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Q9H160

- ING2_HUMAN

UniProt

Q9H160 - ING2_HUMAN

Protein

Inhibitor of growth protein 2

Gene

ING2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei214 – 2141Histone H3K4me3By similarity
    Binding sitei225 – 2251Histone H3K4me3By similarity
    Binding sitei229 – 2291Histone H3K4me3By similarity
    Binding sitei237 – 2371Histone H3K4me3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri212 – 26150PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: ProtInc
    2. DNA binding Source: UniProtKB
    3. methylated histone binding Source: UniProtKB
    4. phosphatidylinositol binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein complex binding Source: UniProtKB
    7. 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 cell proliferation Source: InterPro
    5. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    6. positive regulation of apoptotic process Source: InterPro
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    9. regulation of cellular senescence Source: BHF-UCL
    10. regulation of growth Source: UniProtKB-KW
    11. regulation of response to DNA damage stimulus Source: BHF-UCL
    12. regulation of transcription, DNA-templated Source: UniProtKB
    13. seminiferous tubule development Source: BHF-UCL
    14. signal transduction Source: ProtInc
    15. spermatid development Source: BHF-UCL
    16. spermatogenesis Source: BHF-UCL
    17. sperm motility Source: BHF-UCL
    18. 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
    Short name:
    ING1Lp
    p32
    p33ING2
    Gene namesi
    Name:ING2
    Synonyms:ING1L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6063. ING2.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns5P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29873.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 280280Inhibitor of growth protein 2PRO_0000212663Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki195 – 195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

    Post-translational modificationi

    Sumoylation enhances its association with SIN3A and is required for binding to some target gene promoters, this is the case for TMEM71.1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9H160.
    PaxDbiQ9H160.
    PRIDEiQ9H160.

    PTM databases

    PhosphoSiteiQ9H160.

    Expressioni

    Tissue specificityi

    Widely expressed. Higher expressed in colon-cancer tumor than in normal colon tissues.1 Publication

    Inductioni

    Induced by the DNA-damaging agents etoposide and neocarzinostatin.1 Publication

    Gene expression databases

    ArrayExpressiQ9H160.
    BgeeiQ9H160.
    CleanExiHS_ING2.
    GenevestigatoriQ9H160.

    Organism-specific databases

    HPAiHPA019486.
    HPA021517.

    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 ING2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PCNAP120043EBI-389787,EBI-358311
    SMURF1Q9HCE74EBI-389787,EBI-976466

    Protein-protein interaction databases

    BioGridi109834. 31 interactions.
    IntActiQ9H160. 9 interactions.
    MINTiMINT-2830779.
    STRINGi9606.ENSP00000307183.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H160.
    SMRiQ9H160. Positions 31-119, 211-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni264 – 28017PBRAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili48 – 12073Sequence AnalysisAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me3.1 Publication
    The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P).1 Publication

    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 fingeri212 – 26150PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5034.
    HOGENOMiHOG000239724.
    HOVERGENiHBG006607.
    InParanoidiQ9H160.
    OMAiLCHMTNG.
    OrthoDBiEOG7RBZ9T.
    PhylomeDBiQ9H160.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform ING2a (identifier: Q9H160-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR    50
    ELDNKYQETL KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK 100
    IQIVTQMLEL VENRARQMEL HSQCFQDPAE SERASDKAKM DSSQPERSSR 150
    RPRRQRTSES RDLCHMANGI EDCDDQPPKE KKSKSAKKKK RSKAKQEREA 200
    SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF SCVSLTYKPK 250
    GKWYCPKCRG DNEKTMDKST EKTKKDRRSR 280
    Length:280
    Mass (Da):32,808
    Last modified:February 15, 2005 - v2
    Checksum:iDC85A6ECAF7A5D81
    GO
    Isoform ING2b (identifier: Q9H160-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-58: MLGQQQQQLY...LRELDNKYQE → MDQDGDQQLGPSRILAPQ

    Note: Low expression except in testis, where it reaches half of ING2a levels.

    Show »
    Length:240
    Mass (Da):27,984
    Checksum:iA445AEC5BBFA3B35
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211S → T in CAC20567. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5858MLGQQ…NKYQE → MDQDGDQQLGPSRILAPQ in isoform ING2b. 2 PublicationsVSP_047821Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012853 mRNA. Translation: BAA36419.1.
    AF053537 mRNA. Translation: AAG11395.1.
    AF062748, AF062747 Genomic DNA. Translation: AAG11396.1.
    AB196793 mRNA. Translation: BAF30476.1.
    AJ006851 mRNA. Translation: CAC20567.1.
    AK294310 mRNA. Translation: BAH11731.1.
    AC107214 Genomic DNA. No translation available.
    BC030128 mRNA. Translation: AAH30128.1.
    CCDSiCCDS3833.1. [Q9H160-1]
    RefSeqiNP_001555.1. NM_001564.3. [Q9H160-1]
    UniGeneiHs.107153.

    Genome annotation databases

    EnsembliENST00000302327; ENSP00000307183; ENSG00000168556. [Q9H160-1]
    GeneIDi3622.
    KEGGihsa:3622.
    UCSCiuc003ivs.1. human. [Q9H160-1]

    Polymorphism databases

    DMDMi59798471.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012853 mRNA. Translation: BAA36419.1 .
    AF053537 mRNA. Translation: AAG11395.1 .
    AF062748 , AF062747 Genomic DNA. Translation: AAG11396.1 .
    AB196793 mRNA. Translation: BAF30476.1 .
    AJ006851 mRNA. Translation: CAC20567.1 .
    AK294310 mRNA. Translation: BAH11731.1 .
    AC107214 Genomic DNA. No translation available.
    BC030128 mRNA. Translation: AAH30128.1 .
    CCDSi CCDS3833.1. [Q9H160-1 ]
    RefSeqi NP_001555.1. NM_001564.3. [Q9H160-1 ]
    UniGenei Hs.107153.

    3D structure databases

    ProteinModelPortali Q9H160.
    SMRi Q9H160. Positions 31-119, 211-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109834. 31 interactions.
    IntActi Q9H160. 9 interactions.
    MINTi MINT-2830779.
    STRINGi 9606.ENSP00000307183.

    PTM databases

    PhosphoSitei Q9H160.

    Polymorphism databases

    DMDMi 59798471.

    Proteomic databases

    MaxQBi Q9H160.
    PaxDbi Q9H160.
    PRIDEi Q9H160.

    Protocols and materials databases

    DNASUi 3622.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302327 ; ENSP00000307183 ; ENSG00000168556 . [Q9H160-1 ]
    GeneIDi 3622.
    KEGGi hsa:3622.
    UCSCi uc003ivs.1. human. [Q9H160-1 ]

    Organism-specific databases

    CTDi 3622.
    GeneCardsi GC04P184426.
    HGNCi HGNC:6063. ING2.
    HPAi HPA019486.
    HPA021517.
    MIMi 604215. gene.
    neXtProti NX_Q9H160.
    PharmGKBi PA29873.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5034.
    HOGENOMi HOG000239724.
    HOVERGENi HBG006607.
    InParanoidi Q9H160.
    OMAi LCHMTNG.
    OrthoDBi EOG7RBZ9T.
    PhylomeDBi Q9H160.
    TreeFami TF352014.

    Miscellaneous databases

    GeneWikii ING2.
    GenomeRNAii 3622.
    NextBioi 14173.
    PROi Q9H160.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H160.
    Bgeei Q9H160.
    CleanExi HS_ING2.
    Genevestigatori Q9H160.

    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. "Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor."
      Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M.
      Cytogenet. Cell Genet. 83:232-235(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM ING2A), TISSUE SPECIFICITY.
    2. "DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53."
      Nagashima M., Shiseki M., Miura K., Hagiwara K., Linke S.P., Pedeux R., Wang X.W., Yokota J., Riabowol K., Harris C.C.
      Proc. Natl. Acad. Sci. U.S.A. 98:9671-9676(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A), FUNCTION, INDUCTION.
    3. "A novel ING2 isoform, ING2b, synergizes with ING2a to prevent cell cycle arrest and apoptosis."
      Unoki M., Kumamoto K., Robles A.I., Shen J.C., Zheng Z.-M., Harris C.C.
      FEBS Lett. 582:3868-3874(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2B), ALTERNATIVE SPLICING.
    4. "ING2, a new possible gene suppressor tumor."
      Cal S., Freije J.M., Lopez-Otin C.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A).
      Tissue: Mammary tumor.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ING2B).
      Tissue: Amygdala.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM ING2A).
      Tissue: Lung.
    8. "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)."
      Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.
      Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-44, IDENTIFICATION IN MSIN3A-LIKE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    9. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "The polybasic region that follows the plant homeodomain zinc finger 1 of Pf1 is necessary and sufficient for specific phosphoinositide binding."
      Kaadige M.R., Ayer D.E.
      J. Biol. Chem. 281:28831-28836(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHOINOSITIDE-BINDING.
    11. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN MSIN3A COMPLEX.
    12. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
    13. "Sumoylation of ING2 regulates the transcription mediated by Sin3A."
      Ythier D., Larrieu D., Binet R., Binda O., Brambilla C., Gazzeri S., Pedeux R.
      Oncogene 29:5946-5956(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-195.

    Entry informationi

    Entry nameiING2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H160
    Secondary accession number(s): B6ZDS1, O95698
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3