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Reviewed, UniProtKB/Swiss-Prot P25490 (TYY1_HUMAN)

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

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RybpQ8CCI52EBI-765538,EBI-929290From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Transcriptional repressor protein YY1
PRO_0000047190

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
Region333 – 37139Involved in repression of activated transcription
Region371 – 39727Involved in masking transactivation domain
Compositional bias43 – 5311Asp/Glu-rich (acidic)
Compositional bias54 – 6916Gly-rich
Compositional bias70 – 8011Poly-His
Compositional bias159 – 17012Gly/Ser-rich

Amino acid modifications

Modified residue1181Phosphoserine Ref.8
Modified residue1841Phosphoserine Ref.11
Modified residue2471Phosphoserine Ref.8 Ref.7 Ref.12 Ref.13
Modified residue3481Phosphothreonine Ref.13 Ref.9
Modified residue3781Phosphothreonine Ref.13

Experimental info

Sequence conflict651H → R in AAA59926. Ref.2
Sequence conflict1961G → R in AAA59467. Ref.1

Secondary structure

.................. 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25490-1 [UniParc].

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

FASTA41444,713
        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 

« Hide

References

« Hide '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.

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.
IPIIPI00014513.
PIRA40350.
RefSeqNP_003394.1.
UniGeneHs.388927

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1UBDX-ray2.50C293-414[»]
1ZNMNMR-A352-379[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:150N.
DIP:28144N.
IntActP25490. 2 interactions.

PTM databases

PhosphoSiteP25490.

Proteomic databases

PeptideAtlasP25490.
PRIDEP25490.

Genome annotation databases

EnsemblENSG00000100811. Homo sapiens. [Contig view]
GeneID7528.
KEGGhsa:7528.

Organism-specific databases

GeneCardsGC14P099774.
H-InvDBHIX0026638.
HGNCHGNC:12856. YY1.
HPACAB009392.
HPA001119.
MIM600013. gene.
PharmGKBPA37445.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP25490.
HOVERGENP25490.
OMAP25490. PLVTDDP.

Enzyme and pathway databases

Pathway_Interaction_DBhdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpressP25490.
BgeeP25490.
CleanExHS_YY1.
GermOnlineENSG00000100811. Homo sapiens.

Family and domain databases

InterProIPR017114. TF_Yin_yang.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 3 hits.
PfamPF00096. zf-C2H2. 4 hits.
[Graphical view]
PIRSFPIRSF037113. TF_Yin_yang. 1 hit.
ProDomPD000003. Znf_C2H2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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 Resources

NextBio29449.
PMAP-CutDBP25490.
SOURCESearch...

Entry information

Entry nameTYY1_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents