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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei362 – 3621Histone H3K4me3By similarity
Metal bindingi363 – 3631Zinc 1By similarity
Metal bindingi365 – 3651Zinc 1By similarity
Binding sitei373 – 3731Histone H3K4me3By similarity
Metal bindingi376 – 3761Zinc 2By similarity
Binding sitei377 – 3771Histone H3K4me3By similarity
Metal bindingi381 – 3811Zinc 2By similarity
Binding sitei385 – 3851Histone H3K4me3By similarity
Metal bindingi387 – 3871Zinc 1; via pros nitrogenBy similarity
Metal bindingi390 – 3901Zinc 1By similarity
Metal bindingi403 – 4031Zinc 2By similarity
Metal bindingi406 – 4061Zinc 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri360 – 40950PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • chromatin organization Source: Reactome
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201D → G in HNSCC. 1 Publication
VAR_021263

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiING3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Inhibitor of growth protein 3PRO_0000212665Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9NXR8.
MaxQBiQ9NXR8.
PaxDbiQ9NXR8.
PRIDEiQ9NXR8.

PTM databases

iPTMnetiQ9NXR8.
PhosphoSiteiQ9NXR8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NXR8.
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 interactions.
DIPiDIP-34303N.
IntActiQ9NXR8. 28 interactions.
STRINGi9606.ENSP00000320566.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi371 – 3744Combined sources
Helixi388 – 3914Combined sources
Helixi404 – 41411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4INMR-A362-418[»]
ProteinModelPortaliQ9NXR8.
SMRiQ9NXR8. Positions 2-102, 362-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NXR8.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi313 – 32917Poly-SerAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri360 – 40950PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOVERGENiHBG006607.
InParanoidiQ9NXR8.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG7RBZ9T.
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 AAF28979.1 differs from that shown. Reason: Frameshift at position 90. Curated
The sequence AAH73865.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251C → S (Ref. 2) Curated
Sequence conflicti325 – 3251C → S (PubMed:14702039).Curated
Sequence conflicti367 – 3671Q → QV in CAC48260 (PubMed:17974005).Curated
Sequence conflicti380 – 3801Missing in CAC48260 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201D → G in HNSCC. 1 Publication
VAR_021263

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 934VDRH → DLWN in isoform 3. 2 PublicationsVSP_012887
Alternative sequencei90 – 923VDR → QHF in isoform 2. 2 PublicationsVSP_012885
Alternative sequencei93 – 418326Missing in isoform 2. 2 PublicationsVSP_012886Add
BLAST
Alternative sequencei94 – 418325Missing in isoform 3. 2 PublicationsVSP_012888Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4INMR-A362-418[»]
ProteinModelPortaliQ9NXR8.
SMRiQ9NXR8. Positions 2-102, 362-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9NXR8.
PhosphoSiteiQ9NXR8.

Polymorphism and mutation databases

BioMutaiING3.

Proteomic databases

EPDiQ9NXR8.
MaxQBiQ9NXR8.
PaxDbiQ9NXR8.
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.
GeneCardsiING3.
HGNCiHGNC:14587. ING3.
HPAiHPA058060.
HPA067388.
MalaCardsiING3.
MIMi275355. phenotype.
607493. gene.
neXtProtiNX_Q9NXR8.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA29875.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
COG5034. LUCA.
GeneTreeiENSGT00550000074538.
HOVERGENiHBG006607.
InParanoidiQ9NXR8.
KOiK11319.
OMAiNEFFMNA.
OrthoDBiEOG7RBZ9T.
PhylomeDBiQ9NXR8.
TreeFamiTF106497.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiING3. human.
EvolutionaryTraceiQ9NXR8.
GeneWikiiING3.
GenomeRNAii54556.
NextBioi57036.
PROiQ9NXR8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NXR8.
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...

Publicationsi

« Hide 'large scale' publications
  1. "A novel PHD-finger motif protein, p47ING3, modulates p53-mediated transcription, cell cycle control, and apoptosis."
    Nagashima M., Shiseki M., Pedeux R.M., Okamura S., Kitahama-Shiseki M., Miura K., Yokota J., Harris C.C.
    Oncogene 22:343-350(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ROLE IN P53 MEDIATED GROWTH SUPPRESSION.
  2. "Cloning and characterization of p47ING3, a new member of the p33ING1 family of p53 regulators."
    Zenklusen J.C., Green E.D.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Skeletal muscle.
  4. "Human partial CDS from CD34+ stem cells."
    Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Umbilical cord blood.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 2 AND 3).
    Tissue: Blood, Liver, Lung, Pancreas and Urinary bladder.
  8. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-92, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "The highly conserved and multifunctional NuA4 HAT complex."
    Doyon Y., Cote J.
    Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON NUA4 COMPLEX.
  10. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX.
  11. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
    Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
    Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN NUA4 COMPLEX.
  12. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
  13. "Arabidopsis ING and Alfin1-like protein families localize to the nucleus and bind to H3K4me3/2 via plant homeodomain fingers."
    Lee W.Y., Lee D., Chung W.I., Kwon C.S.
    Plant J. 58:511-524(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
  17. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Solution structure of PHD domain in inhibitor of growth protein 3 (ING3) antigen 7."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 362-418.
  19. "Allelic loss and reduced expression of the ING3, a candidate tumor suppressor gene at 7q31, in human head and neck cancers."
    Gunduz M., Ouchida M., Fukushima K., Ito S., Jitsumori Y., Nakashima T., Nagai N., Nishizaki K., Shimizu K.
    Oncogene 21:4462-4470(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HNSCC GLY-20.

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: May 11, 2016
This is version 141 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.