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Q9UNL4

- ING4_HUMAN

UniProt

Q9UNL4 - ING4_HUMAN

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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

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. transcription coactivator activity Source: UniProtKB
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UNL4.
CleanExiHS_ING4.
ExpressionAtlasiQ9UNL4. baseline and differential.
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 – 128Combined sources
Helixi14 – 163Combined sources
Helixi17 – 5034Combined sources
Helixi58 – 10346Combined sources
Turni199 – 2024Combined sources
Beta strandi207 – 2115Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 2273Combined sources
Helixi240 – 2434Combined sources
Helixi244 – 2463Combined sources

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.
GeneTreeiENSGT00550000074538.
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

        10         20         30         40         50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS
160 170 180 190 200
DEEAPKTAQK KLKLVRTSPE YGMPSVTFGS VHPSDVLDMP VDPNEPTYCL
210 220 230 240
CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK
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.
GeneTreei ENSGT00550000074538.
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

Bgeei Q9UNL4.
CleanExi HS_ING4.
ExpressionAtlasi Q9UNL4. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 131 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