CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021559
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongator complex protein 3 
Protein Synonyms/Alias
 hELP3 
Gene Name
 ELP3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MRQKRKGDLSPAEubiquitination[1]
34IEAHEQGKDIDLNKVubiquitination[1, 2, 3, 4]
40GKDIDLNKVKTKTAAubiquitination[1, 3]
42DIDLNKVKTKTAAKYubiquitination[1]
44DLNKVKTKTAAKYGLubiquitination[1]
48VKTKTAAKYGLSAQPubiquitination[2, 3, 4]
70AVPPQYRKVLMPKLKubiquitination[1]
77KVLMPKLKAKPIRTAubiquitination[3]
156RHRIEQLKQLGHSVDubiquitination[3]
206NNIYEAVKYSERSLTubiquitination[1, 2, 3, 4, 5]
214YSERSLTKCIGITIEubiquitination[1]
275CESFHLAKDSGFKVVubiquitination[1]
280LAKDSGFKVVAHMMPubiquitination[1]
333TGLYELWKSGRYKSYubiquitination[1, 2, 3, 4, 5]
338LWKSGRYKSYSPSDLubiquitination[1, 2, 3, 4]
392ELALARMKDLGIQCRubiquitination[1]
414GIQEIHHKVRPYQVEubiquitination[1]
491VSSRDPTKFQHQGFGubiquitination[3]
517REEHGSGKIAVISGVubiquitination[3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional 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. May also have a methyltransferase activity. Involved in cell migration. 
Sequence Annotation
 DOMAIN 396 547 N-acetyltransferase.
 METAL 99 99 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 METAL 109 109 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 METAL 112 112 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 MOD_RES 202 202 Phosphotyrosine.  
Keyword
 Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 547 AA 
Protein Sequence
MRQKRKGDLS PAELMMLTIG DVIKQLIEAH EQGKDIDLNK VKTKTAAKYG LSAQPRLVDI 60
IAAVPPQYRK VLMPKLKAKP IRTASGIAVV AVMCKPHRCP HISFTGNICV YCPGGPDSDF 120
EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH RIEQLKQLGH SVDKVEFIVM GGTFMALPEE 180
YRDYFIRNLH DALSGHTSNN IYEAVKYSER SLTKCIGITI ETRPDYCMKR HLSDMLTYGC 240
TRLEIGVQSV YEDVARDTNR GHTVKAVCES FHLAKDSGFK VVAHMMPDLP NVGLERDIEQ 300
FTEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYKSY SPSDLVELVA RILALVPPWT 360
RVYRVQRDIP MPLVSSGVEH GNLRELALAR MKDLGIQCRD VRTREVGIQE IHHKVRPYQV 420
ELVRRDYVAN GGWETFLSYE DPDQDILIGL LRLRKCSEET FRFELGGGVS IVRELHVYGS 480
VVPVSSRDPT KFQHQGFGML LMEEAERIAR EEHGSGKIAV ISGVGTRNYY RKIGYRLQGP 540
YMVKMLK 547 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:HGNC.
 GO:0033588; C:Elongator holoenzyme complex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HGNC.
 GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IEA:EC.
 GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008607; F:phosphorylase kinase regulator activity; IDA:UniProtKB.
 GO:0016573; P:histone acetylation; IEA:GOC.
 GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:HGNC. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR006638; Elp3/MiaB/NifB.
 IPR000182; GNAT_dom.
 IPR005910; Hist_AcTrfase_ELP3.
 IPR007197; rSAM.
 IPR023404; rSAM_horseshoe. 
Pfam
 PF00583; Acetyltransf_1
 PF04055; Radical_SAM 
SMART
 SM00729; Elp3 
PROSITE
 PS51186; GNAT 
PRINTS