CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033907
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
156HIPEKKFKSEALLSTacetylation[1]
170TLTSDASKENTLGCRacetylation[1, 2, 3]
253NNDFQLGKEFSIPREacetylation[1, 2, 3]
392LTEAPKGKWFCPQCTacetylation[1, 2]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 410 AA 
Protein Sequence
MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE 60
QMASIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE LAKFKMELEA DNAGITEILE 120
RRSLELDAPS QPVNNHHAHS HTPVETADHI PEKKFKSEAL LSTLTSDASK ENTLGCRNNN 180
STASCNNAYN VNSSQPLASY NIGSLSSGAG AGAITMAAAQ AVQATAQMKE GRRTSSLKAS 240
YEAFKNNDFQ LGKEFSIPRE TAGYSSSSAL MTTLTQNASS SATDSRSGRK SKNNTKSSSQ 300
QSSSSSSSSS SSSLSLCSSS STVVQEVSQQ ATVVPESDSN SQVDWTYDPN EPRYCICNQV 360
SYGEMVGCDN QDCPIEWFHY GCVGLTEAPK GKWFCPQCTA AMKRRGSRHK 410 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
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