Transcriptional repressor protein YY1

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Reviewed, UniProtKB/Swiss-Prot P25490 (TYY1_HUMAN)

Last modified June 16, 2009. Version 110. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Transcriptional repressor protein YY1
Alternative name(s):
    Yin and yang 1
      Short name=YY-1
    Delta transcription factor
    NF-E1
    INO80 complex subunit S

Gene names

Name:	YY1
Synonyms:	INO80S

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. May play an important role in development and differentiation. The function of YY1 as an activator or a repressor is specified by the presence of other proteins. For example it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence.
Subunit structure	Interacts with YAF2 through the region encompassing the first and second zinc fingers. Interacts with INO80. Ref.6 Ref.10
Subcellular location	Nucleus matrix. Note: Associated with the nuclear matrix. Ref.5
Sequence similarities	Belongs to the YY transcription factor family. Contains 4 C2H2-type zinc fingers.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Molecular function	transcription coactivator activity Ref.2 Traceable author statement. Source: ProtInc transcription corepressor activity Ref.1 Traceable author statement. Source: ProtInc transcription factor activity Ref.2 Traceable author statement. Source: ProtInc zinc ion binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rybp	Q8CCI5	2	EBI-765538,EBI-929290	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 414

414

Transcriptional repressor protein YY1

PRO_0000047190

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

Region

333 – 371

Involved in repression of activated transcription

Region

371 – 397

Involved in masking transactivation domain

Compositional bias

43 – 53

Asp/Glu-rich (acidic)

Compositional bias

54 – 69

Gly-rich

Compositional bias

70 – 80

Poly-His

Compositional bias

159 – 170

Gly/Ser-rich

Amino acid modifications

Modified residue

118

Phosphoserine Ref.8

Modified residue

184

Phosphoserine Ref.11

Modified residue

247

Phosphoserine Ref.8 Ref.7 Ref.12 Ref.13

Modified residue

348

Phosphothreonine Ref.13 Ref.9

Modified residue

378

Phosphothreonine Ref.13

Experimental info

Sequence conflict

H → R in AAA59926. Ref.2

Sequence conflict

196

G → R in AAA59467. Ref.1

Secondary structure

414

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P25490-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 058C05A0AD2D04E6
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FASTA

414

44,713

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

        70         80         90        100        110        120 
GGGGHGHAGH HHHHHHHHHH PPMIALQPLV TDDPTQVHHH QEVILVQTRE EVVGGDDSDG 

       130        140        150        160        170        180 
LRAEDGFEDQ ILIPVPAPAG GDDDYIEQTL VTVAAAGKSG GGGSSSSGGG RVKKGGGKKS 

       190        200        210        220        230        240 
GKKSYLSGGA 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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional repression by YY1, a human GLI-Kruppel-related protein, and relief of repression by adenovirus E1A protein." Shi Y., Seto E., Chang L.-S., Shenk T. Cell 67:377-388(1991) [PubMed: 1655281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Isolation of a candidate repressor/activator, NF-E1 (YY-1, delta), that binds to the immunoglobulin kappa 3' enhancer and the immunoglobulin heavy-chain mu E1 site." Park K., Atchison M. Proc. Natl. Acad. Sci. U.S.A. 88:9804-9808(1991) [PubMed: 1946405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Foreskin.
[3]	Whitson R.H., Huang T., Dang J., Itakura K. Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lymph.
[5]	"Targeting of the YY1 transcription factor to the nucleolus and the nuclear matrix in situ: the C-terminus is a principal determinant for nuclear trafficking." McNeil S., Guo B., Stein J.L., Lian J.B., Bushmeyer S., Seto E., Atchison M.L., Penman S., van Wijnen A.J., Stein G.S. J. Cell. Biochem. 68:500-510(1998) [PubMed: 9493912] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1." Kalenik J.L., Chen D., Bradley M.E., Chen S.-J., Lee T.-C. Nucleic Acids Res. 25:843-849(1997) [PubMed: 9016636] [Abstract] Cited for: INTERACTION WITH YAF2.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-247, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"YY1 functions with INO80 to activate transcription." Cai Y., Jin J., Yao T., Gottschalk A.J., Swanson S.K., Wu S., Shi Y., Washburn M.P., Florens L., Conaway R.C., Conaway J.W. Nat. Struct. Mol. Biol. 14:872-874(2007) [PubMed: 17721549] [Abstract] Cited for: INTERACTION WITH INO80.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, MASS SPECTROMETRY.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; THR-348 AND THR-378, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Cocrystal structure of YY1 bound to the adeno-associated virus P5 initiator." Houbaviy H.B., Usheva A., Shenk T., Burley S.K. Proc. Natl. Acad. Sci. U.S.A. 93:13577-13582(1996) [PubMed: 8942976] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 304-414.
[16]	"Design, synthesis and structure of a zinc finger with an artificial beta-turn." Viles J.H., Patel S.U., Mitchell J.B.O., Moody C.M., Justice D.E., Uppenbrink J., Doyle P.M., Harris C.J., Sadler P.J., Thornton J.M. J. Mol. Biol. 279:973-986(1998) [PubMed: 9642075] [Abstract] Cited for: STRUCTURE BY NMR OF 353-379.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

IPI

IPI00014513.

PIR

A40350.

RefSeq

NP_003394.1.

UniGene

Hs.388927

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UBD	X-ray	2.50	C	293-414	[»]
1ZNM	NMR	-	A	352-379	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:150N.
DIP:28144N.

IntAct

P25490. 2 interactions.

PTM databases

PhosphoSite

P25490.

Proteomic databases

PeptideAtlas

P25490.

PRIDE

P25490.

Genome annotation databases

Ensembl

ENSG00000100811. Homo sapiens. [Contig view]

GeneID

7528.

KEGG

hsa:7528.

Organism-specific databases

GeneCards

GC14P099774.

H-InvDB

HIX0026638.

HGNC

HGNC:12856. YY1.

HPA

CAB009392.
HPA001119.

MIM

600013. gene.

PharmGKB

PA37445.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P25490.

HOVERGEN

P25490.

OMA

P25490. PLVTDDP.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpress

P25490.

Bgee

P25490.

CleanEx

HS_YY1.

GermOnline

ENSG00000100811. Homo sapiens.

Family and domain databases

InterPro

IPR017114. TF_Yin_yang.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 3 hits.

Pfam

PF00096. zf-C2H2. 4 hits.
[Graphical view]

PIRSF

PIRSF037113. TF_Yin_yang. 1 hit.

ProDom

PD000003. Znf_C2H2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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 Resources

NextBio

29449.

PMAP-CutDB

P25490.

SOURCE

Search...

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Entry information

Entry name

TYY1_HUMAN

Accession

Primary (citable) accession number: P25490
Secondary accession number(s): Q14935

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 15, 1998
Last modified:	June 16, 2009
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents