Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21709 (EPHA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 1

Short name=hEpha1
EC=2.7.10.1
Alternative name(s):
EPH tyrosine kinase
EPH tyrosine kinase 1
Erythropoietin-producing hepatoma receptor
Tyrosine-protein kinase receptor EPH
Gene names
Name:EPHA1
Synonyms:EPH, EPHT, EPHT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length976 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 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. Ref.9 Ref.10 Ref.11

Catalytic activity

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

Subunit structure

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. Ref.9 Ref.10 Ref.14

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.10.

Tissue specificity

Overexpressed in several carcinomas.

Post-translational modification

Phosphorylated. Autophosphorylation is stimulated by its ligand EFNA1. Ref.10

Ubiquitinated. Ref.12

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 AAA36747.1 differs from that shown. Reason: Frameshift at positions 582, 595 and 601.

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Rho GTPase activity

Inferred from direct assay Ref.10. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 12775584. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of cell-matrix adhesion

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of stress fiber assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from direct assay Ref.10. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentintegral component of plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from direct assay PubMed 12775584. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

transmembrane-ephrin receptor activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 976951Ephrin type-A receptor 1
PRO_0000016798

Regions

Topological domain26 – 547522Extracellular Potential
Transmembrane548 – 56821Helical; Potential
Topological domain569 – 976408Cytoplasmic Potential
Domain27 – 209183Eph LBD
Domain332 – 445114Fibronectin type-III 1
Domain447 – 53892Fibronectin type-III 2
Domain624 – 884261Protein kinase
Domain913 – 97664SAM
Nucleotide binding630 – 6389ATP By similarity
Motif974 – 9763PDZ-binding Potential
Compositional bias191 – 329139Cys-rich

Sites

Active site7491Proton acceptor By similarity
Binding site6561ATP By similarity

Amino acid modifications

Modified residue5991Phosphotyrosine; by autocatalysis Potential
Modified residue6051Phosphotyrosine; by autocatalysis Potential
Modified residue7811Phosphotyrosine; by autocatalysis Potential
Modified residue9061Phosphoserine Ref.13
Modified residue9101Phosphoserine Ref.13
Modified residue9301Phosphotyrosine; by autocatalysis Potential
Glycosylation4141N-linked (GlcNAc...) Potential

Natural variations

Natural variant1601V → A. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.16
Corresponds to variant rs4725617 [ dbSNP | Ensembl ].
VAR_028265
Natural variant3511R → C. Ref.16
Corresponds to variant rs56006153 [ dbSNP | Ensembl ].
VAR_042115
Natural variant4921R → Q. Ref.16
Corresponds to variant rs11768549 [ dbSNP | Ensembl ].
VAR_028266
Natural variant5751R → Q. Ref.16
Corresponds to variant rs35719334 [ dbSNP | Ensembl ].
VAR_042116
Natural variant5851A → T. Ref.16
Corresponds to variant rs34178823 [ dbSNP | Ensembl ].
VAR_042117
Natural variant6971P → L. Ref.16
Corresponds to variant rs34372369 [ dbSNP | Ensembl ].
VAR_042118
Natural variant7031E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.16
VAR_042119
Natural variant8071S → R. Ref.16
Corresponds to variant rs56244405 [ dbSNP | Ensembl ].
VAR_042120
Natural variant9001M → V. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.16 Ref.17
Corresponds to variant rs6967117 [ dbSNP | Ensembl ].
VAR_028267

Experimental info

Sequence conflict3981G → A in AAD43440. Ref.2
Sequence conflict3981G → A in CAA81796. Ref.7

Secondary structure

................ 976
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21709 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 91EFCA69FFE17826

FASTA976108,127
        10         20         30         40         50         60 
MERRWPLGLG LVLLLCAPLP PGARAKEVTL MDTSKAQGEL GWLLDPPKDG WSEQQQILNG 

        70         80         90        100        110        120 
TPLYMYQDCP MQGRRDTDHW LRSNWIYRGE EASRVHVELQ FTVRDCKSFP GGAGPLGCKE 

       130        140        150        160        170        180 
TFNLLYMESD QDVGIQLRRP LFQKVTTVAA DQSFTIRDLV SGSVKLNVER CSLGRLTRRG 

       190        200        210        220        230        240 
LYLAFHNPGA CVALVSVRVF YQRCPETLNG LAQFPDTLPG PAGLVEVAGT CLPHARASPR 

       250        260        270        280        290        300 
PSGAPRMHCS PDGEWLVPVG RCHCEPGYEE GGSGEACVAC PSGSYRMDMD TPHCLTCPQQ 

       310        320        330        340        350        360 
STAESEGATI CTCESGHYRA PGEGPQVACT GPPSAPRNLS FSASGTQLSL RWEPPADTGG 

       370        380        390        400        410        420 
RQDVRYSVRC SQCQGTAQDG GPCQPCGVGV HFSPGARGLT TPAVHVNGLE PYANYTFNVE 

       430        440        450        460        470        480 
AQNGVSGLGS SGHASTSVSI SMGHAESLSG LSLRLVKKEP RQLELTWAGS RPRSPGANLT 

       490        500        510        520        530        540 
YELHVLNQDE ERYQMVLEPR VLLTELQPDT TYIVRVRMLT PLGPGPFSPD HEFRTSPPVS 

       550        560        570        580        590        600 
RGLTGGEIVA VIFGLLLGAA LLLGILVFRS RRAQRQRQQR QRDRATDVDR EDKLWLKPYV 

       610        620        630        640        650        660 
DLQAYEDPAQ GALDFTRELD PAWLMVDTVI GEGEFGEVYR GTLRLPSQDC KTVAIKTLKD 

       670        680        690        700        710        720 
TSPGGQWWNF LREATIMGQF SHPHILHLEG VVTKRKPIMI ITEFMENGAL DAFLREREDQ 

       730        740        750        760        770        780 
LVPGQLVAML QGIASGMNYL SNHNYVHRDL AARNILVNQN LCCKVSDFGL TRLLDDFDGT 

       790        800        810        820        830        840 
YETQGGKIPI RWTAPEAIAH RIFTTASDVW SFGIVMWEVL SFGDKPYGEM SNQEVMKSIE 

       850        860        870        880        890        900 
DGYRLPPPVD CPAPLYELMK NCWAYDRARR PHFQKLQAHL EQLLANPHSL RTIANFDPRM 

       910        920        930        940        950        960 
TLRLPSLSGS DGIPYRTVSE WLESIRMKRY ILHFHSAGLD TMECVLELTA EDLTQMGITL 

       970 
PGHQKRILCS IQGFKD 

« Hide

References

« Hide 'large scale' references
[1]"A novel putative tyrosine kinase receptor encoded by the eph gene."
Hirai H., Maru Y., Hagiwara K., Nishida J., Takaku F.
Science 238:1717-1720(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-160 AND VAL-900.
[2]"Genomic structure of the EPHA1 receptor tyrosine kinase gene."
Owshalimpur D., Kelley M.J.
Mol. Cell. Probes 13:169-173(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-160 AND VAL-900.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-160 AND VAL-900.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-160 AND VAL-900.
[6]"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], VARIANTS ALA-160 AND VAL-900.
Tissue: Brain.
[7]"An EGFR/eph chimeric receptor possesses ligand stimulated tyrosine kinase activity and promotes cell growth."
Tuzi N.L.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 286-976, VARIANT VAL-900.
Tissue: Placenta.
[8]"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.
[9]"Ephrin-A1 stimulates migration of CD8+CCR7+ T lymphocytes."
Hjorthaug H.S., Aasheim H.C.
Eur. J. Immunol. 37:2326-2336(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MIGRATION OF T-LYMPHOCYTES, INTERACTION WITH LCK; PTK2B/PYK2 AND PI3-KINASE.
[10]"EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL SPREADING, FUNCTION IN CELL MIGRATION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1 AND ILK.
[11]"EphA1 receptor silencing by small interfering RNA has antiangiogenic and antitumor efficacy in hepatocellular carcinoma."
Chen G., Wang Y., Zhou M., Shi H., Yu Z., Zhu Y., Yu F.
Oncol. Rep. 23:563-570(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL PROLIFERATION.
[12]"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND SER-910, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1."
Bocharov E.V., Mayzel M.L., Volynsky P.E., Goncharuk M.V., Ermolyuk Y.S., Schulga A.A., Artemenko E.O., Efremov R.G., Arseniev A.S.
J. Biol. Chem. 283:29385-29395(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 536-573, HOMODIMERIZATION.
[15]"Sam domain of human ephrin type-a receptor 1 (epha1)."
Structural genomics consortium (SGC)
Submitted (JUN-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 911-974.
[16]"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] ALA-160; CYS-351; GLN-492; GLN-575; THR-585; LEU-697; LYS-703; ARG-807 AND VAL-900.
[17]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18391 mRNA. Translation: AAA36747.1. Frameshift.
AF101171 expand/collapse EMBL AC list , AF101165, AF101166, AF101167, AF101168, AF101169, AF101170 Genomic DNA. Translation: AAD43440.1.
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.
PIRA34076.
RefSeqNP_005223.4. NM_005232.4.
UniGeneHs.89839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1KNMR-A/B536-573[»]
2K1LNMR-A/B536-573[»]
3HILX-ray2.00A/B911-974[»]
3KKAX-ray2.40A/B911-974[»]
ProteinModelPortalP21709.
SMRP21709. Positions 24-538, 562-974.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108355. 3 interactions.
DIPDIP-34886N.
IntActP21709. 1 interaction.
STRING9606.ENSP00000275815.

Chemistry

BindingDBP21709.
ChEMBLCHEMBL5810.
GuidetoPHARMACOLOGY1821.

PTM databases

PhosphoSiteP21709.

Polymorphism databases

DMDM317373566.

Proteomic databases

PaxDbP21709.
PRIDEP21709.

Protocols and materials databases

DNASU2041.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275815; ENSP00000275815; ENSG00000146904.
GeneID2041.
KEGGhsa:2041.
UCSCuc003wcz.3. human.

Organism-specific databases

CTD2041.
GeneCardsGC07M143087.
H-InvDBHIX0033699.
HGNCHGNC:3385. EPHA1.
HPACAB026144.
MIM179610. gene.
neXtProtNX_P21709.
PharmGKBPA27817.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP21709.
KOK05102.
OMAQAYEDPA.
OrthoDBEOG7VTDM6.
PhylomeDBP21709.
TreeFamTF315363.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP21709.

Gene expression databases

BgeeP21709.
CleanExHS_EPHA1.
GenevestigatorP21709.

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.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
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]
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.
SSF57184. SSF57184. 2 hits.
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

EvolutionaryTraceP21709.
GeneWikiEPH_receptor_A1.
GenomeRNAi2041.
NextBio8291.
PROP21709.
SOURCESearch...

Entry information

Entry nameEPHA1_HUMAN
AccessionPrimary (citable) accession number: P21709
Secondary accession number(s): A1L3V3, Q15405
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 165 of the entry and version 4 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 7

Human chromosome 7: entries, gene names and cross-references to MIM