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Protein

Inhibitor of growth protein 4

Gene

ING4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei197Histone H3K4me3By similarity1
Metal bindingi198Zinc 1By similarity1
Metal bindingi200Zinc 1By similarity1
Binding sitei208Histone H3K4me3By similarity1
Metal bindingi211Zinc 2By similarity1
Binding sitei212Histone H3K4me3By similarity1
Metal bindingi216Zinc 2By similarity1
Metal bindingi222Zinc 1; via pros nitrogenBy similarity1
Metal bindingi225Zinc 1By similarity1
Metal bindingi238Zinc 2By similarity1
Metal bindingi241Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri195 – 244PHD-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

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 4
Alternative name(s):
p29ING4
Gene namesi
Name:ING4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002126671 – 248Inhibitor of growth protein 4Add BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei127N6-acetyllysineBy similarity1
Modified residuei129N6-acetyllysineBy similarity1
Modified residuei132CitrullineBy similarity1
Modified residuei145N6-acetyllysineBy similarity1
Modified residuei147N6-acetyllysineBy similarity1
Modified residuei155N6-acetyllysineBy similarity1
Modified residuei165CitrullineBy 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

PaxDbiQ3T095.
PRIDEiQ3T095.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022686.

Structurei

3D structure databases

ProteinModelPortaliQ3T095.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi127 – 147Bipartite nuclear localization signalBy similarityAdd BLAST21

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 fingeri195 – 244PHD-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ3T095.
KOiK11346.

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]

Sequencei

Sequence statusi: Complete.

Q3T095-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLASEYM
60 70 80 90 100
SSARSRSSEE KLALLRQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK SRTQKEKKAA RARSKGKNSD
160 170 180 190 200
EEAPKAAQKK LKLVRTSPEY GMPSVTFGSV HPSDVLDMPV DPNEPTYCLC
210 220 230 240
HQVSYGEMIG CDNPDCSIER FHFACVGLTT KPRGKWFCPR CSQERKKK
Length:248
Mass (Da):28,429
Last modified:October 11, 2005 - v1
Checksum:iDA0C4EBC3211E1BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102494 mRNA. Translation: AAI02495.1.
RefSeqiNP_001030466.1. NM_001035389.2.
UniGeneiBt.48844.

Genome annotation databases

GeneIDi532483.
KEGGibta:532483.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102494 mRNA. Translation: AAI02495.1.
RefSeqiNP_001030466.1. NM_001035389.2.
UniGeneiBt.48844.

3D structure databases

ProteinModelPortaliQ3T095.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022686.

Proteomic databases

PaxDbiQ3T095.
PRIDEiQ3T095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi532483.
KEGGibta:532483.

Organism-specific databases

CTDi51147.

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ3T095.
KOiK11346.

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_BOVIN
AccessioniPrimary (citable) accession number: Q3T095
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Lacks the Trp (here Arg-220), a conserved feature of the aromatic cage required for the interaction with histone H3K4me3/2.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.