ELP4_HUMAN - dbPTM
ELP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELP4_HUMAN
UniProt AC Q96EB1
Protein Name Elongator complex protein 4
Gene Name ELP4
Organism Homo sapiens (Human).
Sequence Length 424
Subcellular Localization Cytoplasm. Nucleus.
Protein Description 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..
Protein Sequence MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIERLHLPPDLSDTVSRSSKMDLAESAKRLGPGCGMMAGGKKHLDF
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
6O-linked_Glycosylation--MAAVATCGSVAAS
--CCCEEECCHHHHH		15.7130379171
6Phosphorylation--MAAVATCGSVAAS
--CCCEEECCHHHHH		15.7123532336
9O-linked_GlycosylationAAVATCGSVAASTGS
CCEEECCHHHHHCCC		15.6630379171
9PhosphorylationAAVATCGSVAASTGS
CCEEECCHHHHHCCC		15.6623401153
20PhosphorylationSTGSAVATASKSNVT
HCCCHHHHCCCCCCC		25.5123532336
22PhosphorylationGSAVATASKSNVTSF
CCHHHHCCCCCCCCC		32.0623532336
24PhosphorylationAVATASKSNVTSFQR
HHHHCCCCCCCCCCC		33.7526434776
27PhosphorylationTASKSNVTSFQRRGP
HCCCCCCCCCCCCCC		28.2426434776
28PhosphorylationASKSNVTSFQRRGPR
CCCCCCCCCCCCCCC		18.3328857561
37PhosphorylationQRRGPRASVTNDSGP
CCCCCCCEECCCCCC		30.6521955146
39PhosphorylationRGPRASVTNDSGPRL
CCCCCEECCCCCCCE		30.7125137130
42PhosphorylationRASVTNDSGPRLVSI
CCEECCCCCCCEEEE		53.4125137130
52PhosphorylationRLVSIAGTRPSVRNG
CEEEECCCCCCCCCC		30.3128857561
55PhosphorylationSIAGTRPSVRNGQLL
EECCCCCCCCCCEEE		30.3428857561
137UbiquitinationPAPLLDDKCKKEFDE
CCCCCCHHHHHHCCH		47.85-
140UbiquitinationLLDDKCKKEFDEDVY
CCCHHHHHHCCHHHH		73.43-
147PhosphorylationKEFDEDVYNHKTPES
HHCCHHHHCCCCCCH		24.7025159151
150UbiquitinationDEDVYNHKTPESNIK
CHHHHCCCCCCHHCC		63.24-
151PhosphorylationEDVYNHKTPESNIKM
HHHHCCCCCCHHCCC		25.4125159151
154PhosphorylationYNHKTPESNIKMKIA
HCCCCCCHHCCCEEE		45.0925159151
164PhosphorylationKMKIAWRYQLLPKME
CCEEEEEEECCCCCE		7.8823898821
176PhosphorylationKMEIGPVSSSRFGHY
CCEECCCCHHHCCCC		26.2323898821
177PhosphorylationMEIGPVSSSRFGHYY
CEECCCCHHHCCCCC		26.2623898821
183PhosphorylationSSSRFGHYYDASKRM
CHHHCCCCCCHHHCC		11.9227461979
184PhosphorylationSSRFGHYYDASKRMP
HHHCCCCCCHHHCCC		10.2027461979
187PhosphorylationFGHYYDASKRMPQEL
CCCCCCHHHCCCHHH		20.2127461979
188UbiquitinationGHYYDASKRMPQELI
CCCCCHHHCCCHHHH		55.20-
189UbiquitinationHYYDASKRMPQELIE
CCCCHHHCCCHHHHH		39.25-
198PhosphorylationPQELIEASNWHGFFL
CHHHHHHHCCCCCCC		27.8827461979
214UbiquitinationEKISSTLKVEPCSLT
HHHCCCEEEEECCCC		44.64-
215UbiquitinationKISSTLKVEPCSLTP
HHCCCEEEEECCCCC		12.80-
295PhosphorylationLRGLLRTSLSACIIT
HHHHHHHHHHHHHHC		17.5622210691
302PhosphorylationSLSACIITMPTHLIQ
HHHHHHHCCCHHHHC		9.3722210691
341PhosphorylationERETNPLYKDYHGLI
CCCCCCCCCCCCCEE		11.7626657352
367UbiquitinationICDESDVKDLAFKLK
CCCHHHHHHHHHHHH		52.60-
368UbiquitinationCDESDVKDLAFKLKR
CCHHHHHHHHHHHHH		42.98-
376UbiquitinationLAFKLKRKLFTIERL
HHHHHHHHHHEEEEC		46.49-
379PhosphorylationKLKRKLFTIERLHLP
HHHHHHHEEEECCCC		32.1528857561
390PhosphorylationLHLPPDLSDTVSRSS
CCCCCCCHHHCCHHH		38.3228555341
392PhosphorylationLPPDLSDTVSRSSKM
CCCCCHHHCCHHHHH		19.6028555341
404PhosphorylationSKMDLAESAKRLGPG
HHHHHHHHHHHHCCC		33.2221857030
406UbiquitinationMDLAESAKRLGPGCG
HHHHHHHHHHCCCCC		58.39-
419AcetylationCGMMAGGKKHLDF--
CCCCCCCCCCCCC--		35.7825953088
419MethylationCGMMAGGKKHLDF--
CCCCCCCCCCCCC--		35.78-
420MethylationGMMAGGKKHLDF---
CCCCCCCCCCCC---		53.31-
499 (in isoform 2)Phosphorylation-25690035
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 ELP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELP4_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 ELP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRP68_HUMANSRP68physical
22863883
ELP2_HUMANELP2physical
26344197
SF3B3_HUMANSF3B3physical
26344197
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 ELP4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-42, AND MASSSPECTROMETRY.

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