Q9H160 (ING2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of growth protein 2

Alternative name(s):
Inhibitor of growth 1-like protein
Short name=ING1Lp
p32
p33ING2

Gene names

Name:	ING2
Synonyms:	ING1L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs). Ref.2 Ref.6
Subunit structure	Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2. Ref.5 Ref.8 Ref.9
Subcellular location	Nucleus. Note: Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns5P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm. Ref.6
Tissue specificity	Widely expressed. Higher expressed in colon-cancer tumor than in normal colon tissues. Ref.1
Induction	Induced by the DNA-damaging agents etoposide and neocarzinostatin. Ref.2
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Ref.9 The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P). Ref.9
Sequence similarities	Belongs to the ING family. Contains 1 PHD-type zinc finger.

Ontologies

Keywords
Biological process	Growth regulation Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL male germ-line stem cell division Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL male meiosis I Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL negative regulation of apoptotic process Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18334480. Source: UniProtKB positive regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay PubMed 18334480. Source: UniProtKB regulation of cellular senescence Non-traceable author statement PubMed 21124965. Source: BHF-UCL regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of response to DNA damage stimulus Non-traceable author statement PubMed 21124965. Source: BHF-UCL seminiferous tubule development Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL signal transduction Traceable author statement Ref.1. Source: ProtInc sperm motility Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL spermatid development Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CCAAT-binding factor complex Inferred from direct assay PubMed 15243141. Source: UniProtKB Sin3 complex Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay PubMed 15243141. Source: UniProtKB chromatin binding Traceable author statement Ref.1. Source: ProtInc methylated histone residue binding Inferred from direct assay Ref.9. Source: UniProtKB phosphatidylinositol binding Inferred from direct assay Ref.7. Source: UniProtKB protein complex binding Inferred from direct assay PubMed 18334480. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 280	280	Inhibitor of growth protein 2		PRO_0000212663
Regions
	Zinc finger	212 – 261	50	PHD-type
	Region	264 – 280	17	PBR
	Coiled coil	48 – 120	73	Potential
Sites
	Binding site	214	1	Histone H3K4me3 By similarity
	Binding site	225	1	Histone H3K4me3 By similarity
	Binding site	229	1	Histone H3K4me3 By similarity
	Binding site	237	1	Histone H3K4me3 By similarity
Experimental info
	Sequence conflict	21	1	S → T in CAC20567. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9H160 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: DC85A6ECAF7A5D81	FASTA	280	32,808
	10 20 30 40 50 60 MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR ELDNKYQETL 70 80 90 100 110 120 KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK IQIVTQMLEL VENRARQMEL 130 140 150 160 170 180 HSQCFQDPAE SERASDKAKM DSSQPERSSR RPRRQRTSES RDLCHMANGI EDCDDQPPKE 190 200 210 220 230 240 KKSKSAKKKK RSKAKQEREA SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF 250 260 270 280 SCVSLTYKPK GKWYCPKCRG DNEKTMDKST EKTKKDRRSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor." Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M. Cytogenet. Cell Genet. 83:232-235(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[2]	"DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53." Nagashima M., Shiseki M., Miura K., Hagiwara K., Linke S.P., Pedeux R., Wang X.W., Yokota J., Riabowol K., Harris C.C. Proc. Natl. Acad. Sci. U.S.A. 98:9671-9676(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
[3]	"ING2, a new possible gene suppressor tumor." Cal S., Freije J.M., Lopez-Otin C. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary tumor.
[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: Lung.
[5]	"Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)." Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D. Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-44, IDENTIFICATION IN MSIN3A-LIKE COMPLEX, MASS SPECTROMETRY.
[6]	"The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor." Gozani O., Karuman P., Jones D.R., Ivanov D., Cha J., Lugovskoy A.A., Baird C.L., Zhu H., Field S.J., Lessnick S.L., Villasenor J., Mehrotra B., Chen J., Rao V.R., Brugge J.S., Ferguson C.G., Payrastre B., Myszka D.G. , Cantley L.C., Wagner G., Divecha N., Prestwich G.D., Yuan J. Cell 114:99-111(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"The polybasic region that follows the plant homeodomain zinc finger 1 of Pf1 is necessary and sufficient for specific phosphoinositide binding." Kaadige M.R., Ayer D.E. J. Biol. Chem. 281:28831-28836(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHOINOSITIDE-BINDING.
[8]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN MSIN3A COMPLEX.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012853 mRNA. Translation: BAA36419.1. AF053537 mRNA. Translation: AAG11395.1. AF062748, AF062747 Genomic DNA. Translation: AAG11396.1. AJ006851 mRNA. Translation: CAC20567.1. BC030128 mRNA. Translation: AAH30128.1.
IPI	IPI00016930.
RefSeq	NP_001555.1. NM_001564.2.
UniGene	Hs.107153.
3D structure databases
ProteinModelPortal	Q9H160.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H160. 2 interactions.
MINT	MINT-2830779.
STRING	9606.ENSP00000307183.
PTM databases
PhosphoSite	Q9H160.
Polymorphism databases
DMDM	59798471.
Proteomic databases
PaxDb	Q9H160.
PRIDE	Q9H160.
Protocols and materials databases
DNASU	3622.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302327; ENSP00000307183; ENSG00000168556.
GeneID	3622.
KEGG	hsa:3622.
UCSC	uc003ivs.1. human.
Organism-specific databases
CTD	3622.
GeneCards	GC04P184426.
HGNC	HGNC:6063. ING2.
HPA	HPA019486. HPA021517.
MIM	604215. gene.
neXtProt	NX_Q9H160.
PharmGKB	PA29873.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5034.
HOGENOM	HOG000239724.
HOVERGEN	HBG006607.
InParanoid	Q9H160.
OMA	KEDDSNQ.
OrthoDB	EOG42RD87.
PhylomeDB	Q9H160.
Gene expression databases
ArrayExpress	Q9H160.
Bgee	Q9H160.
CleanEx	HS_ING2.
Genevestigator	Q9H160.
GermOnline	ENSG00000168556. Homo sapiens.
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
GenomeRNAi	3622.
NextBio	14173.
SOURCE	Search...

Entry information

Entry name

ING2_HUMAN

Accession

Primary (citable) accession number: Q9H160
Secondary accession number(s): O95698

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.