CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023492
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine-specific demethylase PHF2 
Protein Synonyms/Alias
 GRC5; PHD finger protein 2 
Gene Name
 Phf2 
Gene Synonyms/Alias
 Kiaa0662 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
412AFRSWTKKQALAEHEubiquitination[1]
716ALLMPTSKPKLDSAVacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA (By similarity). 
Sequence Annotation
 DOMAIN 197 353 JmjC.
 ZN_FING 5 56 PHD-type.
 METAL 249 249 Iron; catalytic (By similarity).
 METAL 251 251 Iron; catalytic (By similarity).
 METAL 321 321 Iron; catalytic (By similarity).
 BINDING 193 193 Alpha-ketoglutarate (By similarity).
 BINDING 246 246 Alpha-ketoglutarate (By similarity).
 BINDING 259 259 Alpha-ketoglutarate (By similarity).
 BINDING 266 266 Alpha-ketoglutarate (By similarity).
 BINDING 323 323 Alpha-ketoglutarate (By similarity).
 MOD_RES 458 458 Phosphoserine.
 MOD_RES 459 459 Phosphoserine.
 MOD_RES 474 474 Phosphoserine (By similarity).
 MOD_RES 479 479 Phosphothreonine (By similarity).
 MOD_RES 536 536 Phosphoserine (By similarity).
 MOD_RES 677 677 Phosphoserine.
 MOD_RES 701 701 Phosphoserine (By similarity).
 MOD_RES 734 734 Phosphoserine.
 MOD_RES 876 876 Phosphoserine (By similarity).
 MOD_RES 1057 1057 Phosphoserine; by PKA (By similarity).  
Keyword
 Activator; Chromatin regulator; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1096 AA 
Protein Sequence
MATVPVYCVC RLPYDVTRFM IECDACKDWF HGSCVGVEEE EAPDIDIYHC PNCEKTHGKS 60
TLKKKRTWHK HGPGPTPDVK PVQNGSQLFI KELRSRTFPS AEDVVSRVPG SQLTVGYMEE 120
HGFTEPILVP KKDGLGLAVP APTFYVSDVE NYVGPERSVD VTDVTKQKDC KMKLKEFVDY 180
YYSTNRKRVL NVTNLEFSDT RMSSFVEPPD IVKKLSWVEN YWPDDALLAK PKVTKYCLIC 240
VKDSYTDFHI DSGGASAWYH VLKGEKIFYL IRPASANISL YERWRSASNH SEMFFADQVD 300
RCYKCTVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE VERRLKLGSL 360
TQFPNFETAC WYMGKHLLEA FKGSHKSGKQ LPPHLVQGAK ILNGAFRSWT KKQALAEHED 420
ELPEHFRPSQ LIKDLAKEIR LSENASKTVR PEVNAAASSD EVCDGDREKE EPPSPVETTP 480
PRSLLEKVSK KKTSKTVKMP KPSKIPKPPK SPKPPKTLKL KDGSKKKGKK CKESASPTIP 540
NLDLLEAHTK EALTKMEPPK KGKTPKSVLS VPNKDTVHTQ NDMERLEIRE QTKSKSEAKW 600
KYKNSKPDSL LKMEEEQRLE KSPLAGNKDK FSFSFSNRKL LGSKALRPPS SPGVFGALQS 660
FKEDKAKPVR DEYEYVSDDG ELKIDEFPIR RKKSAPKRDL SFLLDKKEAL LMPTSKPKLD 720
SAVYKSDDSS DEGSLHIDTD TKPGRNAKVK KESGSSAAGI LDLLQASEEV GALEYNPNSQ 780
PPASPSTQEA IQGMLSMANL QASDSCLQTT WGTGQAKGGS LAAHGARKIG GGNKGTGKRL 840
LKRTAKNSVD LEDYEEQDHL DACFKDSDYV YPSLESDEDN PVFKSRSKKR KGSDDAPYSP 900
TARVGPSVPR QDRPVREGTR VASIETGLAA AAAKLSQQEE QKNRKKKNTK RKPAPNTASP 960
SISTSASAST GTTSASTTPA STTPASTTPA STTPASTSTA SSQASQEGSS PEPPPESHSS 1020
SLADHEYTAA GTFSGSQAGR ASQPMAPGVF LTQRRPSASS PNNTAAKGKR TKKGMATAKQ 1080
RLGKILKIHR NGKLLL 1096 
Gene Ontology
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB.
 GO:0005506; F:iron ion binding; ISS:UniProtKB.
 GO:0035064; F:methylated histone residue binding; ISS:UniProtKB.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0003713; F:transcription coactivator activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0061188; P:negative regulation of chromatin silencing at rDNA; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003347; JmjC_dom.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF02373; JmjC
 PF00628; PHD 
SMART
 SM00558; JmjC
 SM00249; PHD 
PROSITE
 PS51184; JMJC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS