ELP3_HUMAN - dbPTM
ELP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELP3_HUMAN
UniProt AC Q9H9T3
Protein Name Elongator complex protein 3
Gene Name ELP3
Organism Homo sapiens (Human).
Sequence Length 547
Subcellular Localization Cytoplasm .
Isoform 1: Nucleus.
Isoform 2: Cytoplasm. Nucleus.
Protein Description Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a 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 acetylation of alpha-tubulin. [PubMed: 19185337 May also have a methyltransferase activity. Involved in cell migration. Involved in neurogenesis. Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation.]
Protein Sequence MRQKRKGDLSPAELMMLTIGDVIKQLIEAHEQGKDIDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRKVLMPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGHTSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPYQVELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKMLK
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
6Ubiquitination--MRQKRKGDLSPAE
--CCCCCCCCCCHHH		64.91-
10PhosphorylationQKRKGDLSPAELMML
CCCCCCCCHHHHHHH		27.1423898821
20 (in isoform 2)Ubiquitination-20.2121890473
26 (in isoform 2)Ubiquitination-3.0321890473
34UbiquitinationIEAHEQGKDIDLNKV
HHHHHCCCCCCHHHC		51.7321890473
34UbiquitinationIEAHEQGKDIDLNKV
HHHHHCCCCCCHHHC		51.7321890473
34 (in isoform 2)Ubiquitination-51.7321890473
34UbiquitinationIEAHEQGKDIDLNKV
HHHHHCCCCCCHHHC		51.7321890473
34 (in isoform 1)Ubiquitination-51.7321890473
37UbiquitinationHEQGKDIDLNKVKTK
HHCCCCCCHHHCCCH		55.08-
40UbiquitinationGKDIDLNKVKTKTAA
CCCCCHHHCCCHHHH		53.0221906983
40 (in isoform 1)Ubiquitination-53.0221890473
42UbiquitinationDIDLNKVKTKTAAKY
CCCHHHCCCHHHHHH		46.01-
44UbiquitinationDLNKVKTKTAAKYGL
CHHHCCCHHHHHHCC		30.37-
48UbiquitinationVKTKTAAKYGLSAQP
CCCHHHHHHCCCCCC		37.0721890473
48UbiquitinationVKTKTAAKYGLSAQP
CCCHHHHHHCCCCCC		37.0721890473
48UbiquitinationVKTKTAAKYGLSAQP
CCCHHHHHHCCCCCC		37.0721890473
48 (in isoform 1)Ubiquitination-37.0721890473
49PhosphorylationKTKTAAKYGLSAQPR
CCHHHHHHCCCCCCC		20.6929496907
63 (in isoform 2)Ubiquitination-12.1621890473
70UbiquitinationAVPPQYRKVLMPKLK
HCCHHHHHHHCHHHC		34.48-
75UbiquitinationYRKVLMPKLKAKPIR
HHHHHCHHHCCCCCE		48.97-
77 (in isoform 1)Ubiquitination-61.5621890473
77UbiquitinationKVLMPKLKAKPIRTA
HHHCHHHCCCCCEEC		61.5621906983
87UbiquitinationPIRTASGIAVVAVMC
CCEECCCEEEEEEEE		2.14-
95UbiquitinationAVVAVMCKPHRCPHI
EEEEEEECCCCCCCE		26.26-
142 (in isoform 2)Ubiquitination-27.3021890473
156UbiquitinationRHRIEQLKQLGHSVD
HHHHHHHHHHCCCCC		43.0721906983
156UbiquitinationRHRIEQLKQLGHSVD
HHHHHHHHHHCCCCC		43.07-
156 (in isoform 1)Ubiquitination-43.0721890473
161UbiquitinationQLKQLGHSVDKVEFI
HHHHHCCCCCEEEEE		30.16-
161AcetylationQLKQLGHSVDKVEFI
HHHHHCCCCCEEEEE		30.16-
161PhosphorylationQLKQLGHSVDKVEFI
HHHHHCCCCCEEEEE		30.16-
192 (in isoform 2)Ubiquitination-7.9021890473
194PhosphorylationRNLHDALSGHTSNNI
HHHHHHHCCCCCCCH		30.1928152594
197PhosphorylationHDALSGHTSNNIYEA
HHHHCCCCCCCHHHH		36.3528152594
198PhosphorylationDALSGHTSNNIYEAV
HHHCCCCCCCHHHHH		23.3928152594
202PhosphorylationGHTSNNIYEAVKYSE
CCCCCCHHHHHHCCH		10.4427273156
206UbiquitinationNNIYEAVKYSERSLT
CCHHHHHHCCHHHCC		50.5421890473
206UbiquitinationNNIYEAVKYSERSLT
CCHHHHHHCCHHHCC		50.5421890473
206 (in isoform 1)Ubiquitination-50.5421890473
206UbiquitinationNNIYEAVKYSERSLT
CCHHHHHHCCHHHCC		50.5421890473
207PhosphorylationNIYEAVKYSERSLTK
CHHHHHHCCHHHCCC		14.79-
214UbiquitinationYSERSLTKCIGITIE
CCHHHCCCEEEEEEE		29.19-
214UbiquitinationYSERSLTKCIGITIE
CCHHHCCCEEEEEEE		29.19-
219UbiquitinationLTKCIGITIETRPDY
CCCEEEEEEECCCCH		13.93-
219PhosphorylationLTKCIGITIETRPDY
CCCEEEEEEECCCCH		13.9329759185
222PhosphorylationCIGITIETRPDYCMK
EEEEEEECCCCHHHH		43.5929759185
226PhosphorylationTIETRPDYCMKRHLS
EEECCCCHHHHHHHH		9.3429759185
229MethylationTRPDYCMKRHLSDML
CCCCHHHHHHHHHHH		32.8624129315
233PhosphorylationYCMKRHLSDMLTYGC
HHHHHHHHHHHHHCC		18.1728064214
238PhosphorylationHLSDMLTYGCTRLEI
HHHHHHHHCCCEEEC		13.2728064214
249PhosphorylationRLEIGVQSVYEDVAR
EEECCCEEHHHHHHC		25.0228796482
251PhosphorylationEIGVQSVYEDVARDT
ECCCEEHHHHHHCCC		16.2028796482
265UbiquitinationTNRGHTVKAVCESFH
CCCCHHHHHHHHHHH		35.94-
273UbiquitinationAVCESFHLAKDSGFK
HHHHHHHCCCCCCCE		6.29-
275UbiquitinationCESFHLAKDSGFKVV
HHHHHCCCCCCCEEE		59.80-
277PhosphorylationSFHLAKDSGFKVVAH
HHHCCCCCCCEEEEE		45.4820068231
280UbiquitinationLAKDSGFKVVAHMMP
CCCCCCCEEEEEECC		39.05-
280AcetylationLAKDSGFKVVAHMMP
CCCCCCCEEEEEECC		39.0523954790
295UbiquitinationDLPNVGLERDIEQFT
CCCCCCCCCCHHHHH		42.24-
316AcetylationAFRPDGLKLYPTLVI
CCCCCCCCEECEEEE		52.0526051181
316UbiquitinationAFRPDGLKLYPTLVI
CCCCCCCCEECEEEE		52.05-
318PhosphorylationRPDGLKLYPTLVIRG
CCCCCCEECEEEEEC		7.8120393185
319 (in isoform 2)Ubiquitination-29.6821890473
324 (in isoform 2)Ubiquitination-29.1921890473
326PhosphorylationPTLVIRGTGLYELWK
CEEEEECCCHHHHHH		17.7329341593
329PhosphorylationVIRGTGLYELWKSGR
EEECCCHHHHHHCCC		15.4328152594
333UbiquitinationTGLYELWKSGRYKSY
CCHHHHHHCCCCCCC		56.5121890473
333 (in isoform 1)Ubiquitination-56.5121890473
333UbiquitinationTGLYELWKSGRYKSY
CCHHHHHHCCCCCCC		56.5121890473
333UbiquitinationTGLYELWKSGRYKSY
CCHHHHHHCCCCCCC		56.5121890473
338UbiquitinationLWKSGRYKSYSPSDL
HHHCCCCCCCCHHHH		41.3721890473
338UbiquitinationLWKSGRYKSYSPSDL
HHHCCCCCCCCHHHH		41.3721890473
338 (in isoform 1)Ubiquitination-41.3721890473
338UbiquitinationLWKSGRYKSYSPSDL
HHHCCCCCCCCHHHH		41.3721890473
360PhosphorylationLALVPPWTRVYRVQR
HHHCCCCCEEEEEEC		18.9421406692
372UbiquitinationVQRDIPMPLVSSGVE
EECCCCCCCCCCCCC		25.02-
392UbiquitinationELALARMKDLGIQCR
HHHHHHHHHHCCCCC		44.22-
398UbiquitinationMKDLGIQCRDVRTRE
HHHHCCCCCCCCCCC		3.66-
414UbiquitinationGIQEIHHKVRPYQVE
CHHHHHHCCCCCEEE		26.27-
424MethylationPYQVELVRRDYVANG
CCEEEEEECEEECCC		38.08-
427PhosphorylationVELVRRDYVANGGWE
EEEEECEEECCCCHH		10.31-
477 (in isoform 2)Ubiquitination-10.1421890473
491UbiquitinationVSSRDPTKFQHQGFG
CCCCCCCCCCCCCCC		48.7121906983
491AcetylationVSSRDPTKFQHQGFG
CCCCCCCCCCCCCCC		48.7125953088
491 (in isoform 1)Ubiquitination-48.7121890473
503 (in isoform 2)Ubiquitination-54.7621890473
517 (in isoform 1)Ubiquitination-29.2321890473
517UbiquitinationREEHGSGKIAVISGV
HHHCCCCCEEEEECC		29.232190698
522PhosphorylationSGKIAVISGVGTRNY
CCCEEEEECCCCCHH		22.3421406692
526PhosphorylationAVISGVGTRNYYRKI
EEEECCCCCHHHHHH		17.2121406692
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
202YPhosphorylationKinaseALKQ9UM73
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELP3_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 ELP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELP1_HUMANIKBKAPphysical
11714725
ELP2_HUMANELP2physical
19834596
ELP1_HUMANIKBKAPphysical
19834596
ELP4_HUMANELP4physical
19834596
PCNA_HUMANPCNAphysical
19834596
H32_HUMANHIST2H3Cphysical
11818576
ELP1_HUMANIKBKAPphysical
11818576
CTDP1_HUMANCTDP1physical
11818576
ELP4_HUMANELP4physical
22939629
ELP2_HUMANELP2physical
22863883
U520_HUMANSNRNP200physical
22863883
WRIP1_HUMANWRNIP1physical
22863883
ELP2_HUMANELP2physical
26344197
WDR36_HUMANWDR36physical
26344197
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-202, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-202, AND MASSSPECTROMETRY.

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