P29317

※ Protein Information

Tag	Content
UniProt Accession	EPHA2_HUMAN; P29317;
Entrez ID	1969
GenBank Protein ID
GenBank Nucleotide ID
Protein Name	Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK)
Gene Name	EPHA2; ECK
Organism	Homo sapiens
NCBI Taxa ID	9606
Functional Description	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. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiat(view all) Functional Description 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. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.;(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.
Sequence (Fasta)	MELQAARACF ALLWGCALAA AAAAQGKEVV LLDFAAAGGE LGWLTHPYGK GWDLMQNIMN 60 DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF TVRDCNSFPG GASSCKETFN 120 LYYAESDLDY GTNFQKRLFT KIDTIAPDEI TVSSDFEARH VKLNVEERSV GPLTRKGFYL 180 AFQDIGACVA LLSVRVYYKK CPELLQGLAH FPETIAGSDA PSLATVAGTC VDHAVVPPGG 240 EEPRMHCAVD GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEASESPC LECPEHTLPS 300 PEGATSCECE EGFFRAPQDP ASMPCTRPPS APHYLTAVGM GAKVELRWTP PQDSGGREDI 360 VYSVTCEQCW PESGECGPCE ASVRYSEPPH GLTRTSVTVS DLEPHMNYTF TVEARNGVSG 420 LVTSRSFRTA SVSINQTEPP KVRLEGRSTT SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN 480 SYNVRRTEGF SVTLDDLAPD TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGNLAVIGG 540 VAVGVVLLLV LAGVGFFIHR RRKNQRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA 600 VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG MLKTSSGKKE VPVAIKTLKA GYTEKQRVDF 660 LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEYMENGAL DKFLREKDGE FSVLQLVGML 720 RGIAAGMKYL ANMNYVHRDL AARNILVNSN LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP 780 IRWTAPEAIS YRKFTSASDV WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM 840 DCPSAIYQLM MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG 900 SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR LPGHQKRIAY 960 SLLGLKDQVN TVGIPI 977 Fasta Sequence >P29317\|EPHA2; ECK\|Homo sapiens (Human) MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI

※ PTM-Disease Association

Num	PTM	Disease	Type	PTM Site	PMID
1	Phosphorylation	Gastric cancer	U		15649254
1	[Reference]: In the gastric cancer cell lines that endogenously expressed EPHA2, stimulation with ephrinA1-Fc led to decreased EPHA2 protein expression and increased EPHA2 phosphorylation.
2	Serine Phosphorylation	Lung cancer/carcinoma	P	S897	26158630
2	[Reference]: co-localized with RSK, associated with overall survival of lung cancer patients
3	Serine Phosphorylation	Cervical cancer/carcinoma	P	S897	23772378
3	[Reference]: Our results suggest that S897-phosphorylated EphA2 recruits Ephexin4 to promote cell migration and anoikis resistance, providing a molecular link between S897 phosphorylation of EphA2 and tumor progression
4	Serine Phosphorylation	Breast cancer/tumor/carcinoma	P	S897	23772378
4	[Reference]: Our results suggest that S897-phosphorylated EphA2 recruits Ephexin4 to promote cell migration and anoikis resistance, providing a molecular link between S897 phosphorylation of EphA2 and tumor progression
5	Serine Phosphorylation	Glioblastoma	U	S897	19573808
5	[Reference]: In human astrocytoma, S897 phosphorylation was correlated with tumor grades and Akt activation, suggesting that the Akt-EphA2 crosstalk may contribute to brain tumor progression

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 5)	OMIM:116600 ; CATARACT 6, MULTIPLE TYPES MESH:D018450 ; Disease Progression MESH:D044542 ; LEOPARD Syndrome MESH:D009369 ; Neoplasms MESH:D009634 ; Noonan Syndrome
DisGeNet (Curated) (count: 12) (view all)	C0008525; Choroideremia C0009691; Congenital cataract C0027092; Myopia C0028326; Noonan Syndrome C0175704; LEOPARD Syndrome C0266539; Congenital total cataract C0392557; Nuclear cataract C1112705; Nuclear non-senile cataract C1861825; CATARACT, POSTERIOR POLAR, 1 C3277059; Congenital Bilateral Cataracts C3665439; Mature cataract C3808377; CATARACT 16, MULTIPLE TYPES
HGMD (count: 4)	CD092930; Cataracts; Small deletions CM092928; Cataracts; Missense/nonsense CM085970; Cataracts; Missense/nonsense CS092929; Cataracts; Splicing

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 46) (view all)	153 APDEITVSSDFEARH dbPAF 373 CEQCWPESGECGPCE dbPAF 426 SGLVTSRSFRTASVS dbPAF 433 SFRTASVSINQTEPP dbPAF 437 ASVSINQTEPPKVRL dbPAF 570 KNQRARQSPEDVYFS dbPAF 575 RQSPEDVYFSKSEQL dbPAF 577 SPEDVYFSKSEQLKP dbPAF 579 EDVYFSKSEQLKPLK dbPAF 587 EQLKPLKTYVDPHTY dbPAF 588 QLKPLKTYVDPHTYE dbPAF 593 KTYVDPHTYEDPNQA dbPAF 594 TYVDPHTYEDPNQAV dbPAF 628 AGEFGEVYKGMLKTS dbPAF 647 EVPVAIKTLKAGYTE dbPAF 67 NDMPIYMYSVCNVMS dbPAF 685 LEGVISKYKPMMIIT dbPAF 692 YKPMMIITEYMENGA dbPAF 694 PMMIITEYMENGALD dbPAF 712 REKDGEFSVLQLVGM dbPAF 735 KYLANMNYVHRDLAA dbPAF 749 ARNILVNSNLVCKVS dbPAF 756 SNLVCKVSDFGLSRV dbPAF 761 KVSDFGLSRVLEDDP dbPAF 771 LEDDPEATYTTSGGK dbPAF 772 EDDPEATYTTSGGKI dbPAF 773 DDPEATYTTSGGKIP dbPAF 774 DPEATYTTSGGKIPI dbPAF 775 PEATYTTSGGKIPIR dbPAF 790 WTAPEAISYRKFTSA dbPAF 791 TAPEAISYRKFTSAS dbPAF 869 PKFADIVSILDKLIR dbPAF 880 KLIRAPDSLKTLADF dbPAF 892 ADFDPRVSIRLPSTS dbPAF 897 RVSIRLPSTSGSEGV dbPAF 898 VSIRLPSTSGSEGVP dbPAF 899 SIRLPSTSGSEGVPF dbPAF 901 RLPSTSGSEGVPFRT dbPAF 908 SEGVPFRTVSEWLES dbPAF 910 GVPFRTVSEWLESIK dbPAF 921 ESIKMQQYTEHFMAA dbPAF 922 SIKMQQYTEHFMAAG dbPAF 930 EHFMAAGYTAIEKVV dbPAF 940 IEKVVQMTNDDIKRI dbPAF 960 GHQKRIAYSLLGLKD dbPAF 961 HQKRIAYSLLGLKDQ dbPAF
Ubiquitination (count: 16) (view all)	136 DYGTNFQKRLFTKID PLMD 141 FQKRLFTKIDTIAPD PLMD 162 DFEARHVKLNVEERS PLMD 578 PEDVYFSKSEQLKPL PLMD 583 FSKSEQLKPLKTYVD PLMD 586 SEQLKPLKTYVDPHT PLMD 603 DPNQAVLKFTTEIHP PLMD 617 PSCVTRQKVIGAGEF PLMD 639 LKTSSGKKEVPVAIK PLMD 686 EGVISKYKPMMIITE PLMD 728 RGIAAGMKYLANMNY PLMD 754 VNSNLVCKVSDFGLS PLMD 778 TYTTSGGKIPIRWTA PLMD 882 IRAPDSLKTLADFDP PLMD 935 AGYTAIEKVVQMTND PLMD 945 QMTNDDIKRIGVRLP PLMD
Malonylation (count: 1)	583 FSKSEQLKPLKTYVD PLMD

※ Protein-Protein Interaction

Network

Interaction

Source

E7ESA6	P29317	HPRD; IntAct
G3XAK2	P29317	HPRD
O00459	P29317	HPRD
O00505	P29317	IntAct
O14493	P29317	HPRD
O43921	P29317	HPRD
P00533	P29317	HPRD; IntAct
P20827	P29317	HPRD; DIP; IntAct
P20936	P29317	HPRD
P22681	P29317	HPRD
P24666	P29317	HPRD
P25098	P29317	IntAct
P28749	P29317	IntAct
P29317	P29317	HPRD
P29317	P29353	HPRD
P29317	P33151	HPRD
P29317	P35222	DIP
P29317	P52797	HPRD
P29317	P52803	HPRD; DIP
P29317	P62993	HPRD
P29317	Q00537	IntAct
P29317	Q06124	IntAct;HPRD
P29317	Q13009	HPRD
P29317	Q13239	HPRD
P29317	Q13829	HPRD
P29317	Q15375	IntAct
P29317	Q8WUU5	IntAct
P29317	Q8WXD9	MINT
P29317	Q9BW91	IntAct
P29317	Q9UK45	IntAct
P29317	Q9UL46	IntAct

PTMD Annotation Information

※ Protein Information

Functional Description

Fasta Sequence

※ PTM-Disease Association

※ Disease Cross-ref Annotation

※ PTM Sites

※ Protein-Protein Interaction