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Q9CZX0

- ELP3_MOUSE

UniProt

Q9CZX0 - ELP3_MOUSE

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Protein

Elongator complex protein 3

Gene

Elp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi109 – 1091Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi112 – 1121Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. histone acetyltransferase activity Source: UniProtKB-EC
  3. iron-sulfur cluster binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. phosphorylase kinase regulator activity Source: UniProtKB

GO - Biological processi

  1. positive regulation of cell migration Source: UniProtKB
  2. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. transcription elongation from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 3 (EC:2.3.1.48)
Gene namesi
Name:Elp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1921445. Elp3.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. DNA-directed RNA polymerase II, holoenzyme Source: Ensembl
  3. Elongator holoenzyme complex Source: UniProtKB
  4. nucleolus Source: Ensembl
  5. transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Elongator complex protein 3PRO_0000283987Add
BLAST

Proteomic databases

MaxQBiQ9CZX0.
PaxDbiQ9CZX0.
PRIDEiQ9CZX0.

PTM databases

PhosphoSiteiQ9CZX0.

Expressioni

Gene expression databases

BgeeiQ9CZX0.
CleanExiMM_ELP3.
GenevestigatoriQ9CZX0.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi216566. 1 interaction.
IntActiQ9CZX0. 1 interaction.
MINTiMINT-4126289.

Structurei

3D structure databases

ProteinModelPortaliQ9CZX0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini396 – 547152N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ELP3 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1243.
GeneTreeiENSGT00390000013141.
HOGENOMiHOG000227514.
HOVERGENiHBG107845.
InParanoidiQ9CZX0.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7V765W.
PhylomeDBiQ9CZX0.
TreeFamiTF105752.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9CZX0-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRQKRKGDLS PAELMMLTIG DVIKQLVEAH EQGKDVDLNK MKTKTAAKYG
60 70 80 90 100
LASQPRLVDI IAAVPPHYRK ILIPKLKAKP VRTASGIAVV AVMCKPHRCP
110 120 130 140 150
HISFTGNICI YCPGGPDSDF EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH
160 170 180 190 200
RIEQLKQLGH SVDKVEFIVM GGTFMALPEE YRDYFIRSLH DALSGHTSNN
210 220 230 240 250
IHEAIKYSER SFTKCVGITI ETRPDYCMKR HLSDMLTYGC TRLEIGVQSV
260 270 280 290 300
YEDVARDTNR GHTVKAACES FHLAKDSGFK VVTHMMPDLP NVGLERDIEQ
310 320 330 340 350
FIEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYRSY SPSDLIELVA
360 370 380 390 400
RILALVPPWT RVYRVQRDIP MPLVSSGVEH GNLRELAFAR MKDLGIQCRD
410 420 430 440 450
VRTREVGIQE IHHRVRPYQV ELVRRDYVAN GGWETFLSYE DPDQDILIGL
460 470 480 490 500
LRLRKCSEET FRFELGGGVS IVRELHVYGS VVPVSSRDPT KFQHQGFGML
510 520 530 540
LMEEAERIAR EEHGSGKMAV ISGVGTRNYY RKIGYRLQGP YMVKMLK
Length:547
Mass (Da):62,385
Last modified:June 1, 2001 - v1
Checksum:i9234BB4DDD145FF4
GO
Isoform 2 (identifier: Q9CZX0-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:566
Mass (Da):64,266
Checksum:i2FF7F992FFFB3EC6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 71G → GAKYVGQGRKGGSGFSEITG in isoform 2. 1 PublicationVSP_024408

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012072 mRNA. Translation: BAB28009.1.
AK088457 mRNA. Translation: BAC40364.1.
BC026461 mRNA. Translation: AAH26461.1.
BC057453 mRNA. Translation: AAH57453.1.
CCDSiCCDS56965.1. [Q9CZX0-2]
RefSeqiNP_001240741.1. NM_001253812.1. [Q9CZX0-2]
NP_083087.1. NM_028811.3. [Q9CZX0-1]
UniGeneiMm.29719.
Mm.474894.

Genome annotation databases

EnsembliENSMUST00000022609; ENSMUSP00000022609; ENSMUSG00000022031. [Q9CZX0-2]
GeneIDi74195.
KEGGimmu:74195.
UCSCiuc007ujk.2. mouse. [Q9CZX0-1]
uc007ujl.2. mouse. [Q9CZX0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012072 mRNA. Translation: BAB28009.1 .
AK088457 mRNA. Translation: BAC40364.1 .
BC026461 mRNA. Translation: AAH26461.1 .
BC057453 mRNA. Translation: AAH57453.1 .
CCDSi CCDS56965.1. [Q9CZX0-2 ]
RefSeqi NP_001240741.1. NM_001253812.1. [Q9CZX0-2 ]
NP_083087.1. NM_028811.3. [Q9CZX0-1 ]
UniGenei Mm.29719.
Mm.474894.

3D structure databases

ProteinModelPortali Q9CZX0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 216566. 1 interaction.
IntActi Q9CZX0. 1 interaction.
MINTi MINT-4126289.

PTM databases

PhosphoSitei Q9CZX0.

Proteomic databases

MaxQBi Q9CZX0.
PaxDbi Q9CZX0.
PRIDEi Q9CZX0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022609 ; ENSMUSP00000022609 ; ENSMUSG00000022031 . [Q9CZX0-2 ]
GeneIDi 74195.
KEGGi mmu:74195.
UCSCi uc007ujk.2. mouse. [Q9CZX0-1 ]
uc007ujl.2. mouse. [Q9CZX0-2 ]

Organism-specific databases

CTDi 55140.
MGIi MGI:1921445. Elp3.

Phylogenomic databases

eggNOGi COG1243.
GeneTreei ENSGT00390000013141.
HOGENOMi HOG000227514.
HOVERGENi HBG107845.
InParanoidi Q9CZX0.
KOi K07739.
OMAi GYKVVSH.
OrthoDBi EOG7V765W.
PhylomeDBi Q9CZX0.
TreeFami TF105752.

Enzyme and pathway databases

Reactomei REACT_226917. HATs acetylate histones.

Miscellaneous databases

NextBioi 340066.
PROi Q9CZX0.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZX0.
CleanExi MM_ELP3.
Genevestigatori Q9CZX0.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view ]
Pfami PF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
TIGRFAMsi TIGR01211. ELP3. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiELP3_MOUSE
AccessioniPrimary (citable) accession number: Q9CZX0
Secondary accession number(s): Q8C2K2, Q8R369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3