dbPTM

EPS8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EPS8_HUMAN
UniProt AC	Q12929
Protein Name	Epidermal growth factor receptor kinase substrate 8
Gene Name	EPS8
Organism	Homo sapiens (Human).
Sequence Length	822
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 (By similarity). L
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	MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDREHGSKTSAKALYEQRKNYARDSVSSVSDISQYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVMHSCSYDSVLALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPDALRMISNADPSIPPPPRAPAPAPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKNKKGKRKGPGEGVLTLRAKPPPPDEFLDCFQKFKHGFNLLAKLKSHIQNPSAADLVHFLFTPLNMVVQATGGPELASSVLSPLLNKDTIDFLNYTVNGDERQLWMSLGGTWMKARAEWPKEQFIPPYVPRFRNGWEPPMLNFMGATMEQDLYQLAESVANVAEHQRKQEIKRLSTEHSSVSEYHPADGYAFSSNIYTRGSHLDQGEAAVAFKPTSNRHIDRNYEPLKTQPKKYAKSKYDFVARNNSELSVLKDDILEILDDRKQWWKVRNASGDSGFVPNNILDIVRPPESGLGRADPPYTHTIQKQRMEYGPRPADTPPAPSPPPTPAPVPVPLPPSTPAPVPVSKVPANITRQNSSSSDSGGSIVRDSQRHKQLPVDRRKSQMEEVQDELIHRLTIGRSAAQKKFHVPRQNVPVINITYDSTPEDVKTWLQSKGFNPVTVNSLGVLNGAQLFSLNKDELRTVCPEGARVYSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MNGHISNHPSSFG --CCCCCCCCCHHCC	24.34	24043423
10	Phosphorylation	GHISNHPSSFGMYPS CCCCCCCHHCCCCHH	30.65	24043423
11	Phosphorylation	HISNHPSSFGMYPSQ CCCCCCHHCCCCHHH	30.21	24043423
15	Phosphorylation	HPSSFGMYPSQMNGY CCHHCCCCHHHCCCC	10.50	27251789
17	Phosphorylation	SSFGMYPSQMNGYGS HHCCCCHHHCCCCCC	25.27	23898821
22	Phosphorylation	YPSQMNGYGSSPTFS CHHHCCCCCCCCCCC	14.61	24043423
24	Phosphorylation	SQMNGYGSSPTFSQT HHCCCCCCCCCCCHH	25.35	24043423
25	Phosphorylation	QMNGYGSSPTFSQTD HCCCCCCCCCCCHHH	24.48	22817900
27	Phosphorylation	NGYGSSPTFSQTDRE CCCCCCCCCCHHHHC	37.56	24043423
29	Phosphorylation	YGSSPTFSQTDREHG CCCCCCCCHHHHCCC	34.35	23898821
31	Phosphorylation	SSPTFSQTDREHGSK CCCCCCHHHHCCCCH	35.51	24043423
45	Phosphorylation	KTSAKALYEQRKNYA HHHHHHHHHHHHHHC	18.18	28152594
51	Phosphorylation	LYEQRKNYARDSVSS HHHHHHHHCHHCCCC	13.17	28152594
55	Phosphorylation	RKNYARDSVSSVSDI HHHHCHHCCCCHHHH	20.53	25159151
57	Phosphorylation	NYARDSVSSVSDISQ HHCHHCCCCHHHHHH	29.04	23663014
58	Phosphorylation	YARDSVSSVSDISQY HCHHCCCCHHHHHHH	24.39	25159151
60	Phosphorylation	RDSVSSVSDISQYRV HHCCCCHHHHHHHHH	31.04	23663014
63	Phosphorylation	VSSVSDISQYRVEHL CCCHHHHHHHHHHHE	26.59	26074081
65	Phosphorylation	SVSDISQYRVEHLTT CHHHHHHHHHHHEEE	15.16	26074081
71	Phosphorylation	QYRVEHLTTFVLDRK HHHHHHEEEEEECCC	21.79	26074081
72	Phosphorylation	YRVEHLTTFVLDRKD HHHHHEEEEEECCCC	20.36	26074081
97	2-Hydroxyisobutyrylation	KLKLLDAKGKVWTQD HHCEECCCCCCCCCE	59.95	-
188	Acetylation	ESAISDSKGGKQKRR HHHHHCCCCCCCCCC	76.35	30588521
191	Acetylation	ISDSKGGKQKRRPDA HHCCCCCCCCCCCCH	62.40	30588527
193	Acetylation	DSKGGKQKRRPDALR CCCCCCCCCCCCHHH	54.59	30588533
203	Phosphorylation	PDALRMISNADPSIP CCHHHHHHCCCCCCC	19.34	22817900
208	Phosphorylation	MISNADPSIPPPPRA HHHCCCCCCCCCCCC	48.55	25404012
223	Phosphorylation	PAPAPPGTVTQVDVR CCCCCCCCEEEEEEH	26.59	30266825
225	Phosphorylation	PAPPGTVTQVDVRSR CCCCCCEEEEEEHHH	23.78	30206219
231	Phosphorylation	VTQVDVRSRVAAWSA EEEEEEHHHHHHHHH	30.84	22817900
248	Ubiquitination	ADQGDFEKPRQYHEQ HCCCCCCCCHHHCCC	45.56	21906983
252	Phosphorylation	DFEKPRQYHEQEETP CCCCCHHHCCCCCCH	14.49	27259358
258	Phosphorylation	QYHEQEETPEMMAAR HHCCCCCCHHHHHHH	24.64	26356563
295	Phosphorylation	QKAAEAFSELSKRKK HHHHHHHHHHHHHHC	44.68	29514088
298	Phosphorylation	AEAFSELSKRKKNKK HHHHHHHHHHHCCCC	26.77	28355574
299	Malonylation	EAFSELSKRKKNKKG HHHHHHHHHHCCCCC	79.46	26320211
302	Acetylation	SELSKRKKNKKGKRK HHHHHHHCCCCCCCC	77.39	30588539
305	Acetylation	SKRKKNKKGKRKGPG HHHHCCCCCCCCCCC	78.16	30588545
317	Phosphorylation	GPGEGVLTLRAKPPP CCCCCCEEEEECCCC	16.28	30266825
429	Phosphorylation	KEQFIPPYVPRFRNG HHHCCCCCCCCCCCC	20.10	-
454	Phosphorylation	ATMEQDLYQLAESVA CCHHHHHHHHHHHHH	15.12	-
476	Phosphorylation	KQEIKRLSTEHSSVS HHHHHHHHCCCCCCC	35.46	21945579
477	Phosphorylation	QEIKRLSTEHSSVSE HHHHHHHCCCCCCCC	42.16	21945579
480	Phosphorylation	KRLSTEHSSVSEYHP HHHHCCCCCCCCCCC	26.63	21945579
481	Phosphorylation	RLSTEHSSVSEYHPA HHHCCCCCCCCCCCC	31.41	21945579
483	Phosphorylation	STEHSSVSEYHPADG HCCCCCCCCCCCCCC	34.09	21945579
484	Phosphorylation	TEHSSVSEYHPADGY CCCCCCCCCCCCCCC	45.78	17016520
485	Phosphorylation	EHSSVSEYHPADGYA CCCCCCCCCCCCCCE	12.95	21945579
491	Phosphorylation	EYHPADGYAFSSNIY CCCCCCCCEECCCEE	12.67	21945579
494	Phosphorylation	PADGYAFSSNIYTRG CCCCCEECCCEEECC	17.82	21945579
495	Phosphorylation	ADGYAFSSNIYTRGS CCCCEECCCEEECCC	22.31	21945579
498	Phosphorylation	YAFSSNIYTRGSHLD CEECCCEEECCCCCC	8.47	21945579
499	Phosphorylation	AFSSNIYTRGSHLDQ EECCCEEECCCCCCC	25.42	21945579
502	Phosphorylation	SNIYTRGSHLDQGEA CCEEECCCCCCCCCE	20.00	23312004
516	Phosphorylation	AAVAFKPTSNRHIDR EEEEECCCCCCCCCC	38.94	26657352
517	Phosphorylation	AVAFKPTSNRHIDRN EEEECCCCCCCCCCC	40.15	24702127
521	Ubiquitination	KPTSNRHIDRNYEPL CCCCCCCCCCCCCCC	4.86	-
525	Phosphorylation	NRHIDRNYEPLKTQP CCCCCCCCCCCCCCC	21.59	21945579
530	Phosphorylation	RNYEPLKTQPKKYAK CCCCCCCCCCHHHHC	58.76	28152594
538	Phosphorylation	QPKKYAKSKYDFVAR CCHHHHCCHHCEECC	28.42	28152594
540	Phosphorylation	KKYAKSKYDFVARNN HHHHCCHHCEECCCC	23.00	28152594
548	Phosphorylation	DFVARNNSELSVLKD CEECCCCCCCEEEHH	43.39	27251275
574	Phosphorylation	WWKVRNASGDSGFVP HEEEECCCCCCCCCC	46.83	23663014
577	Phosphorylation	VRNASGDSGFVPNNI EECCCCCCCCCCCCE	37.34	23663014
593	Phosphorylation	DIVRPPESGLGRADP EEECCCCCCCCCCCC	45.12	28152594
602	Phosphorylation	LGRADPPYTHTIQKQ CCCCCCCCCCCCHHC	19.28	28152594
603	Phosphorylation	GRADPPYTHTIQKQR CCCCCCCCCCCHHCH	20.51	26657352
605	Phosphorylation	ADPPYTHTIQKQRME CCCCCCCCCHHCHHH	19.80	25849741
613	Phosphorylation	IQKQRMEYGPRPADT CHHCHHHHCCCCCCC	24.08	28152594
620	Phosphorylation	YGPRPADTPPAPSPP HCCCCCCCCCCCCCC	33.02	29255136
625	Phosphorylation	ADTPPAPSPPPTPAP CCCCCCCCCCCCCCC	52.74	29255136
629	Phosphorylation	PAPSPPPTPAPVPVP CCCCCCCCCCCCCCC	37.54	26657352
640	Phosphorylation	VPVPLPPSTPAPVPV CCCCCCCCCCCCCCC	45.12	25850435
641	Phosphorylation	PVPLPPSTPAPVPVS CCCCCCCCCCCCCCC	29.28	25850435
648	Phosphorylation	TPAPVPVSKVPANIT CCCCCCCCCCCCCCC	23.13	25850435
655	Phosphorylation	SKVPANITRQNSSSS CCCCCCCCCCCCCCC	26.47	22199227
659	Phosphorylation	ANITRQNSSSSDSGG CCCCCCCCCCCCCCC	24.21	29255136
660	Phosphorylation	NITRQNSSSSDSGGS CCCCCCCCCCCCCCC	41.22	27273156
661	Phosphorylation	ITRQNSSSSDSGGSI CCCCCCCCCCCCCCC	37.68	27273156
662	Phosphorylation	TRQNSSSSDSGGSIV CCCCCCCCCCCCCCC	37.43	29255136
664	Phosphorylation	QNSSSSDSGGSIVRD CCCCCCCCCCCCCCC	47.18	30278072
667	Phosphorylation	SSSDSGGSIVRDSQR CCCCCCCCCCCCCHH	22.80	23927012
672	Phosphorylation	GGSIVRDSQRHKQLP CCCCCCCCHHHCCCC	20.67	27273156
685	Phosphorylation	LPVDRRKSQMEEVQD CCCCHHHHHHHHHHH	32.71	29255136
699	Phosphorylation	DELIHRLTIGRSAAQ HHHHHHHHHCCCHHH	22.72	27422710
722	Phosphorylation	NVPVINITYDSTPED CCCEEEEEECCCHHH	19.45	26356563
723	Phosphorylation	VPVINITYDSTPEDV CCEEEEEECCCHHHH	12.23	27259358
725	Phosphorylation	VINITYDSTPEDVKT EEEEEECCCHHHHHH	35.13	26356563
726	Phosphorylation	INITYDSTPEDVKTW EEEEECCCHHHHHHH	28.00	-
743	Phosphorylation	SKGFNPVTVNSLGVL HCCCCCCCEEHHCEE	18.41	22817900
746	Phosphorylation	FNPVTVNSLGVLNGA CCCCCEEHHCEECCE	23.36	28842319
765	Phosphorylation	LNKDELRTVCPEGAR CCHHHHHHHCCCCCE	38.80	-
774	Phosphorylation	CPEGARVYSQITVQK CCCCCEEEEEEEEEE	6.84	21082442
775	Phosphorylation	PEGARVYSQITVQKA CCCCEEEEEEEEEEH	16.55	28152594
781	Ubiquitination	YSQITVQKAALEDSS EEEEEEEEHHHHCCC	31.15	21906983
787	Phosphorylation	QKAALEDSSGSSELQ EEHHHHCCCCCHHHH	27.50	30108239
788	Phosphorylation	KAALEDSSGSSELQE EHHHHCCCCCHHHHH	55.82	29759185
790	Phosphorylation	ALEDSSGSSELQEIM HHHCCCCCHHHHHHH	23.69	30108239
791	Phosphorylation	LEDSSGSSELQEIMR HHCCCCCHHHHHHHH	45.94	22817900
797	Sulfoxidation	SSELQEIMRRRQEKI CHHHHHHHHHHHHHH	2.41	30846556
805	Phosphorylation	RRRQEKISAAASDSG HHHHHHHHHHHHCCC	23.95	30183078
809	Phosphorylation	EKISAAASDSGVESF HHHHHHHHCCCCCCC	27.81	30108239
811	Phosphorylation	ISAAASDSGVESFDE HHHHHHCCCCCCCCC	42.09	30278072
815	Phosphorylation	ASDSGVESFDEGSSH HHCCCCCCCCCCCCC	35.27	25159151
820	Phosphorylation	VESFDEGSSH----- CCCCCCCCCC-----	24.16	30108239
821	Phosphorylation	ESFDEGSSH------ CCCCCCCCC------	44.03	30108239

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
629	T	Phosphorylation	Kinase	MAPK	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW5	Q969U6	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
625	S	Phosphorylation	24275569
Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation (By similarity).
629	T	Phosphorylation	-
Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation (By similarity).

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DVL1_HUMAN	DVL1	physical	10581192
BL1S6_HUMAN	BLOC1S6	physical	16189514
CC85B_HUMAN	CCDC85B	physical	16189514
AIMP2_HUMAN	AIMP2	physical	16189514
PCM1_HUMAN	PCM1	physical	16189514
HOOK2_HUMAN	HOOK2	physical	16189514
BAIP2_HUMAN	BAIAP2	physical	16189514
EPS8_HUMAN	EPS8	physical	16189514
ABI1_HUMAN	ABI1	physical	14565974
SOS1_HUMAN	SOS1	physical	14565974
IDLC_HUMAN	DNALI1	physical	16169070
RM20_HUMAN	MRPL20	physical	16169070
MYO15_HUMAN	MYO15A	physical	16169070
ABI1_HUMAN	ABI1	physical	9010225
ABI1_HUMAN	ABI1	physical	11099046
EPS8_HUMAN	EPS8	physical	9303002
SHC1_HUMAN	SHC1	physical	7791787
S27A4_HUMAN	SLC27A4	physical	21988832
TYDP2_HUMAN	TDP2	physical	21988832
XRCC6_HUMAN	XRCC6	physical	21988832
M3K11_HUMAN	MAP3K11	physical	21988832
NFKB2_HUMAN	NFKB2	physical	21988832
RFXAP_HUMAN	RFXAP	physical	21988832
SF3B3_HUMAN	SF3B3	physical	21988832
ZZZ3_HUMAN	ZZZ3	physical	21988832
GULP1_HUMAN	GULP1	physical	21988832
SCRN3_HUMAN	SCRN3	physical	21988832
NACC2_HUMAN	NACC2	physical	21988832
GRB2_HUMAN	GRB2	physical	25416956
HNRPC_HUMAN	HNRNPC	physical	25416956
SMCE1_HUMAN	SMARCE1	physical	25416956
BAIP2_HUMAN	BAIAP2	physical	25416956
PI5PA_HUMAN	INPP5J	physical	25416956
BORC6_HUMAN	C17orf59	physical	25416956
CS025_HUMAN	C19orf25	physical	25416956
XAGE2_HUMAN	XAGE2	physical	25814554
CBL_HUMAN	CBL	physical	25814554
BAIP2_HUMAN	BAIAP2	physical	25814554
CF141_HUMAN	C6orf141	physical	25814554
RCAN3_HUMAN	RCAN3	physical	25814554
RSP14_HUMAN	RSPH14	physical	25814554
IPSP_HUMAN	SERPINA5	physical	25814554
BAIP2_HUMAN	BAIAP2	physical	28514442
AMPD2_HUMAN	AMPD2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615974	Deafness, autosomal recessive, 102 (DFNB102)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EPS8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659; SER-661 ANDSER-662, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811 AND SER-815, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-485 AND TYR-774, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-525 AND TYR-774, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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