Q9H9T3 (ELP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongator complex protein 3
Short name=hELP3
EC=2.3.1.48

Gene names

Name:

ELP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5 Ref.6 Ref.7 Ref.9
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.5 Ref.6 Ref.12
Subcellular location	Isoform 1: Nucleus Ref.5 Ref.6 Ref.12 Ref.13. Isoform 2: Cytoplasm. Nucleus Ref.5 Ref.6 Ref.12 Ref.13.
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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone acetylation Inferred from electronic annotation. Source: GOC positive regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.6. Source: UniProtKB transcription elongation from RNA polymerase II promoter Inferred from direct assay Ref.5. Source: HGNC
Cellular_component	DNA-directed RNA polymerase II, holoenzyme Inferred from direct assay Ref.5. Source: HGNC Elongator holoenzyme complex Inferred from direct assay Ref.12. Source: UniProtKB cytoplasm Inferred from direct assay Ref.6Ref.12. Source: UniProtKB nucleolus Inferred from direct assay Ref.5. Source: HGNC transcription elongation factor complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	histone acetyltransferase activity Inferred from electronic annotation. Source: 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.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IKBKAP	O95163	4	EBI-355217,EBI-347559

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 547	547	Elongator complex protein 3		PRO_0000283986
Regions
	Domain	396 – 547	152	N-acetyltransferase
Sites
	Metal binding	99	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	109	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	112	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Amino acid modifications
	Modified residue	202	1	Phosphotyrosine Ref.8
Natural variations
	Alternative sequence	1 – 14	14	Missing in isoform 2.		VSP_024406
Experimental info
	Sequence conflict	10	1	S → G in BAA91600. Ref.1
	Sequence conflict	30	1	H → Y in BAD96767. Ref.4
	Sequence conflict	179	1	E → K in CAH10573. Ref.2
	Sequence conflict	265	1	K → M in BAB14138. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 17, 2007. Version 2. Checksum: 60898ADD3DBAD035	FASTA	547	62,259
	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
	Isoform 2 [UniParc]. Checksum: DF8E71D8D401B90C	FASTA	533	60,648
	10 20 30 40 50 60 MMLTIGDVIK QLIEAHEQGK DIDLNKVKTK TAAKYGLSAQ PRLVDIIAAV PPQYRKVLMP 70 80 90 100 110 120 KLKAKPIRTA SGIAVVAVMC KPHRCPHISF TGNICVYCPG GPDSDFEYST QSYTGYEPTS 130 140 150 160 170 180 MRAIRARYDP FLQTRHRIEQ LKQLGHSVDK VEFIVMGGTF MALPEEYRDY FIRNLHDALS 190 200 210 220 230 240 GHTSNNIYEA VKYSERSLTK CIGITIETRP DYCMKRHLSD MLTYGCTRLE IGVQSVYEDV 250 260 270 280 290 300 ARDTNRGHTV KAVCESFHLA KDSGFKVVAH MMPDLPNVGL ERDIEQFTEF FENPAFRPDG 310 320 330 340 350 360 LKLYPTLVIR GTGLYELWKS GRYKSYSPSD LVELVARILA LVPPWTRVYR VQRDIPMPLV 370 380 390 400 410 420 SSGVEHGNLR ELALARMKDL GIQCRDVRTR EVGIQEIHHK VRPYQVELVR RDYVANGGWE 430 440 450 460 470 480 TFLSYEDPDQ DILIGLLRLR KCSEETFRFE LGGGVSIVRE LHVYGSVVPV SSRDPTKFQH 490 500 510 520 530 QGFGMLLMEE AERIAREEHG SGKIAVISGV GTRNYYRKIG YRLQGPYMVK MLK

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 1).
[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]	"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.
[4]	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.
[5]	"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, MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX.
[6]	"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, MASS SPECTROMETRY, INTERACTION WITH IKBKAP, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX.
[7]	"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.
[8]	"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, MASS SPECTROMETRY.
[9]	"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.
[10]	"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.
[11]	"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].
[12]	"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.
[13]	"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. AL834273 mRNA. Translation: CAD38948.1. BX648011 mRNA. Translation: CAH10573.1. Frameshift. BC001240 mRNA. Translation: AAH01240.1. AK223047 mRNA. Translation: BAD96767.1.
IPI	IPI00165477. IPI00844099.
RefSeq	NP_060561.3. NM_018091.5.
UniGene	Hs.491336.
3D structure databases
ProteinModelPortal	Q9H9T3.
SMR	Q9H9T3. Positions 435-540.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H9T3. 1 interaction.
STRING	9606.ENSP00000256398.
PTM databases
PhosphoSite	Q9H9T3.
Polymorphism databases
DMDM	145558902.
Proteomic databases
PaxDb	Q9H9T3.
PeptideAtlas	Q9H9T3.
PRIDE	Q9H9T3.
Protocols and materials databases
DNASU	55140.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000256398; ENSP00000256398; ENSG00000134014. ENST00000521015; ENSP00000428449; ENSG00000134014.
GeneID	55140.
KEGG	hsa:55140.
UCSC	uc003xgn.4. human.
Organism-specific databases
CTD	55140.
GeneCards	GC08P028006.
HGNC	HGNC:20696. ELP3.
HPA	HPA025812.
MIM	612722. gene.
neXtProt	NX_Q9H9T3.
PharmGKB	PA134992603.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1243.
HOGENOM	HOG000227514.
HOVERGEN	HBG107845.
InParanoid	Q9H9T3.
KO	K07739.
OMA	GIQEVHH.
OrthoDB	EOG41JZBW.
PhylomeDB	Q9H9T3.
Gene expression databases
ArrayExpress	Q9H9T3.
Bgee	Q9H9T3.
CleanEx	HS_ELP3.
Genevestigator	Q9H9T3.
Family and domain databases
Gene3D	3.40.630.30. 1 hit. 3.80.30.20. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR006638. Elp3/MiaB/NifB. IPR000182. GNAT_dom. IPR005910. Hist_AcTrfase_ELP3. IPR007197. rSAM. IPR023404. rSAM_horseshoe. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMs	TIGR01211. ELP3. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55140.
NextBio	58836.
SOURCE	Search...

Entry information

Entry name

ELP3_HUMAN

Accession

Primary (citable) accession number: Q9H9T3
Secondary accession number(s): Q53G84 , Q6AWB0, Q9BVF7, Q9NVZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	April 17, 2007
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.