CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013245
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inhibitor of growth protein 3 
Protein Synonyms/Alias
  
Gene Name
 Ing3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
164ATDHIPEKKFKSEALacetylation[1]
264NNDFQLGKEFSMPREacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 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 (By similarity). 
Sequence Annotation
 ZN_FING 363 412 PHD-type.
 BINDING 365 365 Histone H3K4me3 (By similarity).
 BINDING 376 376 Histone H3K4me3 (By similarity).
 BINDING 380 380 Histone H3K4me3 (By similarity).
 BINDING 388 388 Histone H3K4me3 (By similarity).
 MOD_RES 264 264 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Chromatin regulator; Complete proteome; Growth regulation; Metal-binding; Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 421 AA 
Protein Sequence
MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE 60
QMASIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE LAKFKMELEA DNAGITEILE 120
RRSLELDAPS QPVNNHHAHS HTPVEKRKYN PTSHHTATDH IPEKKFKSEA LLSTLTSDAS 180
KENTLGCRNN NSTASCNNAY NVNSSQPLAS YNIGSLSSGA GAGAITMAAA QAVQATAQMK 240
EGRRTSSLKA SYEAFKNNDF QLGKEFSMPR ETAGYSSSSA LMTTLTQNAS SSAADSRSGR 300
KSKNNTKSSS QQSSSSSSSS SSSSLSLCSS SSTVVQEVSQ QTTVVPESDS NSQVDWTYDP 360
NEPRYCICNQ VSYGEMVGCD NQDCPIEWFH YGCVGLTEAP KGKWFCPQCT AAMKRRGSRH 420
K 421 
Gene Ontology
 GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
 GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 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