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Protein

Ephrin type-A receptor 1

Gene

EPHA1

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 membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei656ATPPROSITE-ProRule annotation1
Active sitei749Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi630 – 638ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  • activation of GTPase activity Source: UniProtKB
  • angiogenesis Source: UniProtKB-KW
  • cell surface receptor signaling pathway Source: UniProtKB
  • ephrin receptor signaling pathway Source: Reactome
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of protein kinase activity Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell-matrix adhesion Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • somatic stem cell population maintenance Source: Reactome
  • substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Cell adhesion

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07379-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-2892247. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP21709.
SIGNORiP21709.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 1 (EC:2.7.10.1)
Short name:
hEpha1
Alternative name(s):
EPH tyrosine kinase
EPH tyrosine kinase 1
Erythropoietin-producing hepatoma receptor
Tyrosine-protein kinase receptor EPH
Gene namesi
Name:EPHA1
Synonyms:EPH, EPHT, EPHT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:3385. EPHA1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 547ExtracellularSequence analysisAdd BLAST522
Transmembranei548 – 568HelicalSequence analysisAdd BLAST21
Topological domaini569 – 976CytoplasmicSequence analysisAdd BLAST408

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2041.
OpenTargetsiENSG00000146904.
PharmGKBiPA27817.

Chemistry databases

ChEMBLiCHEMBL5810.
GuidetoPHARMACOLOGYi1821.

Polymorphism and mutation databases

BioMutaiEPHA1.
DMDMi317373566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000001679826 – 976Ephrin type-A receptor 1Add BLAST951

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi414N-linked (GlcNAc...)Sequence analysis1
Modified residuei599Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei605Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei781Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei906PhosphoserineCombined sources1
Modified residuei910PhosphoserineCombined sources1
Modified residuei930Phosphotyrosine; by autocatalysisSequence analysis1

Post-translational modificationi

Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1.
Ubiquitinated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP21709.
MaxQBiP21709.
PaxDbiP21709.
PeptideAtlasiP21709.
PRIDEiP21709.

PTM databases

iPTMnetiP21709.
PhosphoSitePlusiP21709.

Expressioni

Tissue specificityi

Overexpressed in several carcinomas.

Gene expression databases

BgeeiENSG00000146904.
CleanExiHS_EPHA1.
GenevisibleiP21709. HS.

Organism-specific databases

HPAiCAB026144.

Interactioni

Subunit structurei

Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration. Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by EFNA1 but independent of the kinase activity of EPHA1. Interacts (kinase activity-dependent) with PTK2/FAK1.2 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108355. 69 interactors.
DIPiDIP-34886N.
IntActiP21709. 6 interactors.
STRINGi9606.ENSP00000275815.

Chemistry databases

BindingDBiP21709.

Structurei

Secondary structure

1976
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi538 – 540Combined sources3
Helixi545 – 570Combined sources26
Helixi918 – 924Combined sources7
Helixi928 – 930Combined sources3
Helixi931 – 936Combined sources6
Helixi942 – 945Combined sources4
Helixi950 – 955Combined sources6
Helixi961 – 973Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K1KNMR-A/B536-573[»]
2K1LNMR-A/B536-573[»]
3HILX-ray2.00A/B911-974[»]
3KKAX-ray2.40A/B911-974[»]
ProteinModelPortaliP21709.
SMRiP21709.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21709.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 209Eph LBDPROSITE-ProRule annotationAdd BLAST183
Domaini332 – 445Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST114
Domaini447 – 538Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST92
Domaini624 – 884Protein kinasePROSITE-ProRule annotationAdd BLAST261
Domaini913 – 976SAMPROSITE-ProRule annotationAdd BLAST64

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi974 – 976PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi191 – 329Cys-richAdd BLAST139

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.
InParanoidiP21709.
KOiK05102.
OMAiQAYEDPA.
OrthoDBiEOG091G00W0.
PhylomeDBiP21709.
TreeFamiTF315363.

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.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
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]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 1 hit.
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.
SSF57184. SSF57184. 2 hits.
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 (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P21709-1) [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
MERRWPLGLG LVLLLCAPLP PGARAKEVTL MDTSKAQGEL GWLLDPPKDG
60 70 80 90 100
WSEQQQILNG TPLYMYQDCP MQGRRDTDHW LRSNWIYRGE EASRVHVELQ
110 120 130 140 150
FTVRDCKSFP GGAGPLGCKE TFNLLYMESD QDVGIQLRRP LFQKVTTVAA
160 170 180 190 200
DQSFTIRDLV SGSVKLNVER CSLGRLTRRG LYLAFHNPGA CVALVSVRVF
210 220 230 240 250
YQRCPETLNG LAQFPDTLPG PAGLVEVAGT CLPHARASPR PSGAPRMHCS
260 270 280 290 300
PDGEWLVPVG RCHCEPGYEE GGSGEACVAC PSGSYRMDMD TPHCLTCPQQ
310 320 330 340 350
STAESEGATI CTCESGHYRA PGEGPQVACT GPPSAPRNLS FSASGTQLSL
360 370 380 390 400
RWEPPADTGG RQDVRYSVRC SQCQGTAQDG GPCQPCGVGV HFSPGARGLT
410 420 430 440 450
TPAVHVNGLE PYANYTFNVE AQNGVSGLGS SGHASTSVSI SMGHAESLSG
460 470 480 490 500
LSLRLVKKEP RQLELTWAGS RPRSPGANLT YELHVLNQDE ERYQMVLEPR
510 520 530 540 550
VLLTELQPDT TYIVRVRMLT PLGPGPFSPD HEFRTSPPVS RGLTGGEIVA
560 570 580 590 600
VIFGLLLGAA LLLGILVFRS RRAQRQRQQR QRDRATDVDR EDKLWLKPYV
610 620 630 640 650
DLQAYEDPAQ GALDFTRELD PAWLMVDTVI GEGEFGEVYR GTLRLPSQDC
660 670 680 690 700
KTVAIKTLKD TSPGGQWWNF LREATIMGQF SHPHILHLEG VVTKRKPIMI
710 720 730 740 750
ITEFMENGAL DAFLREREDQ LVPGQLVAML QGIASGMNYL SNHNYVHRDL
760 770 780 790 800
AARNILVNQN LCCKVSDFGL TRLLDDFDGT YETQGGKIPI RWTAPEAIAH
810 820 830 840 850
RIFTTASDVW SFGIVMWEVL SFGDKPYGEM SNQEVMKSIE DGYRLPPPVD
860 870 880 890 900
CPAPLYELMK NCWAYDRARR PHFQKLQAHL EQLLANPHSL RTIANFDPRM
910 920 930 940 950
TLRLPSLSGS DGIPYRTVSE WLESIRMKRY ILHFHSAGLD TMECVLELTA
960 970
EDLTQMGITL PGHQKRILCS IQGFKD
Length:976
Mass (Da):108,127
Last modified:January 11, 2011 - v4
Checksum:i91EFCA69FFE17826
GO
Isoform 2 (identifier: P21709-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-490: ESLSGLSLRL...YELHVLNQDE → DPTLSLWTPR...APKPWGEPDL
     491-976: Missing.

Show »
Length:490
Mass (Da):52,618
Checksum:iC7BF2D396EE54F05
GO
Isoform 3 (identifier: P21709-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-474: ESLSGLSLRLVKKEPRQLELTWAGSRPRS → GERLRGAGTGTWWRQKGLRPQNKLMGRKP
     475-976: Missing.

Show »
Length:474
Mass (Da):51,069
Checksum:i6D263B013A90E9B5
GO

Sequence cautioni

The sequence AAA36747 differs from that shown. Reason: Frameshift at positions 582, 595 and 601.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti398G → A in AAD43440 (PubMed:10369740).Curated1
Sequence conflicti398G → A in CAA81796 (Ref. 8) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028265160V → A.6 PublicationsCorresponds to variant rs4725617dbSNPEnsembl.1
Natural variantiVAR_042115351R → C.1 PublicationCorresponds to variant rs56006153dbSNPEnsembl.1
Natural variantiVAR_028266492R → Q.1 PublicationCorresponds to variant rs11768549dbSNPEnsembl.1
Natural variantiVAR_042116575R → Q.1 PublicationCorresponds to variant rs35719334dbSNPEnsembl.1
Natural variantiVAR_042117585A → T.1 PublicationCorresponds to variant rs34178823dbSNPEnsembl.1
Natural variantiVAR_042118697P → L.1 PublicationCorresponds to variant rs34372369dbSNPEnsembl.1
Natural variantiVAR_042119703E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042120807S → R.1 PublicationCorresponds to variant rs56244405dbSNPEnsembl.1
Natural variantiVAR_028267900M → V.Combined sources7 PublicationsCorresponds to variant rs6967117dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056010446 – 490ESLSG…LNQDE → DPTLSLWTPRVTVRPVSETG EERTEATRADLGGVPAPKPW GEPDL in isoform 2. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_056011446 – 474ESLSG…SRPRS → GERLRGAGTGTWWRQKGLRP QNKLMGRKP in isoform 3. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_056012475 – 976Missing in isoform 3. 1 PublicationAdd BLAST502
Alternative sequenceiVSP_056013491 – 976Missing in isoform 2. 1 PublicationAdd BLAST486

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18391 mRNA. Translation: AAA36747.1. Frameshift.
AF101171
, AF101165, AF101166, AF101167, AF101168, AF101169, AF101170 Genomic DNA. Translation: AAD43440.1.
EU826604 mRNA. Translation: ACF47640.1.
EU826605 mRNA. Translation: ACF47641.1.
AC092214 Genomic DNA. Translation: AAS07458.1.
CH236959 Genomic DNA. Translation: EAL23789.1.
CH471198 Genomic DNA. Translation: EAW51846.1.
CH471198 Genomic DNA. Translation: EAW51847.1.
BC130291 mRNA. Translation: AAI30292.1.
Z27409 mRNA. Translation: CAA81796.1.
CCDSiCCDS5884.1. [P21709-1]
PIRiA34076.
RefSeqiNP_005223.4. NM_005232.4. [P21709-1]
UniGeneiHs.89839.

Genome annotation databases

EnsembliENST00000275815; ENSP00000275815; ENSG00000146904. [P21709-1]
GeneIDi2041.
KEGGihsa:2041.
UCSCiuc003wcz.3. human. [P21709-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18391 mRNA. Translation: AAA36747.1. Frameshift.
AF101171
, AF101165, AF101166, AF101167, AF101168, AF101169, AF101170 Genomic DNA. Translation: AAD43440.1.
EU826604 mRNA. Translation: ACF47640.1.
EU826605 mRNA. Translation: ACF47641.1.
AC092214 Genomic DNA. Translation: AAS07458.1.
CH236959 Genomic DNA. Translation: EAL23789.1.
CH471198 Genomic DNA. Translation: EAW51846.1.
CH471198 Genomic DNA. Translation: EAW51847.1.
BC130291 mRNA. Translation: AAI30292.1.
Z27409 mRNA. Translation: CAA81796.1.
CCDSiCCDS5884.1. [P21709-1]
PIRiA34076.
RefSeqiNP_005223.4. NM_005232.4. [P21709-1]
UniGeneiHs.89839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K1KNMR-A/B536-573[»]
2K1LNMR-A/B536-573[»]
3HILX-ray2.00A/B911-974[»]
3KKAX-ray2.40A/B911-974[»]
ProteinModelPortaliP21709.
SMRiP21709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108355. 69 interactors.
DIPiDIP-34886N.
IntActiP21709. 6 interactors.
STRINGi9606.ENSP00000275815.

Chemistry databases

BindingDBiP21709.
ChEMBLiCHEMBL5810.
GuidetoPHARMACOLOGYi1821.

PTM databases

iPTMnetiP21709.
PhosphoSitePlusiP21709.

Polymorphism and mutation databases

BioMutaiEPHA1.
DMDMi317373566.

Proteomic databases

EPDiP21709.
MaxQBiP21709.
PaxDbiP21709.
PeptideAtlasiP21709.
PRIDEiP21709.

Protocols and materials databases

DNASUi2041.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275815; ENSP00000275815; ENSG00000146904. [P21709-1]
GeneIDi2041.
KEGGihsa:2041.
UCSCiuc003wcz.3. human. [P21709-1]

Organism-specific databases

CTDi2041.
DisGeNETi2041.
GeneCardsiEPHA1.
H-InvDBHIX0033699.
HGNCiHGNC:3385. EPHA1.
HPAiCAB026144.
MIMi179610. gene.
neXtProtiNX_P21709.
OpenTargetsiENSG00000146904.
PharmGKBiPA27817.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP21709.
KOiK05102.
OMAiQAYEDPA.
OrthoDBiEOG091G00W0.
PhylomeDBiP21709.
TreeFamiTF315363.

Enzyme and pathway databases

BioCyciZFISH:HS07379-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-2892247. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP21709.
SIGNORiP21709.

Miscellaneous databases

ChiTaRSiEPHA1. human.
EvolutionaryTraceiP21709.
GeneWikiiEPH_receptor_A1.
GenomeRNAii2041.
PROiP21709.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000146904.
CleanExiHS_EPHA1.
GenevisibleiP21709. 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.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
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]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 1 hit.
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.
SSF57184. SSF57184. 2 hits.
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 nameiEPHA1_HUMAN
AccessioniPrimary (citable) accession number: P21709
Secondary accession number(s): A1L3V3
, B5A966, B5A967, Q15405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 189 of the entry and version 4 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 7
    Human chromosome 7: 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.