EPS15_HUMAN - dbPTM
EPS15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPS15_HUMAN
UniProt AC P42566
Protein Name Epidermal growth factor receptor substrate 15
Gene Name EPS15
Organism Homo sapiens (Human).
Sequence Length 896
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Membrane, clathrin-coated pit. Recruited to the plasma membrane upon EGFR activation and localizes to coated pits. Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregat
Protein Description Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2..
Protein Sequence MAAAAQLSLTQLSSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLSSLNLAVPPPRFHDTSSPLLISGTSAAELPWAVKPEDKAKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQLNWCSSPHSILVNGATDYCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEEDPFNVDSSSLTGPVADTNLDFFQSDPFVGSDPFKDDPFGKIDPFGGDPFKGSDPFASDCFFRQSTDPFATSSTDPFSAANNSSITSVETLKHNDPFAPGGTVVAASDSATDPFASVFGNESFGGGFADFSTLSKVNNEDPFRSATSSSVSNVVITKNVFEETSVKSEDEPPALPPKIGTPTRPCPLPPGKRSINKLDSPDPFKLNDPFQPFPGNDSPKEKDPEIFCDPFTSATTTTNKEADPSNFANFSAYPSEEDMIEWAKRESEREEEQRLARLNQQEQEDLELAIALSKSEISEA
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
2Acetylation------MAAAAQLSL
------CCHHHHHHH		13.0519413330
8PhosphorylationMAAAAQLSLTQLSSG
CCHHHHHHHHHHHCC		19.7930108239
10PhosphorylationAAAQLSLTQLSSGNP
HHHHHHHHHHHCCCC		24.8830108239
13PhosphorylationQLSLTQLSSGNPVYE
HHHHHHHHCCCCCHH		26.7830108239
14PhosphorylationLSLTQLSSGNPVYEK
HHHHHHHCCCCCHHH		51.7024043423
19PhosphorylationLSSGNPVYEKYYRQV
HHCCCCCHHHHEEEC		14.1424043423
28PhosphorylationKYYRQVDTGNTGRVL
HHEEECCCCCCHHHH		33.2123828894
99 (in isoform 2)Ubiquitination-27.8021890473
106PhosphorylationPPPRFHDTSSPLLIS
CCCCCCCCCCCEEEC		23.6423401153
107PhosphorylationPPRFHDTSSPLLISG
CCCCCCCCCCEEECC		35.7023927012
108PhosphorylationPRFHDTSSPLLISGT
CCCCCCCCCEEECCC		22.9723927012
113PhosphorylationTSSPLLISGTSAAEL
CCCCEEECCCCHHHC		35.6723927012
115PhosphorylationSPLLISGTSAAELPW
CCEEECCCCHHHCCC		14.3823927012
116PhosphorylationPLLISGTSAAELPWA
CEEECCCCHHHCCCC		29.0723927012
138PhosphorylationKYDAIFDSLSPVNGF
HCHHHHHCCCCCCCC		21.7223403867
140PhosphorylationDAIFDSLSPVNGFLS
HHHHHCCCCCCCCCC		30.6525159151
181 (in isoform 2)Ubiquitination-47.2821890473
217PhosphorylationVPPSKRKTWVVSPAE
CCCCCCCCEEECHHH		27.7623403867
221PhosphorylationKRKTWVVSPAEKAKY
CCCCEEECHHHHCCC		14.5825159151
227MethylationVSPAEKAKYDEIFLK
ECHHHHCCCCEEEEC		65.39-
227UbiquitinationVSPAEKAKYDEIFLK
ECHHHHCCCCEEEEC		65.39-
228PhosphorylationSPAEKAKYDEIFLKT
CHHHHCCCCEEEECC		24.5427642862
234MethylationKYDEIFLKTDKDMDG
CCCEEEECCCCCCCC		43.88-
234UbiquitinationKYDEIFLKTDKDMDG
CCCEEEECCCCCCCC		43.88-
244PhosphorylationKDMDGFVSGLEVREI
CCCCCCCCCHHHHHH		35.09-
304PhosphorylationIDPPHVLTPEMIPPS
CCCCCCCCHHHCCCC		19.0025159151
315PhosphorylationIPPSDRASLQKNIIG
CCCCHHHHHHHHCCC		32.02-
318UbiquitinationSDRASLQKNIIGSSP
CHHHHHHHHCCCCCC		56.24-
323PhosphorylationLQKNIIGSSPVADFS
HHHHCCCCCCCCCHH		22.5129255136
324PhosphorylationQKNIIGSSPVADFSA
HHHCCCCCCCCCHHH		20.4129255136
324 (in isoform 2)Ubiquitination-20.4121890473
330PhosphorylationSSPVADFSAIKELDT
CCCCCCHHHHHHHHH		29.6328176443
333UbiquitinationVADFSAIKELDTLNN
CCCHHHHHHHHHHCH		52.52-
337PhosphorylationSAIKELDTLNNEIVD
HHHHHHHHHCHHHHH		43.9726434776
357AcetylationNNVEQDLKEKEDTIK
CCHHHHHHHHHHHHH		75.047925961
359AcetylationVEQDLKEKEDTIKQR
HHHHHHHHHHHHHHH		60.347925973
367PhosphorylationEDTIKQRTSEVQDLQ
HHHHHHHHHHHHHHH		27.0923312004
368PhosphorylationDTIKQRTSEVQDLQD
HHHHHHHHHHHHHHH		37.6523312004
386UbiquitinationRENTNLQKLQAQKQQ
HHHHHHHHHHHHHHH		45.81-
391UbiquitinationLQKLQAQKQQVQELL
HHHHHHHHHHHHHHH		45.79-
413UbiquitinationAQLEEQLKEVRKKCA
HHHHHHHHHHHHHHH		54.5821890473
413 (in isoform 1)Ubiquitination-54.5821890473
427PhosphorylationAEEAQLISSLKAELT
HHHHHHHHHHHHHHH		37.9024719451
428PhosphorylationEEAQLISSLKAELTS
HHHHHHHHHHHHHHC		27.2223532336
434PhosphorylationSSLKAELTSQESQIS
HHHHHHHHCCHHHHH		21.6228348404
435PhosphorylationSLKAELTSQESQIST
HHHHHHHCCHHHHHH		44.5725159151
440 (in isoform 2)Ubiquitination-4.6521890473
443PhosphorylationQESQISTYEEELAKA
CHHHHHHHHHHHHHH		17.9822817900
449UbiquitinationTYEEELAKAREELSR
HHHHHHHHHHHHHHH		61.68-
449 (in isoform 2)Ubiquitination-61.6821890473
455PhosphorylationAKAREELSRLQQETA
HHHHHHHHHHHHHHH		33.9421712546
461PhosphorylationLSRLQQETAELEESV
HHHHHHHHHHHHHHH		22.5427251275
467PhosphorylationETAELEESVESGKAQ
HHHHHHHHHHHCHHH		23.0825159151
470PhosphorylationELEESVESGKAQLEP
HHHHHHHHCHHHHHH		43.3625159151
472UbiquitinationEESVESGKAQLEPLQ
HHHHHHCHHHHHHHH		42.09-
474 (in isoform 2)Ubiquitination-50.2521890473
479 (in isoform 2)Ubiquitination-39.0921890473
485PhosphorylationLQQHLQDSQQEISSM
HHHHHHHHHHHHHHH		22.3217525332
487 (in isoform 2)Ubiquitination-54.6821890473
490PhosphorylationQDSQQEISSMQMKLM
HHHHHHHHHHHHHHH		21.0023401153
491PhosphorylationDSQQEISSMQMKLME
HHHHHHHHHHHHHHH		20.7828450419
495UbiquitinationEISSMQMKLMEMKDL
HHHHHHHHHHHHHHH		27.9921890473
495 (in isoform 1)Ubiquitination-27.9921890473
502 (in isoform 2)Ubiquitination-6.2321890473
504 (in isoform 2)Ubiquitination-47.1121890473
507PhosphorylationKDLENHNSQLNWCSS
HHHCCCCCCCCCCCC		28.6126074081
513PhosphorylationNSQLNWCSSPHSILV
CCCCCCCCCCCEEEE		38.2226074081
514PhosphorylationSQLNWCSSPHSILVN
CCCCCCCCCCEEEEC		24.4026074081
517PhosphorylationNWCSSPHSILVNGAT
CCCCCCCEEEECCCC		22.4726074081
522 (in isoform 2)Ubiquitination-23.52-
524PhosphorylationSILVNGATDYCSLST
EEEECCCCCCCCCCC		28.9726074081
546 (in isoform 2)Ubiquitination-18.6821890473
551PhosphorylationEGQSNLESEPIHQES
CCCCCCCCCCCCCCC		52.4126074081
558PhosphorylationSEPIHQESPARSSPE
CCCCCCCCCCCCCCC		19.7926074081
562PhosphorylationHQESPARSSPELLPS
CCCCCCCCCCCCCCC		52.9630266825
563PhosphorylationQESPARSSPELLPSG
CCCCCCCCCCCCCCC		19.4822167270
569PhosphorylationSSPELLPSGVTDENE
CCCCCCCCCCCCCCH		45.9530266825
572PhosphorylationELLPSGVTDENEVTT
CCCCCCCCCCCHHHH		40.9130266825
576 (in isoform 2)Ubiquitination-38.9121890473
578PhosphorylationVTDENEVTTAVTEKV
CCCCCHHHHHHHHHH		11.6723927012
579PhosphorylationTDENEVTTAVTEKVC
CCCCHHHHHHHHHHH		25.0623927012
582PhosphorylationNEVTTAVTEKVCSEL
CHHHHHHHHHHHHHH		27.8523927012
587PhosphorylationAVTEKVCSELDNNRH
HHHHHHHHHHCCCCC		44.1520860994
595PhosphorylationELDNNRHSKEEDPFN
HHCCCCCCCCCCCCC		38.2325159151
605PhosphorylationEDPFNVDSSSLTGPV
CCCCCCCHHHCCCCC		19.9725159151
606PhosphorylationDPFNVDSSSLTGPVA
CCCCCCHHHCCCCCC		25.5525159151
607PhosphorylationPFNVDSSSLTGPVAD
CCCCCHHHCCCCCCC		33.6228387310
609PhosphorylationNVDSSSLTGPVADTN
CCCHHHCCCCCCCCC		41.1925159151
615PhosphorylationLTGPVADTNLDFFQS
CCCCCCCCCCHHHHC		28.1328348404
632UbiquitinationFVGSDPFKDDPFGKI
CCCCCCCCCCCCCCC		67.61-
638UbiquitinationFKDDPFGKIDPFGGD
CCCCCCCCCCCCCCC		44.2921890473
638 (in isoform 1)Ubiquitination-44.2921890473
648UbiquitinationPFGGDPFKGSDPFAS
CCCCCCCCCCCCCHH		63.99-
655PhosphorylationKGSDPFASDCFFRQS
CCCCCCHHHCCCCCC		34.9827251275
662PhosphorylationSDCFFRQSTDPFATS
HHCCCCCCCCCCCCC		30.4425003641
663PhosphorylationDCFFRQSTDPFATSS
HCCCCCCCCCCCCCC		39.08-
668PhosphorylationQSTDPFATSSTDPFS
CCCCCCCCCCCCCCC		24.4822199227
669PhosphorylationSTDPFATSSTDPFSA
CCCCCCCCCCCCCCC		28.0119690332
670PhosphorylationTDPFATSSTDPFSAA
CCCCCCCCCCCCCCC		32.2626657352
671PhosphorylationDPFATSSTDPFSAAN
CCCCCCCCCCCCCCC		47.6729507054
675PhosphorylationTSSTDPFSAANNSSI
CCCCCCCCCCCCCCC		31.6822199227
680PhosphorylationPFSAANNSSITSVET
CCCCCCCCCCCEEEE		23.9522199227
681PhosphorylationFSAANNSSITSVETL
CCCCCCCCCCEEEEC		31.8221815630
683PhosphorylationAANNSSITSVETLKH
CCCCCCCCEEEECCC		28.7722199227
684PhosphorylationANNSSITSVETLKHN
CCCCCCCEEEECCCC		19.1122199227
687PhosphorylationSSITSVETLKHNDPF
CCCCEEEECCCCCCC		38.6627251275
713PhosphorylationSATDPFASVFGNESF
CCCCCCHHHHCCCCC		20.5424275569
719PhosphorylationASVFGNESFGGGFAD
HHHHCCCCCCCCCCC		32.9425159151
741PhosphorylationNNEDPFRSATSSSVS
CCCCCCCCCCCCCEE		35.9623312004
743PhosphorylationEDPFRSATSSSVSNV
CCCCCCCCCCCEEEE		30.3223312004
744PhosphorylationDPFRSATSSSVSNVV
CCCCCCCCCCEEEEE		21.9730108239
745PhosphorylationPFRSATSSSVSNVVI
CCCCCCCCCEEEEEE		30.3330108239
746PhosphorylationFRSATSSSVSNVVIT
CCCCCCCCEEEEEEE		29.3625159151
748PhosphorylationSATSSSVSNVVITKN
CCCCCCEEEEEEECC		26.3430108239
754UbiquitinationVSNVVITKNVFEETS
EEEEEEECCCCCCCC		39.7321890473
754 (in isoform 1)Ubiquitination-39.7321890473
760PhosphorylationTKNVFEETSVKSEDE
ECCCCCCCCCCCCCC		31.4627251275
761PhosphorylationKNVFEETSVKSEDEP
CCCCCCCCCCCCCCC		30.7227251275
763UbiquitinationVFEETSVKSEDEPPA
CCCCCCCCCCCCCCC		48.1421906983
763 (in isoform 1)Ubiquitination-48.1421890473
764PhosphorylationFEETSVKSEDEPPAL
CCCCCCCCCCCCCCC		48.3928348404
774UbiquitinationEPPALPPKIGTPTRP
CCCCCCCCCCCCCCC		52.40-
777PhosphorylationALPPKIGTPTRPCPL
CCCCCCCCCCCCCCC		25.5930266825
779PhosphorylationPPKIGTPTRPCPLPP
CCCCCCCCCCCCCCC		47.2630266825
788AcetylationPCPLPPGKRSINKLD
CCCCCCCCCCCCCCC		49.0625953088
788UbiquitinationPCPLPPGKRSINKLD
CCCCCCCCCCCCCCC		49.0621890473
788 (in isoform 1)Ubiquitination-49.0621890473
790PhosphorylationPLPPGKRSINKLDSP
CCCCCCCCCCCCCCC		33.7225159151
793AcetylationPGKRSINKLDSPDPF
CCCCCCCCCCCCCCC		52.5925953088
793UbiquitinationPGKRSINKLDSPDPF
CCCCCCCCCCCCCCC		52.5921890473
793 (in isoform 1)Ubiquitination-52.5921890473
796PhosphorylationRSINKLDSPDPFKLN
CCCCCCCCCCCCCCC		41.4619664994
801UbiquitinationLDSPDPFKLNDPFQP
CCCCCCCCCCCCCCC		52.3321890473
801 (in isoform 1)Ubiquitination-52.3321890473
814PhosphorylationQPFPGNDSPKEKDPE
CCCCCCCCCCCCCCC		41.7019664994
816UbiquitinationFPGNDSPKEKDPEIF
CCCCCCCCCCCCCCC		79.8021890473
816 (in isoform 1)Ubiquitination-79.8021890473
818UbiquitinationGNDSPKEKDPEIFCD
CCCCCCCCCCCCCCC		82.0521890473
818 (in isoform 1)Ubiquitination-82.0521890473
828PhosphorylationEIFCDPFTSATTTTN
CCCCCCCCCCCCCCC		23.8829632367
829PhosphorylationIFCDPFTSATTTTNK
CCCCCCCCCCCCCCC		24.8123403867
831PhosphorylationCDPFTSATTTTNKEA
CCCCCCCCCCCCCCC		25.1723403867
832PhosphorylationDPFTSATTTTNKEAD
CCCCCCCCCCCCCCC		31.1923403867
833PhosphorylationPFTSATTTTNKEADP
CCCCCCCCCCCCCCC		24.8223403867
834PhosphorylationFTSATTTTNKEADPS
CCCCCCCCCCCCCCC		42.0523403867
836UbiquitinationSATTTTNKEADPSNF
CCCCCCCCCCCCCCC		52.79-
841PhosphorylationTNKEADPSNFANFSA
CCCCCCCCCCCCCCC		45.1625348954
847PhosphorylationPSNFANFSAYPSEED
CCCCCCCCCCCCHHH		27.0527307780
849PhosphorylationNFANFSAYPSEEDMI
CCCCCCCCCCHHHHH		13.1919605366
851PhosphorylationANFSAYPSEEDMIEW
CCCCCCCCHHHHHHH		40.7328102081
860UbiquitinationEDMIEWAKRESEREE
HHHHHHHHHHHHHHH		58.7421906983
860 (in isoform 1)Ubiquitination-58.7421890473
890UbiquitinationELAIALSKSEISEA-
HHHHHHHHHHHHCC-		53.62890473
890 (in isoform 1)Ubiquitination-53.6221890473
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
796SPhosphorylationKinaseMAPK14Q16539
GPS
849YPhosphorylationKinaseEGFRP00533
Uniprot
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:16862145
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:17013377
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:22051607
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPS15_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 EPS15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGFG1_HUMANAGFG1genetic
10613896
HGS_HUMANHGSphysical
10809762
AP2A2_HUMANAP2A2physical
10809762
DYN2_HUMANDNM2physical
11483962
AP2A1_HUMANAP2A1physical
9049247
EGFR_HUMANEGFRphysical
9049247
GRB2_HUMANGRB2physical
7797522
CRK_HUMANCRKphysical
7797522
RFIP2_HUMANRAB11FIP2physical
12364336
SYNJ1_RATSynj1physical
9428629
REPS2_HUMANREPS2physical
10393179
UBP8_HUMANUSP8physical
16771824
EPS15_HUMANEPS15physical
12957285
UBQL1_HUMANUBQLN1physical
17082820
UBC_HUMANUBCphysical
17013377
TGFB1_HUMANTGFB1physical
19109251
EGFR_HUMANEGFRphysical
19109251
GRB2_HUMANGRB2physical
19109251
CXA1_HUMANGJA1physical
19835873
UBQL1_HUMANUBQLN1physical
16159959
EGFR_HUMANEGFRphysical
16429130
EPN1_HUMANEPN1physical
21115825
EPN3_HUMANEPN3physical
21115825
EPS15_HUMANEPS15physical
9407139
AP1B1_HUMANAP1B1physical
12538641
AP2A1_HUMANAP2A1physical
10953014
AGFG1_HUMANAGFG1physical
11062555
AP2A_HUMANTFAP2Aphysical
9490719
EPS15_HUMANEPS15physical
19380743
AP2B1_HUMANAP2B1physical
19380743
AP2A1_HUMANAP2A1physical
19380743
IQGA1_HUMANIQGAP1physical
19380743
KRT85_HUMANKRT85physical
19380743
K2C1_HUMANKRT1physical
19380743
K1C10_HUMANKRT10physical
19380743
K22E_HUMANKRT2physical
19380743
AP2M1_HUMANAP2M1physical
19380743
K1C14_HUMANKRT14physical
19380743
KRT86_HUMANKRT86physical
19380743
AP1B1_HUMANAP1B1physical
19380743
AP2A2_HUMANAP2A2physical
19380743
K2C5_HUMANKRT5physical
19380743
K2C6A_HUMANKRT6Aphysical
19380743
FCHO2_HUMANFCHO2physical
19380743
K1C16_HUMANKRT16physical
19380743
K1C9_HUMANKRT9physical
19380743
HSP7C_HUMANHSPA8physical
19380743
KRT35_HUMANKRT35physical
19380743
GRP75_HUMANHSPA9physical
19380743
STON2_HUMANSTON2physical
19380743
K1C17_HUMANKRT17physical
19380743
KT33B_HUMANKRT33Bphysical
19380743
KRT83_HUMANKRT83physical
19380743
BMP2K_HUMANBMP2Kphysical
19380743
KRT34_HUMANKRT34physical
19380743
KRT82_HUMANKRT82physical
19380743
NONO_HUMANNONOphysical
19380743
KRT38_HUMANKRT38physical
19380743
UBC_HUMANUBCphysical
19380743
K2C75_HUMANKRT75physical
19380743
K2C79_HUMANKRT79physical
19380743
PRDX1_HUMANPRDX1physical
19380743
KRT36_HUMANKRT36physical
19380743
K1H2_HUMANKRT32physical
19380743
MAP4_HUMANMAP4physical
19380743
HS71L_HUMANHSPA1Lphysical
19380743
KRT37_HUMANKRT37physical
19380743
GRP78_HUMANHSPA5physical
19380743
CRK_HUMANCRKphysical
19380743
K2C73_HUMANKRT73physical
19380743
AP2S1_HUMANAP2S1physical
19380743
NECP2_HUMANNECAP2physical
19380743
TRAF2_HUMANTRAF2physical
19380743
MCCB_HUMANMCCC2physical
19380743
ACTB_HUMANACTBphysical
19380743
K2C3_HUMANKRT3physical
19380743
DCAF1_HUMANVPRBPphysical
19380743
ABL1_HUMANABL1physical
19380743
TBB5_HUMANTUBBphysical
19380743
PCCB_HUMANPCCBphysical
19380743
KRA93_HUMANKRTAP9-3physical
19380743
NECP1_HUMANNECAP1physical
19380743
TCPG_HUMANCCT3physical
19380743
CRKL_HUMANCRKLphysical
19380743
STON2_HUMANSTON2physical
18200045
EPN1_HUMANEPN1physical
18375383
RABL6_HUMANRABL6physical
22863883
CORO7_HUMANCORO7physical
24768539
AGFG2_HUMANAGFG2genetic
10613896
NUMB_MOUSENumbphysical
23211419
CLH1_HUMANCLTCphysical
18524853
AP1G1_HUMANAP1G1physical
18524853
AP2A_HUMANTFAP2Aphysical
18524853
SPOPL_HUMANSPOPLphysical
27008177
SGIP1_HUMANSGIP1physical
26822536
FCHO1_HUMANFCHO1physical
26822536
AP2A2_HUMANAP2A2physical
26822536
RNF26_HUMANRNF26physical
27368102
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 EPS15_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-323; SER-324;SER-814 AND TYR-849, AND MASS SPECTROMETRY.
"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-140; SER-323; SER-485AND SER-814, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-814, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; THR-777; SER-796AND SER-814, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND MASSSPECTROMETRY.
"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 SER-323, AND MASSSPECTROMETRY.
"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-814, AND MASSSPECTROMETRY.
"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-849, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory