P29322 (EPHA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EPHA8
Synonyms:	EEK, HEK3, KIAA1459

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1005 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cell adhesion Neurogenesis
Cellular component	Cell membrane Cell projection Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from sequence or structural similarity. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW 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 mediated by integrin Inferred from sequence or structural similarity. Source: UniProtKB substrate-dependent cell migration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB neuron projection Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 1005

978

Ephrin type-A receptor 8

PRO_0000016822

Regions

Topological domain

28 – 542

515

Extracellular Potential

Transmembrane

543 – 563

21

Helical; Potential

Topological domain

564 – 1005

442

Cytoplasmic Potential

Domain

31 – 209

179

Eph LBD

Domain

328 – 430

103

Fibronectin type-III 1

Domain

436 – 531

96

Fibronectin type-III 2

Domain

635 – 896

262

Protein kinase

Domain

930 – 994

65

SAM

Nucleotide binding

641 – 649

9

ATP By similarity

Region

564 – 570

7

Mediates interaction with ANKS1A and ANKS1B By similarity

Region

589 – 644

56

Mediates interaction with PIK3CG and required for endocytosis By similarity

Motif

1003 – 1005

3

PDZ-binding Potential

Compositional bias

191 – 325

135

Cys-rich

Sites

Active site

760

1

Proton acceptor By similarity

Binding site

667

1

ATP By similarity

Amino acid modifications

Modified residue

616

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

839

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

340

1

N-linked (GlcNAc...) Potential

Glycosylation

407

1

N-linked (GlcNAc...) Potential

Glycosylation

432

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

439 – 495

57

APSQV…KAVTT → GRRRNSVPQRPGPPASPASD PSRDQSSAGDVLWAFRQVPL WPCAPHQDPELEALHCL in isoform 2.

VSP_041946

Alternative sequence

496 – 1005

510

Missing in isoform 2.

VSP_041947

Natural variant

45

1

G → S. Ref.11
Corresponds to variant rs45498698 [ dbSNP | Ensembl ].

VAR_042153

Natural variant

60

1

V → L. Ref.11
Corresponds to variant rs56402644 [ dbSNP | Ensembl ].

VAR_042154

Natural variant

123

1

N → K in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.11

VAR_042155

Natural variant

179

1

R → C in a gastric adenocarcinoma sample; somatic mutation. Ref.11

VAR_042156

Natural variant

198

1

R → L in a lung adenocarcinoma sample; somatic mutation. Ref.11

VAR_042157

Natural variant

321

1

P → L.
Corresponds to variant rs56656925 [ dbSNP | Ensembl ].

VAR_061292

Natural variant

444

1

V → M.
Corresponds to variant rs2295021 [ dbSNP | Ensembl ].

VAR_022107

Natural variant

612

1

E → Q. Ref.3
Corresponds to variant rs999765 [ dbSNP | Ensembl ].

VAR_024514

Natural variant

860

1

P → L in a metastatic melanoma sample; somatic mutation. Ref.11

VAR_042158

Experimental info

Sequence conflict

237

1

S → L in BAA95983. Ref.3

Secondary structure

1

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1005

Helix Strand Turn

Details...

Beta strand

456 – 460

5

Beta strand

472 – 482

11

Beta strand

488 – 499

12

Beta strand

507 – 510

4

Beta strand

512 – 516

5

Beta strand

527 – 530

4

Helix

632 – 634

3

Beta strand

635 – 643

9

Turn

644 – 646

3

Beta strand

647 – 655

9

Beta strand

662 – 669

8

Helix

675 – 688

14

Beta strand

699 – 703

5

Helix

705 – 707

3

Beta strand

710 – 714

5

Helix

721 – 726

6

Turn

728 – 730

3

Helix

734 – 753

20

Helix

763 – 765

3

Beta strand

766 – 768

3

Beta strand

774 – 776

3

Helix

802 – 804

3

Helix

807 – 812

6

Helix

817 – 832

16

Turn

833 – 835

3

Turn

838 – 841

4

Helix

844 – 852

9

Helix

865 – 874

10

Helix

879 – 881

3

Helix

885 – 897

13

Helix

935 – 941

7

Helix

945 – 947

3

Helix

948 – 953

6

Helix

959 – 962

4

Helix

967 – 973

7

Helix

978 – 995

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 18, 2001. Version 2. Checksum: 6FBF85535E4212B3	FASTA	1,005	111,003
	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
	Isoform 2 [UniParc]. Checksum: 6CD3AD67ACBCBCB8	FASTA	495	53,900
	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 VNITTNQAGR RRNSVPQRPG PPASPASDPS RDQSSAGDVL WAFRQVPLWP 490 CAPHQDPELE ALHCL

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.

IPI

IPI00021274.

PIR

S23361.

RefSeq

NP_001006944.1. NM_001006943.1.
NP_065387.1. NM_020526.3.

UniGene

Hs.283613.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P29322.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29322. 4 interactions.

STRING

9606.ENSP00000166244.

PTM databases

PhosphoSite

P29322.

Polymorphism databases

DMDM

19857975.

Proteomic databases

PaxDb

P29322.

PRIDE

P29322.

Protocols and materials databases

DNASU

2046.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000166244; ENSP00000166244; ENSG00000070886.
ENST00000374644; ENSP00000363775; ENSG00000070886.
ENST00000538803; ENSP00000440274; ENSG00000070886.

GeneID

2046.

KEGG

hsa:2046.

UCSC

uc001bfx.1. human.

Organism-specific databases

CTD

2046.

GeneCards

GC01P022890.

HGNC

HGNC:3391. EPHA8.

HPA

CAB009660.
HPA031433.

MIM

176945. gene.

neXtProt

NX_P29322.

PharmGKB

PA27823.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233856.

HOVERGEN

HBG062180.

InParanoid

P29322.

KO

K05109.

OMA

VTTRATV.

OrthoDB

EOG4MCWZJ.

PhylomeDB

P29322.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

epha_fwdpathway. EPHA forward signaling.
ephrina_ephapathway. EphrinA-EPHA pathway.

Gene expression databases

Bgee

P29322.

CleanEx

HS_EPHA8.

Genevestigator

P29322.

GermOnline

ENSG00000070886. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
2.60.40.10. 2 hits.

InterPro

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_cat_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]

PANTHER

PTHR24416:SF23. PTHR24416:SF23. 1 hit.

Pfam

PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000666. TyrPK_ephrin_receptor. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.
SSF49785. Gal_bind_like. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.

PROSITE

PS01186. EGF_2. 1 hit. Uncertain.
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]

ProtoNet

Search...

Other

BindingDB

P29322.

ChEMBL

CHEMBL4134.

EvolutionaryTrace

P29322.

GenomeRNAi

2046.

NextBio

8315.

SOURCE

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Entry information

Entry name

EPHA8_HUMAN

Accession

Primary (citable) accession number: P29322
Secondary accession number(s): Q6IN80 , Q8IUX6, Q9NUA9, Q9P269

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 18, 2001
Last modified:	May 1, 2013
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.