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UniProtKB/Swiss-Prot entry Q9ESK4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ING2_MOUSE
Primary accession number Q9ESK4
Secondary accession numbers Q80VI5 Q8BGU8
Integrated into Swiss-Prot on February 15, 2005
Sequence was last modified on February 15, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 74)
Name and origin of the protein
Protein name Inhibitor of growth protein 2
Synonyms p33ING2
Inhibitor of growth 1-like protein
Gene name
Name: Ing2
Synonyms: Ing1l
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Nagashima M., Hagiwara K., Hancock A.R., Harris C.C.;
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, and Hippocampus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
STRUCTURE BY NMR OF 205-262.
RIKEN structural genomics initiative (RSGI);
"Solution structure of PHD domain of inhibitor of growth family, member 1-like.";
Submitted (NOV-2004) to the PDB data bank.
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: 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 PtdIns(5)P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm (By similarity).
  • DOMAIN: The PHD-type zinc finger domain binds to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns(5)P) (By similarity).
  • SIMILARITY: Belongs to the ING family.
  • SIMILARITY: Contains 1 PHD-type zinc finger.
  • SEQUENCE CAUTION:
    • Sequence=AAH50003.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF078834; AAG12173.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK048800; BAC33461.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK083144; BAC38783.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050003; AAH50003.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00308151; -.
RefSeq NP_075992.2; -.
UniGene Mm.430733
3D structure databases
PDB
1WES; NMR; -; A=205-262.[ExPASy / RCSB / EBI]
2G6Q; X-ray; 2.00 A; A=205-264.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WES; -.
2G6Q; -.
ModBase Q9ESK4.
Organism-specific databases
MGI MGI:1916510; Ing2.
Gene expression databases
ArrayExpress Q9ESK4; -.
Bgee Q9ESK4; -.
CleanEx MM_ING2; -.
GermOnline ENSMUSG00000063049; Mus musculus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0016563; Molecular function: transcription activator activity (inferred from direct assay from MGI).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016568; Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0045941; Biological process: positive regulation of transcription (inferred from direct assay from MGI).
GO:0040008; Biological process: regulation of growth (inferred from electronic annotation from UniProtKB-KW).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR019786; Zinc_finger_PHD-type_CS.
IPR001965; Znf_PHD.
IPR019787; Znf_PHD-finger.
Graphical view of domain structure.
Pfam PF00628; PHD; 1.
Pfam graphical view of domain structure.
SMART SM00249; PHD; 1.
SMART graphical view of domain structure.
PROSITE PS01359; ZF_PHD_1; 1.
PS50016; ZF_PHD_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSMUSG00000063049; Mus musculus. [Contig view]
GeneID 69260; -.
KEGG mmu:69260; -.
Phylogenomic databases
HOGENOM Q9ESK4; -.
HOVERGEN Q9ESK4; -.
Other
NextBio 328987; -.
SOURCE Ing2; Mus musculus.
ProtoNet Q9ESK4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chromatin regulator; Coiled coil; Growth regulation; Metal-binding; Nucleus; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   281  281     Inhibitor of growth protein 2. PRO_0000212664
ZN_FING   213   262  50     PHD-type. 
COILED   49   101  53     Potential. 
CONFLICT   26    26        T -> S (in Ref. 2; BAC33461/BAC38783). 
CONFLICT   72    72        K -> E (in Ref. 1; AAG12173). 
CONFLICT   104   104        I -> N (in Ref. 1; AAG12173). 
CONFLICT   110   110        E -> G (in Ref. 1; AAG12173). 
CONFLICT   116   116        A -> S (in Ref. 1; AAG12173). 
CONFLICT   203   203        P -> S (in Ref. 1; AAG12173). 
CONFLICT   250   250        P -> H (in Ref. 1; AAG12173). 
TURN   216   219  4      
STRAND   224   228  5      
STRAND   238   240  3      
HELIX   242   244  3      
HELIX   257   260  4      
Sequence information
Length: 281 AA [This is the length of the unprocessed precursor] Molecular weight: 32992 Da [This is the MW of the unprocessed precursor] CRC64: CDC53B50492C2D8B [This is a checksum on the sequence]
        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 

Q9ESK4 in FASTA format

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