dbPTM

EPHA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EPHA1_HUMAN
UniProt AC	P21709
Protein Name	Ephrin type-A receptor 1
Gene Name	EPHA1
Organism	Homo sapiens (Human).
Sequence Length	976
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein 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. 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..
Protein Sequence	MERRWPLGLGLVLLLCAPLPPGARAKEVTLMDTSKAQGELGWLLDPPKDGWSEQQQILNGTPLYMYQDCPMQGRRDTDHWLRSNWIYRGEEASRVHVELQFTVRDCKSFPGGAGPLGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLVSGSVKLNVERCSLGRLTRRGLYLAFHNPGACVALVSVRVFYQRCPETLNGLAQFPDTLPGPAGLVEVAGTCLPHARASPRPSGAPRMHCSPDGEWLVPVGRCHCEPGYEEGGSGEACVACPSGSYRMDMDTPHCLTCPQQSTAESEGATICTCESGHYRAPGEGPQVACTGPPSAPRNLSFSASGTQLSLRWEPPADTGGRQDVRYSVRCSQCQGTAQDGGPCQPCGVGVHFSPGARGLTTPAVHVNGLEPYANYTFNVEAQNGVSGLGSSGHASTSVSISMGHAESLSGLSLRLVKKEPRQLELTWAGSRPRSPGANLTYELHVLNQDEERYQMVLEPRVLLTELQPDTTYIVRVRMLTPLGPGPFSPDHEFRTSPPVSRGLTGGEIVAVIFGLLLGAALLLGILVFRSRRAQRQRQQRQRDRATDVDREDKLWLKPYVDLQAYEDPAQGALDFTRELDPAWLMVDTVIGEGEFGEVYRGTLRLPSQDCKTVAIKTLKDTSPGGQWWNFLREATIMGQFSHPHILHLEGVVTKRKPIMIITEFMENGALDAFLREREDQLVPGQLVAMLQGIASGMNYLSNHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFQKLQAHLEQLLANPHSLRTIANFDPRMTLRLPSLSGSDGIPYRTVSEWLESIRMKRYILHFHSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	KEVTLMDTSKAQGEL CEEEEEECCCCCCCC	20.40	16964243
34	Phosphorylation	EVTLMDTSKAQGELG EEEEEECCCCCCCCC	23.02	16964243
102	Phosphorylation	VHVELQFTVRDCKSF EEEEEEEEEEECCCC	11.15	27174698
146	Phosphorylation	RPLFQKVTTVAADQS CCHHHCCEEEECCCC	23.69	29978859
147	Phosphorylation	PLFQKVTTVAADQSF CHHHCCEEEECCCCE	15.90	29978859
153	Phosphorylation	TTVAADQSFTIRDLV EEEECCCCEEHHHHH	25.55	29978859
155	Phosphorylation	VAADQSFTIRDLVSG EECCCCEEHHHHHCC	21.98	29978859
196	Phosphorylation	GACVALVSVRVFYQR CCEEEEEEEEHHHHH	12.69	24719451
340	Phosphorylation	PSAPRNLSFSASGTQ CCCCCCEEEEECCCE	22.24	26074081
342	Phosphorylation	APRNLSFSASGTQLS CCCCEEEEECCCEEE	20.39	26074081
344	Phosphorylation	RNLSFSASGTQLSLR CCEEEEECCCEEEEE	40.97	26074081
346	Phosphorylation	LSFSASGTQLSLRWE EEEEECCCEEEEEEE	24.68	26074081
349	Phosphorylation	SASGTQLSLRWEPPA EECCCEEEEEEECCC	13.18	24719451
358	Phosphorylation	RWEPPADTGGRQDVR EEECCCCCCCCCEEE	43.58	26074081
414	N-linked_Glycosylation	NGLEPYANYTFNVEA CCCCCCCCEEEEEEE	30.45	UniProtKB CARBOHYD
478	Ubiquitination	RPRSPGANLTYELHV CCCCCCCCCEEEEEE	38.54	22817900
482	Ubiquitination	PGANLTYELHVLNQD CCCCCEEEEEECCCC	27.45	22817900
493	Phosphorylation	LNQDEERYQMVLEPR CCCCHHHHHHHCCCE	12.30	23403867
504	Phosphorylation	LEPRVLLTELQPDTT CCCEEEEEECCCCCE	30.41	26503514
510	Phosphorylation	LTELQPDTTYIVRVR EEECCCCCEEEEEEE	28.34	26503514
511	Phosphorylation	TELQPDTTYIVRVRM EECCCCCEEEEEEEE	20.73	26503514
512	Phosphorylation	ELQPDTTYIVRVRML ECCCCCEEEEEEEEE	10.26	26503514
593	Ubiquitination	TDVDREDKLWLKPYV CCCCHHHHCCCCCCC	36.49	21906983
597	Ubiquitination	REDKLWLKPYVDLQA HHHHCCCCCCCCCCC	23.79	21906983
599	Phosphorylation	DKLWLKPYVDLQAYE HHCCCCCCCCCCCCC	12.66	22322096
605	Phosphorylation	PYVDLQAYEDPAQGA CCCCCCCCCCCCCCC	14.12	22322096
672	Ubiquitination	GQWWNFLREATIMGQ CHHHHHHHHEEECCC	27.63	22817900
780	Phosphorylation	LLDDFDGTYETQGGK EECCCCCCEECCCCE	21.74	21082442
781	Phosphorylation	LDDFDGTYETQGGKI ECCCCCCEECCCCEE	23.62	27273156
783	Phosphorylation	DFDGTYETQGGKIPI CCCCCEECCCCEECE	23.31	28152594
787	Ubiquitination	TYETQGGKIPIRWTA CEECCCCEECEEEEC	52.73	22817900
805	Phosphorylation	IAHRIFTTASDVWSF HHHHHHCCHHHHHHH	17.26	-
811	Phosphorylation	TTASDVWSFGIVMWE CCHHHHHHHHHHCEE	17.28	-
892	Phosphorylation	ANPHSLRTIANFDPR HCCCHHHHHCCCCCC	29.72	-
906	Phosphorylation	RMTLRLPSLSGSDGI CCEEECCCCCCCCCC	39.50	19664994
908	Phosphorylation	TLRLPSLSGSDGIPY EEECCCCCCCCCCCH	40.36	30278072
910	Phosphorylation	RLPSLSGSDGIPYRT ECCCCCCCCCCCHHC	29.32	19664994
915	Phosphorylation	SGSDGIPYRTVSEWL CCCCCCCHHCHHHHH	19.59	23927012
917	Phosphorylation	SDGIPYRTVSEWLES CCCCCHHCHHHHHHH	23.65	22167270
919	Phosphorylation	GIPYRTVSEWLESIR CCCHHCHHHHHHHHH	23.57	22167270
924	Phosphorylation	TVSEWLESIRMKRYI CHHHHHHHHHHHHHH	17.21	22167270
930	Phosphorylation	ESIRMKRYILHFHSA HHHHHHHHHHHHHHC	11.43	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EPHA1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EPHA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMG1_HUMAN	SMG1	physical	28514442
K1468_HUMAN	KIAA1468	physical	28514442
UBP34_HUMAN	USP34	physical	28514442
SMG9_HUMAN	SMG9	physical	28514442
F1142_HUMAN	FAM114A2	physical	28514442
DYHC2_HUMAN	DYNC2H1	physical	28514442
DIAP3_HUMAN	DIAPH3	physical	28514442
DFNA5_HUMAN	DFNA5	physical	28514442
KIF14_HUMAN	KIF14	physical	28514442
WDR13_HUMAN	WDR13	physical	28514442
ARMC9_HUMAN	ARMC9	physical	28514442
ST17B_HUMAN	STK17B	physical	28514442
CNDH2_HUMAN	NCAPH2	physical	28514442
RRP1_HUMAN	RRP1	physical	28514442
XPO4_HUMAN	XPO4	physical	28514442
MIGA1_HUMAN	FAM73A	physical	28514442
EXC6B_HUMAN	EXOC6B	physical	28514442
STAG1_HUMAN	STAG1	physical	28514442
MTHR_HUMAN	MTHFR	physical	28514442
S39AB_HUMAN	SLC39A11	physical	28514442
SAAL1_HUMAN	SAAL1	physical	28514442
LRBA_HUMAN	LRBA	physical	28514442
CKAP5_HUMAN	CKAP5	physical	28514442
EI2BG_HUMAN	EIF2B3	physical	28514442
CAND2_HUMAN	CAND2	physical	28514442
EI2BE_HUMAN	EIF2B5	physical	28514442
NOP9_HUMAN	NOP9	physical	28514442
HEAT3_HUMAN	HEATR3	physical	28514442
SYAM_HUMAN	AARS2	physical	28514442
SMG8_HUMAN	SMG8	physical	28514442
HOOK2_HUMAN	HOOK2	physical	28514442
PEX19_HUMAN	PEX19	physical	28514442
GTPB3_HUMAN	GTPBP3	physical	28514442
NUCB1_HUMAN	NUCB1	physical	28514442
EI2BD_HUMAN	EIF2B4	physical	28514442
DYM_HUMAN	DYM	physical	28514442
PRKDC_HUMAN	PRKDC	physical	28514442
TNPO2_HUMAN	TNPO2	physical	28514442
IF4G3_HUMAN	EIF4G3	physical	28514442
CNDD3_HUMAN	NCAPD3	physical	28514442
EI2BB_HUMAN	EIF2B2	physical	28514442
DC2L1_HUMAN	DYNC2LI1	physical	28514442
PBIP1_HUMAN	PBXIP1	physical	28514442
TBCD9_HUMAN	TBC1D9	physical	28514442
EXOC7_HUMAN	EXOC7	physical	28514442
RINT1_HUMAN	RINT1	physical	28514442
KNTC1_HUMAN	KNTC1	physical	28514442
NF1_HUMAN	NF1	physical	28514442
EXOC8_HUMAN	EXOC8	physical	28514442
ELMO2_HUMAN	ELMO2	physical	28514442
XPOT_HUMAN	XPOT	physical	28514442
SMC2_HUMAN	SMC2	physical	28514442
HIP1R_HUMAN	HIP1R	physical	28514442
EXOC5_HUMAN	EXOC5	physical	28514442
LTN1_HUMAN	LTN1	physical	28514442
AP3M1_HUMAN	AP3M1	physical	28514442
CNDG2_HUMAN	NCAPG2	physical	28514442
HAUS7_HUMAN	HAUS7	physical	28514442
VPS16_HUMAN	VPS16	physical	28514442
ACOT9_HUMAN	ACOT9	physical	28514442
KCC1A_HUMAN	CAMK1	physical	28514442
IQCB1_HUMAN	IQCB1	physical	28514442
GBF1_HUMAN	GBF1	physical	28514442
BTAF1_HUMAN	BTAF1	physical	28514442
GPN3_HUMAN	GPN3	physical	28514442
OPA1_HUMAN	OPA1	physical	28514442
CTDS2_HUMAN	CTDSP2	physical	28065597
PTN11_HUMAN	PTPN11	physical	28065597
DUS14_HUMAN	DUSP14	physical	28065597
TPTE_HUMAN	TPTE	physical	28065597
MTMRE_HUMAN	MTMR14	physical	28065597

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.

Regulatory Network of EPHA1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-780; TYR-781; SER-906;SER-908; SER-910 AND SER-919, AND MASS SPECTROMETRY.	19369195 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33 AND SER-34, AND MASSSPECTROMETRY.	16964243 [Abstract]