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Protein

Transcription and mRNA export factor ENY2

Gene

ENY2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery.2 Publications

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

mRNA transport, Protein transport, Transcription, Transcription regulation, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription and mRNA export factor ENY2UniRule annotation
Alternative name(s):
Enhancer of yellow 2 transcription factor homologUniRule annotation
Gene namesi
Name:ENY2UniRule annotation
ORF Names:DC6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:24449. ENY2.

Subcellular locationi

  • Nucleusnucleoplasm UniRule annotation1 Publication
  • Nucleusnuclear pore complex UniRule annotation1 Publication

GO - Cellular componenti

  • DUBm complex Source: GO_Central
  • nuclear pore Source: UniProtKB-SubCell
  • SAGA complex Source: UniProtKB
  • transcription export complex 2 Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671907.

Polymorphism and mutation databases

BioMutaiENY2.
DMDMi74752879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Transcription and mRNA export factor ENY2PRO_0000314130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: Q9NPA8-2)
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9NPA8.
MaxQBiQ9NPA8.
PaxDbiQ9NPA8.
PeptideAtlasiQ9NPA8.
PRIDEiQ9NPA8.
TopDownProteomicsiQ9NPA8-1. [Q9NPA8-1]

PTM databases

iPTMnetiQ9NPA8.
PhosphoSiteiQ9NPA8.

Expressioni

Gene expression databases

BgeeiQ9NPA8.
CleanExiHS_ENY2.
ExpressionAtlasiQ9NPA8. baseline and differential.
GenevisibleiQ9NPA8. HS.

Organism-specific databases

HPAiHPA024648.

Interactioni

Subunit structurei

Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3. TREX-2 contains 2 ENY2 chains. The TREX-2 complex interacts with the nucleoporin NUP153. Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with ATXN7L3, GANP and with the RNA polymerase II.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi121267. 19 interactions.
IntActiQ9NPA8. 11 interactions.
MINTiMINT-1370469.
STRINGi9606.ENSP00000429986.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2213Combined sources
Helixi25 – 3915Combined sources
Helixi42 – 5716Combined sources
Turni59 – 613Combined sources
Helixi64 – 7815Combined sources
Helixi81 – 9818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DHXX-ray2.10B/C/E/F1-101[»]
ProteinModelPortaliQ9NPA8.
SMRiQ9NPA8. Positions 7-99.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ENY2 family.UniRule annotation

Phylogenomic databases

eggNOGiKOG4479. Eukaryota.
ENOG4111PHC. LUCA.
GeneTreeiENSGT00390000011748.
HOVERGENiHBG107852.
InParanoidiQ9NPA8.
KOiK11368.
OMAiAHCKDVI.
PhylomeDBiQ9NPA8.
TreeFamiTF326556.

Family and domain databases

HAMAPiMF_03046. ENY2_Sus1.
InterProiIPR018783. TF_ENY2.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NPA8-1) [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
MVVSKMNKDA QMRAAINQKL IETGERERLK ELLRAKLIEC GWKDQLKAHC
60 70 80 90 100
KEVIKEKGLE HVTVDDLVAE ITPKGRALVP DSVKKELLQR IRTFLAQHAS

L
Length:101
Mass (Da):11,529
Last modified:October 1, 2000 - v1
Checksum:iA0617024C59AABFB
GO
Isoform 2 (identifier: Q9NPA8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: Missing.

Note: Gene prediction based on EST data.Combined sources
Show »
Length:96
Mass (Da):10,984
Checksum:i5A6C33C154264A47
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 55Missing in isoform 2. CuratedVSP_046891

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF173296 mRNA. Translation: AAF89829.1.
AF201940 mRNA. Translation: AAF86876.1.
AK290752 mRNA. Translation: BAF83441.1.
AK316560 mRNA. Translation: BAG38149.1.
CR457183 mRNA. Translation: CAG33464.1.
AC021237 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91927.1.
CH471060 Genomic DNA. Translation: EAW91930.1.
BC007870 mRNA. Translation: AAH07870.1.
CCDSiCCDS43762.1. [Q9NPA8-1]
CCDS55270.1. [Q9NPA8-2]
RefSeqiNP_001180486.1. NM_001193557.1. [Q9NPA8-2]
NP_064574.1. NM_020189.5. [Q9NPA8-1]
UniGeneiHs.492555.

Genome annotation databases

EnsembliENST00000521662; ENSP00000429713; ENSG00000120533. [Q9NPA8-2]
ENST00000521688; ENSP00000429986; ENSG00000120533. [Q9NPA8-1]
GeneIDi56943.
KEGGihsa:56943.
UCSCiuc003ync.4. human. [Q9NPA8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF173296 mRNA. Translation: AAF89829.1.
AF201940 mRNA. Translation: AAF86876.1.
AK290752 mRNA. Translation: BAF83441.1.
AK316560 mRNA. Translation: BAG38149.1.
CR457183 mRNA. Translation: CAG33464.1.
AC021237 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91927.1.
CH471060 Genomic DNA. Translation: EAW91930.1.
BC007870 mRNA. Translation: AAH07870.1.
CCDSiCCDS43762.1. [Q9NPA8-1]
CCDS55270.1. [Q9NPA8-2]
RefSeqiNP_001180486.1. NM_001193557.1. [Q9NPA8-2]
NP_064574.1. NM_020189.5. [Q9NPA8-1]
UniGeneiHs.492555.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DHXX-ray2.10B/C/E/F1-101[»]
ProteinModelPortaliQ9NPA8.
SMRiQ9NPA8. Positions 7-99.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121267. 19 interactions.
IntActiQ9NPA8. 11 interactions.
MINTiMINT-1370469.
STRINGi9606.ENSP00000429986.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiQ9NPA8.
PhosphoSiteiQ9NPA8.

Polymorphism and mutation databases

BioMutaiENY2.
DMDMi74752879.

Proteomic databases

EPDiQ9NPA8.
MaxQBiQ9NPA8.
PaxDbiQ9NPA8.
PeptideAtlasiQ9NPA8.
PRIDEiQ9NPA8.
TopDownProteomicsiQ9NPA8-1. [Q9NPA8-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000521662; ENSP00000429713; ENSG00000120533. [Q9NPA8-2]
ENST00000521688; ENSP00000429986; ENSG00000120533. [Q9NPA8-1]
GeneIDi56943.
KEGGihsa:56943.
UCSCiuc003ync.4. human. [Q9NPA8-1]

Organism-specific databases

CTDi56943.
GeneCardsiENY2.
HGNCiHGNC:24449. ENY2.
HPAiHPA024648.
neXtProtiNX_Q9NPA8.
PharmGKBiPA142671907.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4479. Eukaryota.
ENOG4111PHC. LUCA.
GeneTreeiENSGT00390000011748.
HOVERGENiHBG107852.
InParanoidiQ9NPA8.
KOiK11368.
OMAiAHCKDVI.
PhylomeDBiQ9NPA8.
TreeFamiTF326556.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiENY2. human.
GenomeRNAii56943.
PROiQ9NPA8.

Gene expression databases

BgeeiQ9NPA8.
CleanExiHS_ENY2.
ExpressionAtlasiQ9NPA8. baseline and differential.
GenevisibleiQ9NPA8. HS.

Family and domain databases

HAMAPiMF_03046. ENY2_Sus1.
InterProiIPR018783. TF_ENY2.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The novel transcription factor e(y)2 interacts with TAF(II)40 and potentiates transcription activation on chromatin templates."
    Georgieva S., Nabirochkina E., Dilworth F.J., Eickhoff H., Becker P., Tora L., Georgiev P., Soldatov A.
    Mol. Cell. Biol. 21:5223-5231(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Novel genes expressed in human dendritic cell."
    Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Chen Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Dendritic cell.
  3. "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] (ISOFORM 1).
    Tissue: Hippocampus.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Uterus.
  8. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
    Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
    Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SAGA COMPLEX.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements."
    Lang G., Bonnet J., Umlauf D., Karmodiya K., Koffler J., Stierle M., Devys D., Tora L.
    Mol. Cell. Biol. 31:3734-3744(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX.
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export."
    Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.
    Nucleic Acids Res. 40:4562-4573(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH GANP, IDENTIFICATION IN THE TREX-2 COMPLEX, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiENY2_HUMAN
AccessioniPrimary (citable) accession number: Q9NPA8
Secondary accession number(s): B2RE52, G3V117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 116 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.