Q9ESK4 (ING2_MOUSE) 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
p33ING2

Gene names

Name:	Ing2
Synonyms:	Ing1l

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	281 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) By similarity.
Subunit structure	Interacts with H3K4me3 and to a lesser extent with H3K4me2 By similarity. Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2 By similarity.
Subcellular location	Nucleus By similarity. Note: Predominantly cytoplasmic. Localized to chromatin and nuclear matrix. Upon reduced PtdIns5P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm By similarity.
Domain	The PHD-type zinc finger mediates the binding to H3K4me3 By similarity. The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P) By similarity.
Sequence similarities	Belongs to the ING family. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAH50003.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from mutant phenotype. Source: BHF-UCL male germ-line stem cell division Inferred from mutant phenotype. Source: BHF-UCL male meiosis I Inferred from mutant phenotype. Source: BHF-UCL negative regulation of apoptotic process Inferred from mutant phenotype. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: MGI regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW seminiferous tubule development Inferred from mutant phenotype. Source: BHF-UCL sperm motility Inferred from mutant phenotype. Source: BHF-UCL spermatid development Inferred from mutant phenotype. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Sin3 complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	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 – 281

281

Inhibitor of growth protein 2

PRO_0000212664

Regions

Zinc finger

213 – 262

50

PHD-type

Region

265 – 281

17

PBR By similarity

Coiled coil

49 – 101

53

Potential

Sites

Binding site

215

1

Histone H3K4me3 By similarity

Binding site

226

1

Histone H3K4me3 By similarity

Binding site

230

1

Histone H3K4me3 By similarity

Binding site

238

1

Histone H3K4me3 By similarity

Experimental info

Sequence conflict

26

1

T → S in BAC33461. Ref.2

Sequence conflict

26

1

T → S in BAC38783. Ref.2

Sequence conflict

72

1

K → E in AAG12173. Ref.1

Sequence conflict

104

1

I → N in AAG12173. Ref.1

Sequence conflict

110

1

E → G in AAG12173. Ref.1

Sequence conflict

116

1

A → S in AAG12173. Ref.1

Sequence conflict

203

1

P → S in AAG12173. Ref.1

Sequence conflict

250

1

P → H in AAG12173. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

281

Helix Strand Turn

Details...

Turn

216 – 219

4

Beta strand

224 – 228

5

Beta strand

238 – 240

3

Helix

242 – 244

3

Helix

257 – 260

4

Sequences

	Sequence		Length	Mass (Da)
	Q9ESK4 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: CDC53B50492C2D8B	FASTA	281	32,992
	10 20 30 40 50 60 MLGQQQQQQL YSSAALLTGE RSRLLTCYVQ DYLECVESLP HDMQRNVSVL RELDNKYQET 70 80 90 100 110 120 LKEIDDVYEK YKKEDDSNQK KRLQQHLQRA LINSQELGDE KIQIVTQMLE LVENRARQME 130 140 150 160 170 180 LHSQCFQDPA ESERASDKSK MDSSQPERSS RRPRRQRTSE SRDLCHMTNG IDDCDDQPPK 190 200 210 220 230 240 EKRSKSAKKK KRSKAKQERE ASPVEFAIDP NEPTYCLCNQ VSYGEMIGCD NEQCPIEWFH 250 260 270 280 FSCVSLTYKP KGKWYCPKCR GDNEKTMDKS TEKTKKERRA R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Nagashima M., Hagiwara K., Hancock A.R., Harris C.C. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum and Hippocampus.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Mammary gland.
[4]	"Solution structure of PHD domain of inhibitor of growth family, member 1-like." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 205-262.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF078834 mRNA. Translation: AAG12173.1.
AK048800 mRNA. Translation: BAC33461.1.
AK083144 mRNA. Translation: BAC38783.1.
BC050003 mRNA. Translation: AAH50003.1. Sequence problems.

IPI

IPI00308151.

RefSeq

NP_075992.2. NM_023503.3.

UniGene

Mm.430733.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WES	NMR	-	A	205-262	[»]
2G6Q	X-ray	2.00	A	205-264	[»]

ProteinModelPortal

Q9ESK4.

SMR

Q9ESK4. Positions 212-263.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1340342.

STRING

Q9ESK4.

Proteomic databases

PRIDE

Q9ESK4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

69260.

KEGG

mmu:69260.

Organism-specific databases

CTD

3622.

MGI

MGI:1916510. Ing2.

Phylogenomic databases

GeneTree

ENSGT00550000074538.

HOGENOM

HBG716496.

HOVERGEN

HBG006607.

InParanoid

Q9ESK4.

OrthoDB

EOG42RD87.

Gene expression databases

ArrayExpress

Q9ESK4.

Bgee

Q9ESK4.

CleanEx

MM_ING2.

Genevestigator

Q9ESK4.

GermOnline

ENSMUSG00000063049. Mus musculus.

Family and domain databases

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]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

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

328987.

SOURCE

Search...

Entry information

Entry name

ING2_MOUSE

Accession

Primary (citable) accession number: Q9ESK4
Secondary accession number(s): Q80VI5, Q8BGU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program