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Q9H160 (ING2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibitor of growth protein 2
Alternative name(s):
Inhibitor of growth 1-like protein
Short name=ING1Lp
p32
p33ING2
Gene names
Name:ING2
Synonyms:ING1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs). Ref.2 Ref.9

Subunit structure

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2. Ref.8 Ref.11 Ref.12

Subcellular location

Nucleus. Note: Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns5P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm. Ref.9

Tissue specificity

Widely expressed. Higher expressed in colon-cancer tumor than in normal colon tissues. Ref.1

Induction

Induced by the DNA-damaging agents etoposide and neocarzinostatin. Ref.2

Domain

The PHD-type zinc finger mediates the binding to H3K4me3. Ref.12

The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P). Ref.12

Post-translational modification

Sumoylation enhances its association with SIN3A and is required for binding to some target gene promoters, this is the case for TMEM71. Ref.13

Sequence similarities

Belongs to the ING family.

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Biological processGrowth regulation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

male germ-line stem cell division

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

male meiosis I

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from electronic annotation. Source: InterPro

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Traceable author statement PubMed 21124965. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18334480. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 18334480. Source: UniProtKB

regulation of cellular senescence

Non-traceable author statement PubMed 21124965. Source: BHF-UCL

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of response to DNA damage stimulus

Non-traceable author statement PubMed 21124965. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15243141. Source: UniProtKB

seminiferous tubule development

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

signal transduction

Traceable author statement Ref.1. Source: ProtInc

sperm motility

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

spermatid development

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

spermatogenesis

Inferred from sequence or structural similarity PubMed 21124965. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCCAAT-binding factor complex

Inferred from direct assay PubMed 15243141. Source: UniProtKB

Sin3 complex

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15243141PubMed 18334480. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15243141. Source: UniProtKB

chromatin binding

Traceable author statement Ref.1. Source: ProtInc

methylated histone binding

Inferred from direct assay Ref.12. Source: UniProtKB

phosphatidylinositol binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18334480. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 18334480. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PCNAP120043EBI-389787,EBI-358311
SMURF1Q9HCE74EBI-389787,EBI-976466

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform ING2a (identifier: Q9H160-1)

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 ING2b (identifier: Q9H160-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: MLGQQQQQLY...LRELDNKYQE → MDQDGDQQLGPSRILAPQ
Note: Low expression except in testis, where it reaches half of ING2a levels.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 280280Inhibitor of growth protein 2
PRO_0000212663

Regions

Zinc finger212 – 26150PHD-type
Region264 – 28017PBR
Coiled coil48 – 12073 Potential

Sites

Binding site2141Histone H3K4me3 By similarity
Binding site2251Histone H3K4me3 By similarity
Binding site2291Histone H3K4me3 By similarity
Binding site2371Histone H3K4me3 By similarity

Amino acid modifications

Cross-link195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.13

Natural variations

Alternative sequence1 – 5858MLGQQ…NKYQE → MDQDGDQQLGPSRILAPQ in isoform ING2b.
VSP_047821

Experimental info

Sequence conflict211S → T in CAC20567. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform ING2a [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: DC85A6ECAF7A5D81

FASTA28032,808
        10         20         30         40         50         60 
MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR ELDNKYQETL 

        70         80         90        100        110        120 
KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK IQIVTQMLEL VENRARQMEL 

       130        140        150        160        170        180 
HSQCFQDPAE SERASDKAKM DSSQPERSSR RPRRQRTSES RDLCHMANGI EDCDDQPPKE 

       190        200        210        220        230        240 
KKSKSAKKKK RSKAKQEREA SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF 

       250        260        270        280 
SCVSLTYKPK GKWYCPKCRG DNEKTMDKST EKTKKDRRSR 

« Hide

Isoform ING2b [UniParc].

Checksum: A445AEC5BBFA3B35
Show »

FASTA24027,984

References

« Hide 'large scale' references
[1]"Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor."
Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M.
Cytogenet. Cell Genet. 83:232-235(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM ING2A), TISSUE SPECIFICITY.
[2]"DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53."
Nagashima M., Shiseki M., Miura K., Hagiwara K., Linke S.P., Pedeux R., Wang X.W., Yokota J., Riabowol K., Harris C.C.
Proc. Natl. Acad. Sci. U.S.A. 98:9671-9676(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A), FUNCTION, INDUCTION.
[3]"A novel ING2 isoform, ING2b, synergizes with ING2a to prevent cell cycle arrest and apoptosis."
Unoki M., Kumamoto K., Robles A.I., Shen J.C., Zheng Z.-M., Harris C.C.
FEBS Lett. 582:3868-3874(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2B), ALTERNATIVE SPLICING.
[4]"ING2, a new possible gene suppressor tumor."
Cal S., Freije J.M., Lopez-Otin C.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A).
Tissue: Mammary tumor.
[5]"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. expand/collapse author list , 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] (ISOFORM ING2B).
Tissue: Amygdala.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [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] (ISOFORM ING2A).
Tissue: Lung.
[8]"Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)."
Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.
Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-44, IDENTIFICATION IN MSIN3A-LIKE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor."
Gozani O., Karuman P., Jones D.R., Ivanov D., Cha J., Lugovskoy A.A., Baird C.L., Zhu H., Field S.J., Lessnick S.L., Villasenor J., Mehrotra B., Chen J., Rao V.R., Brugge J.S., Ferguson C.G., Payrastre B., Myszka D.G. expand/collapse author list , Cantley L.C., Wagner G., Divecha N., Prestwich G.D., Yuan J.
Cell 114:99-111(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"The polybasic region that follows the plant homeodomain zinc finger 1 of Pf1 is necessary and sufficient for specific phosphoinositide binding."
Kaadige M.R., Ayer D.E.
J. Biol. Chem. 281:28831-28836(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHOINOSITIDE-BINDING.
[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 MSIN3A COMPLEX.
[12]"ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression."
Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y. expand/collapse author list , Cote J., Chua K.F., Gozani O.
Nature 442:96-99(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
[13]"Sumoylation of ING2 regulates the transcription mediated by Sin3A."
Ythier D., Larrieu D., Binet R., Binda O., Brambilla C., Gazzeri S., Pedeux R.
Oncogene 29:5946-5956(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-195.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012853 mRNA. Translation: BAA36419.1.
AF053537 mRNA. Translation: AAG11395.1.
AF062748, AF062747 Genomic DNA. Translation: AAG11396.1.
AB196793 mRNA. Translation: BAF30476.1.
AJ006851 mRNA. Translation: CAC20567.1.
AK294310 mRNA. Translation: BAH11731.1.
AC107214 Genomic DNA. No translation available.
BC030128 mRNA. Translation: AAH30128.1.
CCDSCCDS3833.1. [Q9H160-1]
RefSeqNP_001555.1. NM_001564.3. [Q9H160-1]
UniGeneHs.107153.

3D structure databases

ProteinModelPortalQ9H160.
SMRQ9H160. Positions 31-119, 211-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109834. 31 interactions.
IntActQ9H160. 9 interactions.
MINTMINT-2830779.
STRING9606.ENSP00000307183.

PTM databases

PhosphoSiteQ9H160.

Polymorphism databases

DMDM59798471.

Proteomic databases

MaxQBQ9H160.
PaxDbQ9H160.
PRIDEQ9H160.

Protocols and materials databases

DNASU3622.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302327; ENSP00000307183; ENSG00000168556. [Q9H160-1]
ENST00000434682; ENSP00000412586; ENSG00000168556. [Q9H160-2]
GeneID3622.
KEGGhsa:3622.
UCSCuc003ivs.1. human. [Q9H160-1]

Organism-specific databases

CTD3622.
GeneCardsGC04P184426.
HGNCHGNC:6063. ING2.
HPAHPA019486.
HPA021517.
MIM604215. gene.
neXtProtNX_Q9H160.
PharmGKBPA29873.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5034.
HOGENOMHOG000239724.
HOVERGENHBG006607.
InParanoidQ9H160.
OMALCHMTNG.
OrthoDBEOG7RBZ9T.
PhylomeDBQ9H160.
TreeFamTF352014.

Gene expression databases

ArrayExpressQ9H160.
BgeeQ9H160.
CleanExHS_ING2.
GenevestigatorQ9H160.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028639. ING2.
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:SF37. PTHR10333:SF37. 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

GeneWikiING2.
GenomeRNAi3622.
NextBio14173.
PROQ9H160.
SOURCESearch...

Entry information

Entry nameING2_HUMAN
AccessionPrimary (citable) accession number: Q9H160
Secondary accession number(s): B6ZDS1, O95698
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM