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Protein

Inhibitor of growth protein 4

Gene

Ing4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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) (By similarity). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11 (PubMed:11888890).By similarity1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 4
Alternative name(s):
p29ING4
Gene namesi
Name:Ing4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:107307. Ing4.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • histone acetyltransferase complex Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002126691 – 249Inhibitor of growth protein 4Add BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei127N6-acetyllysineCombined sources1
Modified residuei129N6-acetyllysineCombined sources1
Modified residuei133CitrullineBy similarity1
Modified residuei146N6-acetyllysineCombined sources1
Modified residuei148N6-acetyllysineCombined sources1
Modified residuei156N6-acetyllysineCombined sources1
Modified residuei166CitrullineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Citrullination

Proteomic databases

PaxDbiQ8C0D7.
PeptideAtlasiQ8C0D7.
PRIDEiQ8C0D7.

PTM databases

iPTMnetiQ8C0D7.
PhosphoSitePlusiQ8C0D7.

Expressioni

Tissue specificityi

Isoform 2, isoform 3, isoform 4 and isoform 5 are expressed in the mammary gland, ovary, spleen and muscle.1 Publication

Gene expression databases

BgeeiENSMUSG00000030330.
CleanExiMM_ING4.
GenevisibleiQ8C0D7. MM.

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 (By similarity). Isoform 3, isoform 4 and isoform 5 interact with BCL2A1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205719. 1 interactor.
IntActiQ8C0D7. 3 interactors.
MINTiMINT-1608801.
STRINGi10090.ENSMUSP00000032480.

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi207 – 210Combined sources4
Turni224 – 228Combined sources5
Turni240 – 242Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WENNMR-A188-245[»]
1WEUNMR-A168-245[»]
ProteinModelPortaliQ8C0D7.
SMRiQ8C0D7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8C0D7.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili25 – 118Sequence analysisAdd BLAST94

Motif

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

Domaini

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

Sequence similaritiesi

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

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.
InParanoidiQ8C0D7.
KOiK11346.
OMAiDNCKSAR.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ8C0D7.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028647. ING4.
IPR028651. ING_fam.
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.
[Graphical view]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF40. PTHR10333:SF40. 1 hit.
PfamiPF12998. ING. 1 hit.
[Graphical view]
SMARTiSM01408. ING. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C0D7-1) [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

        10         20         30         40         50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLRQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS
160 170 180 190 200
DEEAPKAAQK KLKLVRTSPE YGMPSVTFGS VHPSDVLDMP VDPNEPTYCL
210 220 230 240
CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK
Length:249
Mass (Da):28,528
Last modified:January 4, 2005 - v2
Checksum:i6C5C5582A249E412
GO
Isoform 2 (identifier: Q8C0D7-2) [UniParc]FASTAAdd to basket
Also known as: mINGh-M1 Publication

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):28,430
Checksum:iE3DAE9EB05C71924
GO
Isoform 3 (identifier: Q8C0D7-3) [UniParc]FASTAAdd to basket
Also known as: mINGh-L21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
     217-228: CSIEWFHFACVG → VRTVSSGLGEEL
     229-249: Missing.

Note: May be due to intron retention.
Show »
Length:227
Mass (Da):25,718
Checksum:iCDAC78AF142ACED3
GO
Isoform 4 (identifier: Q8C0D7-4) [UniParc]FASTAAdd to basket
Also known as: mINGh-L1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
     168-249: Missing.

Note: May be due to intron retention.
Show »
Length:166
Mass (Da):19,176
Checksum:iC1F7459388A4FACD
GO
Isoform 5 (identifier: Q8C0D7-5) [UniParc]FASTAAdd to basket
Also known as: mINGh-S1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     127-130: Missing.
     170-172: EYG → MER
     173-249: Missing.

Note: May be due to a competing acceptor splice site.
Show »
Length:168
Mass (Da):19,433
Checksum:i1B865B7AB7E683A8
GO

Sequence cautioni

The sequence BAC25009 differs from that shown. Reason: Frameshift at positions 226, 232, 239, 246 and 249.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti105A → S in BAC27489 (PubMed:16141072).Curated1
Sequence conflicti179G → S in BAC27489 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012520127 – 130Missing in isoform 5. 1 Publication4
Alternative sequenceiVSP_012521131K → S in isoform 2, isoform 3 and isoform 4. 3 Publications1
Alternative sequenceiVSP_012522132Missing in isoform 2, isoform 3 and isoform 4. 3 Publications1
Alternative sequenceiVSP_012523168 – 249Missing in isoform 4. 1 PublicationAdd BLAST82
Alternative sequenceiVSP_012524170 – 172EYG → MER in isoform 5. 1 Publication3
Alternative sequenceiVSP_012525173 – 249Missing in isoform 5. 1 PublicationAdd BLAST77
Alternative sequenceiVSP_012526217 – 228CSIEW…FACVG → VRTVSSGLGEEL in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_012527229 – 249Missing in isoform 3. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035880 mRNA. Translation: AAK63168.1.
AY035881 mRNA. Translation: AAK63169.1.
AY036107 mRNA. Translation: AAK64509.1.
AK002821 mRNA. Translation: BAC25009.1. Frameshift.
AK009267 mRNA. Translation: BAB26183.1.
AK031633 mRNA. Translation: BAC27489.1.
AK050522 mRNA. Translation: BAC34304.1.
BC009127 mRNA. Translation: AAH09127.1.
CCDSiCCDS39632.1. [Q8C0D7-2]
RefSeqiNP_579923.1. NM_133345.2. [Q8C0D7-2]
UniGeneiMm.262547.

Genome annotation databases

EnsembliENSMUST00000032480; ENSMUSP00000032480; ENSMUSG00000030330. [Q8C0D7-2]
ENSMUST00000112417; ENSMUSP00000108036; ENSMUSG00000030330. [Q8C0D7-5]
ENSMUST00000140131; ENSMUSP00000121519; ENSMUSG00000030330. [Q8C0D7-1]
GeneIDi28019.
KEGGimmu:28019.
UCSCiuc009dtd.1. mouse. [Q8C0D7-2]
uc009dtf.1. mouse. [Q8C0D7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY035880 mRNA. Translation: AAK63168.1.
AY035881 mRNA. Translation: AAK63169.1.
AY036107 mRNA. Translation: AAK64509.1.
AK002821 mRNA. Translation: BAC25009.1. Frameshift.
AK009267 mRNA. Translation: BAB26183.1.
AK031633 mRNA. Translation: BAC27489.1.
AK050522 mRNA. Translation: BAC34304.1.
BC009127 mRNA. Translation: AAH09127.1.
CCDSiCCDS39632.1. [Q8C0D7-2]
RefSeqiNP_579923.1. NM_133345.2. [Q8C0D7-2]
UniGeneiMm.262547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WENNMR-A188-245[»]
1WEUNMR-A168-245[»]
ProteinModelPortaliQ8C0D7.
SMRiQ8C0D7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205719. 1 interactor.
IntActiQ8C0D7. 3 interactors.
MINTiMINT-1608801.
STRINGi10090.ENSMUSP00000032480.

PTM databases

iPTMnetiQ8C0D7.
PhosphoSitePlusiQ8C0D7.

Proteomic databases

PaxDbiQ8C0D7.
PeptideAtlasiQ8C0D7.
PRIDEiQ8C0D7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032480; ENSMUSP00000032480; ENSMUSG00000030330. [Q8C0D7-2]
ENSMUST00000112417; ENSMUSP00000108036; ENSMUSG00000030330. [Q8C0D7-5]
ENSMUST00000140131; ENSMUSP00000121519; ENSMUSG00000030330. [Q8C0D7-1]
GeneIDi28019.
KEGGimmu:28019.
UCSCiuc009dtd.1. mouse. [Q8C0D7-2]
uc009dtf.1. mouse. [Q8C0D7-1]

Organism-specific databases

CTDi51147.
MGIiMGI:107307. Ing4.

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ8C0D7.
KOiK11346.
OMAiDNCKSAR.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ8C0D7.
TreeFamiTF352014.

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ8C0D7.
PROiQ8C0D7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030330.
CleanExiMM_ING4.
GenevisibleiQ8C0D7. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028647. ING4.
IPR028651. ING_fam.
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.
[Graphical view]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF40. PTHR10333:SF40. 1 hit.
PfamiPF12998. ING. 1 hit.
[Graphical view]
SMARTiSM01408. ING. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiING4_MOUSE
AccessioniPrimary (citable) accession number: Q8C0D7
Secondary accession number(s): Q8C1S7
, Q8K3Q5, Q8K3Q6, Q8K3Q7, Q9D7F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: November 2, 2016
This is version 132 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.