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Q9ESK4

- ING2_MOUSE

UniProt

Q9ESK4 - ING2_MOUSE

Protein

Inhibitor of growth protein 2

Gene

Ing2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei215 – 2151Histone H3K4me3By similarity
    Binding sitei226 – 2261Histone H3K4me3By similarity
    Binding sitei230 – 2301Histone H3K4me3By similarity
    Binding sitei238 – 2381Histone H3K4me3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri213 – 26250PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. DNA binding Source: Ensembl
    3. phosphatidylinositol binding Source: Ensembl
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: BHF-UCL
    2. male germ-line stem cell asymmetric division Source: BHF-UCL
    3. male meiosis I Source: BHF-UCL
    4. negative regulation of apoptotic signaling pathway Source: MGI
    5. negative regulation of cell proliferation Source: InterPro
    6. positive regulation of apoptotic process Source: InterPro
    7. positive regulation of transcription, DNA-templated Source: MGI
    8. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    9. regulation of growth Source: UniProtKB-KW
    10. seminiferous tubule development Source: BHF-UCL
    11. spermatid development Source: BHF-UCL
    12. spermatogenesis Source: BHF-UCL
    13. sperm motility Source: BHF-UCL
    14. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Growth regulation, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibitor of growth protein 2
    Alternative name(s):
    Inhibitor of growth 1-like protein
    p33ING2
    Gene namesi
    Name:Ing2
    Synonyms:Ing1l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1916510. Ing2.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. CCAAT-binding factor complex Source: Ensembl
    2. Sin3 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281Inhibitor of growth protein 2PRO_0000212664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki196 – 196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

    Post-translational modificationi

    Sumoylation enhances its association with SIN3A and is required for binding to some target gene promoters, this is the case for TMEM71.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PRIDEiQ9ESK4.

    PTM databases

    PhosphoSiteiQ9ESK4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ESK4.
    CleanExiMM_ING2.
    GenevestigatoriQ9ESK4.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi213322. 3 interactions.
    DIPiDIP-38912N.
    MINTiMINT-1340342.
    STRINGi10090.ENSMUSP00000079226.

    Structurei

    Secondary structure

    1
    281
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi210 – 2123
    Turni216 – 2194
    Beta strandi224 – 2285
    Beta strandi238 – 2403
    Helixi242 – 2443
    Helixi257 – 2604

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WESNMR-A205-262[»]
    2G6QX-ray2.00A205-264[»]
    ProteinModelPortaliQ9ESK4.
    SMRiQ9ESK4. Positions 32-120, 212-263.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ESK4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 28117PBRBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili49 – 10153Sequence AnalysisAdd
    BLAST

    Domaini

    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 similaritiesi

    Belongs to the ING family.Curated
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri213 – 26250PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5034.
    GeneTreeiENSGT00550000074538.
    HOGENOMiHOG000239724.
    HOVERGENiHBG006607.
    InParanoidiQ9ESK4.
    OMAiLCHMTNG.
    OrthoDBiEOG7RBZ9T.
    TreeFamiTF352014.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR028639. 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]
    PANTHERiPTHR10333. PTHR10333. 1 hit.
    PTHR10333:SF37. PTHR10333:SF37. 1 hit.
    PfamiPF12998. ING. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ESK4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGQQQQQQL YSSAALLTGE RSRLLSCYVQ DYLECVESLP HDMQRNVSVL    50
    RELDNKYQET LKEIDDVYEK YKKEDDSNQK KRLQQHLQRA LINSQELGDE 100
    KIQIVTQMLE LVENRARQME LHSQCFQDPA ESERASDKSK MDSSQPERSS 150
    RRPRRQRTSE SRDLCHMTNG IDDCDDQPPK EKRSKSAKKK KRSKAKQERE 200
    ASPVEFAIDP NEPTYCLCNQ VSYGEMIGCD NEQCPIEWFH FSCVSLTYKP 250
    KGKWYCPKCR GDNEKTMDKS TEKTKKERRA R 281
    Length:281
    Mass (Da):32,978
    Last modified:October 3, 2012 - v3
    Checksum:i6D953B52822C2D8A
    GO

    Sequence cautioni

    The sequence AAH50003.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261S → T in AAG12173. 1 PublicationCurated
    Sequence conflicti26 – 261S → T in AAH50003. (PubMed:15489334)Curated
    Sequence conflicti72 – 721K → E in AAG12173. 1 PublicationCurated
    Sequence conflicti104 – 1041I → N in AAG12173. 1 PublicationCurated
    Sequence conflicti110 – 1101E → G in AAG12173. 1 PublicationCurated
    Sequence conflicti116 – 1161A → S in AAG12173. 1 PublicationCurated
    Sequence conflicti203 – 2031P → S in AAG12173. 1 PublicationCurated
    Sequence conflicti250 – 2501P → H in AAG12173. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS22298.1.
    RefSeqiNP_075992.2. NM_023503.3.
    UniGeneiMm.430733.

    Genome annotation databases

    EnsembliENSMUST00000080353; ENSMUSP00000079226; ENSMUSG00000063049.
    GeneIDi69260.
    KEGGimmu:69260.
    UCSCiuc009lrf.2. mouse.
    uc012gdo.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS22298.1.
    RefSeqi NP_075992.2. NM_023503.3.
    UniGenei Mm.430733.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WES NMR - A 205-262 [» ]
    2G6Q X-ray 2.00 A 205-264 [» ]
    ProteinModelPortali Q9ESK4.
    SMRi Q9ESK4. Positions 32-120, 212-263.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213322. 3 interactions.
    DIPi DIP-38912N.
    MINTi MINT-1340342.
    STRINGi 10090.ENSMUSP00000079226.

    PTM databases

    PhosphoSitei Q9ESK4.

    Proteomic databases

    PRIDEi Q9ESK4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080353 ; ENSMUSP00000079226 ; ENSMUSG00000063049 .
    GeneIDi 69260.
    KEGGi mmu:69260.
    UCSCi uc009lrf.2. mouse.
    uc012gdo.1. mouse.

    Organism-specific databases

    CTDi 3622.
    MGIi MGI:1916510. Ing2.

    Phylogenomic databases

    eggNOGi COG5034.
    GeneTreei ENSGT00550000074538.
    HOGENOMi HOG000239724.
    HOVERGENi HBG006607.
    InParanoidi Q9ESK4.
    OMAi LCHMTNG.
    OrthoDBi EOG7RBZ9T.
    TreeFami TF352014.

    Miscellaneous databases

    EvolutionaryTracei Q9ESK4.
    NextBioi 328987.
    PROi Q9ESK4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ESK4.
    CleanExi MM_ING2.
    Genevestigatori Q9ESK4.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR028639. 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 ]
    PANTHERi PTHR10333. PTHR10333. 1 hit.
    PTHR10333:SF37. PTHR10333:SF37. 1 hit.
    Pfami PF12998. ING. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum and Hippocampus.
    3. 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.

    Entry informationi

    Entry nameiING2_MOUSE
    AccessioniPrimary (citable) accession number: Q9ESK4
    Secondary accession number(s): Q4VAD7, Q80VI5, Q8BGU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3