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Q12830

- BPTF_HUMAN

UniProt

Q12830 - BPTF_HUMAN

Protein

Nucleosome-remodeling factor subunit BPTF

Gene

BPTF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei2869 – 28691Histone H3K4me3
    Binding sitei2876 – 28761Histone H3K4me3
    Binding sitei2882 – 28821Histone H3K4me3
    Binding sitei2891 – 28911Histone H3K4me3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri390 – 43748PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri2867 – 291852PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. sequence-specific DNA binding Source: HGNC
    3. transcription factor binding Source: MGI
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. ATP catabolic process Source: GOC
    3. brain development Source: HGNC
    4. chromatin remodeling Source: HGNC
    5. embryonic placenta development Source: Ensembl
    6. endoderm development Source: Ensembl
    7. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    8. positive regulation of transcription, DNA-templated Source: HGNC
    9. regulation of transcription, DNA-templated Source: HGNC
    10. transcription, DNA-templated Source: HGNC

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ12830.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:BPTF
    Synonyms:FAC1, FALZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3581. BPTF.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: In brains of Alzheimer disease patients, present in a subset of amyloid-containing plaques.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. microtubule cytoskeleton Source: HPA
    3. nucleolus Source: HPA
    4. nucleus Source: HGNC
    5. NURF complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2869 – 28691Y → T: Abolishes binding to histone H3K4me3. 1 Publication
    Mutagenesisi2876 – 28761Y → E: Induces binding to histone H3K4me2. 2 Publications
    Mutagenesisi2876 – 28761Y → T: Strongly reduces binding to histone H3K4me3. 2 Publications
    Mutagenesisi2882 – 28821Y → S: Abolishes binding to histone H3K4me3. 1 Publication
    Mutagenesisi2884 – 28841G → E or L: Strongly reduces binding to histone H3K4me3. 1 Publication
    Mutagenesisi2886 – 28861D → N or A: Abolishes binding to histone H3K4me3. 1 Publication
    Mutagenesisi2889 – 28891Q → K: Strongly reduces binding to histone H3K4me3. 1 Publication
    Mutagenesisi2891 – 28911W → E or F: Abolishes binding to histone H3K4me3. 2 Publications

    Organism-specific databases

    PharmGKBiPA162377557.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 30463046Nucleosome-remodeling factor subunit BPTFPRO_0000087176Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei216 – 2161Phosphoserine4 Publications
    Modified residuei572 – 5721Phosphoserine2 Publications
    Modified residuei763 – 7631Phosphoserine4 Publications
    Modified residuei817 – 8171Phosphoserine2 Publications
    Modified residuei880 – 8801N6-acetyllysine1 Publication
    Modified residuei1064 – 10641Phosphothreonine3 Publications
    Modified residuei1231 – 12311Phosphoserine2 Publications
    Modified residuei1251 – 12511Phosphoserine2 Publications
    Modified residuei1300 – 13001Phosphoserine3 Publications
    Modified residuei1310 – 13101Phosphoserine3 Publications
    Modified residuei2098 – 20981Phosphoserine3 Publications
    Modified residuei2465 – 24651Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation enhances DNA-binding.7 Publications
    Highly susceptible to proteolysis.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ12830.
    PaxDbiQ12830.
    PRIDEiQ12830.

    PTM databases

    PhosphoSiteiQ12830.

    Expressioni

    Tissue specificityi

    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).4 Publications

    Developmental stagei

    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).1 Publication

    Gene expression databases

    ArrayExpressiQ12830.
    BgeeiQ12830.
    CleanExiHS_BPTF.
    GenevestigatoriQ12830.

    Organism-specific databases

    HPAiHPA029069.
    HPA048724.

    Interactioni

    Subunit structurei

    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-K4Me2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H3AQ71DI32EBI-4288838,EBI-750650
    HIST2H4BP6280516EBI-4288838,EBI-302023

    Protein-protein interaction databases

    BioGridi108481. 25 interactions.
    DIPiDIP-38919N.
    IntActiQ12830. 6 interactions.
    MINTiMINT-3973225.
    STRINGi9606.ENSP00000307208.

    Structurei

    Secondary structure

    1
    3046
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2870 – 28734
    Beta strandi2882 – 28843
    Turni2886 – 28883
    Beta strandi2891 – 28933
    Helixi2894 – 28974
    Helixi2901 – 29044
    Helixi2913 – 292210
    Turni2923 – 29253
    Helixi2930 – 294415
    Helixi2947 – 29493
    Turni2950 – 29523
    Turni2958 – 29603
    Helixi2962 – 29676
    Helixi2974 – 29829
    Helixi2989 – 300618
    Helixi3012 – 302716
    Turni3028 – 30303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ12830.
    SMRiQ12830. Positions 389-473, 2865-3032.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12830.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini240 – 30061DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini2944 – 301471BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni640 – 749110Interaction with KEAP1Add
    BLAST
    Regioni839 – 92183Interaction with MAZAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili574 – 60431Sequence AnalysisAdd
    BLAST
    Coiled coili978 – 100730Sequence AnalysisAdd
    BLAST
    Coiled coili2022 – 205029Sequence AnalysisAdd
    BLAST
    Coiled coili2706 – 273227Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi143 – 18038Glu-richAdd
    BLAST
    Compositional biasi149 – 18537Asp-richAdd
    BLAST
    Compositional biasi1709 – 180395Thr-richAdd
    BLAST
    Compositional biasi2338 – 236124Thr-richAdd
    BLAST
    Compositional biasi2795 – 281723Pro-richAdd
    BLAST
    Compositional biasi2848 – 28536Poly-Lys

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Belongs to the PBTF family.Curated
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 DDT domain.PROSITE-ProRule annotation
    Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri390 – 43748PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri2867 – 291852PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000231041.
    HOVERGENiHBG080062.
    KOiK11728.
    OMAiPFMNGDV.
    PhylomeDBiQ12830.
    TreeFamiTF316840.

    Family and domain databases

    Gene3Di1.20.920.10. 2 hits.
    3.30.40.10. 2 hits.
    InterProiIPR001487. 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]
    PfamiPF00439. Bromodomain. 1 hit.
    PF02791. DDT. 1 hit.
    PF00628. PHD. 2 hits.
    PF15612. WHIM1. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 2 hits.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEiPS00633. 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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12830-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR     50
    WAAAQAEVAP KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG 100
    RTGGGGGGGH LARTTAARRA VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG 150
    DAEETQDSED DEEDEMEEDD DDSDYPEEME DDDDDASYCT ESSFRSHSTY 200
    SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN EHIMNVIAIY 250
    EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT 300
    SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE 350
    DYPYGPVENK IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG 400
    DLLCCETCSA VYHLECVKPP LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ 450
    KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE EDTENENEKK IWYYSTKVQL 500
    AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK ARGSNKSFLA 550
    AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ 600
    SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS 650
    PSEGRSPVGC LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT 700
    TSIQPNLENS NSSSELNSSQ SESAKAADDP ENGERESHTP VSIQEEIVGD 750
    FKSEKSNGEL SESPGAGKGA SGSTRIITRL RNPDSKLSQL KSQQVAAAAH 800
    EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF KLGQEGKYRV 850
    YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV 900
    LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL 950
    AILECAVKPV VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE 1000
    TMQQATWVKY TFPVKHQVWK QKGEEYRVTG YGGWSWISKT HVYRFVPKLP 1050
    GNTNVNYRKS LEGTKNNMDE NMDESDKRKC SRSPKKIKIE PDSEKDEVKG 1100
    SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE PMEVDDDMKT 1150
    ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE 1200
    EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ 1250
    SPNANNDQPE DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS 1300
    PETKCPKQNS IENDIEEKVS DLASRGQEPS KSKTKGNDFF IDDSKLASAD 1350
    DIGTLICKNK KPLIQEESDT IVSSSKSALH SSVPKSTNDR DATPLSRAMD 1400
    FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES ISEQFRTREQ 1450
    DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK 1500
    CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK 1550
    EISESRVVSG NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED 1600
    FNERNSSETK SHLLSSSDAE GNYRDSLETL PSTKESDSTQ TTTPSASCPE 1650
    SNSVNQVEDM EIETSEVKKV TSSPITSEEE SNLSNDFIDE NGLPINKNEN 1700
    VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV SSTENCAKST 1750
    VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT 1800
    SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP 1850
    NDDLKKLARK GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV 1900
    KSLAGVSLML RLLWASLRWD DMAAKAPPGG GTTRTETSET EITTTEIIKR 1950
    RDVGPYGIRS EYCIRKIICP IGVPETPKET PTPQRKGLRS SALRPKRPET 2000
    PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ QAKKRLEQQK 2050
    PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA 2100
    TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT 2150
    SFQPRTATVT IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG 2200
    KAIIRTPVMV QPGAPQQVMT QIIRGQPVST AVSAPNTVSS TPGQKSLTSA 2250
    TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ LTQGHGGNQG LTVVIQGQGQ 2300
    TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL ATTATTASTT 2350
    TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ 2400
    PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ 2450
    VAAQSQPQSN VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP 2500
    IPIQPHTSLQ IPSQGQPQSQ PQVQSSTQTL SSGQTLNQVT VSSPSRPQLQ 2550
    IQQPQPQVIA VPQLQQQVQV LSQIQSQVVA QIQAQQSGVP QQIKLQLPIQ 2600
    IQQSSAVQTH QIQNVVTVQA ASVQEQLQRV QQLRDQQQKK KQQQIEIKRE 2650
    HTLQASNQSE IIQKQVVMKH NAVIEHLKQK KSMTPAEREE NQRMIVCNQV 2700
    MKYILDKIDK EEKQAAKKRK REESVEQKRS KQNATKLSAL LFKHKEQLRA 2750
    EILKKRALLD KDLQIEVQEE LKRDLKIKKE KDLMQLAQAT AVAAPCPPVT 2800
    PAPPAPPAPP PSPPPPPAVQ HTGLLSTPTL PAASQKRKRE EEKDSSSKSK 2850
    KKKMISTTSK ETKKDTKLYC ICKTPYDESK FYIGCDRCQN WYHGRCVGIL 2900
    QSEAELIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL RSLQAHKMAW 2950
    PFLEPVDPND APDYYGVIKE PMDLATMEER VQRRYYEKLT EFVADMTKIF 3000
    DNCRYYNPSD SPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAS 3046

    Note: No experimental confirmation available.

    Length:3,046
    Mass (Da):338,262
    Last modified:November 25, 2008 - v3
    Checksum:i37D7206977A8DB09
    GO
    Isoform 2 (identifier: Q12830-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,920
    Mass (Da):325,124
    Checksum:iB4C61BE795C1C555
    GO
    Isoform 4 (identifier: Q12830-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,903
    Mass (Da):322,217
    Checksum:i29C8528E762E7D7D
    GO

    Sequence cautioni

    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.
    The sequence AAA97522.1 differs from that shown. Reason: Frameshift at positions 136 and 915.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti752 – 7521K → T in AAA97522. (PubMed:7621746)Curated
    Sequence conflicti757 – 7571N → T in AAA97522. (PubMed:7621746)Curated
    Sequence conflicti969 – 9691S → F in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti1268 – 12681E → Q in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti1330 – 13301S → T in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti1842 – 18421S → T in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti1842 – 18421S → T in AAP22284. (PubMed:14609955)Curated
    Sequence conflicti1926 – 19261A → V in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti1926 – 19261A → V in AAP22284. (PubMed:14609955)Curated
    Sequence conflicti1932 – 19321T → S in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti1932 – 19321T → S in AAP22284. (PubMed:14609955)Curated
    Sequence conflicti1960 – 19601S → F in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2393 – 23931E → K in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2404 – 24041Q → R in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2540 – 25401T → S in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2802 – 28032AP → VL in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2818 – 28181A → G in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2832 – 28321A → V in BAA89208. (PubMed:10662542)Curated
    Sequence conflicti2876 – 28761Y → G in AAH67234. (PubMed:15489334)Curated
    Sequence conflicti2880 – 28801K → Q in AAH67234. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei622 – 747126Missing in isoform 2. 1 PublicationVSP_020402Add
    BLAST
    Alternative sequencei2522 – 2664143Missing in isoform 4. 1 PublicationVSP_020405Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11672.1. [Q12830-4]
    CCDS11673.1. [Q12830-2]
    PIRiG01252.
    RefSeqiNP_004450.3. NM_004459.6. [Q12830-4]
    NP_872579.2. NM_182641.3. [Q12830-2]
    UniGeneiHs.444200.

    Genome annotation databases

    EnsembliENST00000306378; ENSP00000307208; ENSG00000171634. [Q12830-2]
    ENST00000321892; ENSP00000315454; ENSG00000171634. [Q12830-1]
    ENST00000335221; ENSP00000334351; ENSG00000171634. [Q12830-4]
    GeneIDi2186.
    KEGGihsa:2186.
    UCSCiuc002jge.3. human. [Q12830-4]
    uc002jgf.3. human. [Q12830-2]

    Polymorphism databases

    DMDMi215274183.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11672.1. [Q12830-4 ]
    CCDS11673.1. [Q12830-2 ]
    PIRi G01252.
    RefSeqi NP_004450.3. NM_004459.6. [Q12830-4 ]
    NP_872579.2. NM_182641.3. [Q12830-2 ]
    UniGenei Hs.444200.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3UV2 X-ray 1.58 A 2914-3037 [» ]
    ProteinModelPortali Q12830.
    SMRi Q12830. Positions 389-473, 2865-3032.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108481. 25 interactions.
    DIPi DIP-38919N.
    IntActi Q12830. 6 interactions.
    MINTi MINT-3973225.
    STRINGi 9606.ENSP00000307208.

    PTM databases

    PhosphoSitei Q12830.

    Polymorphism databases

    DMDMi 215274183.

    Proteomic databases

    MaxQBi Q12830.
    PaxDbi Q12830.
    PRIDEi Q12830.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306378 ; ENSP00000307208 ; ENSG00000171634 . [Q12830-2 ]
    ENST00000321892 ; ENSP00000315454 ; ENSG00000171634 . [Q12830-1 ]
    ENST00000335221 ; ENSP00000334351 ; ENSG00000171634 . [Q12830-4 ]
    GeneIDi 2186.
    KEGGi hsa:2186.
    UCSCi uc002jge.3. human. [Q12830-4 ]
    uc002jgf.3. human. [Q12830-2 ]

    Organism-specific databases

    CTDi 2186.
    GeneCardsi GC17P065821.
    HGNCi HGNC:3581. BPTF.
    HPAi HPA029069.
    HPA048724.
    MIMi 601819. gene.
    neXtProti NX_Q12830.
    PharmGKBi PA162377557.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000231041.
    HOVERGENi HBG080062.
    KOi K11728.
    OMAi PFMNGDV.
    PhylomeDBi Q12830.
    TreeFami TF316840.

    Enzyme and pathway databases

    SignaLinki Q12830.

    Miscellaneous databases

    ChiTaRSi BPTF. human.
    EvolutionaryTracei Q12830.
    GeneWikii BPTF.
    GenomeRNAii 2186.
    NextBioi 8831.
    PROi Q12830.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12830.
    Bgeei Q12830.
    CleanExi HS_BPTF.
    Genevestigatori Q12830.

    Family and domain databases

    Gene3Di 1.20.920.10. 2 hits.
    3.30.40.10. 2 hits.
    InterProi IPR001487. 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 ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF02791. DDT. 1 hit.
    PF00628. PHD. 2 hits.
    PF15612. WHIM1. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 2914-3037.

    Entry informationi

    Entry nameiBPTF_HUMAN
    AccessioniPrimary (citable) accession number: Q12830
    Secondary accession number(s): Q6NX67, Q7Z7D6, Q9UIG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3