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Protein

Inhibitor of growth protein 3

Gene

Ing3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei365Histone H3K4me3By similarity1
Metal bindingi366Zinc 1By similarity1
Metal bindingi368Zinc 1By similarity1
Binding sitei376Histone H3K4me3By similarity1
Metal bindingi379Zinc 2By similarity1
Binding sitei380Histone H3K4me3By similarity1
Metal bindingi384Zinc 2By similarity1
Binding sitei388Histone H3K4me3By similarity1
Metal bindingi390Zinc 1; via pros nitrogenBy similarity1
Metal bindingi393Zinc 1By similarity1
Metal bindingi406Zinc 2By similarity1
Metal bindingi409Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri363 – 412PHD-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 3
Alternative name(s):
p47ING3
Gene namesi
Name:Ing3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1919027. Ing3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002126661 – 421Inhibitor of growth protein 3Add BLAST421

Amino acid modifications

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

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ8VEK6.
MaxQBiQ8VEK6.
PaxDbiQ8VEK6.
PRIDEiQ8VEK6.

PTM databases

iPTMnetiQ8VEK6.
PhosphoSitePlusiQ8VEK6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029670.
CleanExiMM_ING3.
ExpressionAtlasiQ8VEK6. baseline and differential.
GenevisibleiQ8VEK6. MM.

Interactioni

Subunit structurei

Interacts with H3K4me3 and to a lesser extent with H3K4me2 (By similarity). 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. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Component of a SWR1-like complex (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi214920. 3 interactors.
IntActiQ8VEK6. 3 interactors.
STRINGi10090.ENSMUSP00000031680.

Structurei

3D structure databases

ProteinModelPortaliQ8VEK6.
SMRiQ8VEK6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi313 – 324Poly-SerAdd BLAST12

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.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 fingeri363 – 412PHD-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239725.
HOVERGENiHBG006607.
InParanoidiQ8VEK6.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ8VEK6.
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]

Sequencei

Sequence statusi: Complete.

Q8VEK6-1 [UniParc]FASTAAdd to basket

« 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 RRSLELDAPS QPVNNHHAHS HTPVEKRKYN
160 170 180 190 200
PTSHHAAADH IPEKKFKSEA LLSTLTSDAS KENTLGCRNN NSTASCNNAY
210 220 230 240 250
NVNSSQPLAS YNIGSLSSGA GAGAITMAAA QAVQATAQMK EGRRTSSLKA
260 270 280 290 300
SYEAFKNNDF QLGKEFSIPR ETAGYSSSSA LMTTLTQNAS SSATDSRSGR
310 320 330 340 350
KSKNNTKSSS QQSSSSSSSS SSSSLSLCSS SSTVVQEVSQ QATVVPESDS
360 370 380 390 400
NSQVDWTYDP NEPRYCICNQ VSYGEMVGCD NQDCPIEWFH YGCVGLTEAP
410 420
KGKWFCPQCT AAMKRRGSRH K
Length:421
Mass (Da):46,847
Last modified:February 15, 2005 - v2
Checksum:iE786062A26E3BF96
GO

Sequence cautioni

The sequence AAG23286 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH18342 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAC38021 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti257N → T in AAG23286 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007791 mRNA. Translation: AAG23286.1. Different initiation.
AK080787 mRNA. Translation: BAC38021.1. Different initiation.
BC005721 mRNA. Translation: AAH05721.1.
BC018342 mRNA. Translation: AAH18342.1. Different initiation.
CCDSiCCDS39434.1.
RefSeqiNP_001297990.1. NM_001311061.1.
NP_076115.3. NM_023626.4.
UniGeneiMm.39999.

Genome annotation databases

EnsembliENSMUST00000031680; ENSMUSP00000031680; ENSMUSG00000029670.
GeneIDi71777.
KEGGimmu:71777.
UCSCiuc009bat.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007791 mRNA. Translation: AAG23286.1. Different initiation.
AK080787 mRNA. Translation: BAC38021.1. Different initiation.
BC005721 mRNA. Translation: AAH05721.1.
BC018342 mRNA. Translation: AAH18342.1. Different initiation.
CCDSiCCDS39434.1.
RefSeqiNP_001297990.1. NM_001311061.1.
NP_076115.3. NM_023626.4.
UniGeneiMm.39999.

3D structure databases

ProteinModelPortaliQ8VEK6.
SMRiQ8VEK6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214920. 3 interactors.
IntActiQ8VEK6. 3 interactors.
STRINGi10090.ENSMUSP00000031680.

PTM databases

iPTMnetiQ8VEK6.
PhosphoSitePlusiQ8VEK6.

Proteomic databases

EPDiQ8VEK6.
MaxQBiQ8VEK6.
PaxDbiQ8VEK6.
PRIDEiQ8VEK6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031680; ENSMUSP00000031680; ENSMUSG00000029670.
GeneIDi71777.
KEGGimmu:71777.
UCSCiuc009bat.1. mouse.

Organism-specific databases

CTDi54556.
MGIiMGI:1919027. Ing3.

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239725.
HOVERGENiHBG006607.
InParanoidiQ8VEK6.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG091G0J8Y.
PhylomeDBiQ8VEK6.
TreeFamiTF106497.

Miscellaneous databases

PROiQ8VEK6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029670.
CleanExiMM_ING3.
ExpressionAtlasiQ8VEK6. baseline and differential.
GenevisibleiQ8VEK6. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q8VEK6
Secondary accession number(s): Q99JS6, Q9ERB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.