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Q9ESK4

- ING2_MOUSE

UniProt

Q9ESK4 - ING2_MOUSE

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Protein
Inhibitor of growth protein 2
Gene
Ing2, Ing1l
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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) By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151Histone H3K4me3 By similarity
Binding sitei226 – 2261Histone H3K4me3 By similarity
Binding sitei230 – 2301Histone H3K4me3 By similarity
Binding sitei238 – 2381Histone H3K4me3 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri213 – 26250PHD-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. chromatin binding Source: InterPro
  3. phosphatidylinositol binding Source: Ensembl
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: BHF-UCL
  2. male germ-line stem cell division Source: BHF-UCL
  3. male meiosis I Source: BHF-UCL
  4. negative regulation of apoptotic signaling pathway Source: MGI
  5. negative regulation of cell proliferation Source: InterPro
  6. positive regulation of apoptotic process Source: InterPro
  7. positive regulation of transcription, DNA-templated Source: MGI
  8. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  9. regulation of growth Source: UniProtKB-KW
  10. seminiferous tubule development Source: BHF-UCL
  11. sperm motility Source: BHF-UCL
  12. spermatid development Source: BHF-UCL
  13. spermatogenesis Source: BHF-UCL
  14. 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

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of growth protein 2
Alternative name(s):
Inhibitor of growth 1-like protein
p33ING2
Gene namesi
Name:Ing2
Synonyms:Ing1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1916510. Ing2.

Subcellular locationi

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

GO - Cellular componenti

  1. CCAAT-binding factor complex Source: Ensembl
  2. Sin3 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Inhibitor of growth protein 2
PRO_0000212664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki196 – 196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) By similarity

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PRIDEiQ9ESK4.

PTM databases

PhosphoSiteiQ9ESK4.

Expressioni

Gene expression databases

ArrayExpressiQ9ESK4.
CleanExiMM_ING2.
GenevestigatoriQ9ESK4.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi213322. 3 interactions.
DIPiDIP-38912N.
MINTiMINT-1340342.
STRINGi10090.ENSMUSP00000079226.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2123
Turni216 – 2194
Beta strandi224 – 2285
Beta strandi238 – 2403
Helixi242 – 2443
Helixi257 – 2604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WESNMR-A205-262[»]
2G6QX-ray2.00A205-264[»]
ProteinModelPortaliQ9ESK4.
SMRiQ9ESK4. Positions 32-120, 212-263.

Miscellaneous databases

EvolutionaryTraceiQ9ESK4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 28117PBR By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili49 – 10153 Reviewed prediction
Add
BLAST

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3 By similarity.
The polybasic region (PBR) is responsive to the binding to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns5P) By similarity.

Sequence similaritiesi

Belongs to the ING family.

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5034.
GeneTreeiENSGT00550000074538.
HOGENOMiHOG000239724.
HOVERGENiHBG006607.
InParanoidiQ9ESK4.
OMAiLCHMTNG.
OrthoDBiEOG7RBZ9T.
TreeFamiTF352014.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028639. 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]
PANTHERiPTHR10333. PTHR10333. 1 hit.
PTHR10333:SF37. PTHR10333:SF37. 1 hit.
PfamiPF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. 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.

Q9ESK4-1 [UniParc]FASTAAdd to Basket

« Hide

MLGQQQQQQL YSSAALLTGE RSRLLSCYVQ DYLECVESLP HDMQRNVSVL    50
RELDNKYQET LKEIDDVYEK YKKEDDSNQK KRLQQHLQRA LINSQELGDE 100
KIQIVTQMLE LVENRARQME LHSQCFQDPA ESERASDKSK MDSSQPERSS 150
RRPRRQRTSE SRDLCHMTNG IDDCDDQPPK EKRSKSAKKK KRSKAKQERE 200
ASPVEFAIDP NEPTYCLCNQ VSYGEMIGCD NEQCPIEWFH FSCVSLTYKP 250
KGKWYCPKCR GDNEKTMDKS TEKTKKERRA R 281
Length:281
Mass (Da):32,978
Last modified:October 3, 2012 - v3
Checksum:i6D953B52822C2D8A
GO

Sequence cautioni

The sequence AAH50003.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261S → T in AAG12173. 1 Publication
Sequence conflicti26 – 261S → T in AAH50003. 1 Publication
Sequence conflicti72 – 721K → E in AAG12173. 1 Publication
Sequence conflicti104 – 1041I → N in AAG12173. 1 Publication
Sequence conflicti110 – 1101E → G in AAG12173. 1 Publication
Sequence conflicti116 – 1161A → S in AAG12173. 1 Publication
Sequence conflicti203 – 2031P → S in AAG12173. 1 Publication
Sequence conflicti250 – 2501P → H in AAG12173. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF078834 mRNA. Translation: AAG12173.1.
AK048800 mRNA. Translation: BAC33461.1.
AK083144 mRNA. Translation: BAC38783.1.
AC107236 Genomic DNA. No translation available.
CH466554 Genomic DNA. Translation: EDL35605.1.
BC096433 mRNA. Translation: AAH96433.1.
BC138229 mRNA. Translation: AAI38230.1.
BC050003 mRNA. Translation: AAH50003.1. Sequence problems.
CCDSiCCDS22298.1.
RefSeqiNP_075992.2. NM_023503.3.
UniGeneiMm.430733.

Genome annotation databases

EnsembliENSMUST00000080353; ENSMUSP00000079226; ENSMUSG00000063049.
GeneIDi69260.
KEGGimmu:69260.
UCSCiuc009lrf.2. mouse.
uc012gdo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF078834 mRNA. Translation: AAG12173.1 .
AK048800 mRNA. Translation: BAC33461.1 .
AK083144 mRNA. Translation: BAC38783.1 .
AC107236 Genomic DNA. No translation available.
CH466554 Genomic DNA. Translation: EDL35605.1 .
BC096433 mRNA. Translation: AAH96433.1 .
BC138229 mRNA. Translation: AAI38230.1 .
BC050003 mRNA. Translation: AAH50003.1 . Sequence problems.
CCDSi CCDS22298.1.
RefSeqi NP_075992.2. NM_023503.3.
UniGenei Mm.430733.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WES NMR - A 205-262 [» ]
2G6Q X-ray 2.00 A 205-264 [» ]
ProteinModelPortali Q9ESK4.
SMRi Q9ESK4. Positions 32-120, 212-263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213322. 3 interactions.
DIPi DIP-38912N.
MINTi MINT-1340342.
STRINGi 10090.ENSMUSP00000079226.

PTM databases

PhosphoSitei Q9ESK4.

Proteomic databases

PRIDEi Q9ESK4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000080353 ; ENSMUSP00000079226 ; ENSMUSG00000063049 .
GeneIDi 69260.
KEGGi mmu:69260.
UCSCi uc009lrf.2. mouse.
uc012gdo.1. mouse.

Organism-specific databases

CTDi 3622.
MGIi MGI:1916510. Ing2.

Phylogenomic databases

eggNOGi COG5034.
GeneTreei ENSGT00550000074538.
HOGENOMi HOG000239724.
HOVERGENi HBG006607.
InParanoidi Q9ESK4.
OMAi LCHMTNG.
OrthoDBi EOG7RBZ9T.
TreeFami TF352014.

Miscellaneous databases

EvolutionaryTracei Q9ESK4.
NextBioi 328987.
PROi Q9ESK4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ESK4.
CleanExi MM_ING2.
Genevestigatori Q9ESK4.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR028639. 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 ]
PANTHERi PTHR10333. PTHR10333. 1 hit.
PTHR10333:SF37. PTHR10333:SF37. 1 hit.
Pfami PF12998. ING. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Nagashima M., Hagiwara K., Hancock A.R., Harris C.C.
    Submitted (JUL-1998) 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: Cerebellum and Hippocampus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: FVB/N-3.
    Tissue: Brain, Mammary gland and Olfactory epithelium.
  6. "Solution structure of PHD domain of inhibitor of growth family, member 1-like."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 205-262.

Entry informationi

Entry nameiING2_MOUSE
AccessioniPrimary (citable) accession number: Q9ESK4
Secondary accession number(s): Q4VAD7, Q80VI5, Q8BGU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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