EPHA8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPHA8_HUMAN
• UniProt AC: P29322
• Protein Name: Ephrin type-A receptor 8
• Gene Name: EPHA8
• Organism: Homo sapiens (Human).
• Sequence Length: 1005
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cell projection . Early endosome membrane . Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes.
• Protein Description: Receptor tyrosine kinase which binds promiscuously GPI-anchored 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. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth (By similarity)..
• Protein Sequence: MAPARGRLPPALWVVTAAAAAATCVSAARGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSMPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACVACELGFYKSAPGDQLCARCPPHSHSAAPAAQACHCDLSYYRAALDPPSSACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNYSFWIEAVNGVSDLSPEPRRAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLHHPPGKLPEPQFYAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGDSGEVCYGRLRVPGQRDVPVAIKALKAGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDTFLRTHDGQFTIMQLVGMLRGVGAGMRYLSDLGYVHRDLAARNVLVDSNLVCKVSDFGLSRVLEDDPDAAYTTTGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNRDVISSVEEGYRLPAPMGCPHALHQLMLDCWHKDRAQRPRFSQIVSVLDALIRSPESLRATATVSRCPPPAFVRSCFDLRGGSGGGGGLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLTSTQGPRRHL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
86	Phosphorylation	NQNNWLRTSWVPRDG CCCCCEECCCCCCCC	25.44	-
87	Phosphorylation	QNNWLRTSWVPRDGA CCCCEECCCCCCCCC	21.46	-
104	Phosphorylation	VYAEIKFTLRDCNSM EEEEEEEEEHHCCCC	18.84	24719451
177	Phosphorylation	VRSVGPLSKRGFYLA EEECCCCCCCCEEEE	24.36	-
224	Phosphorylation	AVTGADSSSLVEVRG HHHCCCCCCCEEECC	28.39	-
225	Phosphorylation	VTGADSSSLVEVRGQ HHCCCCCCCEEECCE	40.15	-
340	N-linked_Glycosylation	VNLISSVNGTSVTLE CEEEEEECCCEEEEE	50.39	UniProtKB CARBOHYD
407	N-linked_Glycosylation	ANLLAHMNYSFWIEA HHHHHHCCHHHHHHH	21.30	UniProtKB CARBOHYD
432	N-linked_Glycosylation	PRRAAVVNITTNQAA CCEEEEEEEECCCCC	21.20	UniProtKB CARBOHYD
434 (in isoform 2)	Phosphorylation	-	17.94	-
434	Phosphorylation	RAAVVNITTNQAAPS EEEEEEEECCCCCCC	17.94	-
435 (in isoform 2)	Phosphorylation	-	22.87	-
435	Phosphorylation	AAVVNITTNQAAPSQ EEEEEEECCCCCCCE	22.87	-
454	Phosphorylation	RQERAGQTSVSLLWQ EEECCCCEEEEEEEC	30.12	-
455	Phosphorylation	QERAGQTSVSLLWQE EECCCCEEEEEEECC	11.21	-
457	Phosphorylation	RAGQTSVSLLWQEPE CCCCEEEEEEECCCC	19.94	-
478	Phosphorylation	LEYEIKYYEKDKEMQ EEEEEEEEHHCCCCC	16.11	-
498	Phosphorylation	KAVTTRATVSGLKPG HHHHCCCCCCCCCCC	16.35	-
616	Phosphorylation	FYAEPHTYEEPGRAG CCCCCCCCCCCCCCC	18.43	10498895
625	Phosphorylation	EPGRAGRSFTREIEA CCCCCCCCCCCHHHH	30.01	23403867
627	Phosphorylation	GRAGRSFTREIEASR CCCCCCCCCHHHHHE	28.74	23403867
704	Phosphorylation	IRLEGVVTRGRLAMI EEEEEEEEHHHHEEE	25.62	-
715	Phosphorylation	LAMIVTEYMENGSLD HEEEEHHHHHCCCCC	10.60	-
733	Phosphorylation	RTHDGQFTIMQLVGM ECCCCCEEHHHHHHH	13.98	22964224
770	Phosphorylation	ARNVLVDSNLVCKVS HCCEEECCCCEEEEC	25.28	27461979
777	Phosphorylation	SNLVCKVSDFGLSRV CCCEEEECHHCHHHH	16.83	-
782	Phosphorylation	KVSDFGLSRVLEDDP EECHHCHHHHCCCCC	22.26	19369195
793	Phosphorylation	EDDPDAAYTTTGGKI CCCCCCCCCCCCCCC	13.31	-
839	Phosphorylation	LAYGERPYWNMTNRD HHCCCCCCCCCCCHH	18.68	10498895
905	Phosphorylation	SPESLRATATVSRCP CHHHHCCEEEECCCC	19.21	-
907	Phosphorylation	ESLRATATVSRCPPP HHHCCEEEECCCCCC	18.05	-
909	Phosphorylation	LRATATVSRCPPPAF HCCEEEECCCCCCHH	24.66	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
616	Y	Phosphorylation	Kinase	EPHA8	P29322	PhosphoELM
839	Y	Phosphorylation	Kinase	EPHA8	P29322	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:20100865

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EPHA8_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EPHA8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PK3CG_HUMAN	PIK3CG	physical	11416136
FYN_HUMAN	FYN	physical	10498895
CBL_HUMAN	CBL	physical	20100865
ZN746_HUMAN	ZNF746	physical	21900206
PRS8_HUMAN	PSMC5	physical	21988832
G3BP1_HUMAN	G3BP1	physical	21988832
EFNA5_HUMAN	EFNA5	physical	28514442
NUCG_HUMAN	ENDOG	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.