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Reviewed, UniProtKB/Swiss-Prot P21709 (EPHA1_HUMAN)

Last modified February 9, 2010. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ephrin type-A receptor 1
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor EPH
Gene names
Name: EPHA1
Synonyms: EPH, EPHT, EPHT1
OrganismHomo sapiens (Human) [Complete 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 for members of the ephrin-A family. Binds with a low affinity to ephrin-A1.

Catalytic activity

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

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Overexpressed in several carcinomas.

Sequence similarities

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

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 976953Ephrin type-A receptor 1
PRO_0000016798

Regions

Topological domain24 – 547524Extracellular Potential
Transmembrane548 – 56821 Potential
Topological domain569 – 976408Cytoplasmic Potential
Domain332 – 437106Fibronectin type-III 1
Domain446 – 53590Fibronectin 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 residue331Phosphothreonine Ref.6
Modified residue341Phosphoserine Ref.6
Modified residue5991Phosphotyrosine; by autocatalysis Potential
Modified residue6051Phosphotyrosine; by autocatalysis Potential
Modified residue7801Phosphothreonine
Modified residue7811Phosphotyrosine; by autocatalysis Potential
Modified residue9061Phosphoserine
Modified residue9081Phosphoserine
Modified residue9101Phosphoserine
Modified residue9191Phosphoserine
Modified residue9301Phosphotyrosine; by autocatalysis Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential

Natural variations

Natural variant1601A → V: dbSNP rs4725617. Ref.3 Ref.8
VAR_028265
Natural variant3511R → C: dbSNP rs56006153. Ref.8
VAR_042115
Natural variant4921R → Q: dbSNP rs11768549. Ref.8
VAR_028266
Natural variant5751R → Q: dbSNP rs35719334. Ref.8
VAR_042116
Natural variant5851A → T: dbSNP rs34178823. Ref.8
VAR_042117
Natural variant6971P → L: dbSNP rs34372369. Ref.8
VAR_042118
Natural variant7031E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.8
VAR_042119
Natural variant8071S → R: dbSNP rs56244405. Ref.8
VAR_042120
Natural variant9001V → M: dbSNP rs6967117. Ref.3 Ref.8
VAR_028267

Experimental info

Sequence conflict3981G → A Ref.2
Sequence conflict3981G → A Ref.4
Sequence conflict581 – 61636QRDRA…ALDFT → HVTAPPMWIERTSCAEALCG TSRHTRTLHREPWTLPGGWS NFPS in AAA36747. Ref.1

Secondary structure

............ 976
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21709-1 [UniParc].

Last modified May 10, 2004. Version 3.
Checksum: 9F8F2D6A8E683D95

FASTA976108,067
        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 DQSFTIRDLA 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 RTIANFDPRV 

       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: 2825356] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic structure of the EPHA1 receptor tyrosine kinase gene."
Owshalimpur D., Kelley M.J.
Mol. Cell. Probes 13:169-173(1999) [PubMed: 10369740] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-160 AND MET-900.
[4]"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.
Tissue: Placenta.
[5]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-781, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33 AND SER-34, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-780; TYR-781; SER-906; SER-908; SER-910 AND SER-919, MASS SPECTROMETRY.
[8]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-160; CYS-351; GLN-492; GLN-575; THR-585; LEU-697; LYS-703; ARG-807 AND MET-900.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18391 mRNA. Translation: AAA36747.1. Sequence problems.
AF101171 expand/collapse EMBL AC list , AF101165, AF101166, AF101167, AF101168, AF101169, AF101170 Genomic DNA. Translation: AAD43440.1.
AC092214 Genomic DNA. Translation: AAS07458.1.
Z27409 mRNA. Translation: CAA81796.1.
IPIIPI00294250.
PIRA34076.
RefSeqNP_005223.4.
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[»]
SMRP21709. Positions 26-203, 292-536, 451-538, 616-896, 625-935.
ModBaseSearch...

Protein-protein interaction databases

STRINGP21709.

PTM databases

PhosphoSiteP21709.

Proteomic databases

PRIDEP21709.

Genome annotation databases

EnsemblENST00000275815; ENSP00000275815; ENSG00000146904; Homo sapiens. [Genome view]
GeneID2041.
KEGGhsa:2041.

Organism-specific databases

CTD2041.
GeneCardsGC07M142798.
H-InvDBHIX0033699.
HGNCHGNC:3385. EPHA1.
MIM179610. gene.
PharmGKBPA27817.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG755340.
HOVERGENP21709.
InParanoidP21709.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBepha_fwdpathway. EPHA forward signaling.

Gene expression databases

ArrayExpressP21709.
BgeeP21709.
CleanExHS_EPHA1.
GenevestigatorP21709.
GermOnlineENSG00000146904. Homo sapiens.

Family and domain databases

InterProIPR001090. Ephrin_rcpt_lig-bd.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR008979. Galactose-bd-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR010993. SAM_homology.
IPR013761. SAM_type.
IPR021129. SAM_type1.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
IPR016257. Tyr_prot_kinase_ephrin_rcpt.
IPR001426. Tyr_prot_kinase_rcpt_V_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS01186. EGF_2. 1 hit. Uncertain.
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 Resources

NextBio8291.
SOURCESearch...

Entry information

Entry nameEPHA1_HUMAN
AccessionPrimary (citable) accession number: P21709
Secondary accession number(s): Q15405
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 10, 2004
Last modified: February 9, 2010
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents