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Q9CZX0 (ELP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongator complex protein 3

EC=2.3.1.48
Gene names
Name:Elp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandIron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of cell migration

Inferred from mutant phenotype Ref.3. Source: UniProtKB

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: GOC

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: Ensembl

   Cellular_componentDNA-directed RNA polymerase II, holoenzyme

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

transcription elongation factor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

histone 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 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 547547Elongator complex protein 3
PRO_0000283987

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

Natural variations

Alternative sequence71G → GAKYVGQGRKGGSGFSEITG in isoform 2.
VSP_024408

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 9234BB4DDD145FF4

FASTA54762,385
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2FF7F992FFFB3EC6
Show »

FASTA56664,266

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS56965.1. [Q9CZX0-2]
RefSeqNP_001240741.1. NM_001253812.1. [Q9CZX0-2]
NP_083087.1. NM_028811.3. [Q9CZX0-1]
UniGeneMm.29719.
Mm.474894.

3D structure databases

ProteinModelPortalQ9CZX0.
SMRQ9CZX0. Positions 490-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216566. 1 interaction.
IntActQ9CZX0. 1 interaction.
MINTMINT-4126289.

PTM databases

PhosphoSiteQ9CZX0.

Proteomic databases

PaxDbQ9CZX0.
PRIDEQ9CZX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022609; ENSMUSP00000022609; ENSMUSG00000022031. [Q9CZX0-2]
GeneID74195.
KEGGmmu:74195.
UCSCuc007ujk.2. mouse. [Q9CZX0-1]
uc007ujl.2. mouse. [Q9CZX0-2]

Organism-specific databases

CTD55140.
MGIMGI:1921445. Elp3.

Phylogenomic databases

eggNOGCOG1243.
GeneTreeENSGT00390000013141.
HOGENOMHOG000227514.
HOVERGENHBG107845.
InParanoidQ9CZX0.
KOK07739.
OMAGYKVVSH.
OrthoDBEOG7V765W.
PhylomeDBQ9CZX0.
TreeFamTF105752.

Gene expression databases

BgeeQ9CZX0.
CleanExMM_ELP3.
GenevestigatorQ9CZX0.

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

NextBio340066.
PROQ9CZX0.
SOURCESearch...

Entry information

Entry nameELP3_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot