CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014943
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82PWRQEWEKGVQVPVSubiquitination[1]
114LMFIRPKKYIVSSGSubiquitination[1]
257CALGVQPKCLLCPKKubiquitination[1]
302EKMEPITKVSHIPSSacetylation[2, 3, 4]
302EKMEPITKVSHIPSSubiquitination[1]
373PKHSSHRKPEESLGKacetylation[3]
380KPEESLGKGAAQENGacetylation[2, 3, 4]
380KPEESLGKGAAQENGubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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. 
Sequence Annotation
 ZN_FING 203 253 PHD-type 1.
 ZN_FING 312 371 PHD-type 2; atypical.
 MOD_RES 89 89 Phosphoserine.
 MOD_RES 92 92 Phosphothreonine.
 MOD_RES 603 603 Phosphoserine.
 MOD_RES 743 743 Phosphoserine.  
Keyword
 Activator; Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 842 AA 
Protein Sequence
MKRGRLPSSS EDSDDNGSLS TTWSQNSRSQ HRRSSCSRHE DRKPSEVFRT DLITAMKLHD 60
SYQLNPDEYY VLADPWRQEW EKGVQVPVSP GTIPQPVARV VSEEKSLMFI RPKKYIVSSG 120
SEPPELGYVD IRTLADSVCR YDLNDMDAAW LELTNEEFKE MGMPELDEYT MERVLEEFEQ 180
RCYDNMNHAI ETEEGLGIEY DEDVVCDVCQ SPDGEDGNEM VFCDKCNICV HQACYGILKV 240
PEGSWLCRTC ALGVQPKCLL CPKKGGAMKP TRSGTKWVHV SCALWIPEVS IGSPEKMEPI 300
TKVSHIPSSR WALVCSLCNE KFGASIQCSV KNCRTAFHVT CAFDRGLEMK TILAENDEVK 360
FKSYCPKHSS HRKPEESLGK GAAQENGAPE CSPRNPLEPF ASLEQNREEA HRVSVRKQKL 420
QQLEDEFYTF VNLLDVARAL RLPEEVVDFL YQYWKLKRKV NFNKPLITPK KDEEDNLAKR 480
EQDVLFRRLQ LFTHLRQDLE RVRNLTYMVT RREKIKRSVC KVQEQIFNLY TKLLEQERVS 540
GVPSSCSSSS LENMLLFNSP SVGPDAPKIE DLKWHSAFFR KQMGTSLVHS LKKPHKRDPL 600
QNSPGSEGKT LLKQPDLCGR REGMVVPESF LGLEKTFAEA RLISAQQKNG VVMPDHGKRR 660
DNRFHCDLIK GDLKDKSFKQ SHKPLRSTDV SQRHLDNTRA ATSPGVGQSA PGTRKEIVPK 720
CNGSLIKVNY NQTAVKVPTT PASPVKNWGG FRIPKKGERQ QQGEAHDGAC HQHSDYPYLG 780
LGRVPAKERA KSKLKSDNEN DGYVPDVEMS DSESEASEKK CIHTSSTISR RTDIIRRSIL 840
AS 842 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; NAS:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006950; P:response to stress; NAS:UniProtKB.
 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