CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029974
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Jade-3 
Protein Synonyms/Alias
  
Gene Name
 Phf16 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
33SMYRKKSKNPKEQKKacetylation[1, 2]
36RKKSKNPKEQKKSAEacetylation[1, 2]
372KHSQNKPKLGDAEYHacetylation[3]
462ENGLVQPKEESIHTRacetylation[4]
602PRYPLESKSNCLQTSacetylation[1]
736EDLQYCVKPTKNVSSacetylation[1, 4]
744PTKNVSSKEQLWGRQacetylation[3]
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] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] 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]
 [4] 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
 824 AA 
Protein Sequence
MMKRHRPVSS SESSDECPST SFTSSSMYRK KSKNPKEQKK SAEVFRKDLI SAMKIPDSHH 60
VNPDSYYLFT DTWKEEWEKG VQVPANPDSV PTPSLRIISE KVKEMLFVRP RKYIRCSSPE 120
SAEPGYINTL EQAASTCRYD LDDMDIFWLQ ELNEDLGEMG YGPIDETLME KTIEVLERHC 180
HENMNHAIET VEGLGIEYDE DVICDVCRSP DSEEGNDMVF CDKCNVCVHQ ACYGILKIPE 240
GSWLCRSCVL GIYPQCVLCP KKGGAMKTTR TGTKWAHVSC ALWIPEVSIA CPERMEPVTK 300
ISHIPPSRWA LVCNLCKLKT GACIQCSVKS CITAFHVTCA FEHGLEMKTI LDEGDEVKFK 360
SFCLKHSQNK PKLGDAEYHH HRVAEQSQAK SEKTSLRAQK LRELEEEFYT LVQVEDVAKE 420
MELSAFTVDF IYNYWKLKRK SNFNKPLIPP KEEEENGLVQ PKEESIHTRM RMFMHLRQDL 480
ERVRNLCYMI SRREKLKLSH TKVQEQIFGL QVQLINEEIT EGLSLTNALE NSLFYPPPRI 540
TLKLKMPKST SEDCKDSSTE TEHQLSSPGS SSPGHSKRSP QMPEEPLDMN VKIYPRYPLE 600
SKSNCLQTSR SHSRCETKSS SPTPRAPSAE FYHGQSLGKP LALQAALHGQ VSIGNGKNQP 660
NSRVSSSNGL EGNWSGNITQ KVNSSEVCYD QESMLSSHLP SPGNIRKSSM EHFSRSFKEA 720
TNTWVKPTED LQYCVKPTKN VSSKEQLWGR QLLRRPTGRA SYQETDGYCP DLEPSDSEAE 780
GEGSKETPRV KRESSDRENP SHDSARECHG KTKTHPHSHS SMQR 824 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR019542; Enhancer_polycomb-like_N.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF10513; EPL1 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS