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Q00899 (TYY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional repressor protein YY1
Alternative name(s):
Delta transcription factor
NF-E1
UCR-motif DNA-binding protein
Yin and yang 1
Short name=YY-1
Gene names
Name:Yy1
Synonyms:Ucrbp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Binds to the upstream conserved region (UCR) (5'-CGCCATTTT-3') of Moloney murine leukemia virus (MuLV). 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). Involved in spermatogenesis and may play a role in meiotic DNA double-strand break repair. Ref.5 Ref.7

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 By similarity. Ref.5 Ref.7

Subunit structure

Interacts with YAF2 through the region encompassing the first and second zinc fingers. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Interacts with EED and EZH2; the interactions are indicative for an association with the PRC2/EED-EZH2 complex By similarity. Interacts with SFMBT2. Ref.6

Subcellular location

Nucleus matrix. Note: Associated with the nuclear matrix. In testis, localized to heterochromatin of spermatocytes. Ref.7

Tissue specificity

Expressed in ovary and, at lower levels, in testis. Ref.6

Developmental stage

At 7.5 dpc, highly expressed in the ectoplacental cone and, at lower levels, in the embryonic and extraembryonic ectoderm. At 14.5 dpc, highly expressed in placenta and yolk sac, and, at lower levels, in brain and heart. Ref.6

Post-translational modification

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

Ubiquitinated By similarity.

Disruption phenotype

Spermatocytes have a significant decrease in the global level of the heterochromatin markers and increase in the chromosomal double-strand break (DSB) signals at the leptotene/zygotene stages. Ref.7

Sequence similarities

Belongs to the YY transcription factor family.

Contains 4 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processDifferentiation
DNA damage
DNA recombination
DNA repair
Spermatogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA localization

Inferred from mutant phenotype PubMed 21729784. Source: MGI

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 16624538. Source: MGI

camera-type eye morphogenesis

Inferred from genetic interaction PubMed 16624538. Source: MGI

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.5. Source: UniProtKB

cellular response to UV

Inferred from electronic annotation. Source: Ensembl

chromosome organization

Inferred from mutant phenotype Ref.5. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20843790. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11861914. Source: MGI

response to UV-C

Inferred from mutant phenotype Ref.5. Source: UniProtKB

response to prostaglandin F

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentIno80 complex

Inferred from electronic annotation. Source: Ensembl

PcG protein complex

Inferred from direct assay PubMed 16624538PubMed 17001316. Source: MGI

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 20720167PubMed 9857059. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

transcription factor complex

Inferred from direct assay PubMed 11861914. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12527199PubMed 15161869PubMed 15574595. Source: MGI

RNA binding

Inferred from sequence orthology PubMed 21729784. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 20843790. Source: BHF-UCL

four-way junction DNA binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23531880. Source: IntAct

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11861914. Source: MGI

transcription regulatory region DNA binding

Inferred from sequence orthology PubMed 9857059. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smc4Q8CG472EBI-6921536,EBI-6921575

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Transcriptional repressor protein YY1
PRO_0000047191

Regions

Zinc finger296 – 32025C2H2-type 1
Zinc finger325 – 34723C2H2-type 2
Zinc finger353 – 37725C2H2-type 3
Zinc finger383 – 40725C2H2-type 4
Region257 – 34185Involved in nuclear matrix association By similarity
Region333 – 37139Involved in repression of activated transcription By similarity
Region371 – 39727Involved in masking transactivation domain By similarity
Compositional bias43 – 5311Asp/Glu-rich (acidic)
Compositional bias54 – 7017Gly-rich
Compositional bias71 – 8212Poly-His
Compositional bias161 – 17010Gly/Ser-rich

Sites

Metal binding2981Zinc 1 By similarity
Metal binding3031Zinc 1 By similarity
Metal binding3161Zinc 1 By similarity
Metal binding3201Zinc 1 By similarity
Metal binding3271Zinc 2 By similarity
Metal binding3301Zinc 2 By similarity
Metal binding3431Zinc 2 By similarity
Metal binding3471Zinc 2 By similarity
Metal binding3551Zinc 3 By similarity
Metal binding3601Zinc 3 By similarity
Metal binding3731Zinc 3 By similarity
Metal binding3771Zinc 3 By similarity
Metal binding3851Zinc 4 By similarity
Metal binding3901Zinc 4 By similarity
Metal binding4031Zinc 4 By similarity
Metal binding4071Zinc 4 By similarity

Amino acid modifications

Modified residue1201Phosphoserine By similarity
Modified residue2471Phosphoserine By similarity
Modified residue3781Phosphothreonine By similarity

Experimental info

Sequence conflict2191F → S in AAA37521. Ref.3
Sequence conflict3751R → G in AAA37521. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q00899 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C012378288E984F9

FASTA41444,717
        10         20         30         40         50         60 
MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD DEDGGGGDHG 

        70         80         90        100        110        120 
GGGGGHGHAG HHHHHHHHHH HHPPMIALQP LVTDDPTQVH HHQEVILVQT REEVVGGDDS 

       130        140        150        160        170        180 
DGLRAEDGFE DQILIPVPAP AGGDDDYIEQ TLVTVAAAGK SGGGASSGGG RVKKGGGKKS 

       190        200        210        220        230        240 
GKKSYLGGGA GAAGGGGADP GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE 

       250        260        270        280        290        300 
QIIGENSPPD YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH 

       310        320        330        340        350        360 
KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE KPFQCTFEGC 

       370        380        390        400        410 
GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL KSHILTHAKA KNNQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a negative transcription factor that binds to the upstream conserved region of Moloney murine leukemia virus."
Flanagan J.R., Becker K.G., Ennist D.L., Gleason S.L., Driggers P.H., Levi B.-Z., Appella E., Ozato K.
Mol. Cell. Biol. 12:38-44(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the mouse gene that encodes the delta/YY1/NF-E1/UCRBP transcription factor."
Safrany G., Perry R.P.
Proc. Natl. Acad. Sci. U.S.A. 90:5559-5563(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"Delta, a transcription factor that binds to downstream elements in several polymerase II promoters, is a functionally versatile zinc finger protein."
Hariharan N., Kelley D.E., Perry R.P.
Proc. Natl. Acad. Sci. U.S.A. 88:9799-9803(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR.
[6]"The PcG gene Sfmbt2 is paternally expressed in extraembryonic tissues."
Kuzmin A., Han Z., Golding M.C., Mann M.R., Latham K.E., Varmuza S.
Gene Expr. Patterns 8:107-116(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SFMBT2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Loss of YY1 impacts the heterochromatic state and meiotic double-strand breaks during mouse spermatogenesis."
Wu S., Hu Y.C., Liu H., Shi Y.
Mol. Cell. Biol. 29:6245-6256(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SPERMATOGENESIS, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73963 mRNA. Translation: AAA40522.1.
L13968 expand/collapse EMBL AC list , L13969, L13965, L13966, L13967 Genomic DNA. Translation: AAA40477.1.
M74590 mRNA. Translation: AAA37521.1.
BC055899 mRNA. Translation: AAH55899.1.
CCDSCCDS26163.1.
PIRA48273.
RefSeqNP_033563.2. NM_009537.3.
UniGeneMm.3868.
Mm.458511.

3D structure databases

ProteinModelPortalQ00899.
SMRQ00899. Positions 295-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204624. 12 interactions.
DIPDIP-59285N.
IntActQ00899. 5 interactions.
MINTMINT-4138987.
STRING10090.ENSMUSP00000021692.

PTM databases

PhosphoSiteQ00899.

Proteomic databases

MaxQBQ00899.
PaxDbQ00899.
PRIDEQ00899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021692; ENSMUSP00000021692; ENSMUSG00000021264.
GeneID22632.
KEGGmmu:22632.
UCSCuc007pac.1. mouse.

Organism-specific databases

CTD7528.
MGIMGI:99150. Yy1.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00730000110826.
HOGENOMHOG000008232.
HOVERGENHBG006823.
InParanoidQ00899.
KOK09201.
OMADIDHESV.
OrthoDBEOG769ZJD.
PhylomeDBQ00899.
TreeFamTF106493.

Gene expression databases

BgeeQ00899.
CleanExMM_YY1.
GenevestigatorQ00899.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR017114. TF_Yin_yang.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PIRSFPIRSF037113. TF_Yin_yang. 1 hit.
SMARTSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSYY1. mouse.
NextBio303007.
PROQ00899.
SOURCESearch...

Entry information

Entry nameTYY1_MOUSE
AccessionPrimary (citable) accession number: Q00899
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot