P38806 (YNG2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Meiosis
Cellular component	Nucleus
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from direct assay PubMed 16135807. Source: SGD histone acetylation Inferred from direct assay PubMed 12782659. Source: SGD meiosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Piccolo NuA4 histone acetyltransferase complex Inferred from direct assay PubMed 12782659. Source: SGD
Molecular_function	methylated histone residue binding Inferred from direct assay Ref.11. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EPL1	P43572	4	EBI-24622,EBI-22792

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 282	282	Chromatin modification-related protein YNG2		PRO_0000212679
Regions
	Zinc finger	222 – 271	50	PHD-type
	Coiled coil	35 – 86	52	Potential
Sites
	Binding site	224	1	Histone H3K4me3 By similarity
	Binding site	235	1	Histone H3K4me3 By similarity
	Binding site	239	1	Histone H3K4me3 By similarity
	Binding site	247	1	Histone H3K4me3 By similarity
Amino acid modifications
	Modified residue	188	1	Phosphoserine Ref.12 Ref.13

Sequences

	Sequence		Length	Mass (Da)
	P38806 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 110E0A2536547D03	FASTA	282	32,086
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[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, 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, 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, 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. , 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]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY.
[13]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00060 Genomic DNA. Translation: AAB68930.1. BK006934 Genomic DNA. Translation: DAA06786.1.
PIR	S46722.
RefSeq	NP_011958.1. NM_001179220.1.
3D structure databases
ProteinModelPortal	P38806.
SMR	P38806. Positions 223-269.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2095N.
IntAct	P38806. 18 interactions.
MINT	MINT-561028.
STRING	4932.YHR090C.
Proteomic databases
PaxDb	P38806.
PeptideAtlas	P38806.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR090C; YHR090C; YHR090C.
GeneID	856490.
KEGG	sce:YHR090C.
Organism-specific databases
CYGD	YHR090c.
SGD	S000001132. YNG2.
Phylogenomic databases
eggNOG	COG5034.
GeneTree	ENSGT00700000105531.
HOGENOM	HOG000000883.
KO	K11396.
OMA	WSCVGIT.
OrthoDB	EOG4V9Z11.
Gene expression databases
Genevestigator	P38806.
GermOnline	YHR090C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	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]
Pfam	PF12998. ING. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00249. PHD. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982194.

Entry information

Entry name

YNG2_YEAST

Accession

Primary (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 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program