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Protein
Submitted name:

Protein Yy1

Gene

Yy1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • anterior/posterior pattern specification Source: Ensembl
  • camera-type eye morphogenesis Source: Ensembl
  • cellular response to DNA damage stimulus Source: Ensembl
  • cellular response to interleukin-1 Source: RGD
  • chromosome organization Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • regulation of transcription, DNA-templated Source: RGD
  • response to prostaglandin F Source: RGD
  • response to UV-C Source: Ensembl
  • RNA localization Source: Ensembl
  • spermatogenesis Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-5696394. DNA Damage Recognition in GG-NER.

Names & Taxonomyi

Protein namesi
Submitted name:
Protein Yy1Imported
Submitted name:
Transcription factor YY1Imported
Gene namesi
Name:Yy1Imported
Synonyms:yy1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi3982. Yy1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • nuclear matrix Source: RGD
  • nucleus Source: RGD
  • PcG protein complex Source: Ensembl
  • transcription factor complex Source: RGD
Complete GO annotation...

Interactioni

GO - Molecular functioni

  • histone deacetylase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini293 – 31725C2H2-typeInterPro annotationAdd
BLAST
Domaini322 – 34928C2H2-typeInterPro annotationAdd
BLAST
Domaini350 – 37930C2H2-typeInterPro annotationAdd
BLAST
Domaini380 – 40930C2H2-typeInterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000008232.
HOVERGENiHBG006823.
KOiK09201.
OMAiGGRKWEQ.
OrthoDBiEOG769ZJD.
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.

Q8CHJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEDDDED
60 70 80 90 100
DEDGGGGDHG GGGGHGHAGH HHHHHHHHHP PMIALQPLVT DDPTQVHHHQ
110 120 130 140 150
EVILVQTREE VVGGDDSDGL RAEDGFEDQI LIPVPAPAGG DDDYIEQTLV
160 170 180 190 200
TVAAAGKSGG GSSSGGGRVK KGGGKKSGKK SYLGSGAGAA GGGGADPGNK
210 220 230 240 250
KWEQKQVQIK TLEGEFSVTM WSSDEKKDID HETVVEEQII GENSPPDYSE
260 270 280 290 300
YMTGKKLPPG GIPGIDLSDP KQLAEFARMK PRKIKEDDAP RTIACPHKGC
310 320 330 340 350
TKMFRDNSAM RKHLHTHGPR VHVCAECGKA FVESSKLKRH QLVHTGEKPF
360 370 380 390 400
QCTFEGCGKR FSLDFNLRTH VRIHTGDRPY VCPFDGCNKK FAQSTNLKSH
410
ILTHAKAKNN Q
Length:411
Mass (Da):44,417
Last modified:March 1, 2003 - v1
Checksum:i09EDA4A54449FF8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07065506 Genomic DNA. No translation available.
AY442180 Genomic DNA. Translation: AAR14688.1.
AB080317 mRNA. Translation: BAC53761.1.
RefSeqiNP_775412.1. NM_173290.1.
UniGeneiRn.162877.

Genome annotation databases

EnsembliENSRNOT00000005743; ENSRNOP00000005743; ENSRNOG00000004339.
GeneIDi24919.
KEGGirno:24919.
UCSCiRGD:3982. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07065506 Genomic DNA. No translation available.
AY442180 Genomic DNA. Translation: AAR14688.1.
AB080317 mRNA. Translation: BAC53761.1.
RefSeqiNP_775412.1. NM_173290.1.
UniGeneiRn.162877.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005743; ENSRNOP00000005743; ENSRNOG00000004339.
GeneIDi24919.
KEGGirno:24919.
UCSCiRGD:3982. rat.

Organism-specific databases

CTDi7528.
RGDi3982. Yy1.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000008232.
HOVERGENiHBG006823.
KOiK09201.
OMAiGGRKWEQ.
OrthoDBiEOG769ZJD.
TreeFamiTF106493.

Enzyme and pathway databases

ReactomeiR-RNO-5696394. DNA Damage Recognition in GG-NER.

Miscellaneous databases

NextBioi604859.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE.
  2. "Genetic variation in the multifunctional transcription factor Yy1 and type 1 diabetes mellitus in the BB rat."
    Kloting N., Kloting I.
    Mol. Genet. Metab. 82:255-259(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BB/OKImported.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ8CHJ4_RAT
AccessioniPrimary (citable) accession number: Q8CHJ4
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.