ID   ING2_MOUSE              Reviewed;         281 AA.
AC   Q9ESK4; Q80VI5; Q8BGU8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   25-JAN-2012, entry version 99.
DE   RecName: Full=Inhibitor of growth protein 2;
DE   AltName: Full=Inhibitor of growth 1-like protein;
DE   AltName: Full=p33ING2;
GN   Name=Ing2; Synonyms=Ing1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nagashima M., Hagiwara K., Hancock A.R., Harris C.C.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   STRUCTURE BY NMR OF 205-262.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of PHD domain of inhibitor of growth family,
RT   member 1-like.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Seems to be involved in p53/TP53 activation and
CC       p53/TP53-dependent apoptotic pathways, probably by enhancing
CC       acetylation of p53/TP53. Component of a mSin3A-like corepressor
CC       complex, which is probably involved in deacetylation of
CC       nucleosomal histones. ING2 activity seems to be modulated by
CC       binding to phosphoinositides (PtdInsPs) (By similarity).
CC   -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with
CC       H3K4me2 (By similarity). Component of a mSin3A-like complex at
CC       least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48,
CC       RBBP7/RbAp46, SAP30 and ING2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Predominantly
CC       cytoplasmic. Localized to chromatin and nuclear matrix. Upon
CC       reduced PtdIns(5)P levels seems to be released from chromatin and,
CC       at least partially, translocated to the cytoplasm (By similarity).
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3
CC       (By similarity).
CC   -!- DOMAIN: The polybasic region (PBR) is responsive to the binding to
CC       phosphoinositides (PtdInsPs), including phosphatidylinositol 5-
CC       phosphate (PtdIns(5)P) (By similarity).
CC   -!- SIMILARITY: Belongs to the ING family.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50003.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AF078834; AAG12173.1; -; mRNA.
DR   EMBL; AK048800; BAC33461.1; -; mRNA.
DR   EMBL; AK083144; BAC38783.1; -; mRNA.
DR   EMBL; BC050003; AAH50003.1; ALT_SEQ; mRNA.
DR   IPI; IPI00308151; -.
DR   RefSeq; NP_075992.2; NM_023503.3.
DR   UniGene; Mm.430733; -.
DR   PDB; 1WES; NMR; -; A=205-262.
DR   PDB; 2G6Q; X-ray; 2.00 A; A=205-264.
DR   PDBsum; 1WES; -.
DR   PDBsum; 2G6Q; -.
DR   ProteinModelPortal; Q9ESK4; -.
DR   SMR; Q9ESK4; 212-263.
DR   MINT; MINT-1340342; -.
DR   STRING; Q9ESK4; -.
DR   PRIDE; Q9ESK4; -.
DR   GeneID; 69260; -.
DR   KEGG; mmu:69260; -.
DR   CTD; 3622; -.
DR   MGI; MGI:1916510; Ing2.
DR   GeneTree; ENSGT00550000074538; -.
DR   HOGENOM; HBG716496; -.
DR   HOVERGEN; HBG006607; -.
DR   InParanoid; Q9ESK4; -.
DR   OrthoDB; EOG42RD87; -.
DR   NextBio; 328987; -.
DR   ArrayExpress; Q9ESK4; -.
DR   Bgee; Q9ESK4; -.
DR   CleanEx; MM_ING2; -.
DR   Genevestigator; Q9ESK4; -.
DR   GermOnline; ENSMUSG00000063049; Mus musculus.
DR   GO; GO:0016580; C:Sin3 complex; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IMP:BHF-UCL.
DR   GO; GO:0048133; P:male germ-line stem cell division; IMP:BHF-UCL.
DR   GO; GO:0007141; P:male meiosis I; IMP:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0072520; P:seminiferous tubule development; IMP:BHF-UCL.
DR   GO; GO:0030317; P:sperm motility; IMP:BHF-UCL.
DR   GO; GO:0007286; P:spermatid development; IMP:BHF-UCL.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR024610; ING_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF12998; ING; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Coiled coil; Complete proteome;
KW   Growth regulation; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    281       Inhibitor of growth protein 2.
FT                                /FTId=PRO_0000212664.
FT   ZN_FING     213    262       PHD-type.
FT   REGION      265    281       PBR (By similarity).
FT   COILED       49    101       Potential.
FT   BINDING     215    215       Histone H3K4me3 (By similarity).
FT   BINDING     226    226       Histone H3K4me3 (By similarity).
FT   BINDING     230    230       Histone H3K4me3 (By similarity).
FT   BINDING     238    238       Histone H3K4me3 (By similarity).
FT   CONFLICT     26     26       T -> S (in Ref. 2; BAC33461/BAC38783).
FT   CONFLICT     72     72       K -> E (in Ref. 1; AAG12173).
FT   CONFLICT    104    104       I -> N (in Ref. 1; AAG12173).
FT   CONFLICT    110    110       E -> G (in Ref. 1; AAG12173).
FT   CONFLICT    116    116       A -> S (in Ref. 1; AAG12173).
FT   CONFLICT    203    203       P -> S (in Ref. 1; AAG12173).
FT   CONFLICT    250    250       P -> H (in Ref. 1; AAG12173).
FT   TURN        216    219
FT   STRAND      224    228
FT   STRAND      238    240
FT   HELIX       242    244
FT   HELIX       257    260
SQ   SEQUENCE   281 AA;  32992 MW;  CDC53B50492C2D8B CRC64;
     MLGQQQQQQL YSSAALLTGE RSRLLTCYVQ DYLECVESLP HDMQRNVSVL RELDNKYQET
     LKEIDDVYEK YKKEDDSNQK KRLQQHLQRA LINSQELGDE KIQIVTQMLE LVENRARQME
     LHSQCFQDPA ESERASDKSK MDSSQPERSS RRPRRQRTSE SRDLCHMTNG IDDCDDQPPK
     EKRSKSAKKK KRSKAKQERE ASPVEFAIDP NEPTYCLCNQ VSYGEMIGCD NEQCPIEWFH
     FSCVSLTYKP KGKWYCPKCR GDNEKTMDKS TEKTKKERRA R
//