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Protein

Elongator complex protein 3

Gene

ELP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. Involved in acetylation of alpha-tubulin (PubMed:19185337). May also have a methyltransferase activity. Involved in cell migration. Involved in neurogenesis. Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity).By similarity5 Publications

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. H3 histone acetyltransferase activity Source: BHF-UCL
  2. H4 histone acetyltransferase activity Source: BHF-UCL
  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. central nervous system development Source: UniProtKB
  2. chromatin organization Source: Reactome
  3. histone H3 acetylation Source: BHF-UCL
  4. histone H4 acetylation Source: BHF-UCL
  5. neuron migration Source: UniProtKB
  6. positive regulation of cell migration Source: UniProtKB
  7. regulation of protein kinase activity Source: GOC
  8. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. transcription elongation from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 3 (EC:2.3.1.48)
Short name:
hELP3
Gene namesi
Name:ELP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:20696. ELP3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. Elongator holoenzyme complex Source: UniProtKB
  3. histone acetyltransferase complex Source: BHF-UCL
  4. nucleolus Source: HGNC
  5. transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

ELP3 genetic variations may be associated with an increased risk for neurodegeneration and motor neuron diseases.

Keywords - Diseasei

Neurodegeneration

Organism-specific databases

PharmGKBiPA134992603.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Elongator complex protein 3PRO_0000283986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H9T3.
PaxDbiQ9H9T3.
PeptideAtlasiQ9H9T3.
PRIDEiQ9H9T3.

PTM databases

PhosphoSiteiQ9H9T3.

Expressioni

Tissue specificityi

Expressed in the cerebellum and spinal motor neurons.1 Publication

Gene expression databases

BgeeiQ9H9T3.
CleanExiHS_ELP3.
ExpressionAtlasiQ9H9T3. baseline and differential.
GenevestigatoriQ9H9T3.

Organism-specific databases

HPAiHPA025812.

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 (PubMed:11818576, PubMed:19185337). Interacts with alpha-tubulin (PubMed:19185337).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKAPO951638EBI-355217,EBI-347559

Protein-protein interaction databases

BioGridi120444. 23 interactions.
IntActiQ9H9T3. 4 interactions.
MINTiMINT-3062287.
STRINGi9606.ENSP00000256398.

Structurei

3D structure databases

ProteinModelPortaliQ9H9T3.
SMRiQ9H9T3. Positions 490-532.
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.
InParanoidiQ9H9T3.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7V765W.
PhylomeDBiQ9H9T3.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H9T3-1) [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 DVIKQLIEAH EQGKDIDLNK VKTKTAAKYG
60 70 80 90 100
LSAQPRLVDI IAAVPPQYRK VLMPKLKAKP IRTASGIAVV AVMCKPHRCP
110 120 130 140 150
HISFTGNICV YCPGGPDSDF EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH
160 170 180 190 200
RIEQLKQLGH SVDKVEFIVM GGTFMALPEE YRDYFIRNLH DALSGHTSNN
210 220 230 240 250
IYEAVKYSER SLTKCIGITI ETRPDYCMKR HLSDMLTYGC TRLEIGVQSV
260 270 280 290 300
YEDVARDTNR GHTVKAVCES FHLAKDSGFK VVAHMMPDLP NVGLERDIEQ
310 320 330 340 350
FTEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYKSY SPSDLVELVA
360 370 380 390 400
RILALVPPWT RVYRVQRDIP MPLVSSGVEH GNLRELALAR MKDLGIQCRD
410 420 430 440 450
VRTREVGIQE IHHKVRPYQV ELVRRDYVAN GGWETFLSYE DPDQDILIGL
460 470 480 490 500
LRLRKCSEET FRFELGGGVS IVRELHVYGS VVPVSSRDPT KFQHQGFGML
510 520 530 540
LMEEAERIAR EEHGSGKIAV ISGVGTRNYY RKIGYRLQGP YMVKMLK
Length:547
Mass (Da):62,259
Last modified:April 17, 2007 - v2
Checksum:i60898ADD3DBAD035
GO
Isoform 2 (identifier: Q9H9T3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Show »
Length:533
Mass (Da):60,648
Checksum:iDF8E71D8D401B90C
GO
Isoform 3 (identifier: Q9H9T3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MRQKRKGDLSPA → MSTHQFYRKYMC
     13-131: Missing.

Note: No experimental confirmation available.

Show »
Length:428
Mass (Da):49,405
Checksum:iF11EEC322AAE8964
GO
Isoform 4 (identifier: Q9H9T3-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.

Note: No experimental confirmation available.

Show »
Length:455
Mass (Da):52,202
Checksum:iC64BAB6FED06D973
GO

Sequence cautioni

The sequence BAA91600.1 differs from that shown.Aberrant splicing.Curated
The sequence CAH10573.1 differs from that shown. Reason: Frameshift at position 279. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101S → G in BAA91600. (PubMed:14702039)Curated
Sequence conflicti30 – 301H → Y in BAD96767. 1 PublicationCurated
Sequence conflicti179 – 1791E → K in CAH10573. (PubMed:17974005)Curated
Sequence conflicti265 – 2651K → M in BAB14138. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9292Missing in isoform 4. 1 PublicationVSP_055284Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 2. 1 PublicationVSP_024406Add
BLAST
Alternative sequencei1 – 1212MRQKR…DLSPA → MSTHQFYRKYMC in isoform 3. 1 PublicationVSP_055285Add
BLAST
Alternative sequencei13 – 131119Missing in isoform 3. 1 PublicationVSP_055286Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6065.1. [Q9H9T3-1]
CCDS64860.1. [Q9H9T3-5]
CCDS64861.1. [Q9H9T3-4]
CCDS75717.1. [Q9H9T3-2]
RefSeqiNP_001271151.1. NM_001284222.1. [Q9H9T3-2]
NP_001271153.1. NM_001284224.1. [Q9H9T3-4]
NP_001271154.1. NM_001284225.1. [Q9H9T3-4]
NP_001271155.1. NM_001284226.1. [Q9H9T3-5]
NP_060561.3. NM_018091.5. [Q9H9T3-1]
XP_006716417.1. XM_006716354.1. [Q9H9T3-4]
UniGeneiHs.491336.

Genome annotation databases

EnsembliENST00000256398; ENSP00000256398; ENSG00000134014. [Q9H9T3-1]
ENST00000380353; ENSP00000369711; ENSG00000134014. [Q9H9T3-5]
ENST00000521015; ENSP00000428449; ENSG00000134014. [Q9H9T3-2]
ENST00000537665; ENSP00000445558; ENSG00000134014. [Q9H9T3-4]
GeneIDi55140.
KEGGihsa:55140.
UCSCiuc003xgn.4. human. [Q9H9T3-1]
uc011las.2. human.

Polymorphism databases

DMDMi145558902.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6065.1. [Q9H9T3-1]
CCDS64860.1. [Q9H9T3-5]
CCDS64861.1. [Q9H9T3-4]
CCDS75717.1. [Q9H9T3-2]
RefSeqiNP_001271151.1. NM_001284222.1. [Q9H9T3-2]
NP_001271153.1. NM_001284224.1. [Q9H9T3-4]
NP_001271154.1. NM_001284225.1. [Q9H9T3-4]
NP_001271155.1. NM_001284226.1. [Q9H9T3-5]
NP_060561.3. NM_018091.5. [Q9H9T3-1]
XP_006716417.1. XM_006716354.1. [Q9H9T3-4]
UniGeneiHs.491336.

3D structure databases

ProteinModelPortaliQ9H9T3.
SMRiQ9H9T3. Positions 490-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120444. 23 interactions.
IntActiQ9H9T3. 4 interactions.
MINTiMINT-3062287.
STRINGi9606.ENSP00000256398.

PTM databases

PhosphoSiteiQ9H9T3.

Polymorphism databases

DMDMi145558902.

Proteomic databases

MaxQBiQ9H9T3.
PaxDbiQ9H9T3.
PeptideAtlasiQ9H9T3.
PRIDEiQ9H9T3.

Protocols and materials databases

DNASUi55140.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256398; ENSP00000256398; ENSG00000134014. [Q9H9T3-1]
ENST00000380353; ENSP00000369711; ENSG00000134014. [Q9H9T3-5]
ENST00000521015; ENSP00000428449; ENSG00000134014. [Q9H9T3-2]
ENST00000537665; ENSP00000445558; ENSG00000134014. [Q9H9T3-4]
GeneIDi55140.
KEGGihsa:55140.
UCSCiuc003xgn.4. human. [Q9H9T3-1]
uc011las.2. human.

Organism-specific databases

CTDi55140.
GeneCardsiGC08P027947.
HGNCiHGNC:20696. ELP3.
HPAiHPA025812.
MIMi612722. gene.
neXtProtiNX_Q9H9T3.
PharmGKBiPA134992603.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1243.
GeneTreeiENSGT00390000013141.
HOGENOMiHOG000227514.
HOVERGENiHBG107845.
InParanoidiQ9H9T3.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7V765W.
PhylomeDBiQ9H9T3.
TreeFamiTF105752.

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Miscellaneous databases

GeneWikiiELP3.
GenomeRNAii55140.
NextBioi35471088.
PROiQ9H9T3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H9T3.
CleanExiHS_ELP3.
ExpressionAtlasiQ9H9T3. baseline and differential.
GenevestigatoriQ9H9T3.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1; 3 AND 4).
    Tissue: Amygdala and Hippocampus.
  2. 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.
    , 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. 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. "Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin."
    Creppe C., Malinouskaya L., Volvert M.L., Gillard M., Close P., Malaise O., Laguesse S., Cornez I., Rahmouni S., Ormenese S., Belachew S., Malgrange B., Chapelle J.P., Siebenlist U., Moonen G., Chariot A., Nguyen L.
    Cell 136:551-564(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IKBKAP AND ALPHA-TUBULIN.
  12. Cited for: TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN NEURODEGENERATION.
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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.
  16. "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.

Entry informationi

Entry nameiELP3_HUMAN
AccessioniPrimary (citable) accession number: Q9H9T3
Secondary accession number(s): B4DE19
, B4DIG1, E2QRI5, Q53G84, Q6AWB0, Q9BVF7, Q9NVZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: January 7, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.