Q9CZX0 (ELP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongator complex protein 3
EC=2.3.1.48

Gene names

Name:

Elp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.3
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 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the ELP3 family. Contains 1 N-acetyltransferase domain.

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
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 mutant phenotype Ref.3. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB transcription elongation from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara
Cellular_component	DNA-directed RNA polymerase II, holoenzyme Inferred from electronic annotation. Source: Compara Elongator holoenzyme complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: Compara transcription elongation factor complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara 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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9CZX0-1)

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: Q9CZX0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: G → GAKYVGQGRKGGSGFSEITG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 547	547	Elongator complex protein 3		PRO_0000283987
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
Natural variations
	Alternative sequence	7	1	G → GAKYVGQGRKGGSGFSEITG in isoform 2.		VSP_024408

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9234BB4DDD145FF4	FASTA	547	62,385
	10 20 30 40 50 60 MRQKRKGDLS PAELMMLTIG DVIKQLVEAH EQGKDVDLNK MKTKTAAKYG LASQPRLVDI 70 80 90 100 110 120 IAAVPPHYRK ILIPKLKAKP VRTASGIAVV AVMCKPHRCP HISFTGNICI YCPGGPDSDF 130 140 150 160 170 180 EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH RIEQLKQLGH SVDKVEFIVM GGTFMALPEE 190 200 210 220 230 240 YRDYFIRSLH DALSGHTSNN IHEAIKYSER SFTKCVGITI ETRPDYCMKR HLSDMLTYGC 250 260 270 280 290 300 TRLEIGVQSV YEDVARDTNR GHTVKAACES FHLAKDSGFK VVTHMMPDLP NVGLERDIEQ 310 320 330 340 350 360 FIEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYRSY SPSDLIELVA RILALVPPWT 370 380 390 400 410 420 RVYRVQRDIP MPLVSSGVEH GNLRELAFAR MKDLGIQCRD VRTREVGIQE IHHRVRPYQV 430 440 450 460 470 480 ELVRRDYVAN GGWETFLSYE DPDQDILIGL LRLRKCSEET FRFELGGGVS IVRELHVYGS 490 500 510 520 530 540 VVPVSSRDPT KFQHQGFGML LMEEAERIAR EEHGSGKMAV ISGVGTRNYY RKIGYRLQGP YMVKMLK
	Isoform 2 [UniParc]. Checksum: 2FF7F992FFFB3EC6	FASTA	566	64,266
	10 20 30 40 50 60 MRQKRKGAKY VGQGRKGGSG FSEITGDLSP AELMMLTIGD VIKQLVEAHE QGKDVDLNKM 70 80 90 100 110 120 KTKTAAKYGL ASQPRLVDII AAVPPHYRKI LIPKLKAKPV RTASGIAVVA VMCKPHRCPH 130 140 150 160 170 180 ISFTGNICIY CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR YDPFLQTRHR IEQLKQLGHS 190 200 210 220 230 240 VDKVEFIVMG GTFMALPEEY RDYFIRSLHD ALSGHTSNNI HEAIKYSERS FTKCVGITIE 250 260 270 280 290 300 TRPDYCMKRH LSDMLTYGCT RLEIGVQSVY EDVARDTNRG HTVKAACESF HLAKDSGFKV 310 320 330 340 350 360 VTHMMPDLPN VGLERDIEQF IEFFENPAFR PDGLKLYPTL VIRGTGLYEL WKSGRYRSYS 370 380 390 400 410 420 PSDLIELVAR ILALVPPWTR VYRVQRDIPM PLVSSGVEHG NLRELAFARM KDLGIQCRDV 430 440 450 460 470 480 RTREVGIQEI HHRVRPYQVE LVRRDYVANG GWETFLSYED PDQDILIGLL RLRKCSEETF 490 500 510 520 530 540 RFELGGGVSI VRELHVYGSV VPVSSRDPTK FQHQGFGMLL MEEAERIARE EHGSGKMAVI 550 560 SGVGTRNYYR KIGYRLQGPY MVKMLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J and NOD. Tissue: Thymus.
[2]	"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). Strain: FVB/N. Tissue: Mammary tumor.
[3]	"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: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK012072 mRNA. Translation: BAB28009.1. AK088457 mRNA. Translation: BAC40364.1. BC026461 mRNA. Translation: AAH26461.1. BC057453 mRNA. Translation: AAH57453.1.
IPI	IPI00224682. IPI00844769.
RefSeq	NP_001240741.1. NM_001253812.1. NP_083087.1. NM_028811.3.
UniGene	Mm.29719. Mm.474894.
3D structure databases
ProteinModelPortal	Q9CZX0.
SMR	Q9CZX0. Positions 435-540.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4126289.
PTM databases
PhosphoSite	Q9CZX0.
Proteomic databases
PaxDb	Q9CZX0.
PRIDE	Q9CZX0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022609; ENSMUSP00000022609; ENSMUSG00000022031.
GeneID	74195.
KEGG	mmu:74195.
UCSC	uc007ujk.2. mouse. uc007ujl.2. mouse.
Organism-specific databases
CTD	55140.
MGI	MGI:1921445. Elp3.
Phylogenomic databases
eggNOG	COG1243.
GeneTree	ENSGT00390000013141.
HOGENOM	HOG000227514.
HOVERGEN	HBG107845.
InParanoid	Q9CZX0.
KO	K07739.
OMA	EWQHRGY.
OrthoDB	EOG41JZBW.
Gene expression databases
Bgee	Q9CZX0.
CleanEx	MM_ELP3.
Genevestigator	Q9CZX0.
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
NextBio	340066.
SOURCE	Search...

Entry information

Entry name

ELP3_MOUSE

Accession

Primary (citable) accession number: Q9CZX0
Secondary accession number(s): Q8C2K2, Q8R369

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program