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P29317

- EPHA2_HUMAN

UniProt

P29317 - EPHA2_HUMAN

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Protein

Ephrin type-A receptor 2

Gene

EPHA2

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-A 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. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.7 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei646 – 6461ATPPROSITE-ProRule annotation
Active sitei739 – 7391Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi619 – 6279ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. activation of Rac GTPase activity Source: UniProtKB
  2. angiogenesis Source: UniProtKB-KW
  3. axial mesoderm formation Source: Ensembl
  4. bone remodeling Source: UniProtKB
  5. branching involved in mammary gland duct morphogenesis Source: UniProtKB
  6. cell adhesion Source: UniProtKB-KW
  7. cell chemotaxis Source: UniProtKB
  8. cell migration Source: UniProtKB
  9. ephrin receptor signaling pathway Source: UniProtKB
  10. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  11. keratinocyte differentiation Source: UniProtKB
  12. lens fiber cell morphogenesis Source: UniProtKB
  13. mammary gland epithelial cell proliferation Source: UniProtKB
  14. multicellular organismal development Source: ProtInc
  15. negative regulation of protein kinase B signaling Source: UniProtKB
  16. neural tube development Source: Ensembl
  17. neuron differentiation Source: Ensembl
  18. notochord cell development Source: Ensembl
  19. notochord formation Source: Ensembl
  20. osteoblast differentiation Source: UniProtKB
  21. osteoclast differentiation Source: UniProtKB
  22. peptidyl-tyrosine phosphorylation Source: GOC
  23. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  24. post-anal tail morphogenesis Source: Ensembl
  25. protein kinase B signaling Source: UniProtKB
  26. regulation of angiogenesis Source: UniProtKB
  27. regulation of blood vessel endothelial cell migration Source: UniProtKB
  28. regulation of cell adhesion mediated by integrin Source: UniProtKB
  29. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  30. regulation of lamellipodium assembly Source: UniProtKB
  31. response to growth factor Source: UniProtKB
  32. skeletal system development Source: Ensembl
  33. vasculogenesis Source: Ensembl
  34. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion, Differentiation, Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiP29317.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 2 (EC:2.7.10.1)
Alternative name(s):
Epithelial cell kinase
Tyrosine-protein kinase receptor ECK
Gene namesi
Name:EPHA2
Synonyms:ECK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3386. EPHA2.

Subcellular locationi

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. focal adhesion Source: UniProtKB
  4. integral component of plasma membrane Source: UniProtKB
  5. leading edge membrane Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Involvement in diseasei

Cataract 6, multiple types (CTRCT6) [MIM:116600]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT6 includes posterior polar and age-related cortical cataracts, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. Age-related cortical cataract is a developmental punctate opacity restricted to the cortex. The cataract is white or cerulean, increases in number with age, but rarely affects vision.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti721 – 7211R → Q in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling. 1 Publication
Corresponds to variant rs116506614 [ dbSNP | Ensembl ].
VAR_062532
Natural varianti940 – 9401T → I in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
VAR_058907
Natural varianti948 – 9481G → W in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
VAR_058908
Overexpressed in several cancer types and promotes malignancy.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031R → E: Significantly reduced response to EFNA1. 1 Publication
Mutagenesisi646 – 6461K → M: Loss of kinase activity. 1 Publication
Mutagenesisi739 – 7391D → N: Increases serum-induced chemotaxis. Loss of EFNA1-dependent regulation of cell migration. 1 Publication
Mutagenesisi897 – 8971S → A or D: Loss of serum-induced phosphorylation by PKB. Loss of serum-induced chemotaxis. 1 Publication

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MIMi116600. phenotype.
Orphaneti98993. Posterior polar cataract.
98994. Total congenital cataract.
PharmGKBiPA27818.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 976953Ephrin type-A receptor 2PRO_0000016800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 188
Disulfide bondi105 ↔ 115
Modified residuei153 – 1531Phosphoserine
Modified residuei373 – 3731Phosphoserine
Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi435 – 4351N-linked (GlcNAc...)1 Publication
Modified residuei570 – 5701Phosphoserine3 Publications
Modified residuei575 – 5751Phosphotyrosine
Modified residuei579 – 5791Phosphoserine1 Publication
Modified residuei587 – 5871Phosphothreonine
Modified residuei588 – 5881Phosphotyrosine; by autocatalysisBy similarity
Modified residuei593 – 5931Phosphothreonine
Modified residuei594 – 5941Phosphotyrosine; by autocatalysis
Modified residuei628 – 6281Phosphotyrosine1 Publication
Modified residuei647 – 6471Phosphothreonine2 Publications
Modified residuei735 – 7351Phosphotyrosine; by autocatalysisBy similarity
Modified residuei771 – 7711Phosphothreonine
Modified residuei772 – 7721Phosphotyrosine; by autocatalysis
Modified residuei790 – 7901Phosphoserine
Modified residuei791 – 7911Phosphotyrosine
Modified residuei869 – 8691Phosphoserine1 Publication
Modified residuei880 – 8801Phosphoserine
Modified residuei892 – 8921Phosphoserine1 Publication
Modified residuei897 – 8971Phosphoserine; by PKB1 Publication
Modified residuei898 – 8981Phosphothreonine
Modified residuei899 – 8991Phosphoserine
Modified residuei901 – 9011Phosphoserine1 Publication
Modified residuei910 – 9101Phosphoserine
Modified residuei921 – 9211Phosphotyrosine; by autocatalysisSequence Analysis
Modified residuei930 – 9301Phosphotyrosine1 Publication
Modified residuei960 – 9601Phosphotyrosine

Post-translational modificationi

Autophosphorylates. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-930 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Dephosphorylated by ACP1.7 Publications
Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP29317.
PaxDbiP29317.
PRIDEiP29317.

PTM databases

PhosphoSiteiP29317.

Expressioni

Tissue specificityi

Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary.1 Publication

Inductioni

Up-regulated by UV irradiation via a TP53-independent, MAPK-dependent mechanism.1 Publication

Gene expression databases

BgeeiP29317.
CleanExiHS_EPHA2.
ExpressionAtlasiP29317. baseline and differential.
GenevestigatoriP29317.

Organism-specific databases

HPAiCAB010464.

Interactioni

Subunit structurei

Homodimer. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration (By similarity). Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation. Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form) with PTPN11; regulates integrin-mediated adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-independent activation of RAC1 which stimulates cell migration. Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight junctions. Interacts with ACP1. Interacts (via SAM domain) with ANKS1A (via SAM domain). Interacts with human herpes virus 8/HHV-8 glycoprotein L/gL and glycoprotein H/gH heterodimer; this interaction triggers EPHA2 phosphorylation and endocytosis, allowing virus entry. Interacts with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EFNA1P208277EBI-702104,EBI-715194
EPHA7Q153753EBI-702104,EBI-1383428
HSP90AB1P082382EBI-702104,EBI-352572
PTK2Q053973EBI-702104,EBI-702142

Protein-protein interaction databases

BioGridi108288. 42 interactions.
DIPiDIP-96N.
IntActiP29317. 16 interactions.
MINTiMINT-3972729.
STRINGi9606.ENSP00000351209.

Structurei

Secondary structure

1
976
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336
Helixi34 – 363
Turni37 – 404
Beta strandi44 – 5714
Beta strandi59 – 624
Beta strandi64 – 696
Beta strandi73 – 764
Beta strandi79 – 824
Beta strandi92 – 10312
Helixi105 – 1073
Beta strandi108 – 1103
Turni112 – 1143
Beta strandi119 – 12810
Helixi136 – 1383
Beta strandi139 – 1457
Beta strandi148 – 1514
Helixi153 – 1575
Beta strandi161 – 17010
Beta strandi175 – 18713
Beta strandi189 – 19911
Beta strandi204 – 2063
Beta strandi209 – 2113
Beta strandi218 – 2214
Beta strandi224 – 2274
Beta strandi238 – 2403
Beta strandi244 – 2474
Beta strandi253 – 2575
Beta strandi266 – 2694
Beta strandi272 – 2754
Beta strandi286 – 2883
Beta strandi295 – 2984
Beta strandi335 – 3384
Beta strandi343 – 3486
Beta strandi361 – 3699
Beta strandi376 – 3783
Beta strandi384 – 3874
Beta strandi389 – 3924
Beta strandi394 – 4007
Beta strandi407 – 4159
Helixi419 – 4213
Beta strandi427 – 4337
Beta strandi441 – 4466
Beta strandi453 – 4575
Turni460 – 4656
Beta strandi467 – 4759
Beta strandi483 – 49311
Beta strandi502 – 5109
Beta strandi522 – 5254
Helixi536 – 55621
Beta strandi557 – 5615
Helixi597 – 6004
Turni601 – 6044
Helixi610 – 6123
Beta strandi613 – 6219
Beta strandi623 – 63210
Beta strandi641 – 6477
Helixi654 – 66714
Beta strandi678 – 6825
Beta strandi684 – 6874
Beta strandi689 – 6935
Helixi700 – 7067
Turni707 – 7093
Helixi713 – 73220
Helixi742 – 7443
Beta strandi745 – 7473
Beta strandi753 – 7553
Helixi781 – 7833
Helixi786 – 7916
Helixi796 – 81116
Turni817 – 8204
Helixi823 – 8319
Helixi844 – 85310
Helixi858 – 8603
Helixi864 – 87310
Helixi878 – 8825
Helixi909 – 9157
Helixi919 – 9213
Helixi922 – 9276
Helixi933 – 9375
Helixi941 – 9466
Helixi952 – 96413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQBX-ray2.30A/B596-900[»]
2E8NNMR-A902-976[»]
2K9YNMR-A/B523-563[»]
2KSONMR-A908-972[»]
2X10X-ray3.00A27-534[»]
2X11X-ray4.83A27-534[»]
3C8XX-ray1.95A23-202[»]
3CZUX-ray2.65A23-202[»]
3FL7X-ray2.50A23-531[»]
3HEIX-ray2.00A/C/E/G/I/K/M/O28-201[»]
3HPNX-ray2.52A/B/C/D/E/F28-201[»]
3KKAX-ray2.40C/D/E903-971[»]
3MBWX-ray2.81A23-326[»]
3MX0X-ray3.51A/C27-435[»]
3SKJX-ray2.50E/F23-202[»]
4P2KX-ray1.50A590-876[»]
4PDOX-ray2.10A/B590-876[»]
4TRLX-ray2.45A590-876[»]
ProteinModelPortaliP29317.
SMRiP29317. Positions 25-528, 555-970.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29317.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 537514ExtracellularSequence AnalysisAdd
BLAST
Topological domaini559 – 976418CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei538 – 55821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 206179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini328 – 432105Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini438 – 52992Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini613 – 875263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini904 – 96865SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 206206Mediates interaction with CLDN4Add
BLAST
Regioni606 – 906301Mediates interaction with ARHGEF16 and ELMO2Add
BLAST
Regioni886 – 97691Negatively regulates interaction with ARHGEF16Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi974 – 9763PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi188 – 325138Cys-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.
InParanoidiP29317.
KOiK05103.
OMAiLVPIGQC.
OrthoDBiEOG7VTDM6.
PhylomeDBiP29317.
TreeFamiTF315608.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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.
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. 1 hit.
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 (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: P29317-1) [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
MELQAARACF ALLWGCALAA AAAAQGKEVV LLDFAAAGGE LGWLTHPYGK
60 70 80 90 100
GWDLMQNIMN DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF
110 120 130 140 150
TVRDCNSFPG GASSCKETFN LYYAESDLDY GTNFQKRLFT KIDTIAPDEI
160 170 180 190 200
TVSSDFEARH VKLNVEERSV GPLTRKGFYL AFQDIGACVA LLSVRVYYKK
210 220 230 240 250
CPELLQGLAH FPETIAGSDA PSLATVAGTC VDHAVVPPGG EEPRMHCAVD
260 270 280 290 300
GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEASESPC LECPEHTLPS
310 320 330 340 350
PEGATSCECE EGFFRAPQDP ASMPCTRPPS APHYLTAVGM GAKVELRWTP
360 370 380 390 400
PQDSGGREDI VYSVTCEQCW PESGECGPCE ASVRYSEPPH GLTRTSVTVS
410 420 430 440 450
DLEPHMNYTF TVEARNGVSG LVTSRSFRTA SVSINQTEPP KVRLEGRSTT
460 470 480 490 500
SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN SYNVRRTEGF SVTLDDLAPD
510 520 530 540 550
TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGNLAVIGG VAVGVVLLLV
560 570 580 590 600
LAGVGFFIHR RRKNQRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA
610 620 630 640 650
VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG MLKTSSGKKE VPVAIKTLKA
660 670 680 690 700
GYTEKQRVDF LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEYMENGAL
710 720 730 740 750
DKFLREKDGE FSVLQLVGML RGIAAGMKYL ANMNYVHRDL AARNILVNSN
760 770 780 790 800
LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP IRWTAPEAIS YRKFTSASDV
810 820 830 840 850
WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM DCPSAIYQLM
860 870 880 890 900
MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG
910 920 930 940 950
SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR
960 970
LPGHQKRIAY SLLGLKDQVN TVGIPI
Length:976
Mass (Da):108,266
Last modified:May 5, 2009 - v2
Checksum:i845D7E1BBCCAACCC
GO
Isoform 2 (identifier: P29317-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     477-497: GDSNSYNVRRTEGFSVTLDDL → VTPRGAGLALAGPTAGDRLVT
     498-976: Missing.

Show »
Length:497
Mass (Da):54,305
Checksum:iEB5CEB75AE01F814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 996IFIELK → NNFELN in AAA53375. (PubMed:2174105)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991K → N.
Corresponds to variant rs1058372 [ dbSNP | Ensembl ].
VAR_055989
Natural varianti391 – 3911G → R.1 Publication
Corresponds to variant rs34192549 [ dbSNP | Ensembl ].
VAR_042121
Natural varianti511 – 5111T → M.1 Publication
Corresponds to variant rs55747232 [ dbSNP | Ensembl ].
VAR_042122
Natural varianti568 – 5681R → H.1 Publication
Corresponds to variant rs56198600 [ dbSNP | Ensembl ].
VAR_042123
Natural varianti631 – 6311M → T.
Corresponds to variant rs34021505 [ dbSNP | Ensembl ].
VAR_055990
Natural varianti721 – 7211R → Q in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling. 1 Publication
Corresponds to variant rs116506614 [ dbSNP | Ensembl ].
VAR_062532
Natural varianti777 – 7771G → S in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042124
Natural varianti876 – 8761R → H.1 Publication
Corresponds to variant rs35903225 [ dbSNP | Ensembl ].
VAR_042125
Natural varianti940 – 9401T → I in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
VAR_058907
Natural varianti948 – 9481G → W in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand. 1 Publication
VAR_058908

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei477 – 49721GDSNS…TLDDL → VTPRGAGLALAGPTAGDRLV T in isoform 2. 1 PublicationVSP_056014Add
BLAST
Alternative sequencei498 – 976479Missing in isoform 2. 1 PublicationVSP_056015Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M59371 mRNA. Translation: AAA53375.1.
EU826606 mRNA. Translation: ACF47642.1.
AL451042 Genomic DNA. Translation: CAH71943.1.
CH471167 Genomic DNA. Translation: EAW51769.1.
BC037166 mRNA. Translation: AAH37166.1.
CCDSiCCDS169.1. [P29317-1]
PIRiA36355.
RefSeqiNP_004422.2. NM_004431.3.
UniGeneiHs.171596.

Genome annotation databases

EnsembliENST00000358432; ENSP00000351209; ENSG00000142627. [P29317-1]
ENST00000611929; ENSP00000484980; ENSG00000142627. [P29317-1]
GeneIDi1969.
KEGGihsa:1969.
UCSCiuc001aya.2. human. [P29317-1]

Polymorphism databases

DMDMi229462861.

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
M59371 mRNA. Translation: AAA53375.1 .
EU826606 mRNA. Translation: ACF47642.1 .
AL451042 Genomic DNA. Translation: CAH71943.1 .
CH471167 Genomic DNA. Translation: EAW51769.1 .
BC037166 mRNA. Translation: AAH37166.1 .
CCDSi CCDS169.1. [P29317-1 ]
PIRi A36355.
RefSeqi NP_004422.2. NM_004431.3.
UniGenei Hs.171596.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MQB X-ray 2.30 A/B 596-900 [» ]
2E8N NMR - A 902-976 [» ]
2K9Y NMR - A/B 523-563 [» ]
2KSO NMR - A 908-972 [» ]
2X10 X-ray 3.00 A 27-534 [» ]
2X11 X-ray 4.83 A 27-534 [» ]
3C8X X-ray 1.95 A 23-202 [» ]
3CZU X-ray 2.65 A 23-202 [» ]
3FL7 X-ray 2.50 A 23-531 [» ]
3HEI X-ray 2.00 A/C/E/G/I/K/M/O 28-201 [» ]
3HPN X-ray 2.52 A/B/C/D/E/F 28-201 [» ]
3KKA X-ray 2.40 C/D/E 903-971 [» ]
3MBW X-ray 2.81 A 23-326 [» ]
3MX0 X-ray 3.51 A/C 27-435 [» ]
3SKJ X-ray 2.50 E/F 23-202 [» ]
4P2K X-ray 1.50 A 590-876 [» ]
4PDO X-ray 2.10 A/B 590-876 [» ]
4TRL X-ray 2.45 A 590-876 [» ]
ProteinModelPortali P29317.
SMRi P29317. Positions 25-528, 555-970.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108288. 42 interactions.
DIPi DIP-96N.
IntActi P29317. 16 interactions.
MINTi MINT-3972729.
STRINGi 9606.ENSP00000351209.

Chemistry

BindingDBi P29317.
ChEMBLi CHEMBL2068.
DrugBanki DB01254. Dasatinib.
DB08896. Regorafenib.
GuidetoPHARMACOLOGYi 1822.

PTM databases

PhosphoSitei P29317.

Polymorphism databases

DMDMi 229462861.

Proteomic databases

MaxQBi P29317.
PaxDbi P29317.
PRIDEi P29317.

Protocols and materials databases

DNASUi 1969.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358432 ; ENSP00000351209 ; ENSG00000142627 . [P29317-1 ]
ENST00000611929 ; ENSP00000484980 ; ENSG00000142627 . [P29317-1 ]
GeneIDi 1969.
KEGGi hsa:1969.
UCSCi uc001aya.2. human. [P29317-1 ]

Organism-specific databases

CTDi 1969.
GeneCardsi GC01M016450.
HGNCi HGNC:3386. EPHA2.
HPAi CAB010464.
MIMi 116600. phenotype.
176946. gene.
neXtProti NX_P29317.
Orphaneti 98993. Posterior polar cataract.
98994. Total congenital cataract.
PharmGKBi PA27818.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P29317.
KOi K05103.
OMAi LVPIGQC.
OrthoDBi EOG7VTDM6.
PhylomeDBi P29317.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P29317.

Miscellaneous databases

EvolutionaryTracei P29317.
GeneWikii EPH_receptor_A2.
GenomeRNAii 1969.
NextBioi 35477785.
PROi P29317.
SOURCEi Search...

Gene expression databases

Bgeei P29317.
CleanExi HS_EPHA2.
ExpressionAtlasi P29317. baseline and differential.
Genevestigatori P29317.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProi IPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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.
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. 1 hit.
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. "cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases."
    Lindberg R.A., Hunter T.
    Mol. Cell. Biol. 10:6316-6324(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
    Tissue: Epithelium.
  2. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
    Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
    Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreas.
  6. "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.
  7. "Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
    Miao H., Burnett E., Kinch M., Simon E., Wang B.
    Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTEGRIN-MEDIATED CELL ADHESION, FUNCTION IN CELL MIGRATION, PHOSPHORYLATION, INTERACTION WITH PTK2/FAK1 AND PTPN11, SUBCELLULAR LOCATION.
  8. "EphA2 overexpression causes tumorigenesis of mammary epithelial cells."
    Zelinski D.P., Zantek N.D., Stewart J.C., Irizarry A.R., Kinch M.S.
    Cancer Res. 61:2301-2306(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ONCOGENICITY.
  9. "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation."
    Kikawa K.D., Vidale D.R., Van Etten R.L., Kinch M.S.
    J. Biol. Chem. 277:39274-39279(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACP1, DEPHOSPHORYLATION BY ACP1.
  10. "EphA2 phosphorylates the cytoplasmic tail of Claudin-4 and mediates paracellular permeability."
    Tanaka M., Kamata R., Sakai R.
    J. Biol. Chem. 280:42375-42382(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL-CELL INTERACTION, INTERACTION WITH CLDN4, MUTAGENESIS OF LYS-646.
  11. "Ephrin-A1 is a negative regulator in glioma through down-regulation of EphA2 and FAK."
    Liu D.-P., Wang Y., Koeffler H.P., Xie D.
    Int. J. Oncol. 30:865-871(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation."
    Zhuang G., Hunter S., Hwang Y., Chen J.
    J. Biol. Chem. 282:2683-2694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPPL1.
  13. "EphA2 is an essential mediator of UV radiation-induced apoptosis."
    Zhang G., Njauw C.-N., Park J.M., Naruse C., Asano M., Tsao H.
    Cancer Res. 68:1691-1696(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, INDUCTION BY UV.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-579 AND THR-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor."
    Wykosky J., Palma E., Gibo D.M., Ringler S., Turner C.P., Debinski W.
    Oncogene 27:7260-7273(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-892 AND SER-901, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "EphA2 mediates ligand-dependent inhibition and ligand-independent promotion of cell migration and invasion via a reciprocal regulatory loop with Akt."
    Miao H., Li D.Q., Mukherjee A., Guo H., Petty A., Cutter J., Basilion J.P., Sedor J., Wu J., Danielpour D., Sloan A.E., Cohen M.L., Wang B.
    Cancer Cell 16:9-20(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-739 AND SER-897, PHOSPHORYLATION AT SER-897 BY PKB.
  18. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-435.
    Tissue: Liver.
  19. "Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis."
    Annamalai B., Liu X., Gopal U., Isaacs J.S.
    Mol. Cancer Res. 7:1021-1032(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY STUB1.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; TYR-628; THR-647 AND SER-869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
    Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
    J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH ARHGEF16; DOCK4 AND ELMO2.
  22. "Ligand targeting of EphA2 enhances keratinocyte adhesion and differentiation via desmoglein 1."
    Lin S., Gordon K., Kaplan N., Getsios S.
    Mol. Biol. Cell 21:3902-3914(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KERATINOCYTE ADHESION AND DIFFERENTIATION, SUBCELLULAR LOCATION.
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor."
    Mercurio F.A., Marasco D., Pirone L., Pedone E.M., Pellecchia M., Leone M.
    Biochemistry 51:2136-2145(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKS1A.
  26. Cited for: INTERACTION WITH HHV-8 GLYCOPROTEIN L/GLYCOPROTEIN H.
  27. "Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration."
    Lee H., Bennett A.M.
    Mol. Cell. Biol. 33:1430-1441(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, PHOSPHORYLATION AT TYR-930, DEPHOSPHORYLATION AT TYR-930 BY PTPRF, INTERACTION WITH NCK1.
  28. "Early insights into the function of KIAA1199, a markedly overexpressed protein in human colorectal tumors."
    Tiwari A., Schneider M., Fiorino A., Haider R., Okoniewski M.J., Roschitzki B., Uzozie A., Menigatti M., Jiricny J., Marra G.
    PLoS ONE 8:E69473-E69473(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEMIP.
  29. "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
    Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
    Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 596-900.
  30. "Solution structure of the C-terminal SAM-domain of EPHAA2: ephrin type-A receptor 2 precursor (EC 2.7.10.1)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 902-976.
  31. "Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex."
    Himanen J.P., Goldgur Y., Miao H., Myshkin E., Guo H., Buck M., Nguyen M., Rajashankar K.R., Wang B., Nikolov D.B.
    EMBO Rep. 10:722-728(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 28-201, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-201 IN COMPLEX WITH EFNA1, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ARG-103.
  32. "Ephrin A1 bound to the ligand binding domain of the human ephrin A2 (EPHA2) receptor protein kinase."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-202, DISULFIDE BOND.
  33. "Left-handed dimer of EPHA2 transmembrane domain helix packing diversity among receptor tyrosine kinases."
    Mayzel M.L., Bocharov E.V., Volynsky P.E., Arseniev A.S.
    Submitted (AUG-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 523-563.
  34. Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 23-202 IN COMPLEX WITH EFNA1, SUBUNIT.
  35. "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] ARG-391; MET-511; HIS-568; SER-777 AND HIS-876.
  36. "The EPHA2 gene is associated with cataracts linked to chromosome 1p."
    Shiels A., Bennett T.M., Knopf H.L.S., Maraini G., Li A., Jiao X., Hejtmancik J.F.
    Mol. Vis. 14:2042-2055(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTRCT6 TRP-948.
  37. "Mutations of the EPHA2 receptor tyrosine kinase gene cause autosomal dominant congenital cataract."
    Zhang T., Hua R., Xiao W., Burdon K.P., Bhattacharya S.S., Craig J.E., Shang D., Zhao X., Mackey D.A., Moore A.T., Luo Y., Zhang J., Zhang X.
    Hum. Mutat. 30:E603-E611(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTRCT6 ILE-940.
  38. Cited for: VARIANT CTRCT6 GLN-721, CHARACTERIZATION OF VARIANT CTRCT6 GLN-721.
  39. "Human cataract mutations in EPHA2 SAM domain alter receptor stability and function."
    Park J.E., Son A.I., Hua R., Wang L., Zhang X., Zhou R.
    PLoS ONE 7:E36564-E36564(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS CTRCT6 ILE-940 AND CTRCT6 TRP-948.

Entry informationi

Entry nameiEPHA2_HUMAN
AccessioniPrimary (citable) accession number: P29317
Secondary accession number(s): B5A968, Q8N3Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 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