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P29322

- EPHA8_HUMAN

UniProt

P29322 - EPHA8_HUMAN

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Protein
Ephrin type-A receptor 8
Gene
EPHA8, EEK, HEK3, KIAA1459
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Receptor tyrosine kinase which binds promiscuously GPI-anchored 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. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth By similarity.

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei667 – 6671ATP By similarity
Active sitei760 – 7601Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi641 – 6499ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. axon guidance Source: UniProtKB
  2. cell adhesion Source: UniProtKB-KW
  3. ephrin receptor signaling pathway Source: UniProtKB
  4. neuron projection development Source: UniProtKB
  5. neuron remodeling Source: UniProtKB
  6. positive regulation of MAPK cascade Source: UniProtKB
  7. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  8. protein autophosphorylation Source: UniProtKB
  9. regulation of cell adhesion Source: UniProtKB
  10. regulation of cell adhesion mediated by integrin Source: UniProtKB
  11. substrate-dependent cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Cell adhesion, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiP29322.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 8 (EC:2.7.10.1)
Alternative name(s):
EPH- and ELK-related kinase
EPH-like kinase 3
Short name:
EK3
Short name:
hEK3
Tyrosine-protein kinase receptor EEK
Gene namesi
Name:EPHA8
Synonyms:EEK, HEK3, KIAA1459
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3391. EPHA8.

Subcellular locationi

Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell projection By similarity. Early endosome membrane By similarity
Note: Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 542515Extracellular Reviewed prediction
Add
BLAST
Transmembranei543 – 56321Helical; Reviewed prediction
Add
BLAST
Topological domaini564 – 1005442Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. early endosome membrane Source: UniProtKB-SubCell
  2. integral component of plasma membrane Source: UniProtKB
  3. neuron projection Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27823.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 1005978Ephrin type-A receptor 8
PRO_0000016822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi340 – 3401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi407 – 4071N-linked (GlcNAc...) Reviewed prediction
Glycosylationi432 – 4321N-linked (GlcNAc...) Reviewed prediction
Modified residuei616 – 6161Phosphotyrosine; by autocatalysis By similarity
Modified residuei839 – 8391Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-616 is critical for association with FYN. Autophosphorylation on Tyr-839 modulates tyrosine kinase activity By similarity.
Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation By similarity.

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP29322.
PRIDEiP29322.

PTM databases

PhosphoSiteiP29322.

Expressioni

Gene expression databases

BgeeiP29322.
CleanExiHS_EPHA8.
GenevestigatoriP29322.

Organism-specific databases

HPAiCAB009660.
HPA031433.

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. May also form heterodimers with other ephrin receptors By similarity. Interacts with FYN; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PIK3CG; regulates integrin-mediated cell adhesion to substrate. Interacts with TIAM1; regulates clathrin-mediated endocytosis of EPHA8. Interacts with ANKS1A and ANKS1B; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination.4 Publications

Protein-protein interaction databases

BioGridi108360. 10 interactions.
IntActiP29322. 5 interactions.
STRINGi9606.ENSP00000166244.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi456 – 4605
Beta strandi472 – 48211
Beta strandi488 – 49912
Beta strandi507 – 5104
Beta strandi512 – 5165
Beta strandi527 – 5304
Helixi632 – 6343
Beta strandi635 – 6439
Turni644 – 6463
Beta strandi647 – 6548
Beta strandi662 – 6698
Helixi675 – 68814
Beta strandi699 – 7035
Helixi705 – 7073
Beta strandi710 – 7145
Helixi721 – 7266
Turni727 – 7304
Helixi734 – 75320
Helixi763 – 7653
Beta strandi766 – 7683
Beta strandi774 – 7763
Helixi802 – 8043
Helixi807 – 8126
Helixi817 – 83216
Turni833 – 8353
Turni838 – 8414
Helixi844 – 8529
Helixi865 – 87410
Helixi879 – 8813
Helixi885 – 89713
Helixi935 – 9417
Helixi945 – 9473
Helixi948 – 9536
Helixi959 – 9624
Helixi967 – 9737
Helixi978 – 99518

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UCVNMR-A933-1000[»]
1X5LNMR-A437-534[»]
3KULX-ray2.15A/B602-909[»]
ProteinModelPortaliP29322.
SMRiP29322. Positions 31-534, 570-901, 926-1000.

Miscellaneous databases

EvolutionaryTraceiP29322.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 209179Eph LBD
Add
BLAST
Domaini328 – 438111Fibronectin type-III 1
Add
BLAST
Domaini439 – 53496Fibronectin type-III 2
Add
BLAST
Domaini635 – 896262Protein kinase
Add
BLAST
Domaini930 – 99465SAM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni564 – 5707Mediates interaction with ANKS1A and ANKS1B By similarity
Regioni589 – 64456Mediates interaction with PIK3CG and required for endocytosis By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1003 – 10053PDZ-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 325135Cys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP29322.
KOiK05109.
OMAiVTTRATV.
OrthoDBiEOG7VTDM6.
PhylomeDBiP29322.
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.
IPR020691. EphrinA_rcpt8.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
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]
PANTHERiPTHR24416:SF274. PTHR24416:SF274. 1 hit.
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. 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.
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: P29322-1) [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

MAPARGRLPP ALWVVTAAAA AATCVSAARG EVNLLDTSTI HGDWGWLTYP     50
AHGWDSINEV DESFQPIHTY QVCNVMSPNQ NNWLRTSWVP RDGARRVYAE 100
IKFTLRDCNS MPGVLGTCKE TFNLYYLESD RDLGASTQES QFLKIDTIAA 150
DESFTGADLG VRRLKLNTEV RSVGPLSKRG FYLAFQDIGA CLAILSLRIY 200
YKKCPAMVRN LAAFSEAVTG ADSSSLVEVR GQCVRHSEER DTPKMYCSAE 250
GEWLVPIGKC VCSAGYEERR DACVACELGF YKSAPGDQLC ARCPPHSHSA 300
APAAQACHCD LSYYRAALDP PSSACTRPPS APVNLISSVN GTSVTLEWAP 350
PLDPGGRSDI TYNAVCRRCP WALSRCEACG SGTRFVPQQT SLVQASLLVA 400
NLLAHMNYSF WIEAVNGVSD LSPEPRRAAV VNITTNQAAP SQVVVIRQER 450
AGQTSVSLLW QEPEQPNGII LEYEIKYYEK DKEMQSYSTL KAVTTRATVS 500
GLKPGTRYVF QVRARTSAGC GRFSQAMEVE TGKPRPRYDT RTIVWICLTL 550
ITGLVVLLLL LICKKRHCGY SKAFQDSDEE KMHYQNGQAP PPVFLPLHHP 600
PGKLPEPQFY AEPHTYEEPG RAGRSFTREI EASRIHIEKI IGSGDSGEVC 650
YGRLRVPGQR DVPVAIKALK AGYTERQRRD FLSEASIMGQ FDHPNIIRLE 700
GVVTRGRLAM IVTEYMENGS LDTFLRTHDG QFTIMQLVGM LRGVGAGMRY 750
LSDLGYVHRD LAARNVLVDS NLVCKVSDFG LSRVLEDDPD AAYTTTGGKI 800
PIRWTAPEAI AFRTFSSASD VWSFGVVMWE VLAYGERPYW NMTNRDVISS 850
VEEGYRLPAP MGCPHALHQL MLDCWHKDRA QRPRFSQIVS VLDALIRSPE 900
SLRATATVSR CPPPAFVRSC FDLRGGSGGG GGLTVGDWLD SIRMGRYRDH 950
FAAGGYSSLG MVLRMNAQDV RALGITLMGH QKKILGSIQT MRAQLTSTQG 1000
PRRHL 1005
Length:1,005
Mass (Da):111,003
Last modified:October 18, 2001 - v2
Checksum:i6FBF85535E4212B3
GO
Isoform 2 (identifier: P29322-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     439-495: APSQVVVIRQ...SYSTLKAVTT → GRRRNSVPQR...DPELEALHCL
     496-1005: Missing.

Note: No experimental confirmation available.

Show »
Length:495
Mass (Da):53,900
Checksum:i6CD3AD67ACBCBCB8
GO

Sequence cautioni

The sequence CAA41980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451G → S.1 Publication
Corresponds to variant rs45498698 [ dbSNP | Ensembl ].
VAR_042153
Natural varianti60 – 601V → L.1 Publication
Corresponds to variant rs56402644 [ dbSNP | Ensembl ].
VAR_042154
Natural varianti123 – 1231N → K in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_042155
Natural varianti179 – 1791R → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042156
Natural varianti198 – 1981R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042157
Natural varianti321 – 3211P → L.
Corresponds to variant rs56656925 [ dbSNP | Ensembl ].
VAR_061292
Natural varianti444 – 4441V → M.
Corresponds to variant rs2295021 [ dbSNP | Ensembl ].
VAR_022107
Natural varianti612 – 6121E → Q.1 Publication
Corresponds to variant rs999765 [ dbSNP | Ensembl ].
VAR_024514
Natural varianti860 – 8601P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_042158

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei439 – 49557APSQV…KAVTT → GRRRNSVPQRPGPPASPASD PSRDQSSAGDVLWAFRQVPL WPCAPHQDPELEALHCL in isoform 2.
VSP_041946Add
BLAST
Alternative sequencei496 – 1005510Missing in isoform 2.
VSP_041947Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371S → L in BAA95983. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL035703 Genomic DNA. Translation: CAB81612.1.
AL035703 Genomic DNA. Translation: CAI22039.1.
BC038796 mRNA. Translation: AAH38796.1.
BC072417 mRNA. Translation: AAH72417.2.
AB040892 mRNA. Translation: BAA95983.1.
X59291 Genomic DNA. Translation: CAA41980.1. Different initiation.
CCDSiCCDS225.1. [P29322-1]
CCDS30626.1. [P29322-2]
PIRiS23361.
RefSeqiNP_001006944.1. NM_001006943.1. [P29322-2]
NP_065387.1. NM_020526.3. [P29322-1]
UniGeneiHs.283613.

Genome annotation databases

EnsembliENST00000166244; ENSP00000166244; ENSG00000070886. [P29322-1]
ENST00000374644; ENSP00000363775; ENSG00000070886. [P29322-2]
ENST00000538803; ENSP00000440274; ENSG00000070886. [P29322-2]
GeneIDi2046.
KEGGihsa:2046.
UCSCiuc001bfw.3. human. [P29322-2]
uc001bfx.1. human. [P29322-1]

Polymorphism databases

DMDMi19857975.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL035703 Genomic DNA. Translation: CAB81612.1 .
AL035703 Genomic DNA. Translation: CAI22039.1 .
BC038796 mRNA. Translation: AAH38796.1 .
BC072417 mRNA. Translation: AAH72417.2 .
AB040892 mRNA. Translation: BAA95983.1 .
X59291 Genomic DNA. Translation: CAA41980.1 . Different initiation.
CCDSi CCDS225.1. [P29322-1 ]
CCDS30626.1. [P29322-2 ]
PIRi S23361.
RefSeqi NP_001006944.1. NM_001006943.1. [P29322-2 ]
NP_065387.1. NM_020526.3. [P29322-1 ]
UniGenei Hs.283613.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UCV NMR - A 933-1000 [» ]
1X5L NMR - A 437-534 [» ]
3KUL X-ray 2.15 A/B 602-909 [» ]
ProteinModelPortali P29322.
SMRi P29322. Positions 31-534, 570-901, 926-1000.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108360. 10 interactions.
IntActi P29322. 5 interactions.
STRINGi 9606.ENSP00000166244.

Chemistry

BindingDBi P29322.
ChEMBLi CHEMBL4134.
GuidetoPHARMACOLOGYi 1828.

PTM databases

PhosphoSitei P29322.

Polymorphism databases

DMDMi 19857975.

Proteomic databases

PaxDbi P29322.
PRIDEi P29322.

Protocols and materials databases

DNASUi 2046.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000166244 ; ENSP00000166244 ; ENSG00000070886 . [P29322-1 ]
ENST00000374644 ; ENSP00000363775 ; ENSG00000070886 . [P29322-2 ]
ENST00000538803 ; ENSP00000440274 ; ENSG00000070886 . [P29322-2 ]
GeneIDi 2046.
KEGGi hsa:2046.
UCSCi uc001bfw.3. human. [P29322-2 ]
uc001bfx.1. human. [P29322-1 ]

Organism-specific databases

CTDi 2046.
GeneCardsi GC01P022890.
HGNCi HGNC:3391. EPHA8.
HPAi CAB009660.
HPA031433.
MIMi 176945. gene.
neXtProti NX_P29322.
PharmGKBi PA27823.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P29322.
KOi K05109.
OMAi VTTRATV.
OrthoDBi EOG7VTDM6.
PhylomeDBi P29322.
TreeFami TF315608.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki P29322.

Miscellaneous databases

EvolutionaryTracei P29322.
GeneWikii EPHA8.
GenomeRNAii 2046.
NextBioi 8315.
PROi P29322.
SOURCEi Search...

Gene expression databases

Bgeei P29322.
CleanExi HS_EPHA8.
Genevestigatori P29322.

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.
IPR020691. EphrinA_rcpt8.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
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 ]
PANTHERi PTHR24416:SF274. PTHR24416:SF274. 1 hit.
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. 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.
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. "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].
  2. "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 2).
    Tissue: Brain and Eye.
  3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-1005 (ISOFORM 1), VARIANT GLN-612.
    Tissue: Brain.
  4. "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 706-726.
  5. "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.
  6. "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity."
    Choi S., Park S.
    Oncogene 18:5413-5422(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYN.
  7. "The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner."
    Gu C., Park S.
    Mol. Cell. Biol. 21:4579-4597(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3CG.
  8. "Identification of phosphotyrosine binding domain-containing proteins as novel downstream targets of the EphA8 signaling function."
    Shin J., Gu C., Park E., Park S.
    Mol. Cell. Biol. 27:8113-8126(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKS1B.
  9. "EphA8-ephrinA5 signaling and clathrin-mediated endocytosis is regulated by Tiam-1, a Rac-specific guanine nucleotide exchange factor."
    Yoo S., Shin J., Park S.
    Mol. Cells 29:603-609(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIAM1.
  10. "Solution structure of the second FN3 domain and of sterile alpha motif (SAM) domain of EPH receptor A8 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 437-534 AND 932-1000.
  11. "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-45; LEU-60; LYS-123; CYS-179; LEU-198 AND LEU-860.

Entry informationi

Entry nameiEPHA8_HUMAN
AccessioniPrimary (citable) accession number: P29322
Secondary accession number(s): Q6IN80
, Q8IUX6, Q9NUA9, Q9P269
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 161 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

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