-ray1.25A577-947[»]
2QOQX-ray1.60A577-947[»]
3DZQX-ray1.75A609-947[»]
3FXXX-ray1.70A577-947[»]
3FY2X-ray1.80A577-947[»]
4G2FX-ray1.70A609-947[»]
4GK2X-ray2.20A609-947[»]
4GK3X-ray1.90A609-947[»]
4GK4X-ray2.10A609-947[»]
4L0PX-ray2.26A29-201[»]
4P4CX-ray1.60A609-947[»]
4P5QX-ray1.35A606-947[»]
4P5ZX-ray2.00A606-947[»]
ProteinModelPortaliP29320.
SMRiP29320. Positions 26-529, 613-906, 909-975.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29320.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 541521ExtracellularSequence AnalysisAdd
BLAST
Topological domaini566 – 983418CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei542 – 56524HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 207179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini325 – 435111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 53196Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini621 – 882262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini911 – 97565SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi981 – 9833PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi189 – 322134Cys-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.
InParanoidiP29320.
KOiK05104.
OMAiDMKKVGV.
OrthoDBiEOG7VTDM6.
PhylomeDBiP29320.
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.
IPR011510. SAM_2.
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.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P29320-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDCQLSILLL LSCSVLDSFG ELIPQPSNEV NLLDSKTIQG ELGWISYPSH
60 70 80 90 100
GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK
110 120 130 140 150
FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFREHQF TKIDTIAADE
160 170 180 190 200
SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK
210 220 230 240 250
KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW
260 270 280 290 300
LVPIGKCSCN AGYEERGFMC QACRPGFYKA LDGNMKCAKC PPHSSTQEDG
310 320 330 340 350
SMNCRCENNY FRADKDPPSM ACTRPPSSPR NVISNINETS VILDWSWPLD
360 370 380 390 400
TGGRKDVTFN IICKKCGWNI KQCEPCSPNV RFLPRQFGLT NTTVTVTDLL
410 420 430 440 450
AHTNYTFEID AVNGVSELSS PPRQFAAVSI TTNQAAPSPV LTIKKDRTSR
460 470 480 490 500
NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK
510 520 530 540 550
PDTIYVFQIR ARTAAGYGTN SRKFEFETSP DSFSISGESS QVVMIAISAA
560 570 580 590 600
VAIILLTVVI YVLIGRFCGY KSKHGADEKR LHFGNGHLKL PGLRTYVDPH
610 620 630 640 650
TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV
660 670 680 690 700
AIKTLKVGYT EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPVMIVTE
710 720 730 740 750
YMENGSLDSF LRKHDAQFTV IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR
760 770 780 790 800
NILINSNLVC KVSDFGLSRV LEDDPEAAYT TRGGKIPIRW TSPEAIAYRK
810 820 830 840 850
FTSASDVWSY GIVLWEVMSY GERPYWEMSN QDVIKAVDEG YRLPPPMDCP
860 870 880 890 900
AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN
910 920 930 940 950
LLLDQSNVDI TTFRTTGDWL NGVWTAHCKE IFTGVEYSSC DTIAKISTDD
960 970 980
MKKVGVTVVG PQKKIISSIK ALETQSKNGP VPV
Length:983
Mass (Da):110,131
Last modified:October 17, 2006 - v2
Checksum:iBE04DBF958245424
GO
Isoform 2 (identifier: P29320-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     532-539: SFSISGES → CMYYFNAV
     540-983: Missing.

Show »
Length:539
Mass (Da):60,946
Checksum:i14736950EF1153F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti911 – 9111T → S in AAA58633. (PubMed:1311845)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371T → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036086
Natural varianti85 – 851N → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036087
Natural varianti207 – 2071K → N in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 Publication
Corresponds to variant rs200567888 [ dbSNP | Ensembl ].
VAR_068853
Natural varianti229 – 2291S → Y in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_042126
Natural varianti449 – 4491S → F in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_042127
Natural varianti518 – 5181G → L in a lung squamous cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. 1 Publication
VAR_042128
Natural varianti564 – 5641I → V.1 Publication
Corresponds to variant rs55712516 [ dbSNP | Ensembl ].
VAR_042129
Natural varianti568 – 5681C → S.1 Publication
Corresponds to variant rs56077781 [ dbSNP | Ensembl ].
VAR_042130
Natural varianti590 – 5901L → P.1 Publication
Corresponds to variant rs56081642 [ dbSNP | Ensembl ].
VAR_042131
Natural varianti621 – 6211I → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036088
Natural varianti660 – 6601T → K in a lung carcinoma sample; somatic mutation. 1 Publication
VAR_065831
Natural varianti766 – 7661G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042132
Natural varianti777 – 7771A → G.1 Publication
Corresponds to variant rs34437982 [ dbSNP | Ensembl ].
VAR_042133
Natural varianti806 – 8061D → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036089
Natural varianti914 – 9141R → H.1 Publication
Corresponds to variant rs17801309 [ dbSNP | Ensembl ].
VAR_027919
Natural varianti924 – 9241W → R.2 Publications
Corresponds to variant rs35124509 [ dbSNP | Ensembl ].
VAR_042134
Natural varianti933 – 9331T → M in a lung carcinoma sample; somatic mutation. 1 Publication
VAR_065832

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei532 – 5398SFSISGES → CMYYFNAV in isoform 2. 1 PublicationVSP_002995
Alternative sequencei540 – 983444Missing in isoform 2. 1 PublicationVSP_002996Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83941 mRNA. Translation: AAA58633.1.
AF213459 mRNA. Translation: AAG43576.1.
AF213460 mRNA. Translation: AAG43577.1.
CCDSiCCDS2922.1. [P29320-1]
CCDS46875.1. [P29320-2]
PIRiA38224.
RefSeqiNP_005224.2. NM_005233.5. [P29320-1]
NP_872585.1. NM_182644.2. [P29320-2]
UniGeneiHs.123642.

Genome annotation databases

EnsembliENST00000336596; ENSP00000337451; ENSG00000044524. [P29320-1]
ENST00000452448; ENSP00000399926; ENSG00000044524. [P29320-2]
GeneIDi2042.
KEGGihsa:2042.
UCSCiuc003dqx.1. human. [P29320-2]
uc003dqy.3. human. [P29320-1]

Polymorphism databases

DMDMi116241351.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83941 mRNA. Translation: AAA58633.1 .
AF213459 mRNA. Translation: AAG43576.1 .
AF213460 mRNA. Translation: AAG43577.1 .
CCDSi CCDS2922.1. [P29320-1 ]
CCDS46875.1. [P29320-2 ]
PIRi A38224.
RefSeqi NP_005224.2. NM_005233.5. [P29320-1 ]
NP_872585.1. NM_182644.2. [P29320-2 ]
UniGenei Hs.123642.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GSF X-ray 1.77 A 577-947 [» ]
2QO2 X-ray 1.60 A 577-947 [» ]
2QO7 X-ray 1.60 A 577-947 [» ]
2QO9 X-ray 1.55 A 577-947 [» ]
2QOB X-ray 1.65 A 609-947 [» ]
2QOC X-ray 1.25 A 609-947 [» ]
2QOD X-ray 1.15 A 577-947 [» ]
2QOF X-ray 1.20 A 577-947 [» ]
2QOI X-ray 1.25 A 577-947 [» ]
2QOK X-ray 1.20 A 577-947 [» ]
2QOL X-ray 1.07 A 577-947 [» ]
2QON X-ray 1.79 A 577-947 [» ]
2QOO X-ray 1.25 A 577-947 [» ]
2QOQ X-ray 1.60 A 577-947 [» ]
3DZQ X-ray 1.75 A 609-947 [» ]
3FXX X-ray 1.70 A 577-947 [» ]
3FY2 X-ray 1.80 A 577-947 [» ]
4G2F X-ray 1.70 A 609-947 [» ]
4GK2 X-ray 2.20 A 609-947 [» ]
4GK3 X-ray 1.90 A 609-947 [» ]
4GK4 X-ray 2.10 A 609-947 [» ]
4L0P X-ray 2.26 A 29-201 [» ]
4P4C X-ray 1.60 A 609-947 [» ]
4P5Q X-ray 1.35 A 606-947 [» ]
4P5Z X-ray 2.00 A 606-947 [» ]
ProteinModelPortali P29320.
SMRi P29320. Positions 26-529, 613-906, 909-975.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108356. 18 interactions.
DIPi DIP-40307N.
IntActi P29320. 5 interactions.
MINTi MINT-7145005.
STRINGi 9606.ENSP00000337451.

Chemistry

BindingDBi P29320.
ChEMBLi CHEMBL2363043.
GuidetoPHARMACOLOGYi 1823.

PTM databases

PhosphoSitei P29320.

Polymorphism databases

DMDMi 116241351.

Proteomic databases

MaxQBi P29320.
PaxDbi P29320.
PRIDEi P29320.

Protocols and materials databases

DNASUi 2042.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336596 ; ENSP00000337451 ; ENSG00000044524 . [P29320-1 ]
ENST00000452448 ; ENSP00000399926 ; ENSG00000044524 . [P29320-2 ]
GeneIDi 2042.
KEGGi hsa:2042.
UCSCi uc003dqx.1. human. [P29320-2 ]
uc003dqy.3. human. [P29320-1 ]

Organism-specific databases

CTDi 2042.
GeneCardsi GC03P089239.
HGNCi HGNC:3387. EPHA3.
HPAi CAB010462.
MIMi 114500. phenotype.
179611. gene.
neXtProti NX_P29320.
PharmGKBi PA27819.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P29320.
KOi K05104.
OMAi DMKKVGV.
OrthoDBi EOG7VTDM6.
PhylomeDBi P29320.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P29320.

Miscellaneous databases

EvolutionaryTracei P29320.
GeneWikii EPH_receptor_A3.
GenomeRNAii 2042.
NextBioi 8295.
PROi P29320.
SOURCEi Search...

Gene expression databases

Bgeei P29320.
CleanExi HS_EPHA3.
ExpressionAtlasi P29320. baseline and differential.
Genevestigatori P29320.

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.
IPR011510. SAM_2.
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.
PF07647. SAM_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines."
    Wicks I.P., Wilkinson D., Salvaris E., Boyd A.W.
    Proc. Natl. Acad. Sci. U.S.A. 89:1611-1615(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-924.
  2. "Identification of a tumor-specific shared antigen derived from an Eph receptor and presented to CD4 T cells on HLA class II molecules."
    Chiari R., Hames G., Stroobant V., Texier C., Maillere B., Boon T., Coulie P.G.
    Cancer Res. 60:4855-4863(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Melanoma.
  3. "Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell line."
    Boyd A.W., Ward L.D., Wicks I.P., Simpson R.J., Salvaris E., Wilks A., Welch K., Loudovaris M., Rockman S., Busmanis I.
    J. Biol. Chem. 267:3262-3267(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-29 AND 840-860, CHARACTERIZATION.
  4. "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.
  5. "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
    Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
    J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL-CELL ADHESION, EFNA5-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-596; TYR-602 AND TYR-779.
  6. "Dissecting the EphA3/Ephrin-A5 interactions using a novel functional mutagenesis screen."
    Smith F.M., Vearing C., Lackmann M., Treutlein H., Himanen J., Chen K., Saul A., Nikolov D., Boyd A.W.
    J. Biol. Chem. 279:9522-9531(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: EPHRIN LIGAND-BINDING, OLIGOMERIZATION, MUTAGENESIS OF VAL-133 AND PHE-152, INTERACTION WITH CRK.
  7. "Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans."
    Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H., Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., Nikolov D.B.
    Cell 123:291-304(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ADAM10 AND EFNA5.
  8. "Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3."
    Day B., To C., Himanen J.P., Smith F.M., Nikolov D.B., Boyd A.W., Lackmann M.
    J. Biol. Chem. 280:26526-26532(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFNA5 LIGAND-BINDING.
  9. Cited for: INTERACTION WITH PTPN1, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN1, SUBCELLULAR LOCATION.
  10. "Autoregulation by the juxtamembrane region of the human ephrin receptor tyrosine kinase A3 (EphA3)."
    Davis T.L., Walker J.R., Loppnau P., Butler-Cole C., Allali-Hassani A., Dhe-Paganon S.
    Structure 16:873-884(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) OF 577-947 IN COMPLEX WITH ATP ANALOG, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-596; TYR-602 AND TYR-701, MUTAGENESIS OF TYR-596; TYR-602; TYR-742 AND SER-768.
  11. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-37; SER-85; LEU-621 AND ASN-806.
  12. Cited for: VARIANTS LYS-660 AND MET-933.
  13. "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] TYR-229; PHE-449; LEU-518; VAL-564; SER-568; PRO-590; GLU-766; GLY-777; HIS-914 AND ARG-924.
  14. "Mutational profiling of kinases in human tumours of pancreatic origin identifies candidate cancer genes in ductal and ampulla of vater carcinomas."
    Corbo V., Ritelli R., Barbi S., Funel N., Campani D., Bardelli A., Scarpa A.
    PLoS ONE 5:E12653-E12653(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-207.

Entry informationi

Entry nameiEPHA3_HUMAN
AccessioniPrimary (citable) accession number: P29320
Secondary accession number(s): Q9H2V3, Q9H2V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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