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Protein

Inhibitor of growth protein 4

Gene

ING4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11 (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei198Histone H3K4me3By similarity1
Metal bindingi199Zinc 1By similarity1
Metal bindingi201Zinc 1By similarity1
Binding sitei209Histone H3K4me3By similarity1
Metal bindingi212Zinc 2By similarity1
Binding sitei213Histone H3K4me3By similarity1
Metal bindingi217Zinc 2By similarity1
Binding sitei221Histone H3K4me3By similarity1
Metal bindingi223Zinc 1; via pros nitrogenBy similarity1
Metal bindingi226Zinc 1By similarity1
Metal bindingi239Zinc 2By similarity1
Metal bindingi242Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri196 – 245PHD-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  • DNA replication Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • histone H4-K12 acetylation Source: UniProtKB
  • histone H4-K5 acetylation Source: UniProtKB
  • histone H4-K8 acetylation Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of growth Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • protein acetylation Source: UniProtKB

Keywordsi

Molecular functionChromatin regulator
Biological processApoptosis, Cell cycle
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214847 HATs acetylate histones
SIGNORiQ9UNL4

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000111653.19
HGNCiHGNC:19423 ING4
MIMi608524 gene
neXtProtiNX_Q9UNL4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi51147
OpenTargetsiENSG00000111653
PharmGKBiPA134976283

Polymorphism and mutation databases

BioMutaiING4
DMDMi57012981

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002126681 – 249Inhibitor of growth protein 4Add BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112N6-acetyllysineCombined sources1
Modified residuei127N6-acetyllysineCombined sources1
Modified residuei129N6-acetyllysineBy similarity1
Modified residuei133Citrulline1 Publication1
Modified residuei146N6-acetyllysineCombined sources1
Modified residuei148N6-acetyllysineCombined sources1
Modified residuei156N6-acetyllysineCombined sources1
Modified residuei166Citrulline1 Publication1
Isoform 4 (identifier: Q9UNL4-4)
Modified residuei114N6-acetyllysineCombined sources1
Modified residuei127N6-acetyllysineCombined sources1

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

EPDiQ9UNL4
PaxDbiQ9UNL4
PeptideAtlasiQ9UNL4
PRIDEiQ9UNL4

PTM databases

iPTMnetiQ9UNL4
PhosphoSitePlusiQ9UNL4

Expressioni

Gene expression databases

BgeeiENSG00000111653
CleanExiHS_ING4
ExpressionAtlasiQ9UNL4 baseline and differential
GenevisibleiQ9UNL4 HS

Organism-specific databases

HPAiHPA031817
HPA057338

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. Interacts with BCL2A1 (By similarity).By similarity8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119331, 47 interactors
CORUMiQ9UNL4
DIPiDIP-42222N
IntActiQ9UNL4, 29 interactors
MINTiQ9UNL4
STRINGi9606.ENSP00000380024

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 12Combined sources8
Helixi14 – 16Combined sources3
Helixi17 – 50Combined sources34
Helixi58 – 103Combined sources46
Turni199 – 202Combined sources4
Beta strandi207 – 211Combined sources5
Beta strandi221 – 223Combined sources3
Helixi225 – 227Combined sources3
Helixi240 – 243Combined sources4
Helixi244 – 246Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNL4

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili25 – 1181 PublicationAdd BLAST94

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi127 – 148Bipartite nuclear localization signalAdd BLAST22

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri196 – 245PHD-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1973 Eukaryota
COG5034 LUCA
GeneTreeiENSGT00550000074538
HOGENOMiHOG000239724
HOVERGENiHBG006607
InParanoidiQ9UNL4
KOiK11346
OMAiPRCSQDR
OrthoDBiEOG091G0J8Y
PhylomeDBiQ9UNL4
TreeFamiTF352014

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR028647 ING4
IPR024610 ING_N_histone_binding
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR10333:SF40 PTHR10333:SF40, 1 hit
PfamiView protein in Pfam
PF12998 ING, 1 hit
SMARTiView protein in SMART
SM01408 ING, 1 hit
SM00249 PHD, 1 hit
SUPFAMiSSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

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.Combined sources
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 differs from that shown. Reason: Frameshift at positions 240 and 243.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04128813 – 37SIENL…QRTED → N in isoform 3. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_041289128 – 131GKKK → E in isoform 5. 1 Publication4
Alternative sequenceiVSP_041290128 – 130Missing in isoform 7. 1 Publication3
Alternative sequenceiVSP_041291129 – 132Missing in isoform 4. 1 Publication4
Alternative sequenceiVSP_012518131K → S in isoform 2. 3 Publications1
Alternative sequenceiVSP_041292131Missing in isoform 6. 1 Publication1
Alternative sequenceiVSP_012519132Missing in isoform 2. 3 Publications1
Alternative sequenceiVSP_041293168 – 249SPEYG…ERKKK → VPLSGSILPVWG in isoform 8. 1 PublicationAdd BLAST82

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5 human [Q9UNL4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiING4_HUMAN
AccessioniPrimary (citable) accession number: Q9UNL4
Secondary accession number(s): A4KYM4
, A4KYM6, D3DUR8, Q0EF62, Q0EF63, Q4VBQ6, Q96E15, Q9H3J0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 163 of the entry and version 1 of the sequence. See 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

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