Q12830 (BPTF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleosome-remodeling factor subunit BPTF

Alternative name(s):
Bromodomain and PHD finger-containing transcription factor
Fetal Alz-50 clone 1 protein
Fetal Alzheimer antigen

Gene names

Name:	BPTF
Synonyms:	FAC1, FALZ

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	3046 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with MAZ. Interacts with KEAP1. Part of the nucleosome-remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with histone H3K4me3 and to a lesser extent with histone H3-K4Me2. Ref.9 Ref.10 Ref.13
Subcellular location	Cytoplasm. Nucleus. Note: In brains of Alzheimer disease patients, present in a subset of amyloid-containing plaques. Ref.6 Ref.9 Ref.10
Tissue specificity	Ubiquitously expressed, with highest levels in testis. Present in kidney, liver and brain. In the brain, highest levels are found in motor cortex (at protein level). Ref.1 Ref.3 Ref.6 Ref.9
Developmental stage	Abundantly expressed in the fetal brain. Present throughout the gray and white matter of the developing spinal cord at 18-22 gestational weeks. Expressed at low levels in adult brain and spinal cord and reexpressed in neurodegenerative diseases (at protein level). Ref.6
Domain	The second PHD-type zinc finger mediates binding to histone H3K4Me3. Has specificity for trimethyllysine; introducing a mutation in the Tyr-2876 residue can induce binding to dimethyllysine. Ref.22
Post-translational modification	Phosphorylation enhances DNA-binding. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Highly susceptible to proteolysis.
Sequence similarities	Belongs to the PBTF family. Contains 1 bromo domain. Contains 1 DDT domain. Contains 2 PHD-type zinc fingers.
Sequence caution	The sequence AAA97522.1 differs from that shown. Reason: Frameshift at positions 136 and 915. The sequence AAA97522.1 differs from that shown. Reason: Several sequencing errors. The sequence BAA89208.1 differs from that shown. Reason: Several sequencing errors in the N-terminal part.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	brain development Inferred from mutant phenotype Ref.4. Source: HGNC chromatin remodeling Inferred from direct assay Ref.4. Source: HGNC negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.9. Source: MGI positive regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.4. Source: HGNC transcription, DNA-dependent Inferred from mutant phenotype Ref.4. Source: HGNC
Cellular component	NURF complex Inferred from direct assay. Source: UniProtKB cytoplasm Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct sequence-specific DNA binding Inferred from direct assay Ref.7. Source: HGNC transcription factor binding Inferred from direct assay Ref.9. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST1H4A	P62805	3	EBI-1560273,EBI-302023
HIST2H3D	Q71DI3	2	EBI-4288838,EBI-750650

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12830-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q12830-2)

The sequence of this isoform differs from the canonical sequence as follows:
     622-747: Missing.

Isoform 4 (identifier: Q12830-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2522-2664: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3046

3046

Nucleosome-remodeling factor subunit BPTF

PRO_0000087176

Regions

Domain

240 – 300

61

DDT

Domain

2944 – 3014

71

Bromo

Zinc finger

390 – 437

48

PHD-type 1

Zinc finger

2867 – 2918

52

PHD-type 2

Region

640 – 749

110

Interaction with KEAP1

Region

839 – 921

83

Interaction with MAZ

Coiled coil

574 – 604

31

Potential

Coiled coil

978 – 1007

30

Potential

Coiled coil

2022 – 2050

29

Potential

Coiled coil

2706 – 2732

27

Potential

Compositional bias

143 – 180

38

Glu-rich

Compositional bias

149 – 185

37

Asp-rich

Compositional bias

1709 – 1803

95

Thr-rich

Compositional bias

2338 – 2361

24

Thr-rich

Compositional bias

2795 – 2817

23

Pro-rich

Compositional bias

2848 – 2853

6

Poly-Lys

Sites

Binding site

2869

1

Histone H3K4me3

Binding site

2876

1

Histone H3K4me3

Binding site

2882

1

Histone H3K4me3

Binding site

2891

1

Histone H3K4me3

Amino acid modifications

Modified residue

216

1

Phosphoserine Ref.11 Ref.12 Ref.16 Ref.17

Modified residue

572

1

Phosphoserine Ref.12

Modified residue

763

1

Phosphoserine Ref.17 Ref.18

Modified residue

817

1

Phosphoserine Ref.15

Modified residue

839

1

Phosphotyrosine Ref.14

Modified residue

880

1

N6-acetyllysine Ref.20

Modified residue

909

1

Phosphothreonine Ref.19

Modified residue

1064

1

Phosphothreonine Ref.12

Modified residue

1231

1

Phosphoserine Ref.18

Modified residue

1300

1

Phosphoserine Ref.17

Modified residue

1827

1

Phosphoserine Ref.12

Modified residue

1833

1

Phosphoserine Ref.12

Modified residue

2098

1

Phosphoserine Ref.17 Ref.18 Ref.19

Modified residue

2465

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

622 – 747

126

Missing in isoform 2.

VSP_020402

Alternative sequence

2522 – 2664

143

Missing in isoform 4.

VSP_020405

Experimental info

Mutagenesis

2869

1

Y → T: Abolishes binding to histone H3K4me3. Ref.21

Mutagenesis

2876

1

Y → E: Induces binding to histone H3K4me2. Ref.21 Ref.22

Mutagenesis

2876

1

Y → T: Strongly reduces binding to histone H3K4me3. Ref.21 Ref.22

Mutagenesis

2882

1

Y → S: Abolishes binding to histone H3K4me3. Ref.21

Mutagenesis

2884

1

G → E or L: Strongly reduces binding to histone H3K4me3. Ref.21

Mutagenesis

2886

1

D → N or A: Abolishes binding to histone H3K4me3. Ref.21

Mutagenesis

2889

1

Q → K: Strongly reduces binding to histone H3K4me3. Ref.21

Mutagenesis

2891

1

W → E or F: Abolishes binding to histone H3K4me3. Ref.13 Ref.21

Sequence conflict

752

1

K → T in AAA97522. Ref.3

Sequence conflict

757

1

N → T in AAA97522. Ref.3

Sequence conflict

969

1

S → F in BAA89208. Ref.1

Sequence conflict

1268

1

E → Q in BAA89208. Ref.1

Sequence conflict

1330

1

S → T in BAA89208. Ref.1

Sequence conflict

1842

1

S → T in BAA89208. Ref.1

Sequence conflict

1842

1

S → T in AAP22284. Ref.4

Sequence conflict

1926

1

A → V in BAA89208. Ref.1

Sequence conflict

1926

1

A → V in AAP22284. Ref.4

Sequence conflict

1932

1

T → S in BAA89208. Ref.1

Sequence conflict

1932

1

T → S in AAP22284. Ref.4

Sequence conflict

1960

1

S → F in BAA89208. Ref.1

Sequence conflict

2393

1

E → K in BAA89208. Ref.1

Sequence conflict

2404

1

Q → R in BAA89208. Ref.1

Sequence conflict

2540

1

T → S in BAA89208. Ref.1

Sequence conflict

2802 – 2803

2

AP → VL in BAA89208. Ref.1

Sequence conflict

2818

1

A → G in BAA89208. Ref.1

Sequence conflict

2832

1

A → V in BAA89208. Ref.1

Sequence conflict

2876

1

Y → G in AAH67234. Ref.5

Sequence conflict

2880

1

K → Q in AAH67234. Ref.5

Secondary structure

1

.

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3046

Helix Strand Turn

Details...

Turn

2870 – 2873

4

Beta strand

2882 – 2884

3

Turn

2886 – 2888

3

Beta strand

2891 – 2893

3

Helix

2895 – 2897

3

Helix

2901 – 2905

5

Helix

2913 – 2922

10

Turn

2923 – 2925

3

Helix

2930 – 2945

16

Helix

2947 – 2952

6

Turn

2958 – 2960

3

Helix

2964 – 2967

4

Helix

2974 – 2982

9

Helix

2989 – 3006

18

Helix

3012 – 3028

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 37D7206977A8DB09	FASTA	3,046	338,262
	10 20 30 40 50 60 MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR WAAAQAEVAP 70 80 90 100 110 120 KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG RTGGGGGGGH LARTTAARRA 130 140 150 160 170 180 VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG DAEETQDSED DEEDEMEEDD DDSDYPEEME 190 200 210 220 230 240 DDDDDASYCT ESSFRSHSTY SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN 250 260 270 280 290 300 EHIMNVIAIY EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT 310 320 330 340 350 360 SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE DYPYGPVENK 370 380 390 400 410 420 IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG DLLCCETCSA VYHLECVKPP 430 440 450 460 470 480 LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE 490 500 510 520 530 540 EDTENENEKK IWYYSTKVQL AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK 550 560 570 580 590 600 ARGSNKSFLA AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ 610 620 630 640 650 660 SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS PSEGRSPVGC 670 680 690 700 710 720 LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT TSIQPNLENS NSSSELNSSQ 730 740 750 760 770 780 SESAKAADDP ENGERESHTP VSIQEEIVGD FKSEKSNGEL SESPGAGKGA SGSTRIITRL 790 800 810 820 830 840 RNPDSKLSQL KSQQVAAAAH EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF 850 860 870 880 890 900 KLGQEGKYRV YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV 910 920 930 940 950 960 LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL AILECAVKPV 970 980 990 1000 1010 1020 VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE TMQQATWVKY TFPVKHQVWK 1030 1040 1050 1060 1070 1080 QKGEEYRVTG YGGWSWISKT HVYRFVPKLP GNTNVNYRKS LEGTKNNMDE NMDESDKRKC 1090 1100 1110 1120 1130 1140 SRSPKKIKIE PDSEKDEVKG SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE 1150 1160 1170 1180 1190 1200 PMEVDDDMKT ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE 1210 1220 1230 1240 1250 1260 EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ SPNANNDQPE 1270 1280 1290 1300 1310 1320 DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS PETKCPKQNS IENDIEEKVS 1330 1340 1350 1360 1370 1380 DLASRGQEPS KSKTKGNDFF IDDSKLASAD DIGTLICKNK KPLIQEESDT IVSSSKSALH 1390 1400 1410 1420 1430 1440 SSVPKSTNDR DATPLSRAMD FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES 1450 1460 1470 1480 1490 1500 ISEQFRTREQ DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK 1510 1520 1530 1540 1550 1560 CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK EISESRVVSG 1570 1580 1590 1600 1610 1620 NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED FNERNSSETK SHLLSSSDAE 1630 1640 1650 1660 1670 1680 GNYRDSLETL PSTKESDSTQ TTTPSASCPE SNSVNQVEDM EIETSEVKKV TSSPITSEEE 1690 1700 1710 1720 1730 1740 SNLSNDFIDE NGLPINKNEN VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV 1750 1760 1770 1780 1790 1800 SSTENCAKST VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT 1810 1820 1830 1840 1850 1860 SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP NDDLKKLARK 1870 1880 1890 1900 1910 1920 GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV KSLAGVSLML RLLWASLRWD 1930 1940 1950 1960 1970 1980 DMAAKAPPGG GTTRTETSET EITTTEIIKR RDVGPYGIRS EYCIRKIICP IGVPETPKET 1990 2000 2010 2020 2030 2040 PTPQRKGLRS SALRPKRPET PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ 2050 2060 2070 2080 2090 2100 QAKKRLEQQK PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA 2110 2120 2130 2140 2150 2160 TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT SFQPRTATVT 2170 2180 2190 2200 2210 2220 IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG KAIIRTPVMV QPGAPQQVMT 2230 2240 2250 2260 2270 2280 QIIRGQPVST AVSAPNTVSS TPGQKSLTSA TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ 2290 2300 2310 2320 2330 2340 LTQGHGGNQG LTVVIQGQGQ TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL 2350 2360 2370 2380 2390 2400 ATTATTASTT TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ 2410 2420 2430 2440 2450 2460 PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ VAAQSQPQSN 2470 2480 2490 2500 2510 2520 VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP IPIQPHTSLQ IPSQGQPQSQ 2530 2540 2550 2560 2570 2580 PQVQSSTQTL SSGQTLNQVT VSSPSRPQLQ IQQPQPQVIA VPQLQQQVQV LSQIQSQVVA 2590 2600 2610 2620 2630 2640 QIQAQQSGVP QQIKLQLPIQ IQQSSAVQTH QIQNVVTVQA ASVQEQLQRV QQLRDQQQKK 2650 2660 2670 2680 2690 2700 KQQQIEIKRE HTLQASNQSE IIQKQVVMKH NAVIEHLKQK KSMTPAEREE NQRMIVCNQV 2710 2720 2730 2740 2750 2760 MKYILDKIDK EEKQAAKKRK REESVEQKRS KQNATKLSAL LFKHKEQLRA EILKKRALLD 2770 2780 2790 2800 2810 2820 KDLQIEVQEE LKRDLKIKKE KDLMQLAQAT AVAAPCPPVT PAPPAPPAPP PSPPPPPAVQ 2830 2840 2850 2860 2870 2880 HTGLLSTPTL PAASQKRKRE EEKDSSSKSK KKKMISTTSK ETKKDTKLYC ICKTPYDESK 2890 2900 2910 2920 2930 2940 FYIGCDRCQN WYHGRCVGIL QSEAELIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL 2950 2960 2970 2980 2990 3000 RSLQAHKMAW PFLEPVDPND APDYYGVIKE PMDLATMEER VQRRYYEKLT EFVADMTKIF 3010 3020 3030 3040 DNCRYYNPSD SPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAS
	Isoform 2 [UniParc]. Checksum: B4C61BE795C1C555	FASTA	2,920	325,124
	10 20 30 40 50 60 MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR WAAAQAEVAP 70 80 90 100 110 120 KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG RTGGGGGGGH LARTTAARRA 130 140 150 160 170 180 VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG DAEETQDSED DEEDEMEEDD DDSDYPEEME 190 200 210 220 230 240 DDDDDASYCT ESSFRSHSTY SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN 250 260 270 280 290 300 EHIMNVIAIY EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT 310 320 330 340 350 360 SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE DYPYGPVENK 370 380 390 400 410 420 IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG DLLCCETCSA VYHLECVKPP 430 440 450 460 470 480 LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE 490 500 510 520 530 540 EDTENENEKK IWYYSTKVQL AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK 550 560 570 580 590 600 ARGSNKSFLA AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ 610 620 630 640 650 660 SLEKDSDDKT PDDDPEQGKS EVGDFKSEKS NGELSESPGA GKGASGSTRI ITRLRNPDSK 670 680 690 700 710 720 LSQLKSQQVA AAAHEANKLF KEGKEVLVVN SQGEISRLST KKEVIMKGNI NNYFKLGQEG 730 740 750 760 770 780 KYRVYHNQYS TNSFALNKHQ HREDHDKRRH LAHKFCLTPA GEFKWNGSVH GSKVLTISTL 790 800 810 820 830 840 RLTITQLENN IPSSFLHPNW ASHRANWIKA VQMCSKPREF ALALAILECA VKPVVMLPIW 850 860 870 880 890 900 RESLGHTRLH RMTSIEREEK EKVKKKEKKQ EEEETMQQAT WVKYTFPVKH QVWKQKGEEY 910 920 930 940 950 960 RVTGYGGWSW ISKTHVYRFV PKLPGNTNVN YRKSLEGTKN NMDENMDESD KRKCSRSPKK 970 980 990 1000 1010 1020 IKIEPDSEKD EVKGSDAAKG ADQNEMDISK ITEKKDQDVK ELLDSDSDKP CKEEPMEVDD 1030 1040 1050 1060 1070 1080 DMKTESHVNC QESSQVDVVN VSEGFHLRTS YKKKTKSSKL DGLLERRIKQ FTLEEKQRLE 1090 1100 1110 1120 1130 1140 KIKLEGGIKG IGKTSTNSSK NLSESPVITK AKEGCQSDSM RQEQSPNANN DQPEDLIQGC 1150 1160 1170 1180 1190 1200 SESDSSVLRM SDPSHTTNKL YPKDRVLDDV SIRSPETKCP KQNSIENDIE EKVSDLASRG 1210 1220 1230 1240 1250 1260 QEPSKSKTKG NDFFIDDSKL ASADDIGTLI CKNKKPLIQE ESDTIVSSSK SALHSSVPKS 1270 1280 1290 1300 1310 1320 TNDRDATPLS RAMDFEGKLG CDSESNSTLE NSSDTVSIQD SSEEDMIVQN SNESISEQFR 1330 1340 1350 1360 1370 1380 TREQDVEVLE PLKCELVSGE STGNCEDRLP VKGTEANGKK PSQQKKLEER PVNKCSDQIK 1390 1400 1410 1420 1430 1440 LKNTTDKKNN ENRESEKKGQ RTSTFQINGK DNKPKIYLKG ECLKEISESR VVSGNVEPKV 1450 1460 1470 1480 1490 1500 NNINKIIPEN DIKSLTVKES AIRPFINGDV IMEDFNERNS SETKSHLLSS SDAEGNYRDS 1510 1520 1530 1540 1550 1560 LETLPSTKES DSTQTTTPSA SCPESNSVNQ VEDMEIETSE VKKVTSSPIT SEEESNLSND 1570 1580 1590 1600 1610 1620 FIDENGLPIN KNENVNGESK RKTVITEVTT MTSTVATESK TVIKVEKGDK QTVVSSTENC 1630 1640 1650 1660 1670 1680 AKSTVTTTTT TVTKLSTPST GGSVDIISVK EQSKTVVTTT VTDSLTTTGG TLVTSMTVSK 1690 1700 1710 1720 1730 1740 EYSTRDKVKL MKFSRPKKTR SGTALPSYRK FVTKSSKKSI FVLPNDDLKK LARKGGIREV 1750 1760 1770 1780 1790 1800 PYFNYNAKPA LDIWPYPSPR PTFGITWRYR LQTVKSLAGV SLMLRLLWAS LRWDDMAAKA 1810 1820 1830 1840 1850 1860 PPGGGTTRTE TSETEITTTE IIKRRDVGPY GIRSEYCIRK IICPIGVPET PKETPTPQRK 1870 1880 1890 1900 1910 1920 GLRSSALRPK RPETPKQTGP VIIETWVAEE ELELWEIRAF AERVEKEKAQ AVEQQAKKRL 1930 1940 1950 1960 1970 1980 EQQKPTVIAT STTSPTSSTT STISPAQKVM VAPISGSVTT GTKMVLTTKV GSPATVTFQQ 1990 2000 2010 2020 2030 2040 NKNFHQTFAT WVKQGQSNSG VVQVQQKVLG IIPSSTGTSQ QTFTSFQPRT ATVTIRPNTS 2050 2060 2070 2080 2090 2100 GSGGTTSNSQ VITGPQIRPG MTVIRTPLQQ STLGKAIIRT PVMVQPGAPQ QVMTQIIRGQ 2110 2120 2130 2140 2150 2160 PVSTAVSAPN TVSSTPGQKS LTSATSTSNI QSSASQPPRP QQGQVKLTMA QLTQLTQGHG 2170 2180 2190 2200 2210 2220 GNQGLTVVIQ GQGQTTGQLQ LIPQGVTVLP GPGQQLMQAA MPNGTVQRFL FTPLATTATT 2230 2240 2250 2260 2270 2280 ASTTTTTVST TAAGTGEQRQ SKLSPQMQVH QDKTLPPAQS SSVGPAEAQP QTAQPSAQPQ 2290 2300 2310 2320 2330 2340 PQTQPQSPAQ PEVQTQPEVQ TQTTVSSHVP SEAQPTHAQS SKPQVAAQSQ PQSNVQGQSP 2350 2360 2370 2380 2390 2400 VRVQSPSQTR IRPSTPSQLS PGQQSQVQTT TSQPIPIQPH TSLQIPSQGQ PQSQPQVQSS 2410 2420 2430 2440 2450 2460 TQTLSSGQTL NQVTVSSPSR PQLQIQQPQP QVIAVPQLQQ QVQVLSQIQS QVVAQIQAQQ 2470 2480 2490 2500 2510 2520 SGVPQQIKLQ LPIQIQQSSA VQTHQIQNVV TVQAASVQEQ LQRVQQLRDQ QQKKKQQQIE 2530 2540 2550 2560 2570 2580 IKREHTLQAS NQSEIIQKQV VMKHNAVIEH LKQKKSMTPA EREENQRMIV CNQVMKYILD 2590 2600 2610 2620 2630 2640 KIDKEEKQAA KKRKREESVE QKRSKQNATK LSALLFKHKE QLRAEILKKR ALLDKDLQIE 2650 2660 2670 2680 2690 2700 VQEELKRDLK IKKEKDLMQL AQATAVAAPC PPVTPAPPAP PAPPPSPPPP PAVQHTGLLS 2710 2720 2730 2740 2750 2760 TPTLPAASQK RKREEEKDSS SKSKKKKMIS TTSKETKKDT KLYCICKTPY DESKFYIGCD 2770 2780 2790 2800 2810 2820 RCQNWYHGRC VGILQSEAEL IDEYVCPQCQ STEDAMTVLT PLTEKDYEGL KRVLRSLQAH 2830 2840 2850 2860 2870 2880 KMAWPFLEPV DPNDAPDYYG VIKEPMDLAT MEERVQRRYY EKLTEFVADM TKIFDNCRYY 2890 2900 2910 2920 NPSDSPFYQC AEVLESFFVQ KLKGFKASRS HNNKLQSTAS
	Isoform 4 [UniParc]. Checksum: 29C8528E762E7D7D	FASTA	2,903	322,217
	10 20 30 40 50 60 MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR WAAAQAEVAP 70 80 90 100 110 120 KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG RTGGGGGGGH LARTTAARRA 130 140 150 160 170 180 VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG DAEETQDSED DEEDEMEEDD DDSDYPEEME 190 200 210 220 230 240 DDDDDASYCT ESSFRSHSTY SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN 250 260 270 280 290 300 EHIMNVIAIY EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT 310 320 330 340 350 360 SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE DYPYGPVENK 370 380 390 400 410 420 IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG DLLCCETCSA VYHLECVKPP 430 440 450 460 470 480 LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE 490 500 510 520 530 540 EDTENENEKK IWYYSTKVQL AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK 550 560 570 580 590 600 ARGSNKSFLA AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ 610 620 630 640 650 660 SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS PSEGRSPVGC 670 680 690 700 710 720 LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT TSIQPNLENS NSSSELNSSQ 730 740 750 760 770 780 SESAKAADDP ENGERESHTP VSIQEEIVGD FKSEKSNGEL SESPGAGKGA SGSTRIITRL 790 800 810 820 830 840 RNPDSKLSQL KSQQVAAAAH EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF 850 860 870 880 890 900 KLGQEGKYRV YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV 910 920 930 940 950 960 LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL AILECAVKPV 970 980 990 1000 1010 1020 VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE TMQQATWVKY TFPVKHQVWK 1030 1040 1050 1060 1070 1080 QKGEEYRVTG YGGWSWISKT HVYRFVPKLP GNTNVNYRKS LEGTKNNMDE NMDESDKRKC 1090 1100 1110 1120 1130 1140 SRSPKKIKIE PDSEKDEVKG SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE 1150 1160 1170 1180 1190 1200 PMEVDDDMKT ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE 1210 1220 1230 1240 1250 1260 EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ SPNANNDQPE 1270 1280 1290 1300 1310 1320 DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS PETKCPKQNS IENDIEEKVS 1330 1340 1350 1360 1370 1380 DLASRGQEPS KSKTKGNDFF IDDSKLASAD DIGTLICKNK KPLIQEESDT IVSSSKSALH 1390 1400 1410 1420 1430 1440 SSVPKSTNDR DATPLSRAMD FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES 1450 1460 1470 1480 1490 1500 ISEQFRTREQ DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK 1510 1520 1530 1540 1550 1560 CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK EISESRVVSG 1570 1580 1590 1600 1610 1620 NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED FNERNSSETK SHLLSSSDAE 1630 1640 1650 1660 1670 1680 GNYRDSLETL PSTKESDSTQ TTTPSASCPE SNSVNQVEDM EIETSEVKKV TSSPITSEEE 1690 1700 1710 1720 1730 1740 SNLSNDFIDE NGLPINKNEN VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV 1750 1760 1770 1780 1790 1800 SSTENCAKST VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT 1810 1820 1830 1840 1850 1860 SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP NDDLKKLARK 1870 1880 1890 1900 1910 1920 GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV KSLAGVSLML RLLWASLRWD 1930 1940 1950 1960 1970 1980 DMAAKAPPGG GTTRTETSET EITTTEIIKR RDVGPYGIRS EYCIRKIICP IGVPETPKET 1990 2000 2010 2020 2030 2040 PTPQRKGLRS SALRPKRPET PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ 2050 2060 2070 2080 2090 2100 QAKKRLEQQK PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA 2110 2120 2130 2140 2150 2160 TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT SFQPRTATVT 2170 2180 2190 2200 2210 2220 IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG KAIIRTPVMV QPGAPQQVMT 2230 2240 2250 2260 2270 2280 QIIRGQPVST AVSAPNTVSS TPGQKSLTSA TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ 2290 2300 2310 2320 2330 2340 LTQGHGGNQG LTVVIQGQGQ TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL 2350 2360 2370 2380 2390 2400 ATTATTASTT TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ 2410 2420 2430 2440 2450 2460 PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ VAAQSQPQSN 2470 2480 2490 2500 2510 2520 VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP IPIQPHTSLQ IPSQGQPQSQ 2530 2540 2550 2560 2570 2580 PQVVMKHNAV IEHLKQKKSM TPAEREENQR MIVCNQVMKY ILDKIDKEEK QAAKKRKREE 2590 2600 2610 2620 2630 2640 SVEQKRSKQN ATKLSALLFK HKEQLRAEIL KKRALLDKDL QIEVQEELKR DLKIKKEKDL 2650 2660 2670 2680 2690 2700 MQLAQATAVA APCPPVTPAP PAPPAPPPSP PPPPAVQHTG LLSTPTLPAA SQKRKREEEK 2710 2720 2730 2740 2750 2760 DSSSKSKKKK MISTTSKETK KDTKLYCICK TPYDESKFYI GCDRCQNWYH GRCVGILQSE 2770 2780 2790 2800 2810 2820 AELIDEYVCP QCQSTEDAMT VLTPLTEKDY EGLKRVLRSL QAHKMAWPFL EPVDPNDAPD 2830 2840 2850 2860 2870 2880 YYGVIKEPMD LATMEERVQR RYYEKLTEFV ADMTKIFDNC RYYNPSDSPF YQCAEVLESF 2890 2900 FVQKLKGFKA SRSHNNKLQS TAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of BPTF, a novel bromodomain transcription factor." Jones M.H., Hamana N., Shimane M. Genomics 63:35-39(2000) [PubMed: 10662542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"FAC1, a novel gene identified with the monoclonal antibody Alz50, is developmentally regulated in human brain." Bowser R., Giambrone A., Davies P. Dev. Neurosci. 17:20-37(1995) [PubMed: 7621746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-992 (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Fetal brain.
[4]	"Isolation of human NURF: a regulator of Engrailed gene expression." Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., Shiekhattar R. EMBO J. 22:6089-6100(2003) [PubMed: 14609955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-3046 (ISOFORM 4), IDENTIFICATION IN THE NURF COMPLEX, MASS SPECTROMETRY.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2876-3046 (ISOFORM 1). Tissue: Kidney.
[6]	"FAC1 expression and localization in motor neurons of developing, adult, and amyotrophic lateral sclerosis spinal cord." Mu X., Springer J.E., Bowser R. Exp. Neurol. 146:17-24(1997) [PubMed: 9225734] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[7]	"DNA binding activity of the fetal Alz-50 clone 1 (FAC1) protein is enhanced by phosphorylation." Jordan-Sciutto K.L., Dragich J.M., Bowser R. Biochem. Biophys. Res. Commun. 260:785-789(1999) [PubMed: 10403843] [Abstract] Cited for: DNA-BINDING, PHOSPHORYLATION.
[8]	"Fetal Alz-50 clone 1, a novel zinc finger protein, binds a specific DNA sequence and acts as a transcriptional regulator." Jordan-Sciutto K.L., Dragich J.M., Rhodes J.L., Bowser R. J. Biol. Chem. 274:35262-35268(1999) [PubMed: 10575013] [Abstract] Cited for: DNA-BINDING.
[9]	"Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity." Jordan-Sciutto K.L., Dragich J.M., Caltagarone J., Hall D.J., Bowser R. Biochemistry 39:3206-3215(2000) [PubMed: 10727212] [Abstract] Cited for: INTERACTION WITH MAZ, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[10]	"Fetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like Ech-associated protein." Strachan G.D., Morgan K.L., Otis L.L., Caltagarone J., Gittis A., Bowser R., Jordan-Sciutto K.L. Biochemistry 43:12113-12122(2004) [PubMed: 15379550] [Abstract] Cited for: INTERACTION WITH KEAP1, SUBCELLULAR LOCATION.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-572; THR-1064; SER-1827 AND SER-1833, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling." Wysocka J., Swigut T., Xiao H., Milne T.A., Kwon S.Y., Landry J., Kauer M., Tackett A.J., Chait B.T., Badenhorst P., Wu C., Allis C.D. Nature 442:86-90(2006) [PubMed: 16728976] [Abstract] Cited for: INTERACTION WITH HISTONE H3K4ME3, MUTAGENESIS OF TRP-2891, MASS SPECTROMETRY.
[14]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-839, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-763; SER-1300 AND SER-2098, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763; SER-1231 AND SER-2098, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-909; SER-2098 AND SER-2465, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-880, MASS SPECTROMETRY.
[21]	"Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF." Li H., Ilin S., Wang W., Duncan E.M., Wysocka J., Allis C.D., Patel D.J. Nature 442:91-95(2006) [PubMed: 16728978] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2865-3033, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH H3(1-154)K4ME3, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH H3(1-154)K4ME2, STRUCTURE BY NMR OF 2865-2922, STRUCTURE BY NMR OF 2865-2922 IN COMPLEX WITH H3(1-154)K4ME3, MUTAGENESIS OF TYR-2869; TYR-2876; TYR-2882; GLY-2884; ASP-2886; GLN-2889 AND TRP-2891.
[22]	"Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger." Li H., Fischle W., Wang W., Duncan E.M., Liang L., Murakami-Ishibe S., Allis C.D., Patel D.J. Mol. Cell 28:677-691(2007) [PubMed: 18042461] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH H3(1-154)K4ME2, DOMAIN PHD-FINGER, MUTAGENESIS OF TYR-2876.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB032251 mRNA. Translation: BAA89208.1. Sequence problems.
AC006534 Genomic DNA. No translation available.
AC107377 Genomic DNA. No translation available.
AC134407 Genomic DNA. No translation available.
U05237 mRNA. Translation: AAA97522.1. Sequence problems.
AY282495 mRNA. Translation: AAP22284.1.
BC067234 mRNA. Translation: AAH67234.1.

IPI

IPI00254408.
IPI00376404.
IPI00785110.

PIR

G01252.

RefSeq

NP_004450.3. NM_004459.6.
NP_872579.2. NM_182641.3.

UniGene

Hs.444200.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F6J	X-ray	2.00	A/B/C	2865-3033	[»]
2F6N	X-ray	2.00	A/B	2865-3033	[»]
2FSA	X-ray	1.90	A/B/C	2865-3033	[»]
2FUI	NMR	-	A	2865-2921	[»]
2FUU	NMR	-	A	2865-2921	[»]
2RI7	X-ray	1.45	A	2865-3033	[»]
3QZS	X-ray	1.80	A/B	2924-3033	[»]
3QZT	X-ray	1.50	A	2924-3033	[»]
3QZV	X-ray	2.00	A	2865-3033	[»]

ProteinModelPortal

Q12830.

SMR

Q12830. Positions 388-441, 2865-3032.

ModBase

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Protein-protein interaction databases

IntAct

Q12830. 5 interactions.

STRING

Q12830.

PTM databases

PhosphoSite

Q12830.

Polymorphism databases

DMDM

215274183.

Proteomic databases

PRIDE

Q12830.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000321892; ENSP00000315454; ENSG00000171634.

GeneID

2186.

KEGG

hsa:2186.

UCSC

uc002jgf.1. human.

Organism-specific databases

CTD

2186.

GeneCards

GC17P065821.

HGNC

HGNC:3581. BPTF.

HPA

HPA029069.

MIM

601819. gene.

neXtProt

NX_Q12830.

PharmGKB

PA162377557.

GenAtlas

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Phylogenomic databases

GeneTree

ENSGT00430000030976.

HOGENOM

HBG505875.

HOVERGEN

HBG080062.

OMA

ENVNGES.

PhylomeDB

Q12830.

Gene expression databases

ArrayExpress

Q12830.

Bgee

Q12830.

CleanEx

HS_BPTF.

Genevestigator

Q12830.

GermOnline

ENSG00000171634. Homo sapiens.

Family and domain databases

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.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.
G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits.

KO

K11728.

Pfam

PF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF00628. PHD. 2 hits.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF57903. FYVE_PHD_ZnF. 2 hits.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

ProtoNet

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Other

NextBio

8831.

SOURCE

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Entry information

Entry name

BPTF_HUMAN

Accession

Primary (citable) accession number: Q12830
Secondary accession number(s): Q6NX67, Q7Z7D6, Q9UIG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.