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
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei365 – 3651Histone H3K4me3By similarity
Metal bindingi366 – 3661Zinc 1By similarity
Metal bindingi368 – 3681Zinc 1By similarity
Binding sitei376 – 3761Histone H3K4me3By similarity
Metal bindingi379 – 3791Zinc 2By similarity
Binding sitei380 – 3801Histone H3K4me3By similarity
Metal bindingi384 – 3841Zinc 2By similarity
Binding sitei388 – 3881Histone H3K4me3By similarity
Metal bindingi390 – 3901Zinc 1; via pros nitrogenBy similarity
Metal bindingi393 – 3931Zinc 1By similarity
Metal bindingi406 – 4061Zinc 2By similarity
Metal bindingi409 – 4091Zinc 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri363 – 41250PHD-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Inhibitor of growth protein 3PRO_0000212666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki167 – 167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei181 – 1811N6-acetyllysineCombined sources
Modified residuei264 – 2641N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ8VEK6.
MaxQBiQ8VEK6.
PaxDbiQ8VEK6.
PRIDEiQ8VEK6.

PTM databases

iPTMnetiQ8VEK6.
PhosphoSiteiQ8VEK6.

Expressioni

Gene expression databases

BgeeiQ8VEK6.
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 interactions.
IntActiQ8VEK6. 3 interactions.
STRINGi10090.ENSMUSP00000031680.

Structurei

3D structure databases

ProteinModelPortaliQ8VEK6.
SMRiQ8VEK6. Positions 2-102, 365-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi313 – 32412Poly-SerAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri363 – 41250PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239725.
HOVERGENiHBG006607.
InParanoidiQ8VEK6.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG7RBZ9T.
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 AAG23286.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH18342.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC38021.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571N → T in AAG23286 (Ref. 1) Curated

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. Positions 2-102, 365-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214920. 3 interactions.
IntActiQ8VEK6. 3 interactions.
STRINGi10090.ENSMUSP00000031680.

PTM databases

iPTMnetiQ8VEK6.
PhosphoSiteiQ8VEK6.

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.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ8VEK6.
TreeFamiTF106497.

Miscellaneous databases

NextBioi334493.
PROiQ8VEK6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VEK6.
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...

Publicationsi

« Hide 'large scale' publications
  1. Zenklusen J.C., Green E.D.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-181 AND LYS-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

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: May 11, 2016
This is version 124 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.