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Q9H9T3 (ELP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongator complex protein 3

Short name=hELP3
EC=2.3.1.48
Gene names
Name:ELP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.10

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Subunit structure

Component of the RNA polymerase II elongator complex (Elongator), which consists of IKBKAP/ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. IKBKAP/ELP1, STIP1/ELP2 and ELP3 form the Elongator core complex. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit. Interacts with IKBKAP/ELP1. Ref.6 Ref.7 Ref.13

Subcellular location

Isoform 1: Nucleus Ref.6 Ref.7 Ref.13 Ref.14.

Isoform 2: Cytoplasm. Nucleus Ref.6 Ref.7 Ref.13 Ref.14.

Sequence similarities

Belongs to the ELP3 family.

Contains 1 N-acetyltransferase domain.

Sequence caution

The sequence BAA91600.1 differs from that shown. Reason: Aberrant splicing.

The sequence CAH10573.1 differs from that shown. Reason: Frameshift at position 279.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandIron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein kinase activity

Inferred from direct assay Ref.7. Source: GOC

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: UniProtKB

transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: HGNC

   Cellular_componentDNA-directed RNA polymerase II, holoenzyme

Inferred from direct assay Ref.6. Source: HGNC

Elongator holoenzyme complex

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.7Ref.13. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.6. Source: HGNC

transcription elongation factor complex

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron-sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorylase kinase regulator activity

Inferred from direct assay Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6PubMed 19185337Ref.13. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKBKAPO951638EBI-355217,EBI-347559

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H9T3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H9T3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
Isoform 3 (identifier: Q9H9T3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MRQKRKGDLSPA → MSTHQFYRKYMC
     13-131: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9H9T3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 547547Elongator complex protein 3
PRO_0000283986

Regions

Domain396 – 547152N-acetyltransferase

Sites

Metal binding991Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1091Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1121Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Amino acid modifications

Modified residue2021Phosphotyrosine Ref.9

Natural variations

Alternative sequence1 – 9292Missing in isoform 4.
VSP_055284
Alternative sequence1 – 1414Missing in isoform 2.
VSP_024406
Alternative sequence1 – 1212MRQKR…DLSPA → MSTHQFYRKYMC in isoform 3.
VSP_055285
Alternative sequence13 – 131119Missing in isoform 3.
VSP_055286

Experimental info

Sequence conflict101S → G in BAA91600. Ref.1
Sequence conflict301H → Y in BAD96767. Ref.5
Sequence conflict1791E → K in CAH10573. Ref.2
Sequence conflict2651K → M in BAB14138. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 60898ADD3DBAD035

FASTA54762,259
        10         20         30         40         50         60 
MRQKRKGDLS PAELMMLTIG DVIKQLIEAH EQGKDIDLNK VKTKTAAKYG LSAQPRLVDI 

        70         80         90        100        110        120 
IAAVPPQYRK VLMPKLKAKP IRTASGIAVV AVMCKPHRCP HISFTGNICV YCPGGPDSDF 

       130        140        150        160        170        180 
EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH RIEQLKQLGH SVDKVEFIVM GGTFMALPEE 

       190        200        210        220        230        240 
YRDYFIRNLH DALSGHTSNN IYEAVKYSER SLTKCIGITI ETRPDYCMKR HLSDMLTYGC 

       250        260        270        280        290        300 
TRLEIGVQSV YEDVARDTNR GHTVKAVCES FHLAKDSGFK VVAHMMPDLP NVGLERDIEQ 

       310        320        330        340        350        360 
FTEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYKSY SPSDLVELVA RILALVPPWT 

       370        380        390        400        410        420 
RVYRVQRDIP MPLVSSGVEH GNLRELALAR MKDLGIQCRD VRTREVGIQE IHHKVRPYQV 

       430        440        450        460        470        480 
ELVRRDYVAN GGWETFLSYE DPDQDILIGL LRLRKCSEET FRFELGGGVS IVRELHVYGS 

       490        500        510        520        530        540 
VVPVSSRDPT KFQHQGFGML LMEEAERIAR EEHGSGKIAV ISGVGTRNYY RKIGYRLQGP 


YMVKMLK 

« Hide

Isoform 2 [UniParc].

Checksum: DF8E71D8D401B90C
Show »

FASTA53360,648
Isoform 3 [UniParc].

Checksum: F11EEC322AAE8964
Show »

FASTA42849,405
Isoform 4 [UniParc].

Checksum: C64BAB6FED06D973
Show »

FASTA45552,202

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
Tissue: Amygdala and Hippocampus.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Amygdala and Endometrium.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-547 (ISOFORM 1).
Tissue: Thyroid.
[6]"Purification and characterization of the human elongator complex."
Hawkes N.A., Otero G., Winkler G.S., Marshall N., Dahmus M.E., Krappmann D., Scheidereit C., Thomas C.L., Schiavo G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q.
J. Biol. Chem. 277:3047-3052(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Human Elongator facilitates RNA polymerase II transcription through chromatin."
Kim J.H., Lane W.S., Reinberg D.
Proc. Natl. Acad. Sci. U.S.A. 99:1241-1246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR CORE COMPLEX, INTERACTION WITH IKBKAP, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast."
Li F., Lu J., Han Q., Zhang G., Huang B.
Mol. Genet. Genomics 273:264-272(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Transcription impairment and cell migration defects in elongator-depleted cells: implication for familial dysautonomia."
Close P., Hawkes N., Cornez I., Creppe C., Lambert C.A., Rogister B., Siebenlist U., Merville M.P., Slaugenhaupt S.A., Bours V., Svejstrup J.Q., Chariot A.
Mol. Cell 22:521-531(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of melanoma cells as subunits of Elongator."
Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., Nguyen L., Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., Chariot A.
J. Biol. Chem. 287:32535-32545(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, SUBCELLULAR LOCATION.
[14]"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001284 mRNA. Translation: BAA91600.1. Sequence problems.
AK022626 mRNA. Translation: BAB14138.1.
AK293424 mRNA. Translation: BAG56930.1.
AK295574 mRNA. Translation: BAG58473.1.
AK315985 mRNA. Translation: BAH14356.1.
AL834273 mRNA. Translation: CAD38948.1.
BX648011 mRNA. Translation: CAH10573.1. Frameshift.
AC019031 Genomic DNA. No translation available.
AC021678 Genomic DNA. No translation available.
BC001240 mRNA. Translation: AAH01240.1.
AK223047 mRNA. Translation: BAD96767.1.
CCDSCCDS6065.1. [Q9H9T3-1]
RefSeqNP_001271151.1. NM_001284222.1. [Q9H9T3-2]
NP_060561.3. NM_018091.5. [Q9H9T3-1]
UniGeneHs.491336.

3D structure databases

ProteinModelPortalQ9H9T3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120444. 12 interactions.
IntActQ9H9T3. 4 interactions.
MINTMINT-3062287.
STRING9606.ENSP00000256398.

PTM databases

PhosphoSiteQ9H9T3.

Polymorphism databases

DMDM145558902.

Proteomic databases

MaxQBQ9H9T3.
PaxDbQ9H9T3.
PeptideAtlasQ9H9T3.
PRIDEQ9H9T3.

Protocols and materials databases

DNASU55140.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256398; ENSP00000256398; ENSG00000134014. [Q9H9T3-1]
ENST00000380353; ENSP00000369711; ENSG00000134014.
ENST00000521015; ENSP00000428449; ENSG00000134014. [Q9H9T3-2]
ENST00000537665; ENSP00000445558; ENSG00000134014.
GeneID55140.
KEGGhsa:55140.
UCSCuc003xgn.4. human. [Q9H9T3-1]

Organism-specific databases

CTD55140.
GeneCardsGC08P028006.
HGNCHGNC:20696. ELP3.
HPAHPA025812.
MIM612722. gene.
neXtProtNX_Q9H9T3.
PharmGKBPA134992603.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1243.
HOGENOMHOG000227514.
HOVERGENHBG107845.
InParanoidQ9H9T3.
KOK07739.
OMAGYKVVSH.
OrthoDBEOG7V765W.
PhylomeDBQ9H9T3.
TreeFamTF105752.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ9H9T3.
BgeeQ9H9T3.
CleanExHS_ELP3.
GenevestigatorQ9H9T3.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR01211. ELP3. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiELP3.
GenomeRNAi55140.
NextBio58836.
PROQ9H9T3.
SOURCESearch...

Entry information

Entry nameELP3_HUMAN
AccessionPrimary (citable) accession number: Q9H9T3
Secondary accession number(s): B4DE19 expand/collapse secondary AC list , B4DIG1, E2QRI5, Q53G84, Q6AWB0, Q9BVF7, Q9NVZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM