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P21709

- EPHA1_HUMAN

UniProt

P21709 - EPHA1_HUMAN

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Protein

Ephrin type-A receptor 1

Gene

EPHA1

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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei656 – 6561ATPPROSITE-ProRule annotation
Active sitei749 – 7491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi630 – 6389ATPPROSITE-ProRule annotation

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-matrix adhesion Source: UniProtKB
  9. positive regulation of cell migration Source: UniProtKB
  10. positive regulation of cell proliferation 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 1 Publication; Single-pass type I membrane protein 1 Publication

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 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 976951Ephrin type-A receptor 1PRO_0000016798Add
BLAST

Amino acid modifications

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

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/FAK1.2 Publications

Protein-protein interaction databases

BioGridi108355. 3 interactions.
DIPiDIP-34886N.
IntActiP21709. 2 interactions.
STRINGi9606.ENSP00000275815.

Structurei

Secondary structure

1
976
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, 562-884, 911-974.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21709.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 547522ExtracellularSequence AnalysisAdd
BLAST
Topological domaini569 – 976408CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei548 – 56821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 209183Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini332 – 445114Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini447 – 53892Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini624 – 884261Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini913 – 97664SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi974 – 9763PDZ-bindingSequence Analysis

Compositional bias

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

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118975.
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. 1 hit.
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. Align

Isoform 1 (identifier: P21709) [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 AAA36747.1 differs from that shown. Reason: Frameshift at positions 582, 595 and 601.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti398 – 3981G → A in AAD43440. (PubMed:10369740)Curated
Sequence conflicti398 – 3981G → A in CAA81796. 1 PublicationCurated

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei446 – 49045ESLSG…LNQDE → DPTLSLWTPRVTVRPVSETG EERTEATRADLGGVPAPKPW GEPDL in isoform 2. 1 PublicationVSP_056010Add
BLAST
Alternative sequencei446 – 47429ESLSG…SRPRS → GERLRGAGTGTWWRQKGLRP QNKLMGRKP in isoform 3. 1 PublicationVSP_056011Add
BLAST
Alternative sequencei475 – 976502Missing in isoform 3. 1 PublicationVSP_056012Add
BLAST
Alternative sequencei491 – 976486Missing in isoform 2. 1 PublicationVSP_056013Add
BLAST

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.
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.
UniGeneiHs.89839.

Genome annotation databases

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

Polymorphism databases

DMDMi317373566.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5884.1. [P21709-1 ]
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, 562-884, 911-974.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108355. 3 interactions.
DIPi DIP-34886N.
IntActi P21709. 2 interactions.
STRINGi 9606.ENSP00000275815.

Chemistry

BindingDBi P21709.
ChEMBLi CHEMBL5810.
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 . [P21709-1 ]
GeneIDi 2041.
KEGGi hsa:2041.
UCSCi uc003wcz.3. human. [P21709-1 ]

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.
GeneTreei ENSGT00760000118975.
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 35477784.
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. 1 hit.
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] (ISOFORM 1), 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. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
    Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
    Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING.
  4. "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].
  5. "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.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-160 AND VAL-900.
  7. "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] (ISOFORM 1), VARIANTS ALA-160 AND VAL-900.
    Tissue: Brain.
  8. "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 (ISOFORM 1), VARIANT VAL-900.
    Tissue: Placenta.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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].
  15. "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.
  16. "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.
  17. "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.
  18. 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
, B5A966, B5A967, Q15405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 171 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