CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024572
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PHD finger protein 20-like protein 1 
Protein Synonyms/Alias
  
Gene Name
 PHF20L1 
Gene Synonyms/Alias
 CGI-72 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
618SRSMFTEKTTTYQYPubiquitination[1]
737PGQRWSAKYRYDKEWacetylation[2, 3]
813WACSGKRKDQDQIIAubiquitination[4]
824QIIAGVEKKIAQDTVubiquitination[4]
825IIAGVEKKIAQDTVNubiquitination[1]
909NSLQYSAKEHGMPEKacetylation[2, 3, 5, 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] 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]
 [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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [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] 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
  
Sequence Annotation
 DOMAIN 11 71 Tudor 1.
 DOMAIN 85 141 Tudor 2.
 ZN_FING 681 729 PHD-type.
 MOD_RES 909 909 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1017 AA 
Protein Sequence
MSKKPPNRPG ITFEIGARLE ALDYLQKWYP SRIEKIDYEE GKMLVHFERW SHRYDEWIYW 60
DSNRLRPLER PALRKEGLKD EEDFFDFKAG EEVLARWTDC RYYPAKIEAI NKEGTFTVQF 120
YDGVIRCLKR MHIKAMPEDA KGQVKSQHPL SWCCPIDPAG SCNQSMGSED WIALVKAAAA 180
AAAKNKTGSK PRTSANSNKD KDKDERKWFK VPSKKEETST CIATPDVEKK EDLPTSSETF 240
GLHVENVPKM VFPQPESTLS NKRKNNQGNS FQAKRARLNK ITGLLASKAV GVDGAEKKED 300
YNETAPMLEQ AISPKPQSQK KNEADISSSA NTQKPALLSS TLSSGKARSK KCKHESGDSS 360
GCIKPPKSPL SPELIQVEDL TLVSQLSSSV INKTSPPQPV NPPRPFKHSE RRRRSQRLAT 420
LPMPDDSVEK VSSPSPATDG KVFSISSQNQ QESSVPEVPD VAHLPLEKLG PCLPLDLSRG 480
SEVTAPVASD SSYRNECPRA EKEDTQMLPN PSSKAIADGR GAPAAAGISK TEKKVKLEDK 540
SSTAFGKRKE KDKERREKRD KDHYRPKQKK KKKKKKKSKQ HDYSDYEDSS LEFLERCSSP 600
LTRSSGSSLA SRSMFTEKTT TYQYPRAILS VDLSGENLSD VDFLDDSSTE SLLLSGDEYN 660
QDFDSTNFEE SQDEDDALNE IVRCICEMDE ENGFMIQCEE CLCWQHSVCM GLLEESIPEQ 720
YICYICRDPP GQRWSAKYRY DKEWLNNGRM CGLSFFKENY SHLNAKKIVS THHLLADVYG 780
VTEVLHGLQL KIGILKNKHH PDLHLWACSG KRKDQDQIIA GVEKKIAQDT VNREEKKYVQ 840
NHKEPPRLPL KMEGTYITSE HSYQKPQSFG QDCKSLADPG SSDDDDVSSL EEEQEFHMRS 900
KNSLQYSAKE HGMPEKNPAE GNTVFVYNDK KGTEDPGDSH LQWQLNLLTH IENVQNEVTS 960
RMDLIEKEVD VLESWLDFTG ELEPPDPLAR LPQLKRHIKQ LLIDMGKVQQ IATLCSV 1017 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR022255; DUF3776.
 IPR002999; Tudor.
 IPR014002; Tudor-like_plant.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12618; DUF3776
 PF00628; PHD 
SMART
 SM00743; Agenet
 SM00249; PHD
 SM00333; TUDOR 
PROSITE
 PS50304; TUDOR
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS