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P25490

- TYY1_HUMAN

UniProt

P25490 - TYY1_HUMAN

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Protein

Transcriptional repressor protein YY1

Gene

YY1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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).1 Publication
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi298 – 2981Zinc 1
Metal bindingi303 – 3031Zinc 1
Metal bindingi316 – 3161Zinc 1
Metal bindingi320 – 3201Zinc 1
Metal bindingi327 – 3271Zinc 2
Metal bindingi330 – 3301Zinc 2
Metal bindingi343 – 3431Zinc 2
Metal bindingi347 – 3471Zinc 2
Metal bindingi355 – 3551Zinc 3
Metal bindingi360 – 3601Zinc 3
Metal bindingi373 – 3731Zinc 3
Metal bindingi377 – 3771Zinc 3
Metal bindingi385 – 3851Zinc 4
Metal bindingi390 – 3901Zinc 4
Metal bindingi403 – 4031Zinc 4
Metal bindingi407 – 4071Zinc 4

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri296 – 32025C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri325 – 34723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri353 – 37725C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri383 – 40725C2H2-type 4PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. four-way junction DNA binding Source: UniProtKB
  3. RNA binding Source: MGI
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. transcription coactivator activity Source: ProtInc
  7. transcription corepressor activity Source: ProtInc
  8. transcription regulatory region DNA binding Source: MGI
  9. zinc ion binding Source: ProtInc

GO - Biological processi

  1. anterior/posterior pattern specification Source: Ensembl
  2. camera-type eye morphogenesis Source: Ensembl
  3. cell differentiation Source: UniProtKB-KW
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. cellular response to UV Source: UniProtKB
  6. chromosome organization Source: Ensembl
  7. double-strand break repair via homologous recombination Source: UniProtKB
  8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  9. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  10. response to prostaglandin F Source: Ensembl
  11. response to UV-C Source: UniProtKB
  12. RNA localization Source: Ensembl
  13. spermatogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Differentiation, DNA damage, DNA recombination, DNA repair, Spermatogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiP25490.

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:12856. YY1.

Subcellular locationi

Nucleus matrix 3 Publications
Note: Associated with the nuclear matrix.

GO - Cellular componenti

  1. Ino80 complex Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. PcG protein complex Source: Ensembl
  4. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Transcriptional repressor protein YY1PRO_0000047190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181Phosphoserine3 Publications
Modified residuei247 – 2471Phosphoserine3 Publications
Modified residuei378 – 3781Phosphothreonine1 Publication

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, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25490.
PaxDbiP25490.
PeptideAtlasiP25490.
PRIDEiP25490.

PTM databases

PhosphoSiteiP25490.

Miscellaneous databases

PMAP-CutDBP25490.

Expressioni

Gene expression databases

BgeeiP25490.
CleanExiHS_YY1.
ExpressionAtlasiP25490. baseline and differential.
GenevestigatoriP25490.

Organism-specific databases

HPAiCAB009392.
HPA001119.

Interactioni

Subunit structurei

Found in a complex with SMAD1 and SMAD4. 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. Interacts with SFMBT2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032593EBI-765538,EBI-6947456From a different organism.
ACTL6AO960195EBI-765538,EBI-355018
ARRB1P494074EBI-765538,EBI-743313
E1AQ8JSK44EBI-765538,EBI-7453955From a different organism.
INO80Q9ULG15EBI-765538,EBI-769345
PRKDCP785272EBI-765538,EBI-352053
RUVBL1Q9Y2654EBI-765538,EBI-353675
RUVBL2Q9Y2305EBI-765538,EBI-352939
RybpQ8CCI52EBI-765538,EBI-929290From a different organism.

Protein-protein interaction databases

BioGridi113360. 122 interactions.
DIPiDIP-150N.
IntActiP25490. 41 interactions.
MINTiMINT-157439.
STRINGi9606.ENSP00000262238.

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi207 – 2115
Beta strandi220 – 2245
Beta strandi306 – 3094
Helixi310 – 3178
Helixi318 – 3203
Turni328 – 3303
Beta strandi333 – 3364
Helixi337 – 3437
Helixi344 – 3463
Turni358 – 3603
Beta strandi363 – 3653
Helixi367 – 37812
Turni397 – 4004
Helixi401 – 4077

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UBDX-ray2.50C291-414[»]
1ZNMNMR-A352-379[»]
4C5IX-ray2.59C199-228[»]
ProteinModelPortaliP25490.
SMRiP25490. Positions 295-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25490.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 170170Interaction with the SMAD1/SMAD4 complexAdd
BLAST
Regioni257 – 34185Involved in nuclear matrix associationAdd
BLAST
Regioni295 – 414120Binding to DNAAdd
BLAST
Regioni333 – 37139Involved in repression of activated transcriptionAdd
BLAST
Regioni371 – 39727Involved in masking transactivation domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 5311Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi54 – 6916Gly-richAdd
BLAST
Compositional biasi70 – 8011Poly-HisAdd
BLAST
Compositional biasi159 – 17012Gly/Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the YY transcription factor family.Curated
Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri296 – 32025C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri325 – 34723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri353 – 37725C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri383 – 40725C2H2-type 4PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000008232.
HOVERGENiHBG006823.
InParanoidiP25490.
KOiK09201.
OMAiDIDHESV.
PhylomeDBiP25490.
TreeFamiTF106493.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR017114. TF_Yin_yang.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
PIRSFiPIRSF037113. TF_Yin_yang. 1 hit.
SMARTiSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25490 [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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651H → R in AAA59926. (PubMed:1946405)Curated
Sequence conflicti196 – 1961G → R in AAA59467. (PubMed:1655281)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti380 – 3801D → Y De novo variant found in a patient with mental retardation. 1 Publication
VAR_065086

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.2. human.

Polymorphism databases

DMDMi3915889.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9957.1.
PIRi A40350.
RefSeqi NP_003394.1. NM_003403.4.
UniGenei Hs.388927.
Hs.603118.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UBD X-ray 2.50 C 291-414 [» ]
1ZNM NMR - A 352-379 [» ]
4C5I X-ray 2.59 C 199-228 [» ]
ProteinModelPortali P25490.
SMRi P25490. Positions 295-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113360. 122 interactions.
DIPi DIP-150N.
IntActi P25490. 41 interactions.
MINTi MINT-157439.
STRINGi 9606.ENSP00000262238.

PTM databases

PhosphoSitei P25490.

Polymorphism databases

DMDMi 3915889.

Proteomic databases

MaxQBi P25490.
PaxDbi P25490.
PeptideAtlasi P25490.
PRIDEi P25490.

Protocols and materials databases

DNASUi 7528.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262238 ; ENSP00000262238 ; ENSG00000100811 .
GeneIDi 7528.
KEGGi hsa:7528.
UCSCi uc001ygy.2. human.

Organism-specific databases

CTDi 7528.
GeneCardsi GC14P101221.
HGNCi HGNC:12856. YY1.
HPAi CAB009392.
HPA001119.
MIMi 600013. gene.
neXtProti NX_P25490.
PharmGKBi PA37445.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00760000118771.
HOGENOMi HOG000008232.
HOVERGENi HBG006823.
InParanoidi P25490.
KOi K09201.
OMAi DIDHESV.
PhylomeDBi P25490.
TreeFami TF106493.

Enzyme and pathway databases

SignaLinki P25490.

Miscellaneous databases

ChiTaRSi YY1. human.
EvolutionaryTracei P25490.
GeneWikii YY1.
GenomeRNAii 7528.
NextBioi 29449.
PMAP-CutDB P25490.
PROi P25490.
SOURCEi Search...

Gene expression databases

Bgeei P25490.
CleanExi HS_YY1.
ExpressionAtlasi P25490. baseline and differential.
Genevestigatori P25490.

Family and domain databases

Gene3Di 3.30.160.60. 4 hits.
InterProi IPR017114. TF_Yin_yang.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00096. zf-C2H2. 1 hit.
[Graphical view ]
PIRSFi PIRSF037113. TF_Yin_yang. 1 hit.
SMARTi SM00355. ZnF_C2H2. 4 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YAF2.
  7. "Poly(ADP-ribosyl)ation of transcription factor Yin Yang 1 under conditions of DNA damage."
    Oei S.L., Shi Y.
    Biochem. Biophys. Res. Commun. 285:27-31(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLY-ADP-RIBOSYLATION BY PARP1.
  8. "The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos."
    Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.
    Mol. Cell. Biol. 21:1360-1369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EZH2 AND EZH2.
  9. "SMAD-mediated modulation of YY1 activity regulates the BMP response and cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5 enhancer."
    Lee K.H., Evans S., Ruan T.Y., Lassar A.B.
    Development 131:4709-4723(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH SMAD1 AND SMAD4.
  10. "Transcription factor YY1: structure, function, and therapeutic implications in cancer biology."
    Gordon S., Akopyan G., Garban H., Bonavida B.
    Oncogene 25:1125-1142(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX.
  12. "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, SUBCELLULAR LOCATION, DNA-BINDING, PROTEIN INTERACTION, IDENTIFICATION IN THE INO80 COMPLEX.
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
    Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
    Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "YY1's longer DNA-binding motifs."
    Kim J., Kim J.
    Genomics 93:152-158(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING MOTIF.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
    Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
    PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
    Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Regulation of DU145 prostate cancer cell growth by Scm-like with four mbt domains 2."
    Lee K., Na W., Maeng J.H., Wu H., Ju B.G.
    J. Biosci. 38:105-112(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFMBT2, SUBCELLULAR LOCATION.
  24. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 304-414.
  25. Cited for: STRUCTURE BY NMR OF 353-379.
  26. Cited for: VARIANT TYR-380.

Entry informationi

Entry nameiTYY1_HUMAN
AccessioniPrimary (citable) accession number: P25490
Secondary accession number(s): Q14935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 1998
Last modified: October 29, 2014
This is version 170 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3