Q91YE5
uniprot
Q91YE5
canonical
amino_acid_sequence
MEMEANDHFNFTGLPPAPAASGLKPSPSSGEGLYTNGSPMNFPQQGKSLNGDVNVNGLSTVSHTTTSGILNSAPHSSSTSHLHHPNVAYDCLWNYSQYPSANPGNNLKDPPLLSQFPGGQYPLNGILGGNRQPSSPSHNTNLRAGSQEFWANGTQSPMGLNFDSQELYDSFPDQNFEVMPNGPPSFFTSPQTSPMLGSSIQTFAPSQDVSSDIHPDEAAEKELTSVVAENGTGLVGSLELEEEQPELKMCGYNGSVSSVESLHQEVSVLVPDPTVSCLDDPSHLPDQLEDTPILSEDSLEPFDSLAAEPVSGSLYGIDDAELMGAEDKLPLEGNPVISALDCPALSNANAFSLLADDSQTSASIFVSPTSPPVLGESVLQDNSFGLNSCSDSEQEEIETQSSNFQRPLTEPAPDQPPSTQLHPAVSPTASPAASLTASAEISPAVSPVASSPVPPEVFVAVSPASSPALPAISLEASMTTPVTSPQGSPEPSPAAAFQTVSPARKNVSSAPKARADREETTGGAVAVSGSGDVLKRRIATPEEVRLPLQHGWRREVRIKKGSHRWQGETWYYGPCGKRMKQFPEVIKYLSRNVVHSVRREHFSFSPRMPVGDFFEERDTPEGLQWVQLSAEEIPSRIQAITGKRGRPRNNEKAKNKEVPKVKRGRGRPPKIKMPELLNKTDNRLPKKLETQEILSEDDKAKMTKNKKKMRQKVQRGESQTPVQGQARNKRKQDTKSLKQKDTKKKLKAEKEKMKTKQEKLKEKVKREKKEKVKAKGKEGPRARPSCRADKTLATQKRLEEQQRQQAILEEMKKPTEGMCLSDHQPLPDFTRIPGLTLSSRAFSDCLTIVEFLHSFGKVLGFDLTKDVPSLGVLQEGLLCQGDSLDKVQDLLVRLLKAALHDPGLPPYCQSLKILGEKMSEIPLTRDNVSEILRCFLMAYRVEPPFCDSLRTQPFQAQPPQQKAAILAFLVHELNSSTIIINEIDKTLESVSSCRKNKWIVEGRLRRLKTALAKRTGRPEVMMEGAEDGLGRRRSSRIMEETSGIEEEEEEENTTAVHGRRGRKEGEIDVAASSIPELERHIEKLSKRQLFFRKKLLHSSQMLRAVSLGQDRYRRHYWVLPYLAGIFVEGSEGSTVTEDEIKQETESLMEVVTSTPSSARASVKRELTGSNASTSPARSRGRPRKPKPGSLQPQHLQSTIRECDSEQAQTQVHPEPQPQLQAPTQPHLQPSSGFLEPEGSPFSLGQSQHDLSQSAFLSWLSQTQSHNSLLSSSVLTPDSSPGKLDSAPSQSLEEPEPDEAQSCPGPQGPWFNFSAQIPCDAAPTPPPAVSEDQPTPSLQLLASSKPMNTPGAANPCSPVQLSSTHLPGGTPKRLSGDSEEMSQSPTGLGQPKRRGRPPSKFFKQVEQHYLTQLTAQPIPPEMCSGWWWIRDPETLDVLLKALHPRGIREKALHKHLSKHKDFLQEVCLQPLTDPIFEPNELPALEEGVMSWSPKEKTYETDLAVLQWVEELEQRVVLSDLQIRGWTCPTPDSTREDLTYCEHLPDSPEDIPWRGRGREGTVPQRQNNNPLDLAVMRLAVLEQNVERRYLREPLWAAHEVVVEKALLSTPNGAPDGTSTEISYEITPRVRVWRQTLERCRSAAQVCLCMGQLERSIAWEKSVNKVTCLVCRKGDNDEFLLLCDGCDRGCHIYCHRPKMEAVPEGDWFCAVCLSQQVEEEYTQRPGFPKRGQKRKSSFPLTFPEGDSRRRMLSRSRDSPAVPRYPEDGLSPPKRRRHSMRSHHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRVIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNEDDSEVGKAGHVMRRFFESRWEEFYQGKQANL
uniprot
proteins
function
FUNCTION: Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:11532953). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:11532953). Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex (By similarity). The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex (By similarity). Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (PubMed:11532953). In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription (PubMed:12198165, PubMed:16085498). Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (PubMed:11532953, PubMed:16085498). Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (PubMed:16678107, PubMed:18600236). {ECO:0000250|UniProtKB:Q9UIF9, ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16678107, ECO:0000269|PubMed:18600236}.
uniprot
proteins
mass_dalton
209618
uniprot
proteins
mutagenesis
MUTAGEN 570..571; /note="WY->GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription."; /evidence="ECO:0000269|PubMed:16678107, ECO:0000269|PubMed:19578370"; MUTAGEN 672; /note="K->R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA."; /evidence="ECO:0000269|PubMed:19578370"; MUTAGEN 1814; /note="Y->F: Impairs binding to chromatin."; /evidence="ECO:0000269|PubMed:12198165
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Deubiquitinated by USP21 leading to its stabilization. {ECO:0000250|UniProtKB:Q9UIF9}.; PTM: Acetylation at Lys-672 by KAT8/MOF promotes its dissociation from pRNA, affecting heterochromatin formation, nucleosome positioning and rDNA silencing. Deacetylation by SIRT1 in late S phase enhances pRNA-binding, allowing de novo DNA methylation and heterochromatin formation. Acetylation is high during S phase and declines to background levels in late S phase when the silent copies of rRNA genes are replicated. {ECO:0000269|PubMed:19578370}.
uniprot
proteins
protein_family
WAL family
uniprot
proteins
pubmed
11532953
uniprot
proteins
pubmed
12198165
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
15292447
uniprot
proteins
pubmed
16085498
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16678107
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18600236
uniprot
proteins
pubmed
19578370
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
1889
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:18600236, ECO:0000269|PubMed:19578370}. Note=Co-localizes with the basal RNA polymerase I transcription factor UBF in the nucleolus. {ECO:0000269|PubMed:11532953}.
uniprot
proteins