CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019531
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase UHRF2 
Protein Synonyms/Alias
 Np95/ICBP90-like RING finger protein; Np95-like RING finger protein; Nuclear protein 97; Nuclear zinc finger protein Np97; RING finger protein 107; Ubiquitin-like PHD and RING finger domain-containing protein 2; Ubiquitin-like-containing PHD and RING finger domains protein 2 
Gene Name
 UHRF2 
Gene Synonyms/Alias
 NIRF; RNF107 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
128DPGFGIYKVNELVDAubiquitination[1]
322PLSFADGKFLRRNDPubiquitination[1, 2, 3, 4]
401TDSSEVVKAGERLKMubiquitination[1]
548CDAPLDDKIGAESRNubiquitination[1]
575FKGRKISKYAPEEGNubiquitination[1, 2, 4]
589NRYDGIYKVVKYWPEubiquitination[1, 2, 4, 5]
676DDCPSASKVYKASDSubiquitination[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] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131. 
Sequence Annotation
 DOMAIN 1 78 Ubiquitin-like.
 DOMAIN 448 612 YDG.
 ZN_FING 344 395 PHD-type.
 ZN_FING 733 772 RING-type.
 REGION 117 311 Required for interaction with histone H3
 REGION 194 288 Interaction with PCNP.
 REGION 414 644 Methyl-CpG binding and interaction with
 MOD_RES 667 667 Phosphoserine.
 DISULFID 704 704 Interchain.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Complete proteome; Disulfide bond; DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 802 AA 
Protein Sequence
MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD 60
YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK KAPRVGPSNQ PSTSARARLI 120
DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNIKH 180
KSKENTNKLD SVPSTSNSDC VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN 240
ELNVGDVVMV NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII 300
SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC GGKHEPNMQL 360
LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV KAGERLKMSK KKAKMPSAST 420
ESRRDWGRGM ACVGRTRECT IVPSNHYGPI PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG 480
RSNDGAYSLV LAGGFADEVD RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN 540
CDAPLDDKIG AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS 600
HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKP KGQSKKQPSG 660
TTKRPISDDD CPSASKVYKA SDSAEAIEAF QLTPQQQHLI REDCQNQKLW DEVLSHLVEG 720
PNFLKKLEQS FMCVCCQELV YQPVTTECFH NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI 780
MIPNEILQTL LDLFFPGYSK GR 802 
Gene Ontology
 GO:0005720; C:nuclear heterochromatin; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0042393; F:histone binding; ISS:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:HGNC.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEP:HGNC.
 GO:0008283; P:cell proliferation; IEP:HGNC.
 GO:0071158; P:positive regulation of cell cycle arrest; IDA:UniProtKB.
 GO:0051865; P:protein autoubiquitination; IDA:HGNC.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:HGNC. 
Interpro
 IPR021991; DUF3590.
 IPR014722; Rib_L2_dom2.
 IPR003105; SRA_YDG.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF12148; DUF3590
 PF00628; PHD
 PF00240; ubiquitin
 PF02182; YDG_SRA 
SMART
 SM00249; PHD
 SM00184; RING
 SM00466; SRA
 SM00213; UBQ 
PROSITE
 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2
 PS51015; YDG
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS