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Protein

Nucleosome-remodeling factor subunit BPTF

Gene

BPTF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Binding sitei2869Histone H3K4me31
Binding sitei2876Histone H3K4me31
Binding sitei2882Histone H3K4me31
Binding sitei2891Histone H3K4me31

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 437PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri2867 – 2918PHD-type 2PROSITE-ProRule annotationAdd BLAST52

GO - Molecular functioni

  • sequence-specific DNA binding Source: HGNC
  • transcription factor binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • brain development Source: HGNC
  • cellular response to nerve growth factor stimulus Source: Ensembl
  • chromatin modification Source: UniProtKB-KW
  • chromatin remodeling Source: HGNC
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of transcription, DNA-templated Source: HGNC
  • regulation of transcription, DNA-templated Source: HGNC
  • response to wounding Source: Ensembl
  • transcription, DNA-templated Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171634-MONOMER.
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
Proteomesi
  • UP000005640 Componenti: 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

  • cell body Source: Ensembl
  • cytoplasm Source: ProtInc
  • dendrite Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HGNC
  • NURF complex Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2869Y → T: Abolishes binding to histone H3K4me3. 1 Publication1
Mutagenesisi2876Y → E: Induces binding to histone H3K4me2. 2 Publications1
Mutagenesisi2876Y → T: Strongly reduces binding to histone H3K4me3. 2 Publications1
Mutagenesisi2882Y → S: Abolishes binding to histone H3K4me3. 1 Publication1
Mutagenesisi2884G → E or L: Strongly reduces binding to histone H3K4me3. 1 Publication1
Mutagenesisi2886D → N or A: Abolishes binding to histone H3K4me3. 1 Publication1
Mutagenesisi2889Q → K: Strongly reduces binding to histone H3K4me3. 1 Publication1
Mutagenesisi2891W → E or F: Abolishes binding to histone H3K4me3. 2 Publications1

Organism-specific databases

DisGeNETi2186.
OpenTargetsiENSG00000171634.
PharmGKBiPA162377557.

Chemistry databases

ChEMBLiCHEMBL3085621.
GuidetoPHARMACOLOGYi2723.

Polymorphism and mutation databases

BioMutaiBPTF.
DMDMi215274183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000871761 – 3046Nucleosome-remodeling factor subunit BPTFAdd BLAST3046

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei216PhosphoserineCombined sources1
Modified residuei572PhosphoserineCombined sources1
Modified residuei763PhosphoserineCombined sources1
Modified residuei817PhosphoserineCombined sources1
Modified residuei880N6-acetyllysineCombined sources1
Modified residuei1064PhosphothreonineCombined sources1
Cross-linki1088Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1231PhosphoserineCombined sources1
Modified residuei1300PhosphoserineCombined sources1
Modified residuei1303PhosphothreonineCombined sources1
Modified residuei1310PhosphoserineCombined sources1
Modified residuei2098PhosphoserineCombined sources1
Modified residuei2155Omega-N-methylarginineCombined sources1
Modified residuei2162Asymmetric dimethylarginineCombined sources1
Modified residuei2184Asymmetric dimethylarginineCombined sources1
Modified residuei2191Asymmetric dimethylarginineCombined sources1
Modified residuei2465PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation enhances DNA-binding.1 Publication
Highly susceptible to proteolysis.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ12830.
MaxQBiQ12830.
PaxDbiQ12830.
PeptideAtlasiQ12830.
PRIDEiQ12830.

PTM databases

iPTMnetiQ12830.
PhosphoSitePlusiQ12830.
SwissPalmiQ12830.

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

BgeeiENSG00000171634.
CleanExiHS_BPTF.
ExpressionAtlasiQ12830. baseline and differential.
GenevisibleiQ12830. HS.

Organism-specific databases

HPAiHPA029069.

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
SMARCA1P283706EBI-1560273,EBI-2822460

GO - Molecular functioni

  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi108481. 41 interactors.
DIPiDIP-38919N.
IntActiQ12830. 16 interactors.
MINTiMINT-3973225.
STRINGi9606.ENSP00000307208.

Chemistry databases

BindingDBiQ12830.

Structurei

Secondary structure

13046
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2870 – 2873Combined sources4
Beta strandi2882 – 2884Combined sources3
Turni2886 – 2888Combined sources3
Beta strandi2891 – 2893Combined sources3
Helixi2894 – 2897Combined sources4
Helixi2901 – 2904Combined sources4
Helixi2913 – 2922Combined sources10
Turni2923 – 2925Combined sources3
Helixi2930 – 2944Combined sources15
Helixi2947 – 2949Combined sources3
Turni2950 – 2952Combined sources3
Turni2958 – 2960Combined sources3
Helixi2962 – 2967Combined sources6
Helixi2974 – 2982Combined sources9
Helixi2989 – 3006Combined sources18
Helixi3012 – 3027Combined sources16
Turni3028 – 3030Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini240 – 300DDTPROSITE-ProRule annotationAdd BLAST61
Domaini2944 – 3014BromoPROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni640 – 749Interaction with KEAP11 PublicationAdd BLAST110
Regioni839 – 921Interaction with MAZ1 PublicationAdd BLAST83

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili574 – 604Sequence analysisAdd BLAST31
Coiled coili978 – 1007Sequence analysisAdd BLAST30
Coiled coili2022 – 2050Sequence analysisAdd BLAST29
Coiled coili2706 – 2732Sequence analysisAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi143 – 180Glu-richAdd BLAST38
Compositional biasi149 – 185Asp-richAdd BLAST37
Compositional biasi1709 – 1803Thr-richAdd BLAST95
Compositional biasi2338 – 2361Thr-richAdd BLAST24
Compositional biasi2795 – 2817Pro-richAdd BLAST23
Compositional biasi2848 – 2853Poly-Lys6

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)DescriptionActionsGraphical viewLength
Zinc fingeri390 – 437PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri2867 – 2918PHD-type 2PROSITE-ProRule annotationAdd BLAST52

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1473. Eukaryota.
KOG1632. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000231041.
HOVERGENiHBG080062.
InParanoidiQ12830.
KOiK11728.
OMAiKLYPKDQ.
OrthoDBiEOG091G00NP.
PhylomeDBiQ12830.
TreeFamiTF316840.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
3.30.40.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018501. DDT_dom.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_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.
PF15613. WSD. 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. AlignAdd to basket

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

        10         20         30         40         50
MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR
60 70 80 90 100
WAAAQAEVAP KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG
110 120 130 140 150
RTGGGGGGGH LARTTAARRA VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG
160 170 180 190 200
DAEETQDSED DEEDEMEEDD DDSDYPEEME DDDDDASYCT ESSFRSHSTY
210 220 230 240 250
SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN EHIMNVIAIY
260 270 280 290 300
EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT
310 320 330 340 350
SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE
360 370 380 390 400
DYPYGPVENK IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG
410 420 430 440 450
DLLCCETCSA VYHLECVKPP LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ
460 470 480 490 500
KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE EDTENENEKK IWYYSTKVQL
510 520 530 540 550
AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK ARGSNKSFLA
560 570 580 590 600
AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ
610 620 630 640 650
SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS
660 670 680 690 700
PSEGRSPVGC LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT
710 720 730 740 750
TSIQPNLENS NSSSELNSSQ SESAKAADDP ENGERESHTP VSIQEEIVGD
760 770 780 790 800
FKSEKSNGEL SESPGAGKGA SGSTRIITRL RNPDSKLSQL KSQQVAAAAH
810 820 830 840 850
EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF KLGQEGKYRV
860 870 880 890 900
YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV
910 920 930 940 950
LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL
960 970 980 990 1000
AILECAVKPV VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE
1010 1020 1030 1040 1050
TMQQATWVKY TFPVKHQVWK QKGEEYRVTG YGGWSWISKT HVYRFVPKLP
1060 1070 1080 1090 1100
GNTNVNYRKS LEGTKNNMDE NMDESDKRKC SRSPKKIKIE PDSEKDEVKG
1110 1120 1130 1140 1150
SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE PMEVDDDMKT
1160 1170 1180 1190 1200
ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE
1210 1220 1230 1240 1250
EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ
1260 1270 1280 1290 1300
SPNANNDQPE DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS
1310 1320 1330 1340 1350
PETKCPKQNS IENDIEEKVS DLASRGQEPS KSKTKGNDFF IDDSKLASAD
1360 1370 1380 1390 1400
DIGTLICKNK KPLIQEESDT IVSSSKSALH SSVPKSTNDR DATPLSRAMD
1410 1420 1430 1440 1450
FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES ISEQFRTREQ
1460 1470 1480 1490 1500
DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK
1510 1520 1530 1540 1550
CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK
1560 1570 1580 1590 1600
EISESRVVSG NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED
1610 1620 1630 1640 1650
FNERNSSETK SHLLSSSDAE GNYRDSLETL PSTKESDSTQ TTTPSASCPE
1660 1670 1680 1690 1700
SNSVNQVEDM EIETSEVKKV TSSPITSEEE SNLSNDFIDE NGLPINKNEN
1710 1720 1730 1740 1750
VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV SSTENCAKST
1760 1770 1780 1790 1800
VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT
1810 1820 1830 1840 1850
SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP
1860 1870 1880 1890 1900
NDDLKKLARK GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV
1910 1920 1930 1940 1950
KSLAGVSLML RLLWASLRWD DMAAKAPPGG GTTRTETSET EITTTEIIKR
1960 1970 1980 1990 2000
RDVGPYGIRS EYCIRKIICP IGVPETPKET PTPQRKGLRS SALRPKRPET
2010 2020 2030 2040 2050
PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ QAKKRLEQQK
2060 2070 2080 2090 2100
PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA
2110 2120 2130 2140 2150
TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT
2160 2170 2180 2190 2200
SFQPRTATVT IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG
2210 2220 2230 2240 2250
KAIIRTPVMV QPGAPQQVMT QIIRGQPVST AVSAPNTVSS TPGQKSLTSA
2260 2270 2280 2290 2300
TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ LTQGHGGNQG LTVVIQGQGQ
2310 2320 2330 2340 2350
TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL ATTATTASTT
2360 2370 2380 2390 2400
TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ
2410 2420 2430 2440 2450
PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ
2460 2470 2480 2490 2500
VAAQSQPQSN VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP
2510 2520 2530 2540 2550
IPIQPHTSLQ IPSQGQPQSQ PQVQSSTQTL SSGQTLNQVT VSSPSRPQLQ
2560 2570 2580 2590 2600
IQQPQPQVIA VPQLQQQVQV LSQIQSQVVA QIQAQQSGVP QQIKLQLPIQ
2610 2620 2630 2640 2650
IQQSSAVQTH QIQNVVTVQA ASVQEQLQRV QQLRDQQQKK KQQQIEIKRE
2660 2670 2680 2690 2700
HTLQASNQSE IIQKQVVMKH NAVIEHLKQK KSMTPAEREE NQRMIVCNQV
2710 2720 2730 2740 2750
MKYILDKIDK EEKQAAKKRK REESVEQKRS KQNATKLSAL LFKHKEQLRA
2760 2770 2780 2790 2800
EILKKRALLD KDLQIEVQEE LKRDLKIKKE KDLMQLAQAT AVAAPCPPVT
2810 2820 2830 2840 2850
PAPPAPPAPP PSPPPPPAVQ HTGLLSTPTL PAASQKRKRE EEKDSSSKSK
2860 2870 2880 2890 2900
KKKMISTTSK ETKKDTKLYC ICKTPYDESK FYIGCDRCQN WYHGRCVGIL
2910 2920 2930 2940 2950
QSEAELIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL RSLQAHKMAW
2960 2970 2980 2990 3000
PFLEPVDPND APDYYGVIKE PMDLATMEER VQRRYYEKLT EFVADMTKIF
3010 3020 3030 3040
DNCRYYNPSD SPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAS
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 differs from that shown. Several sequencing errors.Curated
The sequence AAA97522 differs from that shown. Reason: Frameshift at positions 136 and 915.Curated
The sequence BAA89208 differs from that shown. Several sequencing errors in the N-terminal part.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti752K → T in AAA97522 (PubMed:7621746).Curated1
Sequence conflicti757N → T in AAA97522 (PubMed:7621746).Curated1
Sequence conflicti969S → F in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti1268E → Q in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti1330S → T in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti1842S → T in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti1842S → T in AAP22284 (PubMed:14609955).Curated1
Sequence conflicti1926A → V in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti1926A → V in AAP22284 (PubMed:14609955).Curated1
Sequence conflicti1932T → S in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti1932T → S in AAP22284 (PubMed:14609955).Curated1
Sequence conflicti1960S → F in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti2393E → K in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti2404Q → R in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti2540T → S in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti2802 – 2803AP → VL in BAA89208 (PubMed:10662542).Curated2
Sequence conflicti2818A → G in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti2832A → V in BAA89208 (PubMed:10662542).Curated1
Sequence conflicti2876Y → G in AAH67234 (PubMed:15489334).Curated1
Sequence conflicti2880K → Q in AAH67234 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_020402622 – 747Missing in isoform 2. 1 PublicationAdd BLAST126
Alternative sequenceiVSP_0204052522 – 2664Missing in isoform 4. 1 PublicationAdd BLAST143

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS11673.1. [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]
GeneIDi2186.
KEGGihsa:2186.
UCSCiuc002jgf.4. human. [Q12830-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS11673.1. [Q12830-2]
PIRiG01252.
RefSeqiNP_004450.3. NM_004459.6. [Q12830-4]
NP_872579.2. NM_182641.3. [Q12830-2]
UniGeneiHs.444200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108481. 41 interactors.
DIPiDIP-38919N.
IntActiQ12830. 16 interactors.
MINTiMINT-3973225.
STRINGi9606.ENSP00000307208.

Chemistry databases

BindingDBiQ12830.
ChEMBLiCHEMBL3085621.
GuidetoPHARMACOLOGYi2723.

PTM databases

iPTMnetiQ12830.
PhosphoSitePlusiQ12830.
SwissPalmiQ12830.

Polymorphism and mutation databases

BioMutaiBPTF.
DMDMi215274183.

Proteomic databases

EPDiQ12830.
MaxQBiQ12830.
PaxDbiQ12830.
PeptideAtlasiQ12830.
PRIDEiQ12830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306378; ENSP00000307208; ENSG00000171634. [Q12830-2]
ENST00000321892; ENSP00000315454; ENSG00000171634. [Q12830-1]
GeneIDi2186.
KEGGihsa:2186.
UCSCiuc002jgf.4. human. [Q12830-1]

Organism-specific databases

CTDi2186.
DisGeNETi2186.
GeneCardsiBPTF.
HGNCiHGNC:3581. BPTF.
HPAiHPA029069.
MIMi601819. gene.
neXtProtiNX_Q12830.
OpenTargetsiENSG00000171634.
PharmGKBiPA162377557.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1473. Eukaryota.
KOG1632. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000231041.
HOVERGENiHBG080062.
InParanoidiQ12830.
KOiK11728.
OMAiKLYPKDQ.
OrthoDBiEOG091G00NP.
PhylomeDBiQ12830.
TreeFamiTF316840.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171634-MONOMER.
SignaLinkiQ12830.

Miscellaneous databases

ChiTaRSiBPTF. human.
EvolutionaryTraceiQ12830.
GeneWikiiBPTF.
GenomeRNAii2186.
PROiQ12830.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171634.
CleanExiHS_BPTF.
ExpressionAtlasiQ12830. baseline and differential.
GenevisibleiQ12830. HS.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
3.30.40.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018501. DDT_dom.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_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.
PF15613. WSD. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 167 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.