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P21709

- EPHA1_HUMAN

UniProt

P21709 - EPHA1_HUMAN

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Protein
Ephrin type-A receptor 1
Gene
EPHA1, EPH, EPHT, EPHT1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei656 – 6561ATP By similarity
Active sitei749 – 7491Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi630 – 6389ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. transmembrane-ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. activation of Rho GTPase activity Source: UniProtKB
  2. angiogenesis Source: UniProtKB-KW
  3. cell surface receptor signaling pathway Source: UniProtKB
  4. negative regulation of cell migration Source: UniProtKB
  5. negative regulation of protein kinase activity Source: UniProtKB
  6. peptidyl-tyrosine phosphorylation Source: UniProtKB
  7. positive regulation of angiogenesis Source: UniProtKB
  8. positive regulation of cell migration Source: UniProtKB
  9. positive regulation of cell proliferation Source: UniProtKB
  10. positive regulation of cell-matrix adhesion Source: UniProtKB
  11. positive regulation of stress fiber assembly Source: UniProtKB
  12. protein autophosphorylation Source: UniProtKB
  13. regulation of Rac GTPase activity Source: UniProtKB
  14. 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

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
SignaLinkiP21709.

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
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:3385. EPHA1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 547522Extracellular Reviewed prediction
Add
BLAST
Transmembranei548 – 56821Helical; Reviewed prediction
Add
BLAST
Topological domaini569 – 976408Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 976951Ephrin type-A receptor 1
PRO_0000016798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi414 – 4141N-linked (GlcNAc...) Reviewed prediction
Modified residuei599 – 5991Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei605 – 6051Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei781 – 7811Phosphotyrosine; by autocatalysis Reviewed prediction
Modified residuei906 – 9061Phosphoserine1 Publication
Modified residuei910 – 9101Phosphoserine1 Publication
Modified residuei930 – 9301Phosphotyrosine; by autocatalysis Reviewed prediction

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP21709.
PaxDbiP21709.
PRIDEiP21709.

PTM databases

PhosphoSiteiP21709.

Expressioni

Tissue specificityi

Overexpressed in several carcinomas.

Gene expression databases

BgeeiP21709.
CleanExiHS_EPHA1.
GenevestigatoriP21709.

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/FAK1.3 Publications

Protein-protein interaction databases

BioGridi108355. 3 interactions.
DIPiDIP-34886N.
IntActiP21709. 1 interaction.
STRINGi9606.ENSP00000275815.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi538 – 5403
Helixi545 – 57026
Helixi918 – 9247
Helixi928 – 9303
Helixi931 – 9366
Helixi942 – 9454
Helixi950 – 9556
Helixi961 – 97313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1KNMR-A/B536-573[»]
2K1LNMR-A/B536-573[»]
3HILX-ray2.00A/B911-974[»]
3KKAX-ray2.40A/B911-974[»]
ProteinModelPortaliP21709.
SMRiP21709. Positions 24-538, 562-894, 911-974.

Miscellaneous databases

EvolutionaryTraceiP21709.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 209183Eph LBD
Add
BLAST
Domaini332 – 445114Fibronectin type-III 1
Add
BLAST
Domaini447 – 53892Fibronectin type-III 2
Add
BLAST
Domaini624 – 884261Protein kinase
Add
BLAST
Domaini913 – 97664SAM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi974 – 9763PDZ-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 329139Cys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP21709.
KOiK05102.
OMAiQAYEDPA.
OrthoDBiEOG7VTDM6.
PhylomeDBiP21709.
TreeFamiTF315363.

Family and domain databases

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. 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]
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.
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]

Sequencei

Sequence statusi: Complete.

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

P21709-1 [UniParc]FASTAAdd to Basket

« Hide

MERRWPLGLG LVLLLCAPLP PGARAKEVTL MDTSKAQGEL GWLLDPPKDG    50
WSEQQQILNG TPLYMYQDCP MQGRRDTDHW LRSNWIYRGE EASRVHVELQ 100
FTVRDCKSFP GGAGPLGCKE TFNLLYMESD QDVGIQLRRP LFQKVTTVAA 150
DQSFTIRDLV SGSVKLNVER CSLGRLTRRG LYLAFHNPGA CVALVSVRVF 200
YQRCPETLNG LAQFPDTLPG PAGLVEVAGT CLPHARASPR PSGAPRMHCS 250
PDGEWLVPVG RCHCEPGYEE GGSGEACVAC PSGSYRMDMD TPHCLTCPQQ 300
STAESEGATI CTCESGHYRA PGEGPQVACT GPPSAPRNLS FSASGTQLSL 350
RWEPPADTGG RQDVRYSVRC SQCQGTAQDG GPCQPCGVGV HFSPGARGLT 400
TPAVHVNGLE PYANYTFNVE AQNGVSGLGS SGHASTSVSI SMGHAESLSG 450
LSLRLVKKEP RQLELTWAGS RPRSPGANLT YELHVLNQDE ERYQMVLEPR 500
VLLTELQPDT TYIVRVRMLT PLGPGPFSPD HEFRTSPPVS RGLTGGEIVA 550
VIFGLLLGAA LLLGILVFRS RRAQRQRQQR QRDRATDVDR EDKLWLKPYV 600
DLQAYEDPAQ GALDFTRELD PAWLMVDTVI GEGEFGEVYR GTLRLPSQDC 650
KTVAIKTLKD TSPGGQWWNF LREATIMGQF SHPHILHLEG VVTKRKPIMI 700
ITEFMENGAL DAFLREREDQ LVPGQLVAML QGIASGMNYL SNHNYVHRDL 750
AARNILVNQN LCCKVSDFGL TRLLDDFDGT YETQGGKIPI RWTAPEAIAH 800
RIFTTASDVW SFGIVMWEVL SFGDKPYGEM SNQEVMKSIE DGYRLPPPVD 850
CPAPLYELMK NCWAYDRARR PHFQKLQAHL EQLLANPHSL RTIANFDPRM 900
TLRLPSLSGS DGIPYRTVSE WLESIRMKRY ILHFHSAGLD TMECVLELTA 950
EDLTQMGITL PGHQKRILCS IQGFKD 976
Length:976
Mass (Da):108,127
Last modified:January 11, 2011 - v4
Checksum:i91EFCA69FFE17826
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti160 – 1601V → A.6 Publications
Corresponds to variant rs4725617 [ dbSNP | Ensembl ].
VAR_028265
Natural varianti351 – 3511R → C.1 Publication
Corresponds to variant rs56006153 [ dbSNP | Ensembl ].
VAR_042115
Natural varianti492 – 4921R → Q.1 Publication
Corresponds to variant rs11768549 [ dbSNP | Ensembl ].
VAR_028266
Natural varianti575 – 5751R → Q.1 Publication
Corresponds to variant rs35719334 [ dbSNP | Ensembl ].
VAR_042116
Natural varianti585 – 5851A → T.1 Publication
Corresponds to variant rs34178823 [ dbSNP | Ensembl ].
VAR_042117
Natural varianti697 – 6971P → L.1 Publication
Corresponds to variant rs34372369 [ dbSNP | Ensembl ].
VAR_042118
Natural varianti703 – 7031E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
VAR_042119
Natural varianti807 – 8071S → R.1 Publication
Corresponds to variant rs56244405 [ dbSNP | Ensembl ].
VAR_042120
Natural varianti900 – 9001M → V.8 Publications
Corresponds to variant rs6967117 [ dbSNP | Ensembl ].
VAR_028267

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti398 – 3981G → A in AAD43440. 1 Publication
Sequence conflicti398 – 3981G → A in CAA81796. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5884.1.
PIRiA34076.
RefSeqiNP_005223.4. NM_005232.4.
UniGeneiHs.89839.

Genome annotation databases

EnsembliENST00000275815; ENSP00000275815; ENSG00000146904.
GeneIDi2041.
KEGGihsa:2041.
UCSCiuc003wcz.3. human.

Polymorphism databases

DMDMi317373566.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5884.1.
PIRi A34076.
RefSeqi NP_005223.4. NM_005232.4.
UniGenei Hs.89839.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P21709.
SMRi P21709. Positions 24-538, 562-894, 911-974.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108355. 3 interactions.
DIPi DIP-34886N.
IntActi P21709. 1 interaction.
STRINGi 9606.ENSP00000275815.

Chemistry

BindingDBi P21709.
ChEMBLi CHEMBL2363043.
GuidetoPHARMACOLOGYi 1821.

PTM databases

PhosphoSitei P21709.

Polymorphism databases

DMDMi 317373566.

Proteomic databases

MaxQBi P21709.
PaxDbi P21709.
PRIDEi P21709.

Protocols and materials databases

DNASUi 2041.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000275815 ; ENSP00000275815 ; ENSG00000146904 .
GeneIDi 2041.
KEGGi hsa:2041.
UCSCi uc003wcz.3. human.

Organism-specific databases

CTDi 2041.
GeneCardsi GC07M143087.
H-InvDB HIX0033699.
HGNCi HGNC:3385. EPHA1.
HPAi CAB026144.
MIMi 179610. gene.
neXtProti NX_P21709.
PharmGKBi PA27817.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P21709.
KOi K05102.
OMAi QAYEDPA.
OrthoDBi EOG7VTDM6.
PhylomeDBi P21709.
TreeFami TF315363.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_200759. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
SignaLinki P21709.

Miscellaneous databases

EvolutionaryTracei P21709.
GeneWikii EPH_receptor_A1.
GenomeRNAii 2041.
NextBioi 8291.
PROi P21709.
SOURCEi Search...

Gene expression databases

Bgeei P21709.
CleanExi HS_EPHA1.
Genevestigatori P21709.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProi IPR027936. 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 ]
Pfami PF14575. 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 ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS01186. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEPHA1_HUMAN
AccessioniPrimary (citable) accession number: P21709
Secondary accession number(s): A1L3V3, Q15405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 169 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

External Data

Dasty 3

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