CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022005
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein Jade-2 
Protein Synonyms/Alias
 PHD finger protein 15 
Gene Name
 PHF15 
Gene Synonyms/Alias
 JADE2; KIAA0239 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32TSASRCSKLPSSTKSacetylation[1, 2]
38SKLPSSTKSGWPRQNacetylation[1, 2]
298EKMEPITKISHIPASacetylation[2]
Reference
 [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
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. 
Sequence Annotation
 ZN_FING 199 249 PHD-type.
 MOD_RES 32 32 N6-acetyllysine.
 MOD_RES 38 38 N6-acetyllysine.
 MOD_RES 298 298 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Metal-binding; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 790 AA 
Protein Sequence
MEEKRRKYSI SSDNSDTTDS HATSTSASRC SKLPSSTKSG WPRQNEKKPS EVFRTDLITA 60
MKIPDSYQLS PDDYYILADP WRQEWEKGVQ VPAGAEAIPE PVVRILPPLE GPPAQASPSS 120
TMLGEGSQPD WPGGSRYDLD EIDAYWLELI NSELKEMERP ELDELTLERV LEELETLCHQ 180
NMARAIETQE GLGIEYDEDV VCDVCRSPEG EDGNEMVFCD KCNVCVHQAC YGILKVPTGS 240
WLCRTCALGV QPKCLLCPKR GGALKPTRSG TKWVHVSCAL WIPEVSIGCP EKMEPITKIS 300
HIPASRWALS CSLCKECTGT CIQCSMPSCV TAFHVTCAFD HGLEMRTILA DNDEVKFKSF 360
CQEHSDGGPR NEPTSEPTEP SQAGEDLEKV TLRKQRLQQL EEDFYELVEP AEVAERLDLA 420
EALVDFIYQY WKLKRKANAN QPLLTPKTDE VDNLAQQEQD VLYRRLKLFT HLRQDLERVR 480
NLCYMVTRRE RTKHAICKLQ EQIFHLQMKL IEQDLCRGLS TSFPIDGTFF NSWLAQSVQI 540
TAENMAMSEW PLNNGHREDP APGLLSEELL QDEETLLSFM RDPSLRPGDP ARKARGRTRL 600
PAKKKPPPPP PQDGPGSRTT PDKAPKKTWG QDAGSGKGGQ GPPTRKPPRR TSSHLPSSPA 660
AGDCPILATP ESPPPLAPET PDEAASVAAD SDVQVPGPAA SPKPLGRLRP PRESKVTRRL 720
PGARPDAGMG PPSAVAERPK VSLHFDTETD GYFSDGEMSD SDVEAEDGGV QRGPREAGAE 780
EVVRMGVLAS 790 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 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. 
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