SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00000125 
UniProt Accession
Theoretical PI
8.78  
Molecular Weight
300686 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
E(bx) 
Gene Synonyms/Alias
ORFNames=CG32346, CG7022, Nurf301 
Protein Name
Nucleosome-remodeling factor subunit NURF301 
Protein Synonyms/Alias
Enhancer of bithorax; Nucleosome-remodeling factor 215 kDa subunit;NURF-215 
Organism
Drosophila melanogaster (Fruit fly) 
NCBI Taxonomy ID
7227 
Chromosome Location
chr:3L;234101-246901;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. S. Y. Kwon, H. Xiao, C. Wu and P. Badenhorst (2009) Alternative splicing of NURF301 generates distinct NURF chromatin remodeling complexes with altered modified histone binding specificities. PLoS Genet 5(7): e1000574. 

Abstract
Drosophila NURF is an ISWI-containing chromatin remodeling complex that catalyzes ATP-dependent nucleosome sliding. By sliding nucleosomes, NURF can alter chromatin structure and regulate transcription. NURF301/BPTF is the only NURF-specific subunit of NURF and is instrumental in recruiting the complex to target genes. Here we demonstrate that three NURF301 isoforms are expressed and that these encode functionally distinct NURF chromatin remodeling complexes. Full-length NURF301 contains a C-terminal bromodomain and juxtaposed PHD finger that bind histone H3 trimethylated at Lys4 (H3K4me3) and histone H4 acetylated at Lys16 (H4K16Ac) respectively. However, a NURF301 isoform that lacks these C-terminal domains is also detected. This truncated NURF301 isoform assembles a complex containing ISWI, NURF55, and NURF38, indicating that a second class of NURF remodeling complex, deficient in H3K4me3 and H4K16Ac recognition, exists. By comparing microarray expression profiles and phenotypes of null Nurf301 mutants with mutants that remove the C-terminal PHD fingers and bromodomain, we show that full-length NURF301 is not essential for correct expression of the majority of NURF gene targets in larvae. However, full-length NURF301 is required for spermatogenesis. Mutants that lack full-length NURF exhibit a spermatocyte arrest phenotype and fail to express a subset of spermatid differentiation genes. Our data reveal that variants of the NURF ATP-dependent chromatin remodeling complex that recognize post-translational histone modifications are important regulators of primary spermatocyte differentiation in Drosophila. PMID: [19629165] 

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Figures for illustrating the function of this protein/gene
Function
Histone-binding component of NURF (nucleosome remodelingfactor), a complex which catalyzes ATP-dependent nucleosomesliding and facilitates transcription of chromatin. Specificallyrecognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which marktranscription start sites of virtually all active genes. Requiredfor homeotic gene expression, proper larval blood celldevelopment, normal male X chromosome morphology, ecdysteroidsignaling and metamorphosis. 
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Subcellular Location
Nucleus (Potential). 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0016589 C:NURF complex IDA:FlyBase.
GO:0003677 F:DNA binding IEA:UniProtKB-KW.
GO:0008270 F:zinc ion binding IEA:InterPro.
GO:0048813 P:dendrite morphogenesis IMP:FlyBase.
GO:0035076 P:ecdysone receptor-mediated signaling pathway IGI:FlyBase.
GO:0030097 P:hemopoiesis IMP:FlyBase.
GO:0046331 P:lateral inhibition IMP:FlyBase.
GO:0007095 P:mitotic cell cycle G2/M transition DNA damage checkpoint IGI:FlyBase.
GO:0042766 P:nucleosome mobilization IDA:FlyBase.
GO:0045747 P:positive regulation of Notch signaling pathway IMP:FlyBase.
GO:0035073 P:pupariation IMP:FlyBase.
GO:0006355 P:regulation of transcription, DNA-dependent IEA:UniProtKB-KW.
GO:0006351 P:transcription, DNA-dependent IDA:FlyBase.
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Interpro
IPR017956;    AT_hook_DNA-bd_motif.
IPR001487;    Bromodomain.
IPR018359;    Bromodomain_CS.
IPR004022;    DDT_dom.
IPR018500;    DDT_dom_subgr.
IPR018501;    DDT_dom_superfamily.
IPR019786;    Zinc_finger_PHD-type_CS.
IPR011011;    Znf_FYVE_PHD.
IPR001965;    Znf_PHD.
IPR019787;    Znf_PHD-finger.
IPR013083;    Znf_RING/FYVE/PHD.
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Pfam
PF00439;    Bromodomain;    1.
PF02791;    DDT;    1.
PF00628;    PHD;    3.
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SMART
SM00384;    AT_hook;    2.
SM00297;    BROMO;    1.
SM00571;    DDT;    1.
SM00249;    PHD;    3.
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PROSITE
PS00633;    BROMODOMAIN_1;    1.
PS50014;    BROMODOMAIN_2;    1.
PS50827;    DDT;    1.
PS01359;    ZF_PHD_1;    3.
PS50016;    ZF_PHD_2;    2.
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PRINTS
PR00503;    BROMODOMAIN.;   
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Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1   2669       Nucleosome-remodeling factor subunit
                             NURF301.
                             /FTId=PRO_0000249322.
DOMAIN      188    248       DDT.
DOMAIN     2573   2643       Bromo.
DNA_BIND      6     18       A.T hook.
ZN_FING     339    386       PHD-type 1.
ZN_FING    2481   2546       PHD-type 2.
REGION        1    121       Required for function in nucleosome
                             sliding.
COILED      460    515       Potential.
COILED      688    720       Potential.
COILED     2338   2373       Potential.
COMPBIAS    989    993       Poly-Leu.
COMPBIAS   1567   1571       Poly-Ala.
COMPBIAS   1626   1629       Poly-Thr.
COMPBIAS   1707   2113       Gln-rich.
BINDING    2497   2497       Histone H3K4me3 (By similarity).
BINDING    2504   2504       Histone H3K4me3 (By similarity).
BINDING    2510   2510       Histone H3K4me3 (By similarity).
BINDING    2519   2519       Histone H3K4me3 (By similarity).
MOD_RES      40     40       Phosphoserine.
MOD_RES      52     52       Phosphoserine.
MOD_RES      55     55       Phosphoserine.
MOD_RES      59     59       Phosphoserine.
MOD_RES      62     62       Phosphoserine.
MOD_RES    1417   1417       Phosphoserine.
MOD_RES    1527   1527       Phosphothreonine.
MOD_RES    2395   2395       Phosphoserine.
MOD_RES    2398   2398       Phosphoserine.
MOD_RES    2403   2403       Phosphoserine.
VAR_SEQ    1800   1819       Missing (in isoform B and isoform D).
                             /FTId=VSP_020422.
VAR_SEQ    2156   2159       TNNI -> VSSF (in isoform C and isoform
                             D).
                             /FTId=VSP_020423.
VAR_SEQ    2160   2669       Missing (in isoform C and isoform D).
                             /FTId=VSP_020424.
CONFLICT    307    307       D -> Y (in Ref. 1; AAL16644).
CONFLICT   2156   2156       T -> A (in Ref. 1; AAL16644).
CONFLICT   2252   2252       S -> A (in Ref. 1; AAL16644).
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Nucleotide Sequence
Length: 8808 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 2669 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
knBioGRID 
knBioGRID 
Nurf-38BioGRID 
CG13131BioGRID 
CG4236BioGRID 
Caf1BioGRID 
knBioGRID 
Ubx-REBioGRID 
Caf1BioGRID 
knBioGRID 
ewgBioGRID 
Fas2IntAct 
His3BioGRID 
Nurf-38BioGRID 
IswiBioGRID 
hopBioGRID 
Nurf-38BioGRID 
CG4236BioGRID 
Caf1BioGRID 
Ubx-REBioGRID 
Caf1BioGRID 
Nurf-38BioGRID 
IswiBioGRID 
hopBioGRID 
ltBioGRID 
ltBioGRID 
ltBioGRID 
CG13131IntAct 
CG6945BioGRID 
osBioGRID 
UbxBioGRID 
_MINT 
CG13131BioGRID 
_MINT 
CG6945MINT 
osBioGRID 
UbxBioGRID 
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
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