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Q8C0D7 (ING4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibitor of growth protein 4
Alternative name(s):
p29ING4
Gene names
Name:Ing4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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) By similarity.

Subunit structure

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.

Subcellular location

Nucleus By similarity.

Domain

The PHD-type zinc finger mediates the binding to H3K4me3 By similarity.

The N-terminal coiled-coil domain mediates homodimerization By similarity.

Post-translational modification

Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation By similarity.

Sequence similarities

Belongs to the ING family.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence BAC25009.1 differs from that shown. Reason: Frameshift at positions 226, 232, 239, 246 and 249.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
   PTMAcetylation
Citrullination
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K12 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K5 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K8 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componenthistone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functiontranscription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8C0D7-1)

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.
Isoform 2 (identifier: Q8C0D7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
Note: May be due to a competing donor splice site.
Isoform 3 (identifier: Q8C0D7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
     217-228: CSIEWFHFACVG → VRTVSSGLGEEL
     229-249: Missing.
Note: May be due to intron retention.
Isoform 4 (identifier: Q8C0D7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: K → S
     132-132: Missing.
     168-249: Missing.
Note: May be due to intron retention.
Isoform 5 (identifier: Q8C0D7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     127-130: Missing.
     170-172: EYG → MER
     173-249: Missing.
Note: May be due to a competing acceptor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Inhibitor of growth protein 4
PRO_0000212669

Regions

Zinc finger196 – 24550PHD-type
Coiled coil25 – 11894 Potential
Motif127 – 14822Bipartite nuclear localization signal By similarity

Sites

Binding site1981Histone H3K4me3 By similarity
Binding site2091Histone H3K4me3 By similarity
Binding site2131Histone H3K4me3 By similarity
Binding site2211Histone H3K4me3 By similarity

Amino acid modifications

Modified residue1121N6-acetyllysine By similarity
Modified residue1271N6-acetyllysine Ref.4
Modified residue1291N6-acetyllysine Ref.4
Modified residue1331Citrulline By similarity
Modified residue1461N6-acetyllysine Ref.4
Modified residue1481N6-acetyllysine Ref.4
Modified residue1561N6-acetyllysine Ref.4
Modified residue1661Citrulline By similarity

Natural variations

Alternative sequence127 – 1304Missing in isoform 5.
VSP_012520
Alternative sequence1311K → S in isoform 2, isoform 3 and isoform 4.
VSP_012521
Alternative sequence1321Missing in isoform 2, isoform 3 and isoform 4.
VSP_012522
Alternative sequence168 – 24982Missing in isoform 4.
VSP_012523
Alternative sequence170 – 1723EYG → MER in isoform 5.
VSP_012524
Alternative sequence173 – 24977Missing in isoform 5.
VSP_012525
Alternative sequence217 – 22812CSIEW…FACVG → VRTVSSGLGEEL in isoform 3.
VSP_012526
Alternative sequence229 – 24921Missing in isoform 3.
VSP_012527

Experimental info

Sequence conflict1051A → S in BAC27489. Ref.2
Sequence conflict1791G → S in BAC27489. Ref.2

Secondary structure

....... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 6C5C5582A249E412

FASTA24928,528
        10         20         30         40         50         60 
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 

        70         80         90        100        110        120 
KLALLRQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 

       130        140        150        160        170        180 
YDSSSSKGKK KGRTQKEKKA ARARSKGKNS DEEAPKAAQK KLKLVRTSPE YGMPSVTFGS 

       190        200        210        220        230        240 
VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP 


RCSQERKKK 

« Hide

Isoform 2 [UniParc].

Checksum: E3DAE9EB05C71924
Show »

FASTA24828,430
Isoform 3 [UniParc].

Checksum: CDAC78AF142ACED3
Show »

FASTA22725,718
Isoform 4 [UniParc].

Checksum: C1F7459388A4FACD
Show »

FASTA16619,176
Isoform 5 [UniParc].

Checksum: 1B865B7AB7E683A8
Show »

FASTA16819,433

References

« Hide 'large scale' references
[1]"Cloning of mouse ING1 homolog splicing variants."
Ha S., Lee S., Choi Y.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
Strain: ICR.
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Kidney, Pancreas, Testis and Tongue.
[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] (ISOFORM 2).
Strain: 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-127; LYS-129; LYS-146; LYS-148 AND LYS-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[5]"Solution structure of PHD domain in ING1-like protein BAC25079."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 168-245.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY035880 mRNA. Translation: AAK63168.1.
AY035881 mRNA. Translation: AAK63169.1.
AY036107 mRNA. Translation: AAK64509.1.
AK002821 mRNA. Translation: BAC25009.1. Frameshift.
AK009267 mRNA. Translation: BAB26183.1.
AK031633 mRNA. Translation: BAC27489.1.
AK050522 mRNA. Translation: BAC34304.1.
BC009127 mRNA. Translation: AAH09127.1.
CCDSCCDS39632.1. [Q8C0D7-2]
RefSeqNP_579923.1. NM_133345.2. [Q8C0D7-2]
UniGeneMm.262547.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WENNMR-A188-245[»]
1WEUNMR-A168-245[»]
ProteinModelPortalQ8C0D7.
SMRQ8C0D7. Positions 4-105, 169-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205719. 1 interaction.
IntActQ8C0D7. 3 interactions.
MINTMINT-1608801.

PTM databases

PhosphoSiteQ8C0D7.

Proteomic databases

PRIDEQ8C0D7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032480; ENSMUSP00000032480; ENSMUSG00000030330. [Q8C0D7-2]
ENSMUST00000112417; ENSMUSP00000108036; ENSMUSG00000030330. [Q8C0D7-5]
ENSMUST00000140131; ENSMUSP00000121519; ENSMUSG00000030330. [Q8C0D7-1]
ENSMUST00000140883; ENSMUSP00000118561; ENSMUSG00000030330. [Q8C0D7-4]
ENSMUST00000151125; ENSMUSP00000119709; ENSMUSG00000030330. [Q8C0D7-3]
GeneID28019.
KEGGmmu:28019.
UCSCuc009dtd.1. mouse. [Q8C0D7-2]
uc009dtf.1. mouse. [Q8C0D7-1]

Organism-specific databases

CTD51147.
MGIMGI:107307. Ing4.

Phylogenomic databases

eggNOGCOG5034.
GeneTreeENSGT00550000074538.
HOGENOMHOG000239724.
HOVERGENHBG006607.
InParanoidQ8C0D7.
KOK11346.
OMAKLKFVRT.
OrthoDBEOG7RBZ9T.
PhylomeDBQ8C0D7.
TreeFamTF352014.

Gene expression databases

BgeeQ8C0D7.
CleanExMM_ING4.
GenevestigatorQ8C0D7.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028647. ING4.
IPR028651. ING_fam.
IPR024610. ING_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF40. PTHR10333:SF40. 1 hit.
PfamPF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8C0D7.
NextBio306534.
PROQ8C0D7.
SOURCESearch...

Entry information

Entry nameING4_MOUSE
AccessionPrimary (citable) accession number: Q8C0D7
Secondary accession number(s): Q8C1S7 expand/collapse secondary AC list , Q8K3Q5, Q8K3Q6, Q8K3Q7, Q9D7F9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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