ELP1_HUMAN - dbPTM
ELP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELP1_HUMAN
UniProt AC O95163
Protein Name Elongator complex protein 1
Gene Name ELP1 {ECO:0000312|HGNC:HGNC:5959}
Organism Homo sapiens (Human).
Sequence Length 1332
Subcellular Localization Cytoplasm . Nucleus .
Protein Description May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK).; Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration. Involved in neurogenesis (By similarity). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity)..
Protein Sequence MRNLKLFRTLEFRDIQGPGNPQCFSLRTEQGTVLIGSEHGLIEVDPVSREVKNEVSLVAEGFLPEDGSGRIVGVQDLLDQESVCVATASGDVILCSLSTQQLECVGSVASGISVMSWSPDQELVLLATGQQTLIMMTKDFEPILEQQIHQDDFGESKFITVGWGRKETQFHGSEGRQAAFQMQMHESALPWDDHRPQVTWRGDGQFFAVSVVCPETGARKVRVWNREFALQSTSEPVAGLGPALAWKPSGSLIASTQDKPNQQDIVFFEKNGLLHGHFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLQREESSIPKTCVQLWTVGNYHWYLKQSLSFSTCGKSKIVSLMWDPVTPYRLHVLCQGWHYLAYDWHWTTDRSVGDNSSDLSNVAVIDGNRVLVTVFRQTVVPPPMCTYQLLFPHPVNQVTFLAHPQKSNDLAVLDASNQISVYKCGDCPSADPTVKLGAVGGSGFKVCLRTPHLEKRYKIQFENNEDQDVNPLKLGLLTWIEEDVFLAVSHSEFSPRSVIHHLTAASSEMDEEHGQLNVSSSAAVDGVIISLCCNSKTKSVVLQLADGQIFKYLWESPSLAIKPWKNSGGFPVRFPYPCTQTELAMIGEEECVLGLTDRCRFFINDIEVASNITSFAVYDEFLLLTTHSHTCQCFCLRDASFKTLQAGLSSNHVSHGEVLRKVERGSRIVTVVPQDTKLVLQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIYDHNPKVFLGNVETFIKQIDSVNHINLFFTELKEEDVTKTMYPAPVTSSVYLSRDPDGNKIDLVCDAMRAVMESINPHKYCLSILTSHVKKTTPELEIVLQKVHELQGNAPSDPDAVSAEEALKYLLHLVDVNELYDHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKAIGHLSKCGPEYFPECLNLIKDKNLYNEALKLYSPSSQQYQDISIAYGEHLMQEHMYEPAGLMFARCGAHEKALSAFLTCGNWKQALCVAAQLNFTKDQLVGLGRTLAGKLVEQRKHIDAAMVLEECAQDYEEAVLLLLEGAAWEEALRLVYKYNRLDIIETNVKPSILEAQKNYMAFLDSQTATFSRHKKRLLVVRELKEQAQQAGLDDEVPHGQESDLFSETSSVVSGSEMSGKYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEDLALLEALSEVVQNTENLKDEVYHILKVLFLFEFDEQGRELQKAFEDTLQLMERSLPEIWTLTYQQNSATPVLGPNSTANSIMASYQQQKTSVPVLDAELFIPPKINRRTQWKLSLLD
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
157UbiquitinationQDDFGESKFITVGWG
CCCCCCCCEEEEEEC		36.16-
166UbiquitinationITVGWGRKETQFHGS
EEEEECCCCCEECCH		62.26-
173PhosphorylationKETQFHGSEGRQAAF
CCCEECCHHHHHHHH		28.4525159151
232PhosphorylationNREFALQSTSEPVAG
EHHHEECCCCCCCCC		34.4522210691
233PhosphorylationREFALQSTSEPVAGL
HHHEECCCCCCCCCC		24.9322210691
234PhosphorylationEFALQSTSEPVAGLG
HHEECCCCCCCCCCC		45.1922210691
247UbiquitinationLGPALAWKPSGSLIA
CCCCEECCCCCCEEE		24.57-
249PhosphorylationPALAWKPSGSLIAST
CCEECCCCCCEEEEC		36.9722210691
251PhosphorylationLAWKPSGSLIASTQD
EECCCCCCEEEECCC		22.4225159151
343UbiquitinationLSFSTCGKSKIVSLM
EEECCCCCCEEEEEE		51.20-
407PhosphorylationLVTVFRQTVVPPPMC
EEEEEEECCCCCCCE		21.1524043423
415PhosphorylationVVPPPMCTYQLLFPH
CCCCCCEEEEEEECC		14.1924043423
416PhosphorylationVPPPMCTYQLLFPHP
CCCCCEEEEEEECCC		7.7024043423
428PhosphorylationPHPVNQVTFLAHPQK
CCCCCEEEEECCCCC		11.8124043423
436PhosphorylationFLAHPQKSNDLAVLD
EECCCCCCCCEEEEE		30.2630257219
445PhosphorylationDLAVLDASNQISVYK
CEEEEECCCCEEEEE		29.0028122231
449PhosphorylationLDASNQISVYKCGDC
EECCCCEEEEECCCC		15.0528122231
451PhosphorylationASNQISVYKCGDCPS
CCCCEEEEECCCCCC		8.1830257219
464UbiquitinationPSADPTVKLGAVGGS
CCCCCCEEECCCCCC		43.62-
471PhosphorylationKLGAVGGSGFKVCLR
EECCCCCCCEEEEEC		34.8228731282
474UbiquitinationAVGGSGFKVCLRTPH
CCCCCCEEEEECCCC		35.25-
474MethylationAVGGSGFKVCLRTPH
CCCCCCEEEEECCCC		35.25115971393
484UbiquitinationLRTPHLEKRYKIQFE
ECCCCHHHHEEEEEC		68.35-
4842-HydroxyisobutyrylationLRTPHLEKRYKIQFE
ECCCCHHHHEEEEEC		68.35-
487UbiquitinationPHLEKRYKIQFENNE
CCHHHHEEEEECCCC		33.78-
591UbiquitinationESPSLAIKPWKNSGG
CCCCCEEECCCCCCC		38.94-
669PhosphorylationCFCLRDASFKTLQAG
EEEECCCCCCHHHHC		31.4024719451
671UbiquitinationCLRDASFKTLQAGLS
EECCCCCCHHHHCCC		45.92-
695PhosphorylationLRKVERGSRIVTVVP
HHHHHCCCCEEEECC		25.67-
699PhosphorylationERGSRIVTVVPQDTK
HCCCCEEEECCCCCE		17.2621406692
705PhosphorylationVTVVPQDTKLVLQMP
EEECCCCCEEEEECC		22.4921406692
706UbiquitinationTVVPQDTKLVLQMPR
EECCCCCEEEEECCC		44.91-
706AcetylationTVVPQDTKLVLQMPR
EECCCCCEEEEECCC		44.9125953088
735UbiquitinationQIRKWLDKLMFKEAF
HHHHHHHHHHHHHHH		39.4121890473
788UbiquitinationNLFFTELKEEDVTKT
EEEEEECCHHCCCCC		53.47-
794UbiquitinationLKEEDVTKTMYPAPV
CCHHCCCCCCEECCC		31.01-
795PhosphorylationKEEDVTKTMYPAPVT
CHHCCCCCCEECCCE		16.7523186163
797PhosphorylationEDVTKTMYPAPVTSS
HCCCCCCEECCCEEE		11.0620068231
802PhosphorylationTMYPAPVTSSVYLSR
CCEECCCEEEEEEEE		17.7728857561
803PhosphorylationMYPAPVTSSVYLSRD
CEECCCEEEEEEEEC		20.3120068231
804PhosphorylationYPAPVTSSVYLSRDP
EECCCEEEEEEEECC		12.8620068231
806PhosphorylationAPVTSSVYLSRDPDG
CCCEEEEEEEECCCC		10.8320068231
808PhosphorylationVTSSVYLSRDPDGNK
CEEEEEEEECCCCCC		19.5623186163
815UbiquitinationSRDPDGNKIDLVCDA
EECCCCCCCHHHHHH		43.03-
834UbiquitinationMESINPHKYCLSILT
HHHCCHHHHHHHHHH		38.63-
842PhosphorylationYCLSILTSHVKKTTP
HHHHHHHHHHCCCCH		23.88-
846UbiquitinationILTSHVKKTTPELEI
HHHHHHCCCCHHHHH		57.45-
857UbiquitinationELEIVLQKVHELQGN
HHHHHHHHHHHHCCC		41.20-
867PhosphorylationELQGNAPSDPDAVSA
HHCCCCCCCCCCCCH		60.4025159151
873PhosphorylationPSDPDAVSAEEALKY
CCCCCCCCHHHHHHH		31.5129978859
915UbiquitinationEKSQKDPKEYLPFLN
HHCCCCHHHHHHHHH		69.95-
925UbiquitinationLPFLNTLKKMETNYQ
HHHHHHHHHHHHHHH		48.30-
926UbiquitinationPFLNTLKKMETNYQR
HHHHHHHHHHHHHHH		45.11-
935PhosphorylationETNYQRFTIDKYLKR
HHHHHHHCHHHHHHH		30.38-
938UbiquitinationYQRFTIDKYLKRYEK
HHHHCHHHHHHHHHH		48.94-
945UbiquitinationKYLKRYEKAIGHLSK
HHHHHHHHHHHHHHH		36.05-
952UbiquitinationKAIGHLSKCGPEYFP
HHHHHHHHHCHHHCH		49.96-
966UbiquitinationPECLNLIKDKNLYNE
HHHHHHHCCCCHHHH		66.86-
968UbiquitinationCLNLIKDKNLYNEAL
HHHHHCCCCHHHHHH		43.80-
968AcetylationCLNLIKDKNLYNEAL
HHHHHCCCCHHHHHH		43.8025953088
1055UbiquitinationLGRTLAGKLVEQRKH
HHHHHHHHHHHHHHC		43.69-
1097PhosphorylationEEALRLVYKYNRLDI
HHHHHHHHHHCCCCE		16.6129396449
1098UbiquitinationEALRLVYKYNRLDII
HHHHHHHHHCCCCEE		28.68-
1099PhosphorylationALRLVYKYNRLDIIE
HHHHHHHHCCCCEEE		6.4529396449
1107PhosphorylationNRLDIIETNVKPSIL
CCCCEEECCCCHHHH		34.6029396449
1110UbiquitinationDIIETNVKPSILEAQ
CEEECCCCHHHHHHH		34.81-
1163PhosphorylationEVPHGQESDLFSETS
CCCCCCHHHCCCCCC		31.5530576142
1167PhosphorylationGQESDLFSETSSVVS
CCHHHCCCCCCCCCC		47.4630576142
1169PhosphorylationESDLFSETSSVVSGS
HHHCCCCCCCCCCCC		25.7130576142
1170PhosphorylationSDLFSETSSVVSGSE
HHCCCCCCCCCCCCC		19.6530576142
1171PhosphorylationDLFSETSSVVSGSEM
HCCCCCCCCCCCCCC		33.6828348404
1174PhosphorylationSETSSVVSGSEMSGK
CCCCCCCCCCCCCCC		34.1530278072
1176PhosphorylationTSSVVSGSEMSGKYS
CCCCCCCCCCCCCCC		23.7129116813
1179PhosphorylationVVSGSEMSGKYSHSN
CCCCCCCCCCCCCCC		28.2530278072
1182PhosphorylationGSEMSGKYSHSNSRI
CCCCCCCCCCCCCCC		18.3625056879
1183PhosphorylationSEMSGKYSHSNSRIS
CCCCCCCCCCCCCCC		24.7528348404
1185PhosphorylationMSGKYSHSNSRISAR
CCCCCCCCCCCCCCC		30.4728348404
1187PhosphorylationGKYSHSNSRISARSS
CCCCCCCCCCCCCHH		33.7224719451
1190PhosphorylationSHSNSRISARSSKNR
CCCCCCCCCCHHHHH		19.2726074081
1193PhosphorylationNSRISARSSKNRRKA
CCCCCCCHHHHHHHH		45.4326074081
1194PhosphorylationSRISARSSKNRRKAE
CCCCCCHHHHHHHHH		28.5326074081
1208UbiquitinationERKKHSLKEGSPLED
HHHHCCCCCCCCHHH		64.14-
1211PhosphorylationKHSLKEGSPLEDLAL
HCCCCCCCCHHHHHH		27.6625159151
1266SulfoxidationFEDTLQLMERSLPEI
HHHHHHHHHHCCCHH		2.3121406390
1275PhosphorylationRSLPEIWTLTYQQNS
HCCCHHEEEEEECCC		18.1928985074
1291PhosphorylationTPVLGPNSTANSIMA
CCCCCCCCHHHHHHH		31.8428985074
1300PhosphorylationANSIMASYQQQKTSV
HHHHHHHHHCCCCCC		10.7828985074
1319UbiquitinationAELFIPPKINRRTQW
HHHCCCCCCCCCCCC		47.46-
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
1174SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELP1_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 ELP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELP3_HUMANELP3physical
11714725
ELP2_HUMANELP2physical
11714725
ELP4_HUMANELP4physical
11714725
IKKB_HUMANIKBKBphysical
9751059
IKKA_HUMANCHUKphysical
9751059
M3K14_HUMANMAP3K14physical
9751059
IKKA_HUMANCHUKphysical
10094049
M3K7_HUMANMAP3K7physical
10094049
ELP2_HUMANELP2physical
19834596
ELP3_HUMANELP3physical
19834596
ELP4_HUMANELP4physical
19834596
HD_HUMANHTTphysical
15383276
ELP3_HUMANELP3physical
22939629
ELP2_HUMANELP2physical
22939629
ELP4_HUMANELP4physical
22939629
PRKDC_HUMANPRKDCphysical
18303054
DYHC1_HUMANDYNC1H1physical
18303054
FLNA_HUMANFLNAphysical
18303054
USP9X_HUMANUSP9Xphysical
18303054
ACACA_HUMANACACAphysical
18303054
ELP2_HUMANELP2physical
18303054
ELP3_HUMANELP3physical
18303054
KPYM_HUMANPKMphysical
18303054
PRS8_HUMANPSMC5physical
18303054
PRDX1_HUMANPRDX1physical
18303054
PSB5_HUMANPSMB5physical
18303054
BMX_HUMANBMXphysical
18303054
MYLK2_HUMANMYLK2physical
18303054
DJB11_HUMANDNAJB11physical
18303054
NUP50_HUMANNUP50physical
22863883
T22D1_HUMANTSC22D1physical
22863883
DPH3_HUMANDPH3physical
26344197
ELP3_HUMANELP3physical
26344197
FOCAD_HUMANFOCADphysical
26344197
PSA2_HUMANPSMA2physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD12_HUMANPSMD12physical
26344197
PSMD4_HUMANPSMD4physical
26344197
ELP2_HUMANELP2physical
26261306
ELP3_HUMANELP3physical
26261306
ELP1_HUMANIKBKAPphysical
26261306
ELP4_HUMANELP4physical
26261306
ELP5_HUMANELP5physical
26261306
ELP6_HUMANELP6physical
26261306
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
223900Neuropathy, hereditary sensory and autonomic, 3 (HSAN3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELP1_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-471; SER-867; SER-1171AND SER-1174, AND MASS SPECTROMETRY.

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