Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12830 (BPTF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3046 AA.
Sequence statusComplete.
Protein existenceEvidence 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.4 Ref.9 Ref.10 Ref.12

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.

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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.4. Source: GOC

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from mutant phenotype Ref.4. Source: HGNC

chromatin remodeling

Inferred from direct assay Ref.4. Source: HGNC

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

endoderm development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.9. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.4. Source: HGNC

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.8. Source: HGNC

transcription, DNA-templated

Inferred from mutant phenotype Ref.4. Source: HGNC

   Cellular_componentNURF complex

Inferred from direct assay PubMed 20850016. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.7Ref.4. Source: HGNC

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 21596426PubMed 21596426. 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

HIST2H3AQ71DI32EBI-4288838,EBI-750650
HIST2H4BP6280516EBI-4288838,EBI-302023

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 30463046Nucleosome-remodeling factor subunit BPTF
PRO_0000087176

Regions

Domain240 – 30061DDT
Domain2944 – 301471Bromo
Zinc finger390 – 43748PHD-type 1
Zinc finger2867 – 291852PHD-type 2
Region640 – 749110Interaction with KEAP1
Region839 – 92183Interaction with MAZ
Coiled coil574 – 60431 Potential
Coiled coil978 – 100730 Potential
Coiled coil2022 – 205029 Potential
Coiled coil2706 – 273227 Potential
Compositional bias143 – 18038Glu-rich
Compositional bias149 – 18537Asp-rich
Compositional bias1709 – 180395Thr-rich
Compositional bias2338 – 236124Thr-rich
Compositional bias2795 – 281723Pro-rich
Compositional bias2848 – 28536Poly-Lys

Sites

Binding site28691Histone H3K4me3
Binding site28761Histone H3K4me3
Binding site28821Histone H3K4me3
Binding site28911Histone H3K4me3

Amino acid modifications

Modified residue2161Phosphoserine Ref.16 Ref.18 Ref.20
Modified residue5721Phosphoserine Ref.20
Modified residue7631Phosphoserine Ref.14 Ref.18 Ref.20
Modified residue8171Phosphoserine Ref.13
Modified residue8801N6-acetyllysine Ref.17
Modified residue10641Phosphothreonine Ref.11 Ref.20
Modified residue12311Phosphoserine Ref.20
Modified residue12511Phosphoserine Ref.20
Modified residue13001Phosphoserine Ref.14 Ref.20
Modified residue13101Phosphoserine Ref.18 Ref.20
Modified residue20981Phosphoserine Ref.14 Ref.18
Modified residue24651Phosphoserine Ref.20

Natural variations

Alternative sequence622 – 747126Missing in isoform 2.
VSP_020402
Alternative sequence2522 – 2664143Missing in isoform 4.
VSP_020405

Experimental info

Mutagenesis28691Y → T: Abolishes binding to histone H3K4me3. Ref.21
Mutagenesis28761Y → E: Induces binding to histone H3K4me2. Ref.21 Ref.22
Mutagenesis28761Y → T: Strongly reduces binding to histone H3K4me3. Ref.21 Ref.22
Mutagenesis28821Y → S: Abolishes binding to histone H3K4me3. Ref.21
Mutagenesis28841G → E or L: Strongly reduces binding to histone H3K4me3. Ref.21
Mutagenesis28861D → N or A: Abolishes binding to histone H3K4me3. Ref.21
Mutagenesis28891Q → K: Strongly reduces binding to histone H3K4me3. Ref.21
Mutagenesis28911W → E or F: Abolishes binding to histone H3K4me3. Ref.12 Ref.21
Sequence conflict7521K → T in AAA97522. Ref.3
Sequence conflict7571N → T in AAA97522. Ref.3
Sequence conflict9691S → F in BAA89208. Ref.1
Sequence conflict12681E → Q in BAA89208. Ref.1
Sequence conflict13301S → T in BAA89208. Ref.1
Sequence conflict18421S → T in BAA89208. Ref.1
Sequence conflict18421S → T in AAP22284. Ref.4
Sequence conflict19261A → V in BAA89208. Ref.1
Sequence conflict19261A → V in AAP22284. Ref.4
Sequence conflict19321T → S in BAA89208. Ref.1
Sequence conflict19321T → S in AAP22284. Ref.4
Sequence conflict19601S → F in BAA89208. Ref.1
Sequence conflict23931E → K in BAA89208. Ref.1
Sequence conflict24041Q → R in BAA89208. Ref.1
Sequence conflict25401T → S in BAA89208. Ref.1
Sequence conflict2802 – 28032AP → VL in BAA89208. Ref.1
Sequence conflict28181A → G in BAA89208. Ref.1
Sequence conflict28321A → V in BAA89208. Ref.1
Sequence conflict28761Y → G in AAH67234. Ref.5
Sequence conflict28801K → Q in AAH67234. Ref.5

Secondary structure

............................... 3046
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 37D7206977A8DB09

FASTA3,046338,262
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B4C61BE795C1C555
Show »

FASTA2,920325,124
Isoform 4 [UniParc].

Checksum: 29C8528E762E7D7D
Show »

FASTA2,903322,217

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-3046 (ISOFORM 4), IDENTIFICATION IN THE NURF COMPLEX, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KEAP1, SUBCELLULAR LOCATION.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1064, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H3K4ME3, MUTAGENESIS OF TRP-2891, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763; SER-1300 AND SER-2098, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-763; SER-1310 AND SER-2098, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-572; SER-763; THR-1064; SER-1231; SER-1251; SER-1300; SER-1310 AND SER-2465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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] [Europe PMC] [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.
[23]"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 2914-3037.
+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.
CCDSCCDS11672.1. [Q12830-4]
CCDS11673.1. [Q12830-2]
PIRG01252.
RefSeqNP_004450.3. NM_004459.6. [Q12830-4]
NP_872579.2. NM_182641.3. [Q12830-2]
UniGeneHs.444200.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F6JX-ray2.00A/B/C2865-3033[»]
2F6NX-ray2.00A/B2865-3033[»]
2FSAX-ray1.90A/B/C2865-3033[»]
2FUINMR-A2865-2921[»]
2FUUNMR-A2865-2921[»]
2RI7X-ray1.45A2865-3033[»]
3QZSX-ray1.80A/B2924-3033[»]
3QZTX-ray1.50A2924-3033[»]
3QZVX-ray2.00A2865-3033[»]
3UV2X-ray1.58A2914-3037[»]
ProteinModelPortalQ12830.
SMRQ12830. Positions 389-473, 2865-3032.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108481. 24 interactions.
DIPDIP-38919N.
IntActQ12830. 6 interactions.
MINTMINT-3973225.
STRING9606.ENSP00000307208.

PTM databases

PhosphoSiteQ12830.

Polymorphism databases

DMDM215274183.

Proteomic databases

MaxQBQ12830.
PaxDbQ12830.
PRIDEQ12830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306378; ENSP00000307208; ENSG00000171634. [Q12830-2]
ENST00000321892; ENSP00000315454; ENSG00000171634. [Q12830-1]
ENST00000335221; ENSP00000334351; ENSG00000171634. [Q12830-4]
ENST00000573834; ENSP00000461014; ENSG00000262858. [Q12830-2]
GeneID2186.
KEGGhsa:2186.
UCSCuc002jge.3. human. [Q12830-4]
uc002jgf.3. human. [Q12830-2]

Organism-specific databases

CTD2186.
GeneCardsGC17P065821.
HGNCHGNC:3581. BPTF.
HPAHPA029069.
HPA048724.
MIM601819. gene.
neXtProtNX_Q12830.
PharmGKBPA162377557.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000231041.
HOVERGENHBG080062.
KOK11728.
OMAPFMNGDV.
PhylomeDBQ12830.
TreeFamTF316840.

Enzyme and pathway databases

SignaLinkQ12830.

Gene expression databases

ArrayExpressQ12830.
BgeeQ12830.
CleanExHS_BPTF.
GenevestigatorQ12830.

Family and domain databases

Gene3D1.20.920.10. 2 hits.
3.30.40.10. 2 hits.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR004022. DDT_dom.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF00628. PHD. 2 hits.
PF15612. WHIM1. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

ChiTaRSBPTF. human.
EvolutionaryTraceQ12830.
GeneWikiBPTF.
GenomeRNAi2186.
NextBio8831.
PROQ12830.
SOURCESearch...

Entry information

Entry nameBPTF_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM