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Protein

Transcriptional repressor protein YY1

Gene

YY1

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

Functioni

Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Plays a role in regulating enhancer activation (PubMed:28575647).4 Publications
Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi298Zinc 11
Metal bindingi303Zinc 11
Metal bindingi316Zinc 11
Metal bindingi320Zinc 11
Metal bindingi327Zinc 21
Metal bindingi330Zinc 21
Metal bindingi343Zinc 21
Metal bindingi347Zinc 21
Metal bindingi355Zinc 31
Metal bindingi360Zinc 31
Metal bindingi373Zinc 31
Metal bindingi377Zinc 31
Metal bindingi385Zinc 41
Metal bindingi390Zinc 41
Metal bindingi403Zinc 41
Metal bindingi407Zinc 41

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri296 – 320C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri325 – 347C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri353 – 377C2H2-type 3PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri383 – 407C2H2-type 4PROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processDifferentiation, DNA damage, DNA recombination, DNA repair, Spermatogenesis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5689603 UCH proteinases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP25490
SIGNORiP25490

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor protein YY1
Alternative name(s):
Delta transcription factor
INO80 complex subunit S
NF-E1
Yin and yang 1
Short name:
YY-1
Gene namesi
Name:YY1
Synonyms:INO80S
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000100811.10
HGNCiHGNC:12856 YY1
MIMi600013 gene
neXtProtiNX_P25490

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Gabriele-de Vries syndrome (GADEVS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurodevelopmental disorder characterized by delayed psychomotor development and intellectual disability. Most patients have behavioral and feeding problems, movement abnormalities, mild distal skeletal anomalies, and dysmorphic facial features.
See also OMIM:617557
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_079202179 – 414Missing in GADEVS. 1 PublicationAdd BLAST236
Natural variantiVAR_079203320H → Y in GADEVS; unknown pathological significance. 1 Publication1
Natural variantiVAR_079204339K → Q in GADEVS; unknown pathological significance. 1 Publication1
Natural variantiVAR_079205344 – 414Missing in GADEVS. 1 PublicationAdd BLAST71
Natural variantiVAR_079206366L → P in GADEVS; reduced DNA-binding; reduced transcription regulator activity. 1 PublicationCorresponds to variant dbSNP:rs1131692163Ensembl.1
Natural variantiVAR_079207366L → V in GADEVS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1131692044Ensembl.1
Natural variantiVAR_065086380D → Y in GADEVS; reduced DNA-binding; reduced transcription regulator activity. 2 PublicationsCorresponds to variant dbSNP:rs1131692043Ensembl.1
Natural variantiVAR_079208393Missing in GADEVS; unknown pathological significance. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi7528
MalaCardsiYY1
MIMi617557 phenotype
OpenTargetsiENSG00000100811
PharmGKBiPA37445

Polymorphism and mutation databases

DMDMi3915889

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000471901 – 414Transcriptional repressor protein YY1Add BLAST414

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei118PhosphoserineCombined sources1
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki183Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei187PhosphoserineCombined sources1
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei247PhosphoserineCombined sources1
Cross-linki286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei378PhosphothreonineCombined sources1
Cross-linki409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki411Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with the effect of decreasing affinity of YY1 to its cognate DNA binding sites.
Ubiquitinated.1 Publication

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP25490
MaxQBiP25490
PaxDbiP25490
PeptideAtlasiP25490
PRIDEiP25490
ProteomicsDBi54279

PTM databases

iPTMnetiP25490
PhosphoSitePlusiP25490

Miscellaneous databases

PMAP-CutDBiP25490

Expressioni

Gene expression databases

BgeeiENSG00000100811 Expressed in 242 organ(s), highest expression level in amniotic fluid
CleanExiHS_YY1
ExpressionAtlasiP25490 baseline and differential
GenevisibleiP25490 HS

Organism-specific databases

HPAiCAB009392
HPA001119

Interactioni

Subunit structurei

Interacts with YAF2 through the region encompassing the first and second zinc fingers (PubMed:9016636). Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80 (PubMed:17721549, PubMed:18026119, PubMed:18922472, PubMed:21303910). Interacts with EED and EZH2; the interactions are indicative for an association with the PRC2/EED-EZH2 complex (PubMed:11158321). Interacts with SFMBT2 (PubMed:23385818). Found in a complex with SMAD1 and SMAD4 (PubMed:15329343). Found in a complex with YY1, SIN3A and HDAC1 (By similarity).By similarity8 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113360, 133 interactors
ComplexPortaliCPX-846 INO80 chromatin remodeling complex
CORUMiP25490
DIPiDIP-150N
IntActiP25490, 90 interactors
MINTiP25490
STRINGi9606.ENSP00000262238

Structurei

Secondary structure

1414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP25490
SMRiP25490
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25490

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 170Interaction with the SMAD1/SMAD4 complexAdd BLAST170
Regioni257 – 341Involved in nuclear matrix associationAdd BLAST85
Regioni295 – 414Binding to DNAAdd BLAST120
Regioni333 – 371Involved in repression of activated transcriptionAdd BLAST39
Regioni371 – 397Involved in masking transactivation domainAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi43 – 53Asp/Glu-rich (acidic)Add BLAST11
Compositional biasi54 – 69Gly-richAdd BLAST16
Compositional biasi70 – 80Poly-HisAdd BLAST11
Compositional biasi159 – 170Gly/Ser-richAdd BLAST12

Sequence similaritiesi

Belongs to the YY transcription factor family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri296 – 320C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri325 – 347C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri353 – 377C2H2-type 3PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri383 – 407C2H2-type 4PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00910000144040
HOGENOMiHOG000008232
HOVERGENiHBG006823
InParanoidiP25490
KOiK09201
OMAiGGRKWEQ
OrthoDBiEOG091G03FM
PhylomeDBiP25490
TreeFamiTF106493

Family and domain databases

InterProiView protein in InterPro
IPR017114 YY-1-like
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PIRSFiPIRSF037113 TF_Yin_yang, 1 hit
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 4 hits
SUPFAMiSSF57667 SSF57667, 3 hits
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 4 hits
PS50157 ZINC_FINGER_C2H2_2, 4 hits

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.iShow all

P25490-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD
60 70 80 90 100
DEDGGGGDHG GGGGHGHAGH HHHHHHHHHH PPMIALQPLV TDDPTQVHHH
110 120 130 140 150
QEVILVQTRE EVVGGDDSDG LRAEDGFEDQ ILIPVPAPAG GDDDYIEQTL
160 170 180 190 200
VTVAAAGKSG GGGSSSSGGG RVKKGGGKKS GKKSYLSGGA GAAGGGGADP
210 220 230 240 250
GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE QIIGENSPPD
260 270 280 290 300
YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH
310 320 330 340 350
KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE
360 370 380 390 400
KPFQCTFEGC GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL
410
KSHILTHAKA KNNQ
Length:414
Mass (Da):44,713
Last modified:December 15, 1998 - v2
Checksum:i058C05A0AD2D04E6
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YJV7H0YJV7_HUMAN
Transcriptional repressor protein Y...
YY1
190Annotation score:
H0YJU4H0YJU4_HUMAN
Transcriptional repressor protein Y...
YY1
123Annotation score:
G3V3M8G3V3M8_HUMAN
Transcriptional repressor protein Y...
YY1
34Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65H → R in AAA59926 (PubMed:1946405).Curated1
Sequence conflicti196G → R in AAA59467 (PubMed:1655281).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_079202179 – 414Missing in GADEVS. 1 PublicationAdd BLAST236
Natural variantiVAR_079203320H → Y in GADEVS; unknown pathological significance. 1 Publication1
Natural variantiVAR_079204339K → Q in GADEVS; unknown pathological significance. 1 Publication1
Natural variantiVAR_079205344 – 414Missing in GADEVS. 1 PublicationAdd BLAST71
Natural variantiVAR_079206366L → P in GADEVS; reduced DNA-binding; reduced transcription regulator activity. 1 PublicationCorresponds to variant dbSNP:rs1131692163Ensembl.1
Natural variantiVAR_079207366L → V in GADEVS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1131692044Ensembl.1
Natural variantiVAR_074172372T → R Found in patients with late onset insulinomas; alters DNA-binding motif; increases transactivation activity; produces a constitutive activation of cAMP and Ca2+ signaling pathways involved in insulin secretion. 2 PublicationsCorresponds to variant dbSNP:rs386834266EnsemblClinVar.1
Natural variantiVAR_065086380D → Y in GADEVS; reduced DNA-binding; reduced transcription regulator activity. 2 PublicationsCorresponds to variant dbSNP:rs1131692043Ensembl.1
Natural variantiVAR_079208393Missing in GADEVS; unknown pathological significance. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77698 mRNA Translation: AAA59467.1
M76541 mRNA Translation: AAA59926.1
Z14077 mRNA Translation: CAA78455.1
BC037308 mRNA Translation: AAH37308.1
BC065366 mRNA Translation: AAH65366.1
CCDSiCCDS9957.1
PIRiA40350
RefSeqiNP_003394.1, NM_003403.4
UniGeneiHs.388927
Hs.603118

Genome annotation databases

EnsembliENST00000262238; ENSP00000262238; ENSG00000100811
GeneIDi7528
KEGGihsa:7528
UCSCiuc001ygy.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77698 mRNA Translation: AAA59467.1
M76541 mRNA Translation: AAA59926.1
Z14077 mRNA Translation: CAA78455.1
BC037308 mRNA Translation: AAH37308.1
BC065366 mRNA Translation: AAH65366.1
CCDSiCCDS9957.1
PIRiA40350
RefSeqiNP_003394.1, NM_003403.4
UniGeneiHs.388927
Hs.603118

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UBDX-ray2.50C291-414[»]
1ZNMNMR-A352-379[»]
4C5IX-ray2.59C199-228[»]
ProteinModelPortaliP25490
SMRiP25490
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113360, 133 interactors
ComplexPortaliCPX-846 INO80 chromatin remodeling complex
CORUMiP25490
DIPiDIP-150N
IntActiP25490, 90 interactors
MINTiP25490
STRINGi9606.ENSP00000262238

PTM databases

iPTMnetiP25490
PhosphoSitePlusiP25490

Polymorphism and mutation databases

DMDMi3915889

Proteomic databases

EPDiP25490
MaxQBiP25490
PaxDbiP25490
PeptideAtlasiP25490
PRIDEiP25490
ProteomicsDBi54279

Protocols and materials databases

DNASUi7528
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262238; ENSP00000262238; ENSG00000100811
GeneIDi7528
KEGGihsa:7528
UCSCiuc001ygy.3 human

Organism-specific databases

CTDi7528
DisGeNETi7528
EuPathDBiHostDB:ENSG00000100811.10
GeneCardsiYY1
HGNCiHGNC:12856 YY1
HPAiCAB009392
HPA001119
MalaCardsiYY1
MIMi600013 gene
617557 phenotype
neXtProtiNX_P25490
OpenTargetsiENSG00000100811
PharmGKBiPA37445
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00910000144040
HOGENOMiHOG000008232
HOVERGENiHBG006823
InParanoidiP25490
KOiK09201
OMAiGGRKWEQ
OrthoDBiEOG091G03FM
PhylomeDBiP25490
TreeFamiTF106493

Enzyme and pathway databases

ReactomeiR-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5689603 UCH proteinases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP25490
SIGNORiP25490

Miscellaneous databases

ChiTaRSiYY1 human
EvolutionaryTraceiP25490
GeneWikiiYY1
GenomeRNAii7528
PMAP-CutDBiP25490
PROiPR:P25490
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100811 Expressed in 242 organ(s), highest expression level in amniotic fluid
CleanExiHS_YY1
ExpressionAtlasiP25490 baseline and differential
GenevisibleiP25490 HS

Family and domain databases

InterProiView protein in InterPro
IPR017114 YY-1-like
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PIRSFiPIRSF037113 TF_Yin_yang, 1 hit
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 4 hits
SUPFAMiSSF57667 SSF57667, 3 hits
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 4 hits
PS50157 ZINC_FINGER_C2H2_2, 4 hits
ProtoNetiSearch...

Entry informationi

Entry nameiTYY1_HUMAN
AccessioniPrimary (citable) accession number: P25490
Secondary accession number(s): Q14935
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 1998
Last modified: September 12, 2018
This is version 212 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health

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