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Q12830

- BPTF_HUMAN

UniProt

Q12830 - BPTF_HUMAN

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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

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. sequence-specific DNA binding Source: HGNC
  2. transcription factor binding Source: MGI
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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 – 2161Phosphoserine3 Publications
Modified residuei572 – 5721Phosphoserine1 Publication
Modified residuei763 – 7631Phosphoserine3 Publications
Modified residuei817 – 8171Phosphoserine1 Publication
Modified residuei880 – 8801N6-acetyllysine1 Publication
Modified residuei1064 – 10641Phosphothreonine2 Publications
Modified residuei1231 – 12311Phosphoserine1 Publication
Modified residuei1251 – 12511Phosphoserine1 Publication
Modified residuei1300 – 13001Phosphoserine2 Publications
Modified residuei1310 – 13101Phosphoserine2 Publications
Modified residuei2098 – 20981Phosphoserine2 Publications
Modified residuei2465 – 24651Phosphoserine1 Publication

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

BgeeiQ12830.
CleanExiHS_BPTF.
ExpressionAtlasiQ12830. baseline and differential.
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. 26 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 – 28734Combined sources
Beta strandi2882 – 28843Combined sources
Turni2886 – 28883Combined sources
Beta strandi2891 – 28933Combined sources
Helixi2894 – 28974Combined sources
Helixi2901 – 29044Combined sources
Helixi2913 – 292210Combined sources
Turni2923 – 29253Combined sources
Helixi2930 – 294415Combined sources
Helixi2947 – 29493Combined sources
Turni2950 – 29523Combined sources
Turni2958 – 29603Combined sources
Helixi2962 – 29676Combined sources
Helixi2974 – 29829Combined sources
Helixi2989 – 300618Combined sources
Helixi3012 – 302716Combined sources
Turni3028 – 30303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000231041.
HOVERGENiHBG080062.
InParanoidiQ12830.
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

        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 AAA97522.1 differs from that shown. Reason: Several sequencing errors.Curated
The sequence AAA97522.1 differs from that shown. Reason: Frameshift at positions 136 and 915. Curated
The sequence BAA89208.1 differs from that shown. Reason: Several sequencing errors in the N-terminal part.Curated

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:
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.
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:
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 .
CCDSi 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:
PDBei
RCSB PDBi
PDBji
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. 26 interactions.
DIPi DIP-38919N.
IntActi Q12830. 6 interactions.
MINTi MINT-3973225.
STRINGi 9606.ENSP00000307208.

Chemistry

ChEMBLi CHEMBL3085621.

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 ]
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.
GeneTreei ENSGT00760000119099.
HOGENOMi HOG000231041.
HOVERGENi HBG080062.
InParanoidi Q12830.
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

Bgeei Q12830.
CleanExi HS_BPTF.
ExpressionAtlasi Q12830. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 145 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