P21709 (EPHA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	976 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 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.13
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
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 process	Angiogenesis Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of Rho GTPase activity Inferred from direct assay Ref.10. Source: UniProtKB angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW 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_component	integral to plasma membrane Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane-ephrin receptor activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 976

951

Ephrin type-A receptor 1

PRO_0000016798

Regions

Topological domain

26 – 547

522

Extracellular Potential

Transmembrane

548 – 568

21

Helical; Potential

Topological domain

569 – 976

408

Cytoplasmic Potential

Domain

27 – 209

183

Eph LBD

Domain

332 – 437

106

Fibronectin type-III 1

Domain

446 – 535

90

Fibronectin type-III 2

Domain

624 – 884

261

Protein kinase

Domain

913 – 976

64

SAM

Nucleotide binding

630 – 638

9

ATP By similarity

Motif

974 – 976

3

PDZ-binding Potential

Compositional bias

191 – 329

139

Cys-rich

Sites

Active site

749

1

Proton acceptor By similarity

Binding site

656

1

ATP By similarity

Amino acid modifications

Modified residue

599

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

605

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

781

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

906

1

Phosphoserine Ref.12

Modified residue

910

1

Phosphoserine Ref.12

Modified residue

930

1

Phosphotyrosine; by autocatalysis Potential

Glycosylation

414

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

160

1

V → A. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.15
Corresponds to variant rs4725617 [ dbSNP | Ensembl ].

VAR_028265

Natural variant

351

1

R → C. Ref.15
Corresponds to variant rs56006153 [ dbSNP | Ensembl ].

VAR_042115

Natural variant

492

1

R → Q. Ref.15
Corresponds to variant rs11768549 [ dbSNP | Ensembl ].

VAR_028266

Natural variant

575

1

R → Q. Ref.15
Corresponds to variant rs35719334 [ dbSNP | Ensembl ].

VAR_042116

Natural variant

585

1

A → T. Ref.15
Corresponds to variant rs34178823 [ dbSNP | Ensembl ].

VAR_042117

Natural variant

697

1

P → L. Ref.15
Corresponds to variant rs34372369 [ dbSNP | Ensembl ].

VAR_042118

Natural variant

703

1

E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.15

VAR_042119

Natural variant

807

1

S → R. Ref.15
Corresponds to variant rs56244405 [ dbSNP | Ensembl ].

VAR_042120

Natural variant

900

1

M → V. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.15 Ref.16
Corresponds to variant rs6967117 [ dbSNP | Ensembl ].

VAR_028267

Experimental info

Sequence conflict

398

1

G → A in AAD43440. Ref.2

Sequence conflict

398

1

G → A in CAA81796. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

976

Helix Strand Turn

Details...

Beta strand

538 – 540

3

Helix

545 – 570

26

Helix

918 – 924

7

Helix

928 – 930

3

Helix

931 – 936

6

Helix

942 – 945

4

Helix

950 – 955

6

Helix

961 – 973

13

Sequences

	Sequence		Length	Mass (Da)
	P21709 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: 91EFCA69FFE17826	FASTA	976	108,127
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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, MASS SPECTROMETRY.
[13]	"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.
[14]	"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.
[15]	"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] ALA-160; CYS-351; GLN-492; GLN-575; THR-585; LEU-697; LYS-703; ARG-807 AND VAL-900.
[16]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18391 mRNA. Translation: AAA36747.1. Frameshift.
AF101171 , 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.

IPI

IPI00294250.

PIR

A34076.

RefSeq

NP_005223.4. NM_005232.4.

UniGene

Hs.89839.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K1K	NMR	-	A/B	536-573	[»]
2K1L	NMR	-	A/B	536-573	[»]
3HIL	X-ray	2.00	A/B	911-974	[»]
3KKA	X-ray	2.40	A/B	911-974	[»]

ProteinModelPortal

P21709.

SMR

P21709. Positions 24-893, 911-974.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21709. 1 interaction.

STRING

9606.ENSP00000275815.

PTM databases

PhosphoSite

P21709.

Polymorphism databases

DMDM

47117832.

Proteomic databases

PaxDb

P21709.

PRIDE

P21709.

Protocols and materials databases

DNASU

2041.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000275815; ENSP00000275815; ENSG00000146904.

GeneID

2041.

KEGG

hsa:2041.

UCSC

uc003wcz.3. human.

Organism-specific databases

CTD

2041.

GeneCards

GC07M143087.

H-InvDB

HIX0033699.

HGNC

HGNC:3385. EPHA1.

HPA

CAB026144.

MIM

179610. gene.

neXtProt

NX_P21709.

PharmGKB

PA27817.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233856.

HOVERGEN

HBG062180.

InParanoid

P21709.

KO

K05102.

OMA

GWSEVQQ.

OrthoDB

EOG42BX7S.

PhylomeDB

P21709.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

epha_fwdpathway. EPHA forward signaling.

Gene expression databases

Bgee

P21709.

CleanEx

HS_EPHA1.

Genevestigator

P21709.

GermOnline

ENSG00000146904. 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.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
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]

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.
SSF57184. Grow_fac_recept. 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

P21709.

ChEMBL

CHEMBL5810.

EvolutionaryTrace

P21709.

GenomeRNAi

2041.

NextBio

8291.

SOURCE

Search...

Entry information

Entry name

EPHA1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 155 of the entry and version 4 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.