ES8L2_HUMAN - dbPTM
ES8L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ES8L2_HUMAN
UniProt AC Q9H6S3
Protein Name Epidermal growth factor receptor kinase substrate 8-like protein 2
Gene Name EPS8L2
Organism Homo sapiens (Human).
Sequence Length 715
Subcellular Localization Cytoplasm . Cell projection, stereocilium . Localizes at the tips of the stereocilia of the inner and outer hair cells.
Protein Description Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. In the cochlea, is required for stereocilia maintenance in adult hair cells (By similarity)..
Protein Sequence MSQSGAVSCCPGATNGSLGRSDGVAKMSPKDLFEQRKKYSNSNVIMHETSQYHVQHLATFIMDKSEAITSVDDAIRKLVQLSSKEKIWTQEMLLQVNDQSLRLLDIESQEELEDFPLPTVQRSQTVLNQLRYPSVLLLVCQDSEQSKPDVHFFHCDEVEAELVHEDIESALADCRLGKKMRPQTLKGHQEKIRQRQSILPPPQGPAPIPFQHRGGDSPEAKNRVGPQVPLSEPGFRRRESQEEPRAVLAQKIEKETQILNCALDDIEWFVARLQKAAEAFKQLNQRKKGKKKGKKAPAEGVLTLRARPPSEGEFIDCFQKIKLAINLLAKLQKHIQNPSAAELVHFLFGPLDLIVNTCSGPDIARSVSCPLLSRDAVDFLRGHLVPKEMSLWESLGESWMRPRSEWPREPQVPLYVPKFHSGWEPPVDVLQEAPWEVEGLASAPIEEVSPVSRQSIRNSQKHSPTSEPTPPGDALPPVSSPHTHRGYQPTPAMAKYVKILYDFTARNANELSVLKDEVLEVLEDGRQWWKLRSRSGQAGYVPCNILGEARPEDAGAPFEQAGQKYWGPASPTHKLPPSFPGNKDELMQHMDEVNDELIRKISNIRAQPQRHFRVERSQPVSQPLTYESGPDEVRAWLEAKAFSPRIVENLGILTGPQLFSLNKEELKKVCGEEGVRVYSQLTMQKAFLEKQQSGSELEELMNKFHSMNQRRGEDS
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 Orthologous
Protein Cluster
2Phosphorylation------MSQSGAVSC
------CCCCCCCCC		32.8125159151
4Phosphorylation----MSQSGAVSCCP
----CCCCCCCCCCC		22.7823663014
8O-linked_GlycosylationMSQSGAVSCCPGATN
CCCCCCCCCCCCCCC		14.9629485866
8PhosphorylationMSQSGAVSCCPGATN
CCCCCCCCCCCCCCC		14.9630619164
14PhosphorylationVSCCPGATNGSLGRS
CCCCCCCCCCCCCCC		46.1323663014
17PhosphorylationCPGATNGSLGRSDGV
CCCCCCCCCCCCCCC		29.7125159151
21PhosphorylationTNGSLGRSDGVAKMS
CCCCCCCCCCCCCCC		36.6025159151
28PhosphorylationSDGVAKMSPKDLFEQ
CCCCCCCCHHHHHHH		28.2622617229
30UbiquitinationGVAKMSPKDLFEQRK
CCCCCCHHHHHHHHH		60.8129967540
39PhosphorylationLFEQRKKYSNSNVIM
HHHHHHHHCCCCCEE		19.0024275569
40PhosphorylationFEQRKKYSNSNVIMH
HHHHHHHCCCCCEEE		42.5328985074
42PhosphorylationQRKKYSNSNVIMHET
HHHHHCCCCCEEEEC		26.9127251275
50PhosphorylationNVIMHETSQYHVQHL
CCEEEECCHHHHHHH		26.2528985074
65PhosphorylationATFIMDKSEAITSVD
HHHHCCHHHHCCCHH		28.1728985074
77UbiquitinationSVDDAIRKLVQLSSK
CHHHHHHHHHHHHCC		47.0729967540
82PhosphorylationIRKLVQLSSKEKIWT
HHHHHHHHCCCCCCC		23.4429083192
83PhosphorylationRKLVQLSSKEKIWTQ
HHHHHHHCCCCCCCH		54.1229083192
84UbiquitinationKLVQLSSKEKIWTQE
HHHHHHCCCCCCCHH		60.7029967540
100PhosphorylationLLQVNDQSLRLLDIE
HHHHCHHHEEEECCC		20.5127251275
108PhosphorylationLRLLDIESQEELEDF
EEEECCCCHHHHHCC		43.1328102081
125PhosphorylationPTVQRSQTVLNQLRY
CCCCCHHHHHHHCCC		28.3628857561
184PhosphorylationGKKMRPQTLKGHQEK
CCCCCCHHHHHHHHH		32.8727422710
197PhosphorylationEKIRQRQSILPPPQG
HHHHHHHCCCCCCCC		28.4328857561
217PhosphorylationFQHRGGDSPEAKNRV
CCCCCCCCHHHHHCC		28.1028355574
231PhosphorylationVGPQVPLSEPGFRRR
CCCCCCCCCCCCCCC		35.3630243723
240PhosphorylationPGFRRRESQEEPRAV
CCCCCCCCCCCHHHH		40.8727273156
251UbiquitinationPRAVLAQKIEKETQI
HHHHHHHHHHHHHHH		47.4229967540
275UbiquitinationWFVARLQKAAEAFKQ
HHHHHHHHHHHHHHH		54.9029967540
303PhosphorylationAPAEGVLTLRARPPS
CCCCCEEEEEECCCC		16.2828355574
310PhosphorylationTLRARPPSEGEFIDC
EEEECCCCCCCCHHH		62.0023898821
366PhosphorylationSGPDIARSVSCPLLS
CCHHHHHHCCCCCCC		14.9023312004
368PhosphorylationPDIARSVSCPLLSRD
HHHHHHCCCCCCCCH		15.9727499020
390PhosphorylationHLVPKEMSLWESLGE
CCCCHHHHHHHHHHH		31.2721406692
394PhosphorylationKEMSLWESLGESWMR
HHHHHHHHHHHCCCC		30.0521406692
398PhosphorylationLWESLGESWMRPRSE
HHHHHHHCCCCCCCC		25.1121406692
421PhosphorylationLYVPKFHSGWEPPVD
EECCCCCCCCCCCCC		49.0522199227
442PhosphorylationWEVEGLASAPIEEVS
CEEEEHHCCCHHHCC		39.3522199227
449PhosphorylationSAPIEEVSPVSRQSI
CCCHHHCCCCCHHHH		23.9025159151
452PhosphorylationIEEVSPVSRQSIRNS
HHHCCCCCHHHHHCC		28.1723663014
455PhosphorylationVSPVSRQSIRNSQKH
CCCCCHHHHHCCCCC		23.5427422710
459PhosphorylationSRQSIRNSQKHSPTS
CHHHHHCCCCCCCCC		30.6622167270
463PhosphorylationIRNSQKHSPTSEPTP
HHCCCCCCCCCCCCC		36.5922167270
465PhosphorylationNSQKHSPTSEPTPPG
CCCCCCCCCCCCCCC		49.0522167270
466PhosphorylationSQKHSPTSEPTPPGD
CCCCCCCCCCCCCCC		44.9922167270
469PhosphorylationHSPTSEPTPPGDALP
CCCCCCCCCCCCCCC		37.7622167270
479PhosphorylationGDALPPVSSPHTHRG
CCCCCCCCCCCCCCC		43.8822167270
480PhosphorylationDALPPVSSPHTHRGY
CCCCCCCCCCCCCCC		22.4222167270
483PhosphorylationPPVSSPHTHRGYQPT
CCCCCCCCCCCCCCC		19.3622167270
487PhosphorylationSPHTHRGYQPTPAMA
CCCCCCCCCCCHHHH		15.9827642862
490PhosphorylationTHRGYQPTPAMAKYV
CCCCCCCCHHHHHHH		14.2521659604
501PhosphorylationAKYVKILYDFTARNA
HHHHHHHHHHHCCCC		16.6927642862
512PhosphorylationARNANELSVLKDEVL
CCCCCHHHHCHHHHH		21.16-
540PhosphorylationSRSGQAGYVPCNILG
CCCCCCCEEECCCCC		12.30-
565PhosphorylationFEQAGQKYWGPASPT
HHHCCCCCCCCCCCC		14.0128985074
570PhosphorylationQKYWGPASPTHKLPP
CCCCCCCCCCCCCCC		33.2025159151
572PhosphorylationYWGPASPTHKLPPSF
CCCCCCCCCCCCCCC		29.1930266825
578PhosphorylationPTHKLPPSFPGNKDE
CCCCCCCCCCCCHHH		41.9826330541
602PhosphorylationDELIRKISNIRAQPQ
HHHHHHHHCCCCCCC		29.2824719451
617PhosphorylationRHFRVERSQPVSQPL
CCCCCCCCCCCCCCC		25.9028857561
621PhosphorylationVERSQPVSQPLTYES
CCCCCCCCCCCEECC		32.5328857561
625PhosphorylationQPVSQPLTYESGPDE
CCCCCCCEECCCHHH		31.7420071362
626PhosphorylationPVSQPLTYESGPDEV
CCCCCCEECCCHHHH		18.7720071362
628PhosphorylationSQPLTYESGPDEVRA
CCCCEECCCHHHHHH		45.25-
643PhosphorylationWLEAKAFSPRIVENL
HHHHHCCCHHHHHHC		20.3724719451
663AcetylationPQLFSLNKEELKKVC
HHHHCCCHHHHHHHH		58.8330588551
678PhosphorylationGEEGVRVYSQLTMQK
CCCHHHHHHHHHHHH		4.7122817900
690UbiquitinationMQKAFLEKQQSGSEL
HHHHHHHHHCCCHHH		56.6429967540
693PhosphorylationAFLEKQQSGSELEEL
HHHHHHCCCHHHHHH		41.6228857561
695PhosphorylationLEKQQSGSELEELMN
HHHHCCCHHHHHHHH		44.2330624053
701SulfoxidationGSELEELMNKFHSMN
CHHHHHHHHHHHHHH		6.0821406390
703UbiquitinationELEELMNKFHSMNQR
HHHHHHHHHHHHHHH		30.4129967540
706PhosphorylationELMNKFHSMNQRRGE
HHHHHHHHHHHHCCC		23.6628857561
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

Oops, there are no upstream regulatory protein records of ES8L2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ES8L2_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 ES8L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABI1_HUMANABI1physical
14565974
SOS1_HUMANSOS1physical
14565974
ACTG_HUMANACTG1physical
14565974
A4_HUMANAPPphysical
21832049
RL23_HUMANRPL23physical
21988832
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 ES8L2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; THR-469; SER-480AND SER-570, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-21, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASSSPECTROMETRY.

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