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Q9ESK4 (ING2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibitor of growth protein 2
Alternative name(s):
Inhibitor of growth 1-like protein
p33ING2
Gene names
Name:Ing2
Synonyms:Ing1l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Post-translational modification

Sumoylation enhances its association with SIN3A and is required for binding to some target gene promoters, this is the case for TMEM71 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 processGrowth regulation
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

male germ-line stem cell division

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

male meiosis I

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

negative regulation of apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21124965. Source: MGI

negative regulation of cell proliferation

Inferred from electronic annotation. Source: InterPro

positive regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16098148. Source: MGI

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

seminiferous tubule development

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

sperm motility

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

spermatid development

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

spermatogenesis

Inferred from mutant phenotype PubMed 21124965. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCCAAT-binding factor complex

Inferred from electronic annotation. Source: Ensembl

Sin3 complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Inhibitor of growth protein 2
PRO_0000212664

Regions

Zinc finger213 – 26250PHD-type
Region265 – 28117PBR By similarity
Coiled coil49 – 10153 Potential

Sites

Binding site2151Histone H3K4me3 By similarity
Binding site2261Histone H3K4me3 By similarity
Binding site2301Histone H3K4me3 By similarity
Binding site2381Histone H3K4me3 By similarity

Amino acid modifications

Cross-link196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) By similarity

Experimental info

Sequence conflict261S → T in AAG12173. Ref.1
Sequence conflict261S → T in AAH50003. Ref.5
Sequence conflict721K → E in AAG12173. Ref.1
Sequence conflict1041I → N in AAG12173. Ref.1
Sequence conflict1101E → G in AAG12173. Ref.1
Sequence conflict1161A → S in AAG12173. Ref.1
Sequence conflict2031P → S in AAG12173. Ref.1
Sequence conflict2501P → H in AAG12173. Ref.1

Secondary structure

............. 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ESK4 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 6D953B52822C2D8A

FASTA28132,978
        10         20         30         40         50         60 
MLGQQQQQQL YSSAALLTGE RSRLLSCYVQ 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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum and Hippocampus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Strain: FVB/N-3.
Tissue: Brain, Mammary gland and Olfactory epithelium.
[6]"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.
AC107236 Genomic DNA. No translation available.
CH466554 Genomic DNA. Translation: EDL35605.1.
BC096433 mRNA. Translation: AAH96433.1.
BC138229 mRNA. Translation: AAI38230.1.
BC050003 mRNA. Translation: AAH50003.1. Sequence problems.
CCDSCCDS22298.1.
RefSeqNP_075992.2. NM_023503.3.
UniGeneMm.430733.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WESNMR-A205-262[»]
2G6QX-ray2.00A205-264[»]
ProteinModelPortalQ9ESK4.
SMRQ9ESK4. Positions 32-120, 212-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213322. 3 interactions.
DIPDIP-38912N.
MINTMINT-1340342.
STRING10090.ENSMUSP00000079226.

PTM databases

PhosphoSiteQ9ESK4.

Proteomic databases

PRIDEQ9ESK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080353; ENSMUSP00000079226; ENSMUSG00000063049.
GeneID69260.
KEGGmmu:69260.
UCSCuc009lrf.2. mouse.
uc012gdo.1. mouse.

Organism-specific databases

CTD3622.
MGIMGI:1916510. Ing2.

Phylogenomic databases

eggNOGCOG5034.
GeneTreeENSGT00550000074538.
HOGENOMHOG000239724.
HOVERGENHBG006607.
InParanoidQ9ESK4.
OMALCHMTNG.
OrthoDBEOG7RBZ9T.
TreeFamTF352014.

Gene expression databases

ArrayExpressQ9ESK4.
CleanExMM_ING2.
GenevestigatorQ9ESK4.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028639. ING2.
IPR028651. 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.
PTHR10333:SF37. PTHR10333:SF37. 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

EvolutionaryTraceQ9ESK4.
NextBio328987.
PROQ9ESK4.
SOURCESearch...

Entry information

Entry nameING2_MOUSE
AccessionPrimary (citable) accession number: Q9ESK4
Secondary accession number(s): Q4VAD7, Q80VI5, Q8BGU8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot