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Q12830

- BPTF_HUMAN

UniProt

Q12830 - BPTF_HUMAN

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Protein
Nucleosome-remodeling factor subunit BPTF
Gene
BPTF, FAC1, FALZ
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 1
Add
BLAST
Zinc fingeri2867 – 291852PHD-type 2
Add
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. ATP catabolic process Source: GOC
  2. anterior/posterior pattern specification Source: Ensembl
  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.3 Publications

GO - Cellular componenti

  1. NURF complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. microtubule cytoskeleton Source: HPA
  4. nucleolus Source: HPA
  5. nucleus Source: HGNC
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 BPTF
PRO_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.
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-K4Me2.4 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

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.

Miscellaneous databases

EvolutionaryTraceiQ12830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini240 – 30061DDT
Add
BLAST
Domaini2944 – 301471Bromo
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni640 – 749110Interaction with KEAP1
Add
BLAST
Regioni839 – 92183Interaction with MAZ
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili574 – 60431 Reviewed prediction
Add
BLAST
Coiled coili978 – 100730 Reviewed prediction
Add
BLAST
Coiled coili2022 – 205029 Reviewed prediction
Add
BLAST
Coiled coili2706 – 273227 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi143 – 18038Glu-rich
Add
BLAST
Compositional biasi149 – 18537Asp-rich
Add
BLAST
Compositional biasi1709 – 180395Thr-rich
Add
BLAST
Compositional biasi2338 – 236124Thr-rich
Add
BLAST
Compositional biasi2795 – 281723Pro-rich
Add
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.
Contains 1 bromo domain.
Contains 1 DDT domain.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei622 – 747126Missing in isoform 2.
VSP_020402Add
BLAST
Alternative sequencei2522 – 2664143Missing in isoform 4.
VSP_020405Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti752 – 7521K → T in AAA97522. 1 Publication
Sequence conflicti757 – 7571N → T in AAA97522. 1 Publication
Sequence conflicti969 – 9691S → F in BAA89208. 1 Publication
Sequence conflicti1268 – 12681E → Q in BAA89208. 1 Publication
Sequence conflicti1330 – 13301S → T in BAA89208. 1 Publication
Sequence conflicti1842 – 18421S → T in BAA89208. 1 Publication
Sequence conflicti1842 – 18421S → T in AAP22284. 1 Publication
Sequence conflicti1926 – 19261A → V in BAA89208. 1 Publication
Sequence conflicti1926 – 19261A → V in AAP22284. 1 Publication
Sequence conflicti1932 – 19321T → S in BAA89208. 1 Publication
Sequence conflicti1932 – 19321T → S in AAP22284. 1 Publication
Sequence conflicti1960 – 19601S → F in BAA89208. 1 Publication
Sequence conflicti2393 – 23931E → K in BAA89208. 1 Publication
Sequence conflicti2404 – 24041Q → R in BAA89208. 1 Publication
Sequence conflicti2540 – 25401T → S in BAA89208. 1 Publication
Sequence conflicti2802 – 28032AP → VL in BAA89208. 1 Publication
Sequence conflicti2818 – 28181A → G in BAA89208. 1 Publication
Sequence conflicti2832 – 28321A → V in BAA89208. 1 Publication
Sequence conflicti2876 – 28761Y → G in AAH67234. 1 Publication
Sequence conflicti2880 – 28801K → Q in AAH67234. 1 Publication

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]
ENST00000573834; ENSP00000461014; ENSG00000262858. [Q12830-2]
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 ]
ENST00000573834 ; ENSP00000461014 ; ENSG00000262858 . [Q12830-2 ]
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

« 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: September 3, 2014
This is version 142 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

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