Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Amino-terminal enhancer of split

Gene

AES

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

Functioni

Transcriptional corepressor. Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development.2 Publications

GO - Molecular functioni

  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • cellular response to extracellular stimulus Source: Ensembl
  • multicellular organismal development Source: ProtInc
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of protein binding Source: BHF-UCL
  • negative regulation of response to cytokine stimulus Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • organ morphogenesis Source: ProtInc
  • positive regulation of anoikis Source: UniProtKB
  • regulation of growth Source: Ensembl
  • response to interleukin-1 Source: BHF-UCL
  • skeletal system development Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_264567. repression of WNT target genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Amino-terminal enhancer of split
Short name:
Amino enhancer of split
Alternative name(s):
Gp130-associated protein GAM
Grg-5
Groucho-related protein 5
Protein ESP1
Protein GRG
Gene namesi
Name:AES
Synonyms:GRG, GRG5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:307. AES.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24606.

Polymorphism and mutation databases

BioMutaiAES.
DMDMi23503062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197Amino-terminal enhancer of splitPRO_0000050834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by XIAP/BIRC4.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ08117.
PaxDbiQ08117.
PRIDEiQ08117.

PTM databases

PhosphoSiteiQ08117.

Expressioni

Tissue specificityi

Found predominantly in muscle, heart and Placenta. In fetal tissues, abundantly expressed in the heart, lung, kidney, brain and liver.

Gene expression databases

BgeeiQ08117.
CleanExiHS_AES.
ExpressionAtlasiQ08117. baseline and differential.
GenevisibleiQ08117. HS.

Interactioni

Subunit structurei

Homooligomer and heterooligomer with other family members. Binds TCF7 (By similarity). Binds the NF-kappa-B subunit RELA. Interacts with PHF12. Interacts (via Q domain) with SIX3. Interacts with SIX6.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9H6143EBI-717810,EBI-10249899
ABI2Q9NYB93EBI-717810,EBI-743598
AENQ8WTP83EBI-717810,EBI-8637627
ARHGAP32A7KAX93EBI-717810,EBI-308663
BAHD1Q8TBE03EBI-717810,EBI-742750
BCL6P411823EBI-717810,EBI-765407
BHLHE40O145033EBI-717810,EBI-711810
BIRC7Q96CA53EBI-717810,EBI-517623
BYSLQ138955EBI-717810,EBI-358049
C1orf109Q9NX043EBI-717810,EBI-8643161
C1orf216Q8TAB53EBI-717810,EBI-747505
C1orf94Q6P1W53EBI-717810,EBI-946029
C6orf165Q8IYR03EBI-717810,EBI-749051
CALCOCO2Q131373EBI-717810,EBI-739580
CARD9Q9H2573EBI-717810,EBI-751319
CCDC57Q2TAC23EBI-717810,EBI-2808286
CCNJLF6RF563EBI-717810,EBI-10177725
CCNKO759093EBI-717810,EBI-739806
CIB3Q96Q773EBI-717810,EBI-10292696
CPSF7Q8N6843EBI-717810,EBI-746909
CRACR2AQ9BSW23EBI-717810,EBI-739773
CRXO431863EBI-717810,EBI-748171
CTAGE5O153203EBI-717810,EBI-1050253
DDX6P261963EBI-717810,EBI-351257
DIP2AQ14689-63EBI-717810,EBI-10233719
EAF1Q96JC93EBI-717810,EBI-769261
EIF4E2O605733EBI-717810,EBI-398610
FAM124AQ86V423EBI-717810,EBI-744506
FAM124BQ9H5Z63EBI-717810,EBI-741626
FBF1Q8TES7-63EBI-717810,EBI-10244131
FOXP2O154093EBI-717810,EBI-983612
FRS3O435593EBI-717810,EBI-725515
FSD2A1L4K13EBI-717810,EBI-5661036
GFAPP141363EBI-717810,EBI-744302
GOLGA2Q083793EBI-717810,EBI-618309
GORASP2Q9H8Y83EBI-717810,EBI-739467
GRB2P629933EBI-717810,EBI-401755
HNRNPFP525973EBI-717810,EBI-352986
HOMEZQ8IX15-33EBI-717810,EBI-10172004
IKZF3Q9UKT93EBI-717810,EBI-747204
KANK2Q63ZY33EBI-717810,EBI-2556193
KIFC3Q9BVG83EBI-717810,EBI-2125614
KRT13A1A4E93EBI-717810,EBI-10171552
KRT15P190123EBI-717810,EBI-739566
KRT31Q153233EBI-717810,EBI-948001
KRT40Q6A1623EBI-717810,EBI-10171697
KRTAP10-7P604093EBI-717810,EBI-10172290
KRTAP10-8P604103EBI-717810,EBI-10171774
KRTAP10-9P604113EBI-717810,EBI-10172052
L3MBTL2Q969R53EBI-717810,EBI-739909
LDOC1O957513EBI-717810,EBI-740738
LINC00526Q96FQ73EBI-717810,EBI-10286106
LMO1P258003EBI-717810,EBI-8639312
LMO2P257913EBI-717810,EBI-739696
LMO4P619683EBI-717810,EBI-2798728
LSM2Q9Y3333EBI-717810,EBI-347416
MAGOHBQ96A723EBI-717810,EBI-746778
MBNL1Q86VM63EBI-717810,EBI-10225084
MED4Q9NPJ63EBI-717810,EBI-394607
MFAP1P550813EBI-717810,EBI-1048159
MLXQ9UH923EBI-717810,EBI-741109
MORF4L2Q150143EBI-717810,EBI-399257
MTUS2Q5JR593EBI-717810,EBI-742948
NAB2Q157423EBI-717810,EBI-8641936
NCDNQ9UBB63EBI-717810,EBI-1053490
NEK6Q9HC983EBI-717810,EBI-740364
NOTCH2NLQ7Z3S93EBI-717810,EBI-945833
NUDT22Q9BRQ33EBI-717810,EBI-10297093
OLIG3Q7RTU33EBI-717810,EBI-10225049
OSGIN1Q9UJX03EBI-717810,EBI-9057006
PARVGQ9HBI03EBI-717810,EBI-3921217
PPP1R16AQ96I343EBI-717810,EBI-710402
PRKAA1Q131313EBI-717810,EBI-1181405
PRKAA2P546463EBI-717810,EBI-1383852
PROP1O753604EBI-717810,EBI-9027467
PRPF31F1T0A53EBI-717810,EBI-10177194
PRR3P795223EBI-717810,EBI-2803328
PTRH2Q9Y3E57EBI-717810,EBI-1056751
QARSP478973EBI-717810,EBI-347462
QARSP47897-23EBI-717810,EBI-10209725
RBM10P981753EBI-717810,EBI-721525
RBPMSQ930623EBI-717810,EBI-740322
RELQ048643EBI-717810,EBI-307352
RFX6Q8HWS33EBI-717810,EBI-746118
RHOXF2Q9BQY43EBI-717810,EBI-372094
RIMBP3Q9UFD93EBI-717810,EBI-10182375
RNF31Q96EP0-33EBI-717810,EBI-10225152
SCNM1Q9BWG63EBI-717810,EBI-748391
SDCBPO005603EBI-717810,EBI-727004
SIX1Q154753EBI-717810,EBI-743675
SKILP127573EBI-717810,EBI-2902468
SMAD3P840223EBI-717810,EBI-347161
SNRPCQ5TAL43EBI-717810,EBI-10246938
SOX5P357113EBI-717810,EBI-3505701
SRPK2P783623EBI-717810,EBI-593303
STK16O757163EBI-717810,EBI-749295
STX11O755583EBI-717810,EBI-714135
TBX3O151193EBI-717810,EBI-3452216
TCF4P158843EBI-717810,EBI-533224
TMCC2Q7Z6C63EBI-717810,EBI-10177480
TRAF1Q130773EBI-717810,EBI-359224
TRAF2Q129333EBI-717810,EBI-355744
TRIM26Q128993EBI-717810,EBI-2341136
TRIM27P143733EBI-717810,EBI-719493
TRIM41Q8WV443EBI-717810,EBI-725997
TSC22D4Q8IV543EBI-717810,EBI-10261521
TSGA10Q9BZW73EBI-717810,EBI-744794
TSSK3Q96PN83EBI-717810,EBI-3918381
U2AF2P263683EBI-717810,EBI-742339
UBXN11Q5T1243EBI-717810,EBI-746004
VPS37BQ9H9H43EBI-717810,EBI-4400866
VPS37CA5D8V63EBI-717810,EBI-2559305
ZBTB24O431673EBI-717810,EBI-744471
ZGPATQ8N5A53EBI-717810,EBI-3439227
ZGPATQ8N5A5-23EBI-717810,EBI-10183064
ZNF576Q9H6093EBI-717810,EBI-3921014

Protein-protein interaction databases

BioGridi106675. 140 interactions.
IntActiQ08117. 145 interactions.
MINTiMINT-1382079.
STRINGi9606.ENSP00000221561.

Structurei

3D structure databases

ProteinModelPortaliQ08117.
SMRiQ08117. Positions 24-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 19732CCN domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 131131Gln-rich (Q domain)Add
BLAST
Compositional biasi132 – 16534Gly/Pro-rich (GP domain)Add
BLAST

Domaini

Lacks the C-terminal WD repeats.

Sequence similaritiesi

Belongs to the WD repeat Groucho/TLE family.Curated

Phylogenomic databases

eggNOGiNOG258600.
GeneTreeiENSGT00550000074465.
HOGENOMiHOG000033830.
HOVERGENiHBG000205.
InParanoidiQ08117.
OMAiMFPQARH.
OrthoDBiEOG7HQNC3.
PhylomeDBiQ08117.

Family and domain databases

InterProiIPR005617. Groucho/TLE_N.
[Graphical view]
PfamiPF03920. TLE_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q08117-1) [UniParc]FASTAAdd to basket

Also known as: AES-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.

« Hide

        10         20         30         40         50
MMFPQSRHSG SSHLPQQLKF TTSDSCDRIK DEFQLLQAQY HSLKLECDKL
60 70 80 90 100
ASEKSEMQRH YVMYYEMSYG LNIEMHKQAE IVKRLNGICA QVLPYLSQEH
110 120 130 140 150
QQQVLGAIER AKQVTAPELN SIIRQQLQAH QLSQLQALAL PLTPLPVGLQ
160 170 180 190
PPSLPAVSAG TGLLSLSALG SQAHLSKEDK NGHDGDTHQE DDGEKSD
Length:197
Mass (Da):21,970
Last modified:September 19, 2002 - v4
Checksum:i3851663AA6921A9F
GO
Isoform 2 (identifier: Q08117-2) [UniParc]FASTAAdd to basket

Also known as: AES-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MMFPQSRHS → MCHKNGFPQE...WGNRGPAGCR

Show »
Length:264
Mass (Da):29,091
Checksum:i8E6CD80583D0B82D
GO

Sequence cautioni

The sequence AAC35517.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301K → T (PubMed:9809752).Curated
Sequence conflicti30 – 301K → T (PubMed:15057824).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681A → E.
Corresponds to variant rs1802578 [ dbSNP | Ensembl ].
VAR_011958

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99MMFPQSRHS → MCHKNGFPQEGGITAAFLQK RKLRLSKNHRPARAKVTEHV RGTRPGRATAGPAASTRAAG SLFFDRWGNRGPAGCR in isoform 2. 3 PublicationsVSP_043527

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04241 mRNA. Translation: AAA16223.1.
U88832, U88831 Genomic DNA. Translation: AAD00654.1.
AF072902 mRNA. Translation: AAC35517.1. Different initiation.
AK094591 mRNA. Translation: BAG52894.1.
AK314713 mRNA. Translation: BAG37257.1.
AC005944 Genomic DNA. Translation: AAC72103.1.
CH471139 Genomic DNA. Translation: EAW69345.1.
CH471139 Genomic DNA. Translation: EAW69347.1.
BC113735 mRNA. Translation: AAI13736.1.
BC113737 mRNA. Translation: AAI13738.1.
X73358 mRNA. Translation: CAA51768.1.
CCDSiCCDS12101.1. [Q08117-2]
CCDS12102.1. [Q08117-1]
PIRiG01236.
S35678.
S35679.
RefSeqiNP_001121.2. NM_001130.5. [Q08117-1]
NP_945320.1. NM_198969.1. [Q08117-2]
NP_945321.1. NM_198970.1.
UniGeneiHs.515053.

Genome annotation databases

EnsembliENST00000221561; ENSP00000221561; ENSG00000104964. [Q08117-2]
ENST00000327141; ENSP00000317537; ENSG00000104964.
GeneIDi166.
KEGGihsa:166.
UCSCiuc002lwy.1. human. [Q08117-1]
uc002lxb.1. human. [Q08117-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04241 mRNA. Translation: AAA16223.1.
U88832, U88831 Genomic DNA. Translation: AAD00654.1.
AF072902 mRNA. Translation: AAC35517.1. Different initiation.
AK094591 mRNA. Translation: BAG52894.1.
AK314713 mRNA. Translation: BAG37257.1.
AC005944 Genomic DNA. Translation: AAC72103.1.
CH471139 Genomic DNA. Translation: EAW69345.1.
CH471139 Genomic DNA. Translation: EAW69347.1.
BC113735 mRNA. Translation: AAI13736.1.
BC113737 mRNA. Translation: AAI13738.1.
X73358 mRNA. Translation: CAA51768.1.
CCDSiCCDS12101.1. [Q08117-2]
CCDS12102.1. [Q08117-1]
PIRiG01236.
S35678.
S35679.
RefSeqiNP_001121.2. NM_001130.5. [Q08117-1]
NP_945320.1. NM_198969.1. [Q08117-2]
NP_945321.1. NM_198970.1.
UniGeneiHs.515053.

3D structure databases

ProteinModelPortaliQ08117.
SMRiQ08117. Positions 24-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106675. 140 interactions.
IntActiQ08117. 145 interactions.
MINTiMINT-1382079.
STRINGi9606.ENSP00000221561.

PTM databases

PhosphoSiteiQ08117.

Polymorphism and mutation databases

BioMutaiAES.
DMDMi23503062.

Proteomic databases

MaxQBiQ08117.
PaxDbiQ08117.
PRIDEiQ08117.

Protocols and materials databases

DNASUi166.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221561; ENSP00000221561; ENSG00000104964. [Q08117-2]
ENST00000327141; ENSP00000317537; ENSG00000104964.
GeneIDi166.
KEGGihsa:166.
UCSCiuc002lwy.1. human. [Q08117-1]
uc002lxb.1. human. [Q08117-2]

Organism-specific databases

CTDi166.
GeneCardsiGC19M003052.
HGNCiHGNC:307. AES.
MIMi600188. gene.
neXtProtiNX_Q08117.
PharmGKBiPA24606.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258600.
GeneTreeiENSGT00550000074465.
HOGENOMiHOG000033830.
HOVERGENiHBG000205.
InParanoidiQ08117.
OMAiMFPQARH.
OrthoDBiEOG7HQNC3.
PhylomeDBiQ08117.

Enzyme and pathway databases

ReactomeiREACT_264567. repression of WNT target genes.

Miscellaneous databases

ChiTaRSiAES. human.
GenomeRNAii166.
NextBioi669.
PROiQ08117.
SOURCEiSearch...

Gene expression databases

BgeeiQ08117.
CleanExiHS_AES.
ExpressionAtlasiQ08117. baseline and differential.
GenevisibleiQ08117. HS.

Family and domain databases

InterProiIPR005617. Groucho/TLE_N.
[Graphical view]
PfamiPF03920. TLE_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequence analysis and characterization of a human homolog of Drosophila enhancer of split m9/m10."
    Scala L.A., Piparo K.E., Tirumalai P.S., Howells R.D.
    Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Neuroblastoma.
  2. "Genomic organization and chromosome localization to band 19p13.3 of the human AES gene: gene product exhibits strong similarity to the N-terminal domain of Drosophila enhancer of split Groucho protein."
    Hou E.W., Li S.S.-L.
    DNA Cell Biol. 17:911-913(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lymphocyte and Umbilical cord.
  3. "Cloning and eukaryotic expressing of a novel gp130 associated molecule."
    Liu Y., Jin B.Q., Liu F.
    Zhonghua Wei Sheng Wu Xue He Mian Yi Xue Za Zhi 18:106-110(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  4. "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 AND 2).
    Tissue: Amygdala and Cerebellum.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [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 2).
    Tissue: Brain.
  8. "Molecular cloning and expression of mouse and human cDNA encoding AES and ESG proteins with strong similarity to Drosophila enhancer of split groucho protein."
    Miyasaka H., Choudhury B.K., Hou E.W., Li S.S.-L.
    Eur. J. Biochem. 216:343-352(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-197 (ISOFORMS 1 AND 2).
    Tissue: Testis.
  9. "Inhibition of nuclear factor-kappaB-mediated transcription by association with the amino-terminal enhancer of split, a Groucho-related protein lacking WD40 repeats."
    Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N., Asamitsu K., Okamoto T.
    J. Biol. Chem. 275:4383-4390(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RELA.
  10. "Transducin-like enhancer of split proteins, the human homologs of Drosophila groucho, interact with hepatic nuclear factor 3beta."
    Wang J.-C., Waltner-Law M., Yamada K., Osawa H., Stifani S., Granner D.K.
    J. Biol. Chem. 275:18418-18423(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, OLIGOMERIZATION.
  11. "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex."
    Yochum G.S., Ayer D.E.
    Mol. Cell. Biol. 21:4110-4118(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHF12.
  12. "Six3 and Six6 activity is modulated by members of the groucho family."
    Lopez-Rios J., Tessmar K., Loosli F., Wittbrodt J., Bovolenta P.
    Development 130:185-195(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIX3.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling."
    Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.
    Mol. Cell 45:619-628(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY XIAP/BIRC4.

Entry informationi

Entry nameiAES_HUMAN
AccessioniPrimary (citable) accession number: Q08117
Secondary accession number(s): B2RBL0
, Q12808, Q14CJ1, Q96TG9, Q9UDY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 19, 2002
Last modified: July 22, 2015
This is version 140 of the entry and version 4 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.