Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inhibitor of growth protein 3

Gene

ING3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei362Histone H3K4me3By similarity1
Metal bindingi363Zinc 1By similarity1
Metal bindingi365Zinc 1By similarity1
Binding sitei373Histone H3K4me3By similarity1
Metal bindingi376Zinc 2By similarity1
Binding sitei377Histone H3K4me3By similarity1
Metal bindingi381Zinc 2By similarity1
Binding sitei385Histone H3K4me3By similarity1
Metal bindingi387Zinc 1; via pros nitrogenBy similarity1
Metal bindingi390Zinc 1By similarity1
Metal bindingi403Zinc 2By similarity1
Metal bindingi406Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri360 – 409PHD-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • histone H2A acetylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • regulation of growth Source: UniProtKB-KW
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 3
Alternative name(s):
p47ING3
Gene namesi
Name:ING3
ORF Names:HSPC301
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:14587. ING3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • Piccolo NuA4 histone acetyltransferase complex Source: UniProtKB
  • Swr1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Squamous cell carcinoma of the head and neck (HNSCC)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
See also OMIM:275355
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02126320D → G in HNSCC. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi54556.
MalaCardsiING3.
MIMi275355. phenotype.
OpenTargetsiENSG00000071243.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA29875.

Polymorphism and mutation databases

BioMutaiING3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002126651 – 418Inhibitor of growth protein 3Add BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei181N6-acetyllysineBy similarity1
Modified residuei264N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9NXR8.
MaxQBiQ9NXR8.
PaxDbiQ9NXR8.
PeptideAtlasiQ9NXR8.
PRIDEiQ9NXR8.

PTM databases

iPTMnetiQ9NXR8.
PhosphoSitePlusiQ9NXR8.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, lung, ovaries, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus.

Gene expression databases

BgeeiENSG00000071243.
CleanExiHS_ING3.
ExpressionAtlasiQ9NXR8. baseline and differential.
GenevisibleiQ9NXR8. HS.

Organism-specific databases

HPAiHPA058060.
HPA067388.

Interactioni

Subunit structurei

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Component of a SWR1-like complex.6 Publications

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120041. 50 interactors.
DIPiDIP-34303N.
IntActiQ9NXR8. 28 interactors.
STRINGi9606.ENSP00000320566.

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi371 – 374Combined sources4
Helixi388 – 391Combined sources4
Helixi404 – 414Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X4INMR-A362-418[»]
ProteinModelPortaliQ9NXR8.
SMRiQ9NXR8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NXR8.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi313 – 329Poly-SerAdd BLAST17

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.2 Publications

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 fingeri360 – 409PHD-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOVERGENiHBG006607.
InParanoidiQ9NXR8.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ9NXR8.
TreeFamiTF106497.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028651. 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.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NXR8-1) [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
MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA
60 70 80 90 100
KKNKPEWREE QMASIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE
110 120 130 140 150
LAKFKMELEA DNAGITEILE RRSLELDTPS QPVNNHHAHS HTPVEKRKYN
160 170 180 190 200
PTSHHTTTDH IPEKKFKSEA LLSTLTSDAS KENTLGCRNN NSTASSNNAY
210 220 230 240 250
NVNSSQPLGS YNIGSLSSGT GAGAITMAAA QAVQATAQMK EGRRTSSLKA
260 270 280 290 300
SYEAFKNNDF QLGKEFSMAR ETVGYSSSSA LMTTLTQNAS SSAADSRSGR
310 320 330 340 350
KSKNNNKSSS QQSSSSSSSS SLSSCSSSST VVQEISQQTT VVPESDSNSQ
360 370 380 390 400
VDWTYDPNEP RYCICNQVSY GEMVGCDNQD CPIEWFHYGC VGLTEAPKGK
410
WYCPQCTAAM KRRGSRHK
Length:418
Mass (Da):46,743
Last modified:February 15, 2005 - v2
Checksum:iAA127416912D87F5
GO
Isoform 2 (identifier: Q9NXR8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-92: VDR → QHF
     93-418: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:92
Mass (Da):11,333
Checksum:iEC143EFFA9888741
GO
Isoform 3 (identifier: Q9NXR8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-93: VDRH → DLWN
     94-418: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:93
Mass (Da):11,449
Checksum:i0966A2E28FA98887
GO

Sequence cautioni

The sequence AAF28979 differs from that shown. Reason: Frameshift at position 90.Curated
The sequence AAH73865 differs from that shown. Intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti325C → S (Ref. 2) Curated1
Sequence conflicti325C → S (PubMed:14702039).Curated1
Sequence conflicti367Q → QV in CAC48260 (PubMed:17974005).Curated1
Sequence conflicti380Missing in CAC48260 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02126320D → G in HNSCC. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01288790 – 93VDRH → DLWN in isoform 3. 2 Publications4
Alternative sequenceiVSP_01288590 – 92VDR → QHF in isoform 2. 2 Publications3
Alternative sequenceiVSP_01288693 – 418Missing in isoform 2. 2 PublicationsAdd BLAST326
Alternative sequenceiVSP_01288894 – 418Missing in isoform 3. 2 PublicationsAdd BLAST325

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074968 mRNA. Translation: AAG12172.1.
AY007790 mRNA. Translation: AAG23285.1.
AK000096 mRNA. Translation: BAA90942.1.
AK291905 mRNA. Translation: BAF84594.1.
AF161419 mRNA. Translation: AAF28979.1. Frameshift.
AL603623 Transcribed RNA. Translation: CAC48260.2.
AC004537 Genomic DNA. Translation: AAQ93373.1.
BC009777 mRNA. Translation: AAH09777.1.
BC009777 mRNA. Translation: AAQ93374.1.
BC010851 mRNA. Translation: AAH10851.1.
BC062634 mRNA. Translation: AAH09776.1.
BC062634 mRNA. Translation: AAH62634.1.
BC073865 mRNA. Translation: AAH73865.1. Sequence problems.
BC093091 mRNA. Translation: AAH93091.1.
BC093689 mRNA. Translation: AAH93689.1.
BC101609 mRNA. Translation: AAI01610.1.
CCDSiCCDS35497.1. [Q9NXR8-2]
CCDS5778.1. [Q9NXR8-1]
RefSeqiNP_061944.2. NM_019071.2. [Q9NXR8-1]
NP_938008.1. NM_198267.1. [Q9NXR8-2]
UniGeneiHs.489811.

Genome annotation databases

EnsembliENST00000315870; ENSP00000320566; ENSG00000071243. [Q9NXR8-1]
ENST00000339121; ENSP00000341697; ENSG00000071243. [Q9NXR8-2]
ENST00000427726; ENSP00000410406; ENSG00000071243. [Q9NXR8-3]
GeneIDi54556.
KEGGihsa:54556.
UCSCiuc003vjl.4. human. [Q9NXR8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074968 mRNA. Translation: AAG12172.1.
AY007790 mRNA. Translation: AAG23285.1.
AK000096 mRNA. Translation: BAA90942.1.
AK291905 mRNA. Translation: BAF84594.1.
AF161419 mRNA. Translation: AAF28979.1. Frameshift.
AL603623 Transcribed RNA. Translation: CAC48260.2.
AC004537 Genomic DNA. Translation: AAQ93373.1.
BC009777 mRNA. Translation: AAH09777.1.
BC009777 mRNA. Translation: AAQ93374.1.
BC010851 mRNA. Translation: AAH10851.1.
BC062634 mRNA. Translation: AAH09776.1.
BC062634 mRNA. Translation: AAH62634.1.
BC073865 mRNA. Translation: AAH73865.1. Sequence problems.
BC093091 mRNA. Translation: AAH93091.1.
BC093689 mRNA. Translation: AAH93689.1.
BC101609 mRNA. Translation: AAI01610.1.
CCDSiCCDS35497.1. [Q9NXR8-2]
CCDS5778.1. [Q9NXR8-1]
RefSeqiNP_061944.2. NM_019071.2. [Q9NXR8-1]
NP_938008.1. NM_198267.1. [Q9NXR8-2]
UniGeneiHs.489811.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X4INMR-A362-418[»]
ProteinModelPortaliQ9NXR8.
SMRiQ9NXR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120041. 50 interactors.
DIPiDIP-34303N.
IntActiQ9NXR8. 28 interactors.
STRINGi9606.ENSP00000320566.

PTM databases

iPTMnetiQ9NXR8.
PhosphoSitePlusiQ9NXR8.

Polymorphism and mutation databases

BioMutaiING3.

Proteomic databases

EPDiQ9NXR8.
MaxQBiQ9NXR8.
PaxDbiQ9NXR8.
PeptideAtlasiQ9NXR8.
PRIDEiQ9NXR8.

Protocols and materials databases

DNASUi54556.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315870; ENSP00000320566; ENSG00000071243. [Q9NXR8-1]
ENST00000339121; ENSP00000341697; ENSG00000071243. [Q9NXR8-2]
ENST00000427726; ENSP00000410406; ENSG00000071243. [Q9NXR8-3]
GeneIDi54556.
KEGGihsa:54556.
UCSCiuc003vjl.4. human. [Q9NXR8-1]

Organism-specific databases

CTDi54556.
DisGeNETi54556.
GeneCardsiING3.
HGNCiHGNC:14587. ING3.
HPAiHPA058060.
HPA067388.
MalaCardsiING3.
MIMi275355. phenotype.
607493. gene.
neXtProtiNX_Q9NXR8.
OpenTargetsiENSG00000071243.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA29875.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOVERGENiHBG006607.
InParanoidiQ9NXR8.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ9NXR8.
TreeFamiTF106497.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiING3. human.
EvolutionaryTraceiQ9NXR8.
GeneWikiiING3.
GenomeRNAii54556.
PROiQ9NXR8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000071243.
CleanExiHS_ING3.
ExpressionAtlasiQ9NXR8. baseline and differential.
GenevisibleiQ9NXR8. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028651. 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.
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 nameiING3_HUMAN
AccessioniPrimary (citable) accession number: Q9NXR8
Secondary accession number(s): A8K790
, O60394, Q567P3, Q6GMT3, Q7Z762, Q969G0, Q96DT4, Q9HC99, Q9P081
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 146 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.