dbPTM

EPS8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EPS8_MOUSE
UniProt AC	Q08509
Protein Name	Epidermal growth factor receptor kinase substrate 8
Gene Name	Eps8
Organism	Mus musculus (Mouse).
Sequence Length	821
Subcellular Localization	Cytoplasm, cell cortex. Cell projection, ruffle membrane. Cell projection, growth cone. Cell projection, stereocilium . Cell junction, synapse, synaptosome. Localizes at the tips of the stereocilia of the inner and outer hair cells (PubMed:24741995,
Protein Description	Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes..
Protein Sequence	MNGHMSNRSSGYGVYPSQLNGYGSSPPYSQMDREHSSRTSAKALYEQRKNYARDSVSSVSDVSQYRVEHLTTFVLDRKDAMITVEDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTISHCQAVVHACSYDSILALVCKEPTQSKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPEALRMIAKADPGIPPPPRAPAPVPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKSKKSKRKGPGEGVLTLRAKPPPPDEFVDCFQKFKHGFNLLAKLKSHIQNPSASDLVHFLFTPLNMVVQATGGPELASSVLSPLLTKDTVDFLNYTATAEERKLWMSLGDSWVKVRAEWPKEQFIPPYVPRFRNGWEPPMLNFMGAPTEQDMYQLAESVANAEHQRKQDSKRLSTEHSNVSDYPPADGYAYSSSMYHRGPHADHGEAAMPFKSTPNHQVDRNYDAVKTQPKKYAKSKYDFVARNSSELSVMKDDVLEILDDRRQWWKVRNASGDSGFVPNNILDIMRTPESGVGRADPPYTHTIQKQRTEYGLRSADTPSAPSPPPTPAPVPVPLPPSVPAPVSVPKVPANVTRQNSSSSDSGGSIVRDSQRYKQLPVDRRKSQMEEVQDELFQRLTIGRSAAQRKFHVPRQNVPVINITYDSSPEEVKTWLQSKGFNPVTVNSLGVLNGAQLFSLNKDELRSVCPEGARVFNQITVQKAALEDSNGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	RSSGYGVYPSQLNGY CCCCCCCCHHHCCCC	7.87	29514104
22	Phosphorylation	YPSQLNGYGSSPPYS CHHHCCCCCCCCCHH	16.86	29514104
25	Phosphorylation	QLNGYGSSPPYSQMD HCCCCCCCCCHHHCC	26.07	29514104
28	Phosphorylation	GYGSSPPYSQMDREH CCCCCCCHHHCCCHH	18.21	29514104
29	Phosphorylation	YGSSPPYSQMDREHS CCCCCCHHHCCCHHC	25.46	29514104
45	Phosphorylation	RTSAKALYEQRKNYA HHHHHHHHHHHHHHC	18.18	25367039
55	Phosphorylation	RKNYARDSVSSVSDV HHHHCHHCCCCHHHH	20.53	29899451
57	Phosphorylation	NYARDSVSSVSDVSQ HHCHHCCCCHHHHHH	29.04	26370283
58	Phosphorylation	YARDSVSSVSDVSQY HCHHCCCCHHHHHHH	24.39	30635358
60	Phosphorylation	RDSVSSVSDVSQYRV HHCCCCHHHHHHHHH	33.95	30635358
63	Phosphorylation	VSSVSDVSQYRVEHL CCCHHHHHHHHHHHE	26.87	30635358
185	Phosphorylation	EDIESAISDSKGGKQ HHHHHHHHCCCCCCC	35.23	-
187	Phosphorylation	IESAISDSKGGKQKR HHHHHHCCCCCCCCC	26.81	-
223	Phosphorylation	PAPVPPGTVTQVDVR CCCCCCCCEEEEECH	26.59	25619855
295	Phosphorylation	QKAAEAFSELSKRKK HHHHHHHHHHHHHHH	44.68	19854140
298	Phosphorylation	AEAFSELSKRKKSKK HHHHHHHHHHHHCCC	26.77	29514104
317	Phosphorylation	GPGEGVLTLRAKPPP CCCCCEEEEEECCCC	16.28	27180971
475	Phosphorylation	KQDSKRLSTEHSNVS HHHHHCCCCCCCCCC	35.46	28638064
476	Phosphorylation	QDSKRLSTEHSNVSD HHHHCCCCCCCCCCC	42.16	26643407
479	Phosphorylation	KRLSTEHSNVSDYPP HCCCCCCCCCCCCCC	32.47	26643407
482	Phosphorylation	STEHSNVSDYPPADG CCCCCCCCCCCCCCC	35.36	26643407
484	Phosphorylation	EHSNVSDYPPADGYA CCCCCCCCCCCCCCE	12.01	18563927
490	Phosphorylation	DYPPADGYAYSSSMY CCCCCCCCEECCCCC	11.69	25777480
492	Phosphorylation	PPADGYAYSSSMYHR CCCCCCEECCCCCCC	10.70	25777480
493	Phosphorylation	PADGYAYSSSMYHRG CCCCCEECCCCCCCC	14.04	25777480
494	Phosphorylation	ADGYAYSSSMYHRGP CCCCEECCCCCCCCC	13.37	25777480
495	Phosphorylation	DGYAYSSSMYHRGPH CCCEECCCCCCCCCC	19.88	25777480
497	Phosphorylation	YAYSSSMYHRGPHAD CEECCCCCCCCCCCC	7.13	25777480
514	Phosphorylation	EAAMPFKSTPNHQVD CCCCCCCCCCCCCCC	49.85	25777480
524	Phosphorylation	NHQVDRNYDAVKTQP CCCCCCCHHHHHCCC	13.23	20116462
534	Phosphorylation	VKTQPKKYAKSKYDF HHCCCHHHHHCHHCE	25.95	-
539	Phosphorylation	KKYAKSKYDFVARNS HHHHHCHHCEECCCC	23.00	28418008
546	Phosphorylation	YDFVARNSSELSVMK HCEECCCCCCCCEEC	21.45	27180971
547	Phosphorylation	DFVARNSSELSVMKD CEECCCCCCCCEECH	46.21	29472430
573	Phosphorylation	WWKVRNASGDSGFVP HEEEECCCCCCCCCC	46.83	27180971
601	Phosphorylation	VGRADPPYTHTIQKQ CCCCCCCCCCCCCCC	19.28	25367039
602	Phosphorylation	GRADPPYTHTIQKQR CCCCCCCCCCCCCCC	20.51	25367039
604	Phosphorylation	ADPPYTHTIQKQRTE CCCCCCCCCCCCCCH	19.80	29514104
610	Phosphorylation	HTIQKQRTEYGLRSA CCCCCCCCHHCCCCC	30.94	25367039
612	Phosphorylation	IQKQRTEYGLRSADT CCCCCCHHCCCCCCC	22.35	25367039
616	Phosphorylation	RTEYGLRSADTPSAP CCHHCCCCCCCCCCC	35.22	25619855
619	Phosphorylation	YGLRSADTPSAPSPP HCCCCCCCCCCCCCC	20.89	25619855
621	Phosphorylation	LRSADTPSAPSPPPT CCCCCCCCCCCCCCC	55.71	25619855
624	Phosphorylation	ADTPSAPSPPPTPAP CCCCCCCCCCCCCCC	50.16	27087446
628	Phosphorylation	SAPSPPPTPAPVPVP CCCCCCCCCCCCCCC	37.54	22942356
639	Phosphorylation	VPVPLPPSVPAPVSV CCCCCCCCCCCCCCC	38.50	25619855
645	Phosphorylation	PSVPAPVSVPKVPAN CCCCCCCCCCCCCCC	31.48	25619855
654	Phosphorylation	PKVPANVTRQNSSSS CCCCCCCCCCCCCCC	26.75	26643407
658	Phosphorylation	ANVTRQNSSSSDSGG CCCCCCCCCCCCCCC	24.21	25521595
659	Phosphorylation	NVTRQNSSSSDSGGS CCCCCCCCCCCCCCC	41.22	23684622
660	Phosphorylation	VTRQNSSSSDSGGSI CCCCCCCCCCCCCCC	37.68	23375375
661	Phosphorylation	TRQNSSSSDSGGSIV CCCCCCCCCCCCCCC	37.43	25521595
663	Phosphorylation	QNSSSSDSGGSIVRD CCCCCCCCCCCCCCC	47.18	27087446
666	Phosphorylation	SSSDSGGSIVRDSQR CCCCCCCCCCCCCHH	22.80	29514104
671	Phosphorylation	GGSIVRDSQRYKQLP CCCCCCCCHHHHCCC	13.14	29899451
674	Phosphorylation	IVRDSQRYKQLPVDR CCCCCHHHHCCCCHH	8.75	25367039
683	Ubiquitination	QLPVDRRKSQMEEVQ CCCCHHHHHHHHHHH	46.03	-
684	Phosphorylation	LPVDRRKSQMEEVQD CCCHHHHHHHHHHHH	32.71	25521595
725	Phosphorylation	INITYDSSPEEVKTW EEEEECCCHHHHHHH	33.17	25521595
786	Phosphorylation	QKAALEDSNGSSELQ EHHHHHCCCCCHHHH	33.44	19060867
789	Phosphorylation	ALEDSNGSSELQEIM HHHCCCCCHHHHHHH	25.53	30635358
790	Phosphorylation	LEDSNGSSELQEIMR HHCCCCCHHHHHHHH	43.66	30635358
804	Phosphorylation	RRRQEKISAAASDSG HHHHHHHHHHHHCCC	23.95	25619855
808	Phosphorylation	EKISAAASDSGVESF HHHHHHHHCCCCCCC	27.81	25619855
810	Phosphorylation	ISAAASDSGVESFDE HHHHHHCCCCCCCCC	42.09	27087446
814	Phosphorylation	ASDSGVESFDEGSSH HHCCCCCCCCCCCCC	35.27	27087446
819	Phosphorylation	VESFDEGSSH----- CCCCCCCCCC-----	24.16	25619855
820	Phosphorylation	ESFDEGSSH------ CCCCCCCCC------	44.03	25619855

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
497	Y	Phosphorylation	Kinase	BRK	Q64434	PSP
524	Y	Phosphorylation	Kinase	BRK	Q64434	PSP
534	Y	Phosphorylation	Kinase	BRK	Q64434	PSP
624	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
624	S	Phosphorylation	Kinase	MAPK	-	Uniprot
628	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
628	T	Phosphorylation	Kinase	MAPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
624	S	Phosphorylation	19564905
Phosphorylation at Ser-624 and Thr-628 by MAPK following BDNF treatment promotes removal from actin and filopodia formation.
628	T	Phosphorylation	19564905
Phosphorylation at Ser-624 and Thr-628 by MAPK following BDNF treatment promotes removal from actin and filopodia formation.

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 EPS8_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBL_MOUSE	Cbl	physical	7517397
NMDZ1_MOUSE	Grin1	physical	17018287
NMDE1_MOUSE	Grin2a	physical	17018287
NMDE3_MOUSE	Grin2c	physical	17018287
P85A_MOUSE	Pik3r1	physical	12515821
ABI1_MOUSE	Abi1	physical	12515821
SOS1_MOUSE	Sos1	physical	12515821

Drug and Disease Associations

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

Regulatory Network of EPS8_MOUSE

Related Literatures of Post-Translational Modification

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