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Q9UNL4

- ING4_HUMAN

UniProt

Q9UNL4 - ING4_HUMAN

Protein

Inhibitor of growth protein 4

Gene

ING4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1).6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei198 – 1981Histone H3K4me3By similarity
    Binding sitei209 – 2091Histone H3K4me3By similarity
    Binding sitei213 – 2131Histone H3K4me3By similarity
    Binding sitei221 – 2211Histone H3K4me3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri196 – 24550PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transcription coactivator activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cell cycle arrest Source: UniProtKB
    3. chromatin organization Source: Reactome
    4. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
    5. DNA replication Source: UniProtKB
    6. histone H3 acetylation Source: UniProtKB
    7. histone H4-K12 acetylation Source: UniProtKB
    8. histone H4-K5 acetylation Source: UniProtKB
    9. histone H4-K8 acetylation Source: UniProtKB
    10. negative regulation of cell proliferation Source: UniProtKB
    11. negative regulation of growth Source: UniProtKB
    12. negative regulation of transcription, DNA-templated Source: UniProtKB
    13. positive regulation of apoptotic process Source: UniProtKB
    14. protein acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibitor of growth protein 4
    Alternative name(s):
    p29ING4
    Gene namesi
    Name:ING4
    ORF Names:My036
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:19423. ING4.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. histone acetyltransferase complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA134976283.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249Inhibitor of growth protein 4PRO_0000212668Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei112 – 1121N6-acetyllysine1 Publication
    Modified residuei127 – 1271N6-acetyllysine1 Publication
    Modified residuei129 – 1291N6-acetyllysine1 Publication
    Modified residuei133 – 1331Citrulline1 Publication
    Modified residuei146 – 1461N6-acetyllysine1 Publication
    Modified residuei148 – 1481N6-acetyllysine1 Publication
    Modified residuei156 – 1561N6-acetyllysine1 Publication
    Modified residuei166 – 1661Citrulline1 Publication

    Post-translational modificationi

    Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation.1 Publication

    Keywords - PTMi

    Acetylation, Citrullination

    Proteomic databases

    MaxQBiQ9UNL4.
    PaxDbiQ9UNL4.
    PRIDEiQ9UNL4.

    PTM databases

    PhosphoSiteiQ9UNL4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UNL4.
    BgeeiQ9UNL4.
    CleanExiHS_ING4.
    GenevestigatoriQ9UNL4.

    Organism-specific databases

    HPAiHPA057338.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with H3K4me3 and to a lesser extent with H3K4me2, the interaction augments HBO1 acetylation activity on H3 tails. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts with EP300, RELA and TP53; these interactions may be indirect. Interacts with EGLN1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST1H3DP684313EBI-2866661,EBI-79722
    HNRNPDQ141039EBI-2866661,EBI-299674
    HNRNPDQ14103-42EBI-2866661,EBI-432545

    Protein-protein interaction databases

    BioGridi119331. 28 interactions.
    DIPiDIP-42222N.
    IntActiQ9UNL4. 9 interactions.
    MINTiMINT-1202585.
    STRINGi9606.ENSP00000380024.

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 128
    Helixi14 – 163
    Helixi17 – 5034
    Helixi58 – 10346
    Turni199 – 2024
    Beta strandi207 – 2115
    Beta strandi221 – 2233
    Helixi225 – 2273
    Helixi240 – 2434
    Helixi244 – 2463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K1JNMR-A188-249[»]
    2M1RNMR-A188-249[»]
    2PNXX-ray1.80A/C194-246[»]
    2VNFX-ray1.76A/C188-246[»]
    4AFLX-ray2.28A/B/C/D/E/F2-105[»]
    ProteinModelPortaliQ9UNL4.
    SMRiQ9UNL4. Positions 4-105, 169-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UNL4.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili25 – 118941 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi127 – 14822Bipartite nuclear localization signalAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me3.
    The N-terminal coiled-coil domain mediates homodimerization.

    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 fingeri196 – 24550PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5034.
    HOVERGENiHBG006607.
    InParanoidiQ9UNL4.
    KOiK11346.
    OMAiKLKFVRT.
    OrthoDBiEOG7RBZ9T.
    PhylomeDBiQ9UNL4.
    TreeFamiTF352014.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR028647. ING4.
    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:SF40. PTHR10333:SF40. 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 (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNL4-1) [UniParc]FASTAAdd to Basket

    Also known as: ING4_v1

    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

    MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM    50
    SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL 100
    DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS 150
    DEEAPKTAQK KLKLVRTSPE YGMPSVTFGS VHPSDVLDMP VDPNEPTYCL 200
    CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK 249
    Length:249
    Mass (Da):28,530
    Last modified:May 1, 2000 - v1
    Checksum:iCE3FD9CC9F0CE949
    GO
    Isoform 2 (identifier: Q9UNL4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         131-131: K → S
         132-132: Missing.

    Note: May be due to a competing donor splice site.

    Show »
    Length:248
    Mass (Da):28,432
    Checksum:i76907CB2119B07E8
    GO
    Isoform 3 (identifier: Q9UNL4-3) [UniParc]FASTAAdd to Basket

    Also known as: deltaEx2

    The sequence of this isoform differs from the canonical sequence as follows:
         13-37: SIENLPFELQRNFQLMRDLDQRTED → N

    Show »
    Length:225
    Mass (Da):25,554
    Checksum:i56E4C5F4AB305918
    GO
    Isoform 4 (identifier: Q9UNL4-4) [UniParc]FASTAAdd to Basket

    Also known as: ING4_v4

    The sequence of this isoform differs from the canonical sequence as follows:
         129-132: Missing.

    Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization. Contains a N6-acetyllysine at position 127. Contains a N6-acetyllysine at position 114.

    Show »
    Length:245
    Mass (Da):28,089
    Checksum:iD6D1003F066112AC
    GO
    Isoform 5 (identifier: Q9UNL4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-131: GKKK → E

    Show »
    Length:246
    Mass (Da):28,218
    Checksum:iAE5F98B0081B189B
    GO
    Isoform 6 (identifier: Q9UNL4-6) [UniParc]FASTAAdd to Basket

    Also known as: ING4_v2

    The sequence of this isoform differs from the canonical sequence as follows:
         131-131: Missing.

    Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.

    Show »
    Length:248
    Mass (Da):28,402
    Checksum:i86907CA611946A45
    GO
    Isoform 7 (identifier: Q9UNL4-7) [UniParc]FASTAAdd to Basket

    Also known as: ING4_v3

    The sequence of this isoform differs from the canonical sequence as follows:
         128-130: Missing.

    Note: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization.

    Show »
    Length:246
    Mass (Da):28,217
    Checksum:i405F98B0061B1C31
    GO
    Isoform 8 (identifier: Q9UNL4-8) [UniParc]FASTAAdd to Basket

    Also known as: deltaEx6A

    The sequence of this isoform differs from the canonical sequence as follows:
         168-249: SPEYGMPSVT...PRCSQERKKK → VPLSGSILPVWG

    Show »
    Length:179
    Mass (Da):20,482
    Checksum:iCE8BCDAD65CECE67
    GO

    Sequence cautioni

    The sequence AAG43153.1 differs from that shown. Reason: Frameshift at positions 240 and 243.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei13 – 3725SIENL…QRTED → N in isoform 3. 1 PublicationVSP_041288Add
    BLAST
    Alternative sequencei128 – 1314GKKK → E in isoform 5. 1 PublicationVSP_041289
    Alternative sequencei128 – 1303Missing in isoform 7. 1 PublicationVSP_041290
    Alternative sequencei129 – 1324Missing in isoform 4. 1 PublicationVSP_041291
    Alternative sequencei131 – 1311K → S in isoform 2. 3 PublicationsVSP_012518
    Alternative sequencei131 – 1311Missing in isoform 6. 1 PublicationVSP_041292
    Alternative sequencei132 – 1321Missing in isoform 2. 3 PublicationsVSP_012519
    Alternative sequencei168 – 24982SPEYG…ERKKK → VPLSGSILPVWG in isoform 8. 1 PublicationVSP_041293Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156552 mRNA. Translation: AAL79773.1.
    AB197695 mRNA. Translation: BAF30477.1.
    AB197696 mRNA. Translation: BAF30478.1.
    AB197697 mRNA. Translation: BAF30479.1.
    EF152349 mRNA. Translation: ABO61139.1.
    EF152351 mRNA. Translation: ABO61141.1.
    AF063594 mRNA. Translation: AAG43153.1. Frameshift.
    AF110645 mRNA. Translation: AAD48585.1.
    CH471116 Genomic DNA. Translation: EAW88763.1.
    CH471116 Genomic DNA. Translation: EAW88768.1.
    CH471116 Genomic DNA. Translation: EAW88770.1.
    CH471116 Genomic DNA. Translation: EAW88772.1.
    BC007781 mRNA. Translation: AAH07781.1.
    BC013038 mRNA. Translation: AAH13038.2.
    BC095434 mRNA. Translation: AAH95434.1.
    CCDSiCCDS44812.1. [Q9UNL4-3]
    CCDS44813.1. [Q9UNL4-1]
    CCDS44814.1. [Q9UNL4-5]
    CCDS44815.1. [Q9UNL4-4]
    CCDS44816.1. [Q9UNL4-8]
    CCDS8555.1. [Q9UNL4-2]
    RefSeqiNP_001121054.1. NM_001127582.1. [Q9UNL4-1]
    NP_001121055.1. NM_001127583.1. [Q9UNL4-5]
    NP_001121056.1. NM_001127584.1. [Q9UNL4-4]
    NP_001121057.1. NM_001127585.1. [Q9UNL4-3]
    NP_001121058.1. NM_001127586.1. [Q9UNL4-8]
    NP_057246.2. NM_016162.3. [Q9UNL4-2]
    UniGeneiHs.524210.

    Genome annotation databases

    EnsembliENST00000341550; ENSP00000343396; ENSG00000111653. [Q9UNL4-2]
    ENST00000396807; ENSP00000380024; ENSG00000111653. [Q9UNL4-1]
    ENST00000412586; ENSP00000412705; ENSG00000111653. [Q9UNL4-5]
    ENST00000423703; ENSP00000414008; ENSG00000111653. [Q9UNL4-8]
    ENST00000444704; ENSP00000397343; ENSG00000111653. [Q9UNL4-3]
    ENST00000446105; ENSP00000415903; ENSG00000111653. [Q9UNL4-4]
    GeneIDi51147.
    KEGGihsa:51147.
    UCSCiuc001qpv.4. human. [Q9UNL4-2]
    uc001qpw.4. human. [Q9UNL4-1]
    uc001qpx.4. human. [Q9UNL4-5]
    uc001qpy.4. human. [Q9UNL4-4]
    uc009zes.3. human. [Q9UNL4-8]
    uc009zet.3. human. [Q9UNL4-3]

    Polymorphism databases

    DMDMi57012981.

    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
    AF156552 mRNA. Translation: AAL79773.1 .
    AB197695 mRNA. Translation: BAF30477.1 .
    AB197696 mRNA. Translation: BAF30478.1 .
    AB197697 mRNA. Translation: BAF30479.1 .
    EF152349 mRNA. Translation: ABO61139.1 .
    EF152351 mRNA. Translation: ABO61141.1 .
    AF063594 mRNA. Translation: AAG43153.1 . Frameshift.
    AF110645 mRNA. Translation: AAD48585.1 .
    CH471116 Genomic DNA. Translation: EAW88763.1 .
    CH471116 Genomic DNA. Translation: EAW88768.1 .
    CH471116 Genomic DNA. Translation: EAW88770.1 .
    CH471116 Genomic DNA. Translation: EAW88772.1 .
    BC007781 mRNA. Translation: AAH07781.1 .
    BC013038 mRNA. Translation: AAH13038.2 .
    BC095434 mRNA. Translation: AAH95434.1 .
    CCDSi CCDS44812.1. [Q9UNL4-3 ]
    CCDS44813.1. [Q9UNL4-1 ]
    CCDS44814.1. [Q9UNL4-5 ]
    CCDS44815.1. [Q9UNL4-4 ]
    CCDS44816.1. [Q9UNL4-8 ]
    CCDS8555.1. [Q9UNL4-2 ]
    RefSeqi NP_001121054.1. NM_001127582.1. [Q9UNL4-1 ]
    NP_001121055.1. NM_001127583.1. [Q9UNL4-5 ]
    NP_001121056.1. NM_001127584.1. [Q9UNL4-4 ]
    NP_001121057.1. NM_001127585.1. [Q9UNL4-3 ]
    NP_001121058.1. NM_001127586.1. [Q9UNL4-8 ]
    NP_057246.2. NM_016162.3. [Q9UNL4-2 ]
    UniGenei Hs.524210.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K1J NMR - A 188-249 [» ]
    2M1R NMR - A 188-249 [» ]
    2PNX X-ray 1.80 A/C 194-246 [» ]
    2VNF X-ray 1.76 A/C 188-246 [» ]
    4AFL X-ray 2.28 A/B/C/D/E/F 2-105 [» ]
    ProteinModelPortali Q9UNL4.
    SMRi Q9UNL4. Positions 4-105, 169-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119331. 28 interactions.
    DIPi DIP-42222N.
    IntActi Q9UNL4. 9 interactions.
    MINTi MINT-1202585.
    STRINGi 9606.ENSP00000380024.

    PTM databases

    PhosphoSitei Q9UNL4.

    Polymorphism databases

    DMDMi 57012981.

    Proteomic databases

    MaxQBi Q9UNL4.
    PaxDbi Q9UNL4.
    PRIDEi Q9UNL4.

    Protocols and materials databases

    DNASUi 51147.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341550 ; ENSP00000343396 ; ENSG00000111653 . [Q9UNL4-2 ]
    ENST00000396807 ; ENSP00000380024 ; ENSG00000111653 . [Q9UNL4-1 ]
    ENST00000412586 ; ENSP00000412705 ; ENSG00000111653 . [Q9UNL4-5 ]
    ENST00000423703 ; ENSP00000414008 ; ENSG00000111653 . [Q9UNL4-8 ]
    ENST00000444704 ; ENSP00000397343 ; ENSG00000111653 . [Q9UNL4-3 ]
    ENST00000446105 ; ENSP00000415903 ; ENSG00000111653 . [Q9UNL4-4 ]
    GeneIDi 51147.
    KEGGi hsa:51147.
    UCSCi uc001qpv.4. human. [Q9UNL4-2 ]
    uc001qpw.4. human. [Q9UNL4-1 ]
    uc001qpx.4. human. [Q9UNL4-5 ]
    uc001qpy.4. human. [Q9UNL4-4 ]
    uc009zes.3. human. [Q9UNL4-8 ]
    uc009zet.3. human. [Q9UNL4-3 ]

    Organism-specific databases

    CTDi 51147.
    GeneCardsi GC12M006759.
    HGNCi HGNC:19423. ING4.
    HPAi HPA057338.
    MIMi 608524. gene.
    neXtProti NX_Q9UNL4.
    PharmGKBi PA134976283.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5034.
    HOVERGENi HBG006607.
    InParanoidi Q9UNL4.
    KOi K11346.
    OMAi KLKFVRT.
    OrthoDBi EOG7RBZ9T.
    PhylomeDBi Q9UNL4.
    TreeFami TF352014.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi ING4. human.
    EvolutionaryTracei Q9UNL4.
    GeneWikii ING4.
    GenomeRNAii 51147.
    NextBioi 54021.
    PROi Q9UNL4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNL4.
    Bgeei Q9UNL4.
    CleanExi HS_ING4.
    Genevestigatori Q9UNL4.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR028647. ING4.
    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:SF40. PTHR10333:SF40. 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. "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity."
      Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.
      Cancer Res. 63:2373-2378(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300 AND TP53.
      Tissue: Placenta.
    2. "Novel splice variants of ING4 and their possible roles in the regulation of cell growth and motility."
      Unoki M., Shen J.C., Zheng Z.M., Harris C.C.
      J. Biol. Chem. 281:34677-34686(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5; 6 AND 7), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    3. "Detection of novel mRNA splice variants of human ING4 tumor suppressor gene."
      Raho G., Miranda C., Tamborini E., Pierotti M.A., Greco A.
      Oncogene 26:5247-5257(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 8), ALTERNATIVE SPLICING (ISOFORM 8).
    4. Mao Y.M., Xie Y., Zheng Z.H.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pituitary.
    6. 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] (ISOFORMS 1 AND 2).
      Tissue: B-cell, Lung and Pituitary.
    8. "ING4 induces G2/M cell cycle arrest and enhances the chemosensitivity to DNA-damage agents in HepG2 cells."
      Zhang X., Xu L.-S., Wang Z.-Q., Wang K.-S., Li N., Cheng Z.-H., Huang S.-Z., Wei D.-Z., Han Z.-G.
      FEBS Lett. 570:7-12(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis."
      Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K.
      Nature 428:328-332(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION.
    10. "A screen for genes that suppress loss of contact inhibition: Identification of ING4 as a candidate tumor suppressor gene in human cancer."
      Kim S., Chin K., Gray J.W., Bishop J.M.
      Proc. Natl. Acad. Sci. U.S.A. 101:16251-16256(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Nuclear localization signal of ING4 plays a key role in its binding to p53."
      Zhang X., Wang K.S., Wang Z.Q., Xu L.S., Wang Q.W., Chen F., Wei D.Z., Han Z.G.
      Biochem. Biophys. Res. Commun. 331:1032-1038(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL.
    12. "The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)."
      Ozer A., Wu L.C., Bruick R.K.
      Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EGLN1.
    13. "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: FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX.
    14. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-127; LYS-129; LYS-146; LYS-148 AND LYS-156, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-127 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53."
      Guo Q., Fast W.
      J. Biol. Chem. 286:17069-17078(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CITRULLINATION AT ARG-133 AND ARG-166, NUCLEAR LOCALIZATION SIGNAL.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 188-245 IN COMPLEX WITH H3K4ME3, DOMAIN PHD, SUBUNIT.
    18. "ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation."
      Hung T., Binda O., Champagne K.S., Kuo A.J., Johnson K., Chang H.Y., Simon M.D., Kutateladze T.G., Gozani O.
      Mol. Cell 33:248-256(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 194-246, SUBUNIT.
    19. "Crystal structure of inhibitor of growth 4 (ING4) dimerization domain reveals functional organization of ING family of chromatin-binding proteins."
      Culurgioni S., Munoz I.G., Moreno A., Palacios A., Villate M., Palmero I., Montoya G., Blanco F.J.
      J. Biol. Chem. 287:10876-10884(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-105, COILED-COIL DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiING4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNL4
    Secondary accession number(s): A4KYM4
    , A4KYM6, D3DUR8, Q0EF62, Q0EF63, Q4VBQ6, Q96E15, Q9H3J0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3