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P38806 (YNG2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromatin modification-related protein YNG2
Alternative name(s):
ESA1-associated factor 4
ING1 homolog 2
Gene names
Name:YNG2
Synonyms:EAF4, NBN1
Ordered Locus Names:YHR090C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis. Ref.3 Ref.4 Ref.5 Ref.6

Subunit structure

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2. Ref.3 Ref.5 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus Ref.3 Ref.4 Ref.7.

Domain

The PHD-type zinc finger mediates the binding to H3K4me3. Ref.11

Sequence similarities

Belongs to the ING family.

Contains 1 PHD-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EPL1P435724EBI-24622,EBI-22792

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Chromatin modification-related protein YNG2
PRO_0000212679

Regions

Zinc finger222 – 27150PHD-type
Coiled coil35 – 8652 Potential

Sites

Binding site2241Histone H3K4me3 By similarity
Binding site2351Histone H3K4me3 By similarity
Binding site2391Histone H3K4me3 By similarity
Binding site2471Histone H3K4me3 By similarity

Amino acid modifications

Modified residue1831Phosphoserine Ref.13
Modified residue1851Phosphothreonine Ref.13
Modified residue1881Phosphoserine Ref.13

Sequences

Sequence LengthMass (Da)Tools
P38806 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 110E0A2536547D03

FASTA28232,086
        10         20         30         40         50         60 
MDPSLVLEQT IQDVSNLPSE FRYLLEEIGS NDLKLIEEKK KYEQKESQIH KFIRQQGSIP 

        70         80         90        100        110        120 
KHPQEDGLDK EIKESLLKCQ SLQREKCVLA NTALFLIARH LNKLEKNIAL LEEDGVLAPV 

       130        140        150        160        170        180 
EEDGDMDSAA EASRESSVVS NSSVKKRRAA SSSGSVPPTL KKKKTSRTSK LQNEIDVSSR 

       190        200        210        220        230        240 
EKSVTPVSPS IEKKIARTKE FKNSRNGKGQ NGSPENEEED KTLYCFCQRV SFGEMVACDG 

       250        260        270        280 
PNCKYEWFHY DCVNLKEPPK GTWYCPECKI EMEKNKLKRK RN 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities."
Loewith R., Meijer M., Lees-Miller S.P., Riabowol K., Young D.
Mol. Cell. Biol. 20:3807-3816(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NUA4 COMPLEX.
[4]"Yng2p-dependent NuA4 histone H4 acetylation activity is required for mitotic and meiotic progression."
Choy J.S., Tobe B.T.D., Huh J.H., Kron S.J.
J. Biol. Chem. 276:43653-43662(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]"Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex."
Nourani A., Doyon Y., Utley R.T., Allard S., Lane W.S., Cote J.
Mol. Cell. Biol. 21:7629-7640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-34; 62-70; 107-161; 171-180 AND 184-193, IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION.
[6]"NuA4 subunit Yng2 function in intra-S-phase DNA damage response."
Choy J.S., Kron S.J.
Mol. Cell. Biol. 22:8215-8225(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres."
Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.
Mol. Cell. Biol. 24:9424-9436(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.
PLoS Biol. 2:587-599(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4."
Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F.
Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression."
Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y. expand/collapse author list , Cote J., Chua K.F., Gozani O.
Nature 442:96-99(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
[12]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; THR-185 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00060 Genomic DNA. Translation: AAB68930.1.
BK006934 Genomic DNA. Translation: DAA06786.1.
PIRS46722.
RefSeqNP_011958.1. NM_001179220.1.

3D structure databases

ProteinModelPortalP38806.
SMRP38806. Positions 223-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36525. 284 interactions.
DIPDIP-2095N.
IntActP38806. 18 interactions.
MINTMINT-561028.
STRING4932.YHR090C.

Proteomic databases

PaxDbP38806.
PeptideAtlasP38806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR090C; YHR090C; YHR090C.
GeneID856490.
KEGGsce:YHR090C.

Organism-specific databases

CYGDYHR090c.
SGDS000001132. YNG2.

Phylogenomic databases

eggNOGCOG5034.
GeneTreeENSGT00550000074538.
HOGENOMHOG000000883.
KOK11396.
OMATLTKHPK.
OrthoDBEOG7G1VHM.

Enzyme and pathway databases

BioCycYEAST:G3O-31137-MONOMER.

Gene expression databases

GenevestigatorP38806.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028651. ING_fam.
IPR024610. ING_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10333. PTHR10333. 1 hit.
PfamPF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982194.
PROP38806.

Entry information

Entry nameYNG2_YEAST
AccessionPrimary (citable) accession number: P38806
Secondary accession number(s): D3DL42
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families