CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011922
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleosome-remodeling factor subunit BPTF 
Protein Synonyms/Alias
 Bromodomain and PHD finger-containing transcription factor; Fetal Alz-50 clone 1 protein; Fetal Alzheimer antigen 
Gene Name
 BPTF 
Gene Synonyms/Alias
 FAC1; FALZ 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
546NKARGSNKSFLAAANubiquitination[1]
880KRRHLAHKFCLTPAGacetylation[2]
942KAVQMCSKPREFALAubiquitination[1]
1048HVYRFVPKLPGNTNVubiquitination[1]
1226KTSTNSSKNLSESPVubiquitination[1]
1579IIPENDIKSLTVKESubiquitination[3, 4]
1844FVTKSSKKSIFVLPNubiquitination[1, 3, 4, 5]
1855VLPNDDLKKLARKGGubiquitination[1]
1856LPNDDLKKLARKGGIubiquitination[1]
1949ITTTEIIKRRDVGPYubiquitination[3, 4]
2032AFAERVEKEKAQAVEubiquitination[1]
2034AERVEKEKAQAVEQQubiquitination[1]
2095TKMVLTTKVGSPATVubiquitination[1]
2743KLSALLFKHKEQLRAubiquitination[1]
2772IEVQEELKRDLKIKKubiquitination[1]
2863STTSKETKKDTKLYCacetylation[2]
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] 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]
 [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] 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
Functional Description
 Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors. 
Sequence Annotation
 DOMAIN 240 300 DDT.
 DOMAIN 2944 3014 Bromo.
 ZN_FING 390 437 PHD-type 1.
 ZN_FING 2867 2918 PHD-type 2.
 REGION 640 749 Interaction with KEAP1.
 REGION 839 921 Interaction with MAZ.
 BINDING 2869 2869 Histone H3K4me3.
 BINDING 2876 2876 Histone H3K4me3.
 BINDING 2882 2882 Histone H3K4me3.
 BINDING 2891 2891 Histone H3K4me3.
 MOD_RES 216 216 Phosphoserine.
 MOD_RES 572 572 Phosphoserine.
 MOD_RES 763 763 Phosphoserine.
 MOD_RES 817 817 Phosphoserine.
 MOD_RES 880 880 N6-acetyllysine.
 MOD_RES 1064 1064 Phosphothreonine.
 MOD_RES 1231 1231 Phosphoserine.
 MOD_RES 1251 1251 Phosphoserine.
 MOD_RES 1300 1300 Phosphoserine.
 MOD_RES 1310 1310 Phosphoserine.
 MOD_RES 2098 2098 Phosphoserine.
 MOD_RES 2465 2465 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Coiled coil; Complete proteome; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3046 AA 
Protein Sequence
MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR WAAAQAEVAP 60
KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG RTGGGGGGGH LARTTAARRA 120
VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG DAEETQDSED DEEDEMEEDD DDSDYPEEME 180
DDDDDASYCT ESSFRSHSTY SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN 240
EHIMNVIAIY EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT 300
SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE DYPYGPVENK 360
IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG DLLCCETCSA VYHLECVKPP 420
LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE 480
EDTENENEKK IWYYSTKVQL AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK 540
ARGSNKSFLA AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ 600
SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS PSEGRSPVGC 660
LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT TSIQPNLENS NSSSELNSSQ 720
SESAKAADDP ENGERESHTP VSIQEEIVGD FKSEKSNGEL SESPGAGKGA SGSTRIITRL 780
RNPDSKLSQL KSQQVAAAAH EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF 840
KLGQEGKYRV YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV 900
LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL AILECAVKPV 960
VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE TMQQATWVKY TFPVKHQVWK 1020
QKGEEYRVTG YGGWSWISKT HVYRFVPKLP GNTNVNYRKS LEGTKNNMDE NMDESDKRKC 1080
SRSPKKIKIE PDSEKDEVKG SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE 1140
PMEVDDDMKT ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE 1200
EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ SPNANNDQPE 1260
DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS PETKCPKQNS IENDIEEKVS 1320
DLASRGQEPS KSKTKGNDFF IDDSKLASAD DIGTLICKNK KPLIQEESDT IVSSSKSALH 1380
SSVPKSTNDR DATPLSRAMD FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES 1440
ISEQFRTREQ DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK 1500
CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK EISESRVVSG 1560
NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED FNERNSSETK SHLLSSSDAE 1620
GNYRDSLETL PSTKESDSTQ TTTPSASCPE SNSVNQVEDM EIETSEVKKV TSSPITSEEE 1680
SNLSNDFIDE NGLPINKNEN VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV 1740
SSTENCAKST VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT 1800
SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP NDDLKKLARK 1860
GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV KSLAGVSLML RLLWASLRWD 1920
DMAAKAPPGG GTTRTETSET EITTTEIIKR RDVGPYGIRS EYCIRKIICP IGVPETPKET 1980
PTPQRKGLRS SALRPKRPET PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ 2040
QAKKRLEQQK PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA 2100
TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT SFQPRTATVT 2160
IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG KAIIRTPVMV QPGAPQQVMT 2220
QIIRGQPVST AVSAPNTVSS TPGQKSLTSA TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ 2280
LTQGHGGNQG LTVVIQGQGQ TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL 2340
ATTATTASTT TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ 2400
PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ VAAQSQPQSN 2460
VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP IPIQPHTSLQ IPSQGQPQSQ 2520
PQVQSSTQTL SSGQTLNQVT VSSPSRPQLQ IQQPQPQVIA VPQLQQQVQV LSQIQSQVVA 2580
QIQAQQSGVP QQIKLQLPIQ IQQSSAVQTH QIQNVVTVQA ASVQEQLQRV QQLRDQQQKK 2640
KQQQIEIKRE HTLQASNQSE IIQKQVVMKH NAVIEHLKQK KSMTPAEREE NQRMIVCNQV 2700
MKYILDKIDK EEKQAAKKRK REESVEQKRS KQNATKLSAL LFKHKEQLRA EILKKRALLD 2760
KDLQIEVQEE LKRDLKIKKE KDLMQLAQAT AVAAPCPPVT PAPPAPPAPP PSPPPPPAVQ 2820
HTGLLSTPTL PAASQKRKRE EEKDSSSKSK KKKMISTTSK ETKKDTKLYC ICKTPYDESK 2880
FYIGCDRCQN WYHGRCVGIL QSEAELIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL 2940
RSLQAHKMAW PFLEPVDPND APDYYGVIKE PMDLATMEER VQRRYYEKLT EFVADMTKIF 3000
DNCRYYNPSD SPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAS 3046 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0016589; C:NURF complex; IDA:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; IDA:HGNC.
 GO:0008134; F:transcription factor binding; IDA:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0009952; P:anterior/posterior pattern specification; IEA:Compara.
 GO:0007420; P:brain development; IMP:HGNC.
 GO:0006338; P:chromatin remodeling; IDA:HGNC.
 GO:0001892; P:embryonic placenta development; IEA:Compara.
 GO:0007492; P:endoderm development; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:HGNC.
 GO:0006351; P:transcription, DNA-dependent; IMP:HGNC. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR004022; DDT_dom.
 IPR018500; DDT_dom_subgr.
 IPR018501; DDT_dom_superfamily.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF02791; DDT
 PF00628; PHD 
SMART
 SM00297; BROMO
 SM00571; DDT
 SM00249; PHD 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50827; DDT
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.