CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015514
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein Jade-1 
Protein Synonyms/Alias
 PHD finger protein 17 
Gene Name
 Phf17 
Gene Synonyms/Alias
 Jade1; Kiaa1807 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
303EKMEPITKVSHIPSSacetylation[1, 2]
609NSSGTEGKTSHKQPGacetylation[2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753] 
Functional Description
 Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Transcriptional coactivator it may also promote acetylation of nucleosomal histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor suppressor (By similarity). 
Sequence Annotation
 ZN_FING 204 254 PHD-type 1.
 ZN_FING 313 372 PHD-type 2; atypical.
 MOD_RES 90 90 Phosphoserine (By similarity).
 MOD_RES 93 93 Phosphothreonine (By similarity).
 MOD_RES 603 603 Phosphoserine (By similarity).
 MOD_RES 735 735 Phosphoserine (By similarity).  
Keyword
 Activator; Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 834 AA 
Protein Sequence
MKRGRLPSSS EDSDDNGSLS TTWSQHSRSQ HGRSSTCSRP EDRKPSEVFR TDLITAMKLH 60
DSYQLNPDDY YVLADPWRQE WEKGVQVPVS PGTIPQPVAR VVSEEKSLMF IRPKKYIASS 120
GSEPPALGYV DIRTLADSVC RYDLNDMDAA WLEVTNEEFK EMGMPELDEY TMERVLEEFE 180
QRCYDNMNHA IETEEGLGIE YDEDVVCDVC QSPDGEDGNE MVFCDKCNIC VHQACYGILK 240
VPEGSWLCRT CALGVQPKCL LCPKKGGAMK PTRSGTKWVH VSCALWIPEV SIGSPEKMEP 300
ITKVSHIPSS RWALVCSLCN EKFGASIQCS VKNCRTAFHV TCAFDRGLEM KTILAENDEV 360
KFKSYCPKHS SHRKPEEGLG EGAAQENGAP ESSPQSPLEP YGSLEPNREE AHRVSVRKQK 420
LQQLEDEFYT FVNLLDVARA LRLPEEVVDF LYQYWKLKRK INFNKPLITP KKDEEDNLAK 480
REQDVLFRRL QLFTHLRQDL ERVRNLTYMV TRREKIKRSV CKVQEQIFTQ YTKLLEQEKV 540
SGVPSSCSSA LENMLFFNSP SVGPNAPKIE DLKWHSAFFR KQMGTSLVHP LKKSHKRDAV 600
QNSSGTEGKT SHKQPGLCGR REGLEVSESL LSLEKTFAEA RLLSSAQQKN GVVTPDHGKR 660
RDNRFHCDLV KGDLKDKSFK QSHKPLRSTD TSQRHLDNTR AATSPGVGQS APGTRKEIVP 720
KCNGSLVKVP ITPASPVKSW GGFRIPKKGE RQQQGEAHDG ACHQHSDCSH LGVSRAPAKE 780
RAKSRLRADS ENDGYAPDGE MSDSESEASE KKCIHASSTI SRRTDIIRRS ILAS 834 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
 GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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