Transcriptional repressor protein YY1

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Q00899 (TYY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subcellular location	Nucleus matrix. Note: Associated with the nuclear matrix. In testis, localized to heterochromatin of spermatocytes. Ref.7
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.
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 process	DNA damage DNA recombination DNA repair Differentiation Spermatogenesis Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Repressor
PTM	ADP-ribosylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA 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 UV Inferred from electronic annotation. Source: Compara chromosome organization Inferred from mutant phenotype Ref.5. Source: UniProtKB double-strand break repair via homologous recombination Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from mutant phenotype Ref.5. Source: UniProtKB response to UV-C Inferred from mutant phenotype Ref.5. Source: UniProtKB response to prostaglandin F stimulus Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular_component	Ino80 complex Inferred from electronic annotation. Source: Compara PcG protein complex Inferred from direct assay PubMed 16624538. Source: MGI nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara transcription factor complex Inferred from direct assay PubMed 11861914. Source: MGI
Molecular_function	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: Compara transcription regulatory region DNA binding Inferred from sequence orthology PubMed 9857059. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 414

414

Transcriptional repressor protein YY1

PRO_0000047191

Regions

Zinc finger

296 – 320

C2H2-type 1

Zinc finger

325 – 347

C2H2-type 2

Zinc finger

353 – 377

C2H2-type 3

Zinc finger

383 – 407

C2H2-type 4

Region

257 – 341

Involved in nuclear matrix association By similarity

Region

333 – 371

Involved in repression of activated transcription By similarity

Region

371 – 397

Involved in masking transactivation domain By similarity

Compositional bias

43 – 53

Asp/Glu-rich (acidic)

Compositional bias

54 – 70

Gly-rich

Compositional bias

71 – 82

Poly-His

Compositional bias

161 – 170

Gly/Ser-rich

Sites

Metal binding

298

Zinc 1 By similarity

Metal binding

303

Zinc 1 By similarity

Metal binding

316

Zinc 1 By similarity

Metal binding

320

Zinc 1 By similarity

Metal binding

327

Zinc 2 By similarity

Metal binding

330

Zinc 2 By similarity

Metal binding

343

Zinc 2 By similarity

Metal binding

347

Zinc 2 By similarity

Metal binding

355

Zinc 3 By similarity

Metal binding

360

Zinc 3 By similarity

Metal binding

373

Zinc 3 By similarity

Metal binding

377

Zinc 3 By similarity

Metal binding

385

Zinc 4 By similarity

Metal binding

390

Zinc 4 By similarity

Metal binding

403

Zinc 4 By similarity

Metal binding

407

Zinc 4 By similarity

Amino acid modifications

Modified residue

120

Phosphoserine By similarity

Modified residue

247

Phosphoserine Ref.6

Modified residue

378

Phosphothreonine By similarity

Experimental info

Sequence conflict

219

F → S in AAA37521. Ref.3

Sequence conflict

375

R → G in AAA37521. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q00899 [UniParc].

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

414

44,717

        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' referencesShow '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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY. Tissue: Melanoma.
[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 , L13969, L13965, L13966, L13967 Genomic DNA. Translation: AAA40477.1. M74590 mRNA. Translation: AAA37521.1. BC055899 mRNA. Translation: AAH55899.1.
IPI	IPI00311892.
PIR	A48273.
RefSeq	NP_033563.2. NM_009537.3.
UniGene	Mm.3868. Mm.458511.
3D structure databases
ProteinModelPortal	Q00899.
SMR	Q00899. Positions 295-408.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59285N.
STRING	10090.ENSMUSP00000021692.
PTM databases
PhosphoSite	Q00899.
Proteomic databases
PaxDb	Q00899.
PRIDE	Q00899.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021692; ENSMUSP00000021692; ENSMUSG00000021264.
GeneID	22632.
KEGG	mmu:22632.
UCSC	uc007pac.1. mouse.
Organism-specific databases
CTD	7528.
MGI	MGI:99150. Yy1.
Phylogenomic databases
eggNOG	COG5048.
GeneTree	ENSGT00660000095182.
HOGENOM	HOG000008232.
HOVERGEN	HBG006823.
InParanoid	Q00899.
KO	K09201.
OMA	DIDHESV.
OrthoDB	EOG4D26QN.
Gene expression databases
Bgee	Q00899.
CleanEx	MM_YY1.
Genevestigator	Q00899.
GermOnline	ENSMUSG00000021264. Mus musculus.
Family and domain databases
Gene3D	3.30.160.60. 4 hits.
InterPro	IPR017114. TF_Yin_yang. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
PIRSF	PIRSF037113. TF_Yin_yang. 1 hit.
SMART	SM00355. ZnF_C2H2. 4 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 4 hits. PS50157. ZINC_FINGER_C2H2_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	YY1. mouse.
NextBio	303007.
SOURCE	Search...

Entry information

Entry name

TYY1_MOUSE

Accession

Primary (citable) accession number: Q00899

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents