Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ephrin type-A receptor 8

Gene

EPHA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei667ATPPROSITE-ProRule annotation1
Active sitei760Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi641 – 649ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:HS01017-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP29322.
SIGNORiP29322.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3391. EPHA8.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • 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)DescriptionActionsGraphical viewLength
Topological domaini28 – 542ExtracellularSequence analysisAdd BLAST515
Transmembranei543 – 563HelicalSequence analysisAdd BLAST21
Topological domaini564 – 1005CytoplasmicSequence analysisAdd BLAST442

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2046.
OpenTargetsiENSG00000070886.
PharmGKBiPA27823.

Chemistry databases

ChEMBLiCHEMBL4134.
GuidetoPHARMACOLOGYi1828.

Polymorphism and mutation databases

BioMutaiEPHA8.
DMDMi19857975.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001682228 – 1005Ephrin type-A receptor 8Add BLAST978

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi407N-linked (GlcNAc...)Sequence analysis1
Glycosylationi432N-linked (GlcNAc...)Sequence analysis1
Modified residuei616Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei839Phosphotyrosine; by autocatalysisBy similarity1

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).By similarity
Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP29322.
PaxDbiP29322.
PeptideAtlasiP29322.
PRIDEiP29322.

PTM databases

iPTMnetiP29322.
PhosphoSitePlusiP29322.

Expressioni

Gene expression databases

BgeeiENSG00000070886.
CleanExiHS_EPHA8.
GenevisibleiP29322. HS.

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.By similarity4 Publications

Protein-protein interaction databases

BioGridi108360. 12 interactors.
IntActiP29322. 7 interactors.
STRINGi9606.ENSP00000166244.

Chemistry databases

BindingDBiP29322.

Structurei

Secondary structure

11005
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi456 – 460Combined sources5
Beta strandi472 – 482Combined sources11
Beta strandi488 – 499Combined sources12
Beta strandi507 – 510Combined sources4
Beta strandi512 – 516Combined sources5
Beta strandi527 – 530Combined sources4
Helixi632 – 634Combined sources3
Beta strandi635 – 643Combined sources9
Turni644 – 646Combined sources3
Beta strandi647 – 654Combined sources8
Beta strandi662 – 669Combined sources8
Helixi675 – 688Combined sources14
Beta strandi699 – 703Combined sources5
Helixi705 – 707Combined sources3
Beta strandi710 – 714Combined sources5
Helixi721 – 726Combined sources6
Turni727 – 730Combined sources4
Helixi734 – 753Combined sources20
Helixi763 – 765Combined sources3
Beta strandi766 – 768Combined sources3
Beta strandi774 – 776Combined sources3
Helixi802 – 804Combined sources3
Helixi807 – 812Combined sources6
Helixi817 – 832Combined sources16
Turni833 – 835Combined sources3
Turni838 – 841Combined sources4
Helixi844 – 852Combined sources9
Helixi865 – 874Combined sources10
Helixi879 – 881Combined sources3
Helixi885 – 897Combined sources13
Helixi935 – 941Combined sources7
Helixi945 – 947Combined sources3
Helixi948 – 953Combined sources6
Helixi959 – 962Combined sources4
Helixi967 – 973Combined sources7
Helixi978 – 995Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UCVNMR-A933-1000[»]
1X5LNMR-A437-534[»]
3KULX-ray2.15A/B602-909[»]
ProteinModelPortaliP29322.
SMRiP29322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29322.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 209Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini328 – 438Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini439 – 534Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini635 – 896Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini930 – 994SAMPROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni564 – 570Mediates interaction with ANKS1A and ANKS1BBy similarity7
Regioni589 – 644Mediates interaction with PIK3CG and required for endocytosisBy similarityAdd BLAST56

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1003 – 1005PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi191 – 325Cys-richAdd BLAST135

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

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP29322.
KOiK05109.
OMAiEPHNYEE.
OrthoDBiEOG091G00W0.
PhylomeDBiP29322.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
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.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PANTHERiPTHR24416:SF339. PTHR24416:SF339. 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.
SM01411. Ephrin_rec_like. 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. AlignAdd to basket

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

        10         20         30         40         50
MAPARGRLPP ALWVVTAAAA AATCVSAARG EVNLLDTSTI HGDWGWLTYP
60 70 80 90 100
AHGWDSINEV DESFQPIHTY QVCNVMSPNQ NNWLRTSWVP RDGARRVYAE
110 120 130 140 150
IKFTLRDCNS MPGVLGTCKE TFNLYYLESD RDLGASTQES QFLKIDTIAA
160 170 180 190 200
DESFTGADLG VRRLKLNTEV RSVGPLSKRG FYLAFQDIGA CLAILSLRIY
210 220 230 240 250
YKKCPAMVRN LAAFSEAVTG ADSSSLVEVR GQCVRHSEER DTPKMYCSAE
260 270 280 290 300
GEWLVPIGKC VCSAGYEERR DACVACELGF YKSAPGDQLC ARCPPHSHSA
310 320 330 340 350
APAAQACHCD LSYYRAALDP PSSACTRPPS APVNLISSVN GTSVTLEWAP
360 370 380 390 400
PLDPGGRSDI TYNAVCRRCP WALSRCEACG SGTRFVPQQT SLVQASLLVA
410 420 430 440 450
NLLAHMNYSF WIEAVNGVSD LSPEPRRAAV VNITTNQAAP SQVVVIRQER
460 470 480 490 500
AGQTSVSLLW QEPEQPNGII LEYEIKYYEK DKEMQSYSTL KAVTTRATVS
510 520 530 540 550
GLKPGTRYVF QVRARTSAGC GRFSQAMEVE TGKPRPRYDT RTIVWICLTL
560 570 580 590 600
ITGLVVLLLL LICKKRHCGY SKAFQDSDEE KMHYQNGQAP PPVFLPLHHP
610 620 630 640 650
PGKLPEPQFY AEPHTYEEPG RAGRSFTREI EASRIHIEKI IGSGDSGEVC
660 670 680 690 700
YGRLRVPGQR DVPVAIKALK AGYTERQRRD FLSEASIMGQ FDHPNIIRLE
710 720 730 740 750
GVVTRGRLAM IVTEYMENGS LDTFLRTHDG QFTIMQLVGM LRGVGAGMRY
760 770 780 790 800
LSDLGYVHRD LAARNVLVDS NLVCKVSDFG LSRVLEDDPD AAYTTTGGKI
810 820 830 840 850
PIRWTAPEAI AFRTFSSASD VWSFGVVMWE VLAYGERPYW NMTNRDVISS
860 870 880 890 900
VEEGYRLPAP MGCPHALHQL MLDCWHKDRA QRPRFSQIVS VLDALIRSPE
910 920 930 940 950
SLRATATVSR CPPPAFVRSC FDLRGGSGGG GGLTVGDWLD SIRMGRYRDH
960 970 980 990 1000
FAAGGYSSLG MVLRMNAQDV RALGITLMGH QKKILGSIQT MRAQLTSTQG

PRRHL
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti237S → L in BAA95983 (PubMed:10819331).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04215345G → S.1 PublicationCorresponds to variant rs45498698dbSNPEnsembl.1
Natural variantiVAR_04215460V → L.1 PublicationCorresponds to variant rs56402644dbSNPEnsembl.1
Natural variantiVAR_042155123N → K in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042156179R → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042157198R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_061292321P → L.Corresponds to variant rs56656925dbSNPEnsembl.1
Natural variantiVAR_022107444V → M.Corresponds to variant rs2295021dbSNPEnsembl.1
Natural variantiVAR_024514612E → Q.1 PublicationCorresponds to variant rs999765dbSNPEnsembl.1
Natural variantiVAR_042158860P → L in a metastatic melanoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041946439 – 495APSQV…KAVTT → GRRRNSVPQRPGPPASPASD PSRDQSSAGDVLWAFRQVPL WPCAPHQDPELEALHCL in isoform 2. 1 PublicationAdd BLAST57
Alternative sequenceiVSP_041947496 – 1005Missing in isoform 2. 1 PublicationAdd BLAST510

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001006943.2. [P29322-2]
NP_065387.1. NM_020526.4. [P29322-1]
UniGeneiHs.283613.

Genome annotation databases

EnsembliENST00000166244; ENSP00000166244; ENSG00000070886. [P29322-1]
ENST00000374644; ENSP00000363775; ENSG00000070886. [P29322-2]
GeneIDi2046.
KEGGihsa:2046.
UCSCiuc001bfw.4. human. [P29322-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001006943.2. [P29322-2]
NP_065387.1. NM_020526.4. [P29322-1]
UniGeneiHs.283613.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UCVNMR-A933-1000[»]
1X5LNMR-A437-534[»]
3KULX-ray2.15A/B602-909[»]
ProteinModelPortaliP29322.
SMRiP29322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108360. 12 interactors.
IntActiP29322. 7 interactors.
STRINGi9606.ENSP00000166244.

Chemistry databases

BindingDBiP29322.
ChEMBLiCHEMBL4134.
GuidetoPHARMACOLOGYi1828.

PTM databases

iPTMnetiP29322.
PhosphoSitePlusiP29322.

Polymorphism and mutation databases

BioMutaiEPHA8.
DMDMi19857975.

Proteomic databases

MaxQBiP29322.
PaxDbiP29322.
PeptideAtlasiP29322.
PRIDEiP29322.

Protocols and materials databases

DNASUi2046.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000166244; ENSP00000166244; ENSG00000070886. [P29322-1]
ENST00000374644; ENSP00000363775; ENSG00000070886. [P29322-2]
GeneIDi2046.
KEGGihsa:2046.
UCSCiuc001bfw.4. human. [P29322-1]

Organism-specific databases

CTDi2046.
DisGeNETi2046.
GeneCardsiEPHA8.
HGNCiHGNC:3391. EPHA8.
HPAiCAB009660.
HPA031433.
MIMi176945. gene.
neXtProtiNX_P29322.
OpenTargetsiENSG00000070886.
PharmGKBiPA27823.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP29322.
KOiK05109.
OMAiEPHNYEE.
OrthoDBiEOG091G00W0.
PhylomeDBiP29322.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS01017-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP29322.
SIGNORiP29322.

Miscellaneous databases

EvolutionaryTraceiP29322.
GeneWikiiEPHA8.
GenomeRNAii2046.
PROiP29322.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000070886.
CleanExiHS_EPHA8.
GenevisibleiP29322. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
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.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PANTHERiPTHR24416:SF339. PTHR24416:SF339. 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.
SM01411. Ephrin_rec_like. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.