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Q9H9T3

- ELP3_HUMAN

UniProt

Q9H9T3 - ELP3_HUMAN

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Protein
Elongator complex protein 3
Gene
ELP3
Organism
Homo sapiens (Human)
Status
Reviewed - 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. May also have a methyltransferase activity. Involved in cell migration.4 Publications

Catalytic activityi

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

Cofactori

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. N-acetyltransferase activity Source: InterPro
  2. histone acetyltransferase activity Source: UniProtKB-EC
  3. iron-sulfur cluster binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. phosphorylase kinase regulator activity Source: UniProtKB
  6. protein binding Source: IntAct

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. positive regulation of cell migration Source: Ensembl
  3. regulation of protein kinase activity Source: GOC
  4. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. transcription elongation from RNA polymerase II promoter Source: HGNC
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_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

Isoform 1 : Nucleus 4 Publications
Isoform 2 : Cytoplasm. Nucleus 4 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992603.

PTM / Processingi

Molecule processing

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

Gene expression databases

ArrayExpressiQ9H9T3.
BgeeiQ9H9T3.
CleanExiHS_ELP3.
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/ELP1.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi120444. 13 interactions.
IntActiQ9H9T3. 4 interactions.
MINTiMINT-3062287.
STRINGi9606.ENSP00000256398.

Structurei

3D structure databases

ProteinModelPortaliQ9H9T3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini396 – 547152N-acetyltransferase
Add
BLAST

Sequence similaritiesi

Belongs to the ELP3 family.

Phylogenomic databases

eggNOGiCOG1243.
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

MRQKRKGDLS PAELMMLTIG DVIKQLIEAH EQGKDIDLNK VKTKTAAKYG    50
LSAQPRLVDI IAAVPPQYRK VLMPKLKAKP IRTASGIAVV AVMCKPHRCP 100
HISFTGNICV YCPGGPDSDF EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH 150
RIEQLKQLGH SVDKVEFIVM GGTFMALPEE YRDYFIRNLH DALSGHTSNN 200
IYEAVKYSER SLTKCIGITI ETRPDYCMKR HLSDMLTYGC TRLEIGVQSV 250
YEDVARDTNR GHTVKAVCES FHLAKDSGFK VVAHMMPDLP NVGLERDIEQ 300
FTEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYKSY SPSDLVELVA 350
RILALVPPWT RVYRVQRDIP MPLVSSGVEH GNLRELALAR MKDLGIQCRD 400
VRTREVGIQE IHHKVRPYQV ELVRRDYVAN GGWETFLSYE DPDQDILIGL 450
LRLRKCSEET FRFELGGGVS IVRELHVYGS VVPVSSRDPT KFQHQGFGML 500
LMEEAERIAR EEHGSGKIAV ISGVGTRNYY RKIGYRLQGP YMVKMLK 547
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. Reason: Aberrant splicing.
The sequence CAH10573.1 differs from that shown. Reason: Frameshift at position 279.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9292Missing in isoform 4.
VSP_055284Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 2.
VSP_024406Add
BLAST
Alternative sequencei1 – 1212MRQKR…DLSPA → MSTHQFYRKYMC in isoform 3.
VSP_055285Add
BLAST
Alternative sequencei13 – 131119Missing in isoform 3.
VSP_055286Add
BLAST

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
RefSeqiNP_001271151.1. NM_001284222.1. [Q9H9T3-2]
NP_001271153.1. NM_001284224.1.
NP_001271154.1. NM_001284225.1.
NP_001271155.1. NM_001284226.1.
NP_060561.3. NM_018091.5. [Q9H9T3-1]
XP_006716417.1. XM_006716354.1.
UniGeneiHs.491336.

Genome annotation databases

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

Polymorphism databases

DMDMi145558902.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6065.1. [Q9H9T3-1 ]
RefSeqi NP_001271151.1. NM_001284222.1. [Q9H9T3-2 ]
NP_001271153.1. NM_001284224.1.
NP_001271154.1. NM_001284225.1.
NP_001271155.1. NM_001284226.1.
NP_060561.3. NM_018091.5. [Q9H9T3-1 ]
XP_006716417.1. XM_006716354.1.
UniGenei Hs.491336.

3D structure databases

ProteinModelPortali Q9H9T3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120444. 13 interactions.
IntActi Q9H9T3. 4 interactions.
MINTi MINT-3062287.
STRINGi 9606.ENSP00000256398.

PTM databases

PhosphoSitei Q9H9T3.

Polymorphism databases

DMDMi 145558902.

Proteomic databases

MaxQBi Q9H9T3.
PaxDbi Q9H9T3.
PeptideAtlasi Q9H9T3.
PRIDEi Q9H9T3.

Protocols and materials databases

DNASUi 55140.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256398 ; ENSP00000256398 ; ENSG00000134014 . [Q9H9T3-1 ]
ENST00000380353 ; ENSP00000369711 ; ENSG00000134014 .
ENST00000521015 ; ENSP00000428449 ; ENSG00000134014 . [Q9H9T3-2 ]
ENST00000537665 ; ENSP00000445558 ; ENSG00000134014 .
GeneIDi 55140.
KEGGi hsa:55140.
UCSCi uc003xgn.4. human. [Q9H9T3-1 ]

Organism-specific databases

CTDi 55140.
GeneCardsi GC08P028006.
HGNCi HGNC:20696. ELP3.
HPAi HPA025812.
MIMi 612722. gene.
neXtProti NX_Q9H9T3.
PharmGKBi PA134992603.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1243.
HOGENOMi HOG000227514.
HOVERGENi HBG107845.
InParanoidi Q9H9T3.
KOi K07739.
OMAi GYKVVSH.
OrthoDBi EOG7V765W.
PhylomeDBi Q9H9T3.
TreeFami TF105752.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

GeneWikii ELP3.
GenomeRNAii 55140.
NextBioi 35471088.
PROi Q9H9T3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H9T3.
Bgeei Q9H9T3.
CleanExi HS_ELP3.
Genevestigatori Q9H9T3.

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. "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. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. "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: September 3, 2014
This is version 116 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

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