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P29322 (EPHA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EPHA8
Synonyms:EEK, HEK3, KIAA1459
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1005 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

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.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Neurogenesis
   Cellular componentCell membrane
Cell projection
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

neuron remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: UniProtKB

substrate-dependent cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentearly endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GPI-linked ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29322-1)

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.
Isoform 2 (identifier: P29322-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 1005978Ephrin type-A receptor 8
PRO_0000016822

Regions

Topological domain28 – 542515Extracellular Potential
Transmembrane543 – 56321Helical; Potential
Topological domain564 – 1005442Cytoplasmic Potential
Domain31 – 209179Eph LBD
Domain328 – 438111Fibronectin type-III 1
Domain439 – 53496Fibronectin type-III 2
Domain635 – 896262Protein kinase
Domain930 – 99465SAM
Nucleotide binding641 – 6499ATP By similarity
Region564 – 5707Mediates interaction with ANKS1A and ANKS1B By similarity
Region589 – 64456Mediates interaction with PIK3CG and required for endocytosis By similarity
Motif1003 – 10053PDZ-binding Potential
Compositional bias191 – 325135Cys-rich

Sites

Active site7601Proton acceptor By similarity
Binding site6671ATP By similarity

Amino acid modifications

Modified residue6161Phosphotyrosine; by autocatalysis By similarity
Modified residue8391Phosphotyrosine; by autocatalysis By similarity
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence439 – 49557APSQV…KAVTT → GRRRNSVPQRPGPPASPASD PSRDQSSAGDVLWAFRQVPL WPCAPHQDPELEALHCL in isoform 2.
VSP_041946
Alternative sequence496 – 1005510Missing in isoform 2.
VSP_041947
Natural variant451G → S. Ref.11
Corresponds to variant rs45498698 [ dbSNP | Ensembl ].
VAR_042153
Natural variant601V → L. Ref.11
Corresponds to variant rs56402644 [ dbSNP | Ensembl ].
VAR_042154
Natural variant1231N → K in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.11
VAR_042155
Natural variant1791R → C in a gastric adenocarcinoma sample; somatic mutation. Ref.11
VAR_042156
Natural variant1981R → L in a lung adenocarcinoma sample; somatic mutation. Ref.11
VAR_042157
Natural variant3211P → L.
Corresponds to variant rs56656925 [ dbSNP | Ensembl ].
VAR_061292
Natural variant4441V → M.
Corresponds to variant rs2295021 [ dbSNP | Ensembl ].
VAR_022107
Natural variant6121E → Q. Ref.3
Corresponds to variant rs999765 [ dbSNP | Ensembl ].
VAR_024514
Natural variant8601P → L in a metastatic melanoma sample; somatic mutation. Ref.11
VAR_042158

Experimental info

Sequence conflict2371S → L in BAA95983. Ref.3

Secondary structure

.................................................................. 1005
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 6FBF85535E4212B3

FASTA1,005111,003
        10         20         30         40         50         60 
MAPARGRLPP ALWVVTAAAA AATCVSAARG EVNLLDTSTI HGDWGWLTYP AHGWDSINEV 

        70         80         90        100        110        120 
DESFQPIHTY QVCNVMSPNQ NNWLRTSWVP RDGARRVYAE IKFTLRDCNS MPGVLGTCKE 

       130        140        150        160        170        180 
TFNLYYLESD RDLGASTQES QFLKIDTIAA DESFTGADLG VRRLKLNTEV RSVGPLSKRG 

       190        200        210        220        230        240 
FYLAFQDIGA CLAILSLRIY YKKCPAMVRN LAAFSEAVTG ADSSSLVEVR GQCVRHSEER 

       250        260        270        280        290        300 
DTPKMYCSAE GEWLVPIGKC VCSAGYEERR DACVACELGF YKSAPGDQLC ARCPPHSHSA 

       310        320        330        340        350        360 
APAAQACHCD LSYYRAALDP PSSACTRPPS APVNLISSVN GTSVTLEWAP PLDPGGRSDI 

       370        380        390        400        410        420 
TYNAVCRRCP WALSRCEACG SGTRFVPQQT SLVQASLLVA NLLAHMNYSF WIEAVNGVSD 

       430        440        450        460        470        480 
LSPEPRRAAV VNITTNQAAP SQVVVIRQER AGQTSVSLLW QEPEQPNGII LEYEIKYYEK 

       490        500        510        520        530        540 
DKEMQSYSTL KAVTTRATVS GLKPGTRYVF QVRARTSAGC GRFSQAMEVE TGKPRPRYDT 

       550        560        570        580        590        600 
RTIVWICLTL ITGLVVLLLL LICKKRHCGY SKAFQDSDEE KMHYQNGQAP PPVFLPLHHP 

       610        620        630        640        650        660 
PGKLPEPQFY AEPHTYEEPG RAGRSFTREI EASRIHIEKI IGSGDSGEVC YGRLRVPGQR 

       670        680        690        700        710        720 
DVPVAIKALK AGYTERQRRD FLSEASIMGQ FDHPNIIRLE GVVTRGRLAM IVTEYMENGS 

       730        740        750        760        770        780 
LDTFLRTHDG QFTIMQLVGM LRGVGAGMRY LSDLGYVHRD LAARNVLVDS NLVCKVSDFG 

       790        800        810        820        830        840 
LSRVLEDDPD AAYTTTGGKI PIRWTAPEAI AFRTFSSASD VWSFGVVMWE VLAYGERPYW 

       850        860        870        880        890        900 
NMTNRDVISS VEEGYRLPAP MGCPHALHQL MLDCWHKDRA QRPRFSQIVS VLDALIRSPE 

       910        920        930        940        950        960 
SLRATATVSR CPPPAFVRSC FDLRGGSGGG GGLTVGDWLD SIRMGRYRDH FAAGGYSSLG 

       970        980        990       1000 
MVLRMNAQDV RALGITLMGH QKKILGSIQT MRAQLTSTQG PRRHL 

« Hide

Isoform 2 [UniParc].

Checksum: 6CD3AD67ACBCBCB8
Show »

FASTA49553,900

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS225.1. [P29322-1]
CCDS30626.1. [P29322-2]
PIRS23361.
RefSeqNP_001006944.1. NM_001006943.1. [P29322-2]
NP_065387.1. NM_020526.3. [P29322-1]
UniGeneHs.283613.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UCVNMR-A933-1000[»]
1X5LNMR-A437-534[»]
3KULX-ray2.15A/B602-909[»]
ProteinModelPortalP29322.
SMRP29322. Positions 31-534, 570-901, 926-1000.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108360. 10 interactions.
IntActP29322. 5 interactions.
STRING9606.ENSP00000166244.

Chemistry

BindingDBP29322.
ChEMBLCHEMBL4134.
GuidetoPHARMACOLOGY1828.

PTM databases

PhosphoSiteP29322.

Polymorphism databases

DMDM19857975.

Proteomic databases

PaxDbP29322.
PRIDEP29322.

Protocols and materials databases

DNASU2046.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000166244; ENSP00000166244; ENSG00000070886. [P29322-1]
ENST00000374644; ENSP00000363775; ENSG00000070886. [P29322-2]
ENST00000538803; ENSP00000440274; ENSG00000070886. [P29322-2]
GeneID2046.
KEGGhsa:2046.
UCSCuc001bfw.3. human. [P29322-2]
uc001bfx.1. human. [P29322-1]

Organism-specific databases

CTD2046.
GeneCardsGC01P022890.
HGNCHGNC:3391. EPHA8.
HPACAB009660.
HPA031433.
MIM176945. gene.
neXtProtNX_P29322.
PharmGKBPA27823.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP29322.
KOK05109.
OMAVTTRATV.
OrthoDBEOG7VTDM6.
PhylomeDBP29322.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP29322.

Gene expression databases

BgeeP29322.
CleanExHS_EPHA8.
GenevestigatorP29322.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. 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]
PANTHERPTHR24416:SF274. PTHR24416:SF274. 1 hit.
PfamPF14575. 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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS01186. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP29322.
GeneWikiEPHA8.
GenomeRNAi2046.
NextBio8315.
PROP29322.
SOURCESearch...

Entry information

Entry nameEPHA8_HUMAN
AccessionPrimary (citable) accession number: P29322
Secondary accession number(s): Q6IN80 expand/collapse secondary AC list , Q8IUX6, Q9NUA9, Q9P269
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM