CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020242
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PHD finger protein 20 
Protein Synonyms/Alias
 Glioma-expressed antigen 2; Hepatocellular carcinoma-associated antigen 58; Novel zinc finger protein; Transcription factor TZP 
Gene Name
 PHF20 
Gene Synonyms/Alias
 C20orf104; GLEA2; HCA58; NZF; TZP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
713GFKYWYDKEWLSRGHubiquitination[1]
818TLNGAVEKPRPLALPacetylation[2]
843TSEHCYQKPRAYYPAacetylation[2, 3, 4, 5]
843TSEHCYQKPRAYYPAubiquitination[6]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage. 
Sequence Annotation
 DOMAIN 4 69 Tudor 1.
 DOMAIN 83 147 Tudor 2.
 DNA_BIND 257 269 A.T hook.
 ZN_FING 452 477 C2H2-type.
 ZN_FING 654 700 PHD-type.
 MOD_RES 159 159 Phosphoserine.
 MOD_RES 843 843 N6-acetyllysine.
 MOD_RES 878 878 Phosphoserine.
 MOD_RES 880 880 Phosphoserine.
 DISULFID 96 96 Interchain (with C-100) (Probable).
 DISULFID 100 100 Interchain (with C-96) (Probable).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Disulfide bond; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1012 AA 
Protein Sequence
MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GKVLIHFKRW NHRYDEWFCW 60
DSPYLRPLEK IQLRKEGLHE EDGSSEFQIN EQVLACWSDC RFYPAKVTAV NKDGTYTVKF 120
YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE TDHKSLSSSP DKREKFKEQR KATVNVKKDK 180
EDKPLKTEKR PKQPDKEGKL ICSEKGKVSE KSLPKNEKED KENISENDRE YSGDAQVDKK 240
PENDIVKSPQ ENLREPKRKR GRPPSIAPTA VDSNSQTLQP ITLELRRRKI SKGCEVPLKR 300
PRLDKNSSQE KSKNYSENTD KDLSRRRSSR LSTNGTHEIL DPDLVVSDLV DTDPLQDTLS 360
STKESEEGQL KSALEAGQVS SALTCHSFGD GSGAAGLELN CPSMGENTMK TEPTSPLVEL 420
QEISTVEVTN TFKKTDDFGS SNAPAVDLDH KFRCKVVDCL KFFRKAKLLH YHMKYFHGME 480
KSLEPEESPG KRHVQTRGPS ASDKPSQETL TRKRVSASSP TTKDKEKNKE KKFKEFVRVK 540
PKKKKKKKKK TKPECPCSEE ISDTSQEPSP PKAFAVTRCG SSHKPGVHMS PQLHGPESGH 600
HKGKVKALEE DNLSESSSES FLWSDDEYGQ DVDVTTNPDE ELDGDDRYDF EVVRCICEVQ 660
EENDFMIQCE ECQCWQHGVC MGLLEENVPE KYTCYVCQDP PGQRPGFKYW YDKEWLSRGH 720
MHGLAFLEEN YSHQNAKKIV ATHQLLGDVQ RVIEVLHGLQ LKMSILQSRE HPDLPLWCQP 780
WKQHSGEGRS HFRNIPVTDT RSKEEAPSYR TLNGAVEKPR PLALPLPRSV EESYITSEHC 840
YQKPRAYYPA VEQKLVVETR GSALDDAVNP LHENGDDSLS PRLGWPLDQD RSKGDSDPKP 900
GSPKVKEYVS KKALPEEAPA RKLLDRGGEG LLSSQHQWQF NLLTHVESLQ DEVTHRMDSI 960
EKELDVLESW LDYTGELEPP EPLARLPQLK HCIKQLLMDL GKVQQIALCC ST 1012 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR017956; AT_hook_DNA-bd_motif.
 IPR022255; DUF3776.
 IPR002999; Tudor.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12618; DUF3776
 PF00628; PHD 
SMART
 SM00384; AT_hook
 SM00249; PHD
 SM00333; TUDOR
 SM00355; ZnF_C2H2 
PROSITE
 PS50304; TUDOR
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS