CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018773
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein Jade-3 
Protein Synonyms/Alias
 PHD finger protein 16 
Gene Name
 PHF16 
Gene Synonyms/Alias
 JADE3; KIAA0215 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30SGSMYRIKSKIPNEHacetylation[1]
32SMYRIKSKIPNEHKKacetylation[1]
38SKIPNEHKKPAEVFRacetylation[1]
46KPAEVFRKDLISAMKubiquitination[2]
299ERMEPITKISHIPPSacetylation[3, 4]
318VCNLCKLKTGACIQCubiquitination[2]
357LDEGDEVKFKSYCLKubiquitination[2]
371KHSQNRQKLGEAEYPacetylation[5]
383EYPHHRAKEQSQAKSacetylation[4]
389AKEQSQAKSEKTSLRacetylation[4]
461ENGLVQPKEESIHTRacetylation[1, 3, 4]
638YHGQSLGKPLVLQAAacetylation[1, 3, 4, 5]
656QSSIGNGKSQPNSKFacetylation[5]
735EDLQCYVKPTKNMSPacetylation[1, 3, 4, 5]
735EDLQCYVKPTKNMSPubiquitination[5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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]
 [5] 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. 
Sequence Annotation
 ZN_FING 200 250 PHD-type.
 MOD_RES 30 30 N6-acetyllysine.
 MOD_RES 32 32 N6-acetyllysine.
 MOD_RES 38 38 N6-acetyllysine.
 MOD_RES 85 85 Phosphoserine.
 MOD_RES 566 566 Phosphoserine.
 MOD_RES 638 638 N6-acetyllysine.
 MOD_RES 774 774 Phosphoserine.
 MOD_RES 776 776 Phosphoserine.
 MOD_RES 780 780 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 823 AA 
Protein Sequence
MKRHRPVSSS DSSDESPSTS FTSGSMYRIK SKIPNEHKKP AEVFRKDLIS AMKLPDSHHI 60
NPDSYYLFAD TWKEEWEKGV QVPASPDTVP QPSLRIIAEK VKDVLFIRPR KYIHCSSPDT 120
TEPGYINIME LAASVCRYDL DDMDIFWLQE LNEDLAEMGC GPVDENLMEK TVEVLERHCH 180
ENMNHAIETE EGLGIEYDED VICDVCRSPD SEEGNDMVFC DKCNVCVHQA CYGILKVPEG 240
SWLCRSCVLG IYPQCVLCPK KGGALKTTKT GTKWAHVSCA LWIPEVSIAC PERMEPITKI 300
SHIPPSRWAL VCNLCKLKTG ACIQCSIKSC ITAFHVTCAF EHGLEMKTIL DEGDEVKFKS 360
YCLKHSQNRQ KLGEAEYPHH RAKEQSQAKS EKTSLRAQKL RELEEEFYSL VRVEDVAAEL 420
GMPTLAVDFI YNYWKLKRKS NFNKPLFPPK EDEENGLVQP KEESIHTRMR MFMHLRQDLE 480
RVRNLCYMIS RREKLKLSHN KIQEQIFGLQ VQLLNQEIDA GLPLTNALEN SLFYPPPRIT 540
LKLKMPKSTP EDHRNSSTET DQQPHSPDSS SSVHSIRNMQ VPQESLEMRT KSYPRYPLES 600
KNNRLLASLS HSRSEAKESS PAWRTPSSEC YHGQSLGKPL VLQAALHGQS SIGNGKSQPN 660
SKFAKSNGLE GSWSGNVTQK DSSSEMFCDQ EPVFSPHLVS QGSFRKSTVE HFSRSFKETT 720
NRWVKNTEDL QCYVKPTKNM SPKEQFWGRQ VLRRSAGRAP YQENDGYCPD LELSDSEAES 780
DGNKEKVRVR KDSSDRENPP HDSRRDCHGK SKTHPLSHSS MQR 823 
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
 PF00628; PHD 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS