CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021260
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inhibitor of growth protein 2 
Protein Synonyms/Alias
 Inhibitor of growth 1-like protein; ING1Lp; p32; p33ING2 
Gene Name
 ING2 
Gene Synonyms/Alias
 ING1L 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
195KKKRSKAKQEREASPsumoylation[1]
Reference
 [1] Sumoylation of ING2 regulates the transcription mediated by Sin3A.
 Ythier D, Larrieu D, Binet R, Binda O, Brambilla C, Gazzeri S, Pedeux R.
 Oncogene. 2010 Nov 4;29(44):5946-56. [PMID: 20676127] 
Functional Description
 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). 
Sequence Annotation
 ZN_FING 212 261 PHD-type.
 REGION 264 280 PBR.
 BINDING 214 214 Histone H3K4me3 (By similarity).
 BINDING 225 225 Histone H3K4me3 (By similarity).
 BINDING 229 229 Histone H3K4me3 (By similarity).
 BINDING 237 237 Histone H3K4me3 (By similarity).  
Keyword
 Chromatin regulator; Coiled coil; Complete proteome; Direct protein sequencing; Growth regulation; Metal-binding; Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 280 AA 
Protein Sequence
MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR ELDNKYQETL 60
KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK IQIVTQMLEL VENRARQMEL 120
HSQCFQDPAE SERASDKAKM DSSQPERSSR RPRRQRTSES RDLCHMANGI EDCDDQPPKE 180
KKSKSAKKKK RSKAKQEREA SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF 240
SCVSLTYKPK GKWYCPKCRG DNEKTMDKST EKTKKDRRSR 280 
Gene Ontology
 GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
 GO:0016580; C:Sin3 complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; TAS:ProtInc.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0032403; F:protein complex binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; ISS:BHF-UCL.
 GO:0048133; P:male germ-line stem cell division; ISS:BHF-UCL.
 GO:0007141; P:male meiosis I; ISS:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
 GO:2000772; P:regulation of cellular senescence; NAS:BHF-UCL.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:2001020; P:regulation of response to DNA damage stimulus; NAS:BHF-UCL.
 GO:0072520; P:seminiferous tubule development; ISS:BHF-UCL.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0030317; P:sperm motility; ISS:BHF-UCL.
 GO:0007286; P:spermatid development; ISS:BHF-UCL.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 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. 
Pfam
 PF12998; ING
 PF00628; PHD 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS