UniProt Accession

 SMCA5_MOUSE; Q91ZW3; Q8C791; Q8CA22; Q8VDG1; Q925M9 

Genbank Protein ID

 AF375046; AF325921; BC021922; BC053069; AK039811; AK052320 

Genbank Nucleotide ID

 AAL25793.1; AAK52454.1; AAH21922.1; AAH53069.1; BAC30458.1; BAC34934.2 

Protein Name

 SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 

Protein Synonyms/Alias

 Sucrose nonfermenting protein 2 homolog; mSnf2h 

Gene Name

 Smarca5 

Gene Synonyms/Alias

 Snf2h 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
439	DILNSAGKMDKMRLL	acetylation	[1, 2]
489	GKMVVLDKLLPKLKE	acetylation	[3]
646	QNLNKIGKDEMLQMI	acetylation	[2]
835	EELEEKEKLLTQGFT	ubiquitination	[4]
965	LHKLGFDKENVYDEL	acetylation	[3]

Reference

 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. 

Sequence Annotation

 DOMAIN 191 356 Helicase ATP-binding.
 DOMAIN 486 637 Helicase C-terminal.
 DOMAIN 839 891 SANT 1.
 DOMAIN 942 1006 SANT 2.
 NP_BIND 204 211 ATP (Potential).
 MOTIF 307 310 DEAH box.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 55 55 Phosphothreonine.
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 112 112 Phosphothreonine (By similarity).
 MOD_RES 115 115 Phosphoserine (By similarity).
 MOD_RES 136 136 Phosphoserine.
 MOD_RES 439 439 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; ATP-binding; Chromatin regulator; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1051 AA 

Protein Sequence

Gene Ontology

 GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0043596; C:nuclear replication fork; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0016589; C:NURF complex; IEA:Compara.
 GO:0031213; C:RSF complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0031491; F:nucleosome binding; IEA:InterPro.
 GO:0043044; P:ATP-dependent chromatin remodeling; IEA:Compara.
 GO:0006333; P:chromatin assembly or disassembly; IDA:MGI.
 GO:0006338; P:chromatin remodeling; IDA:MGI.
 GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
 GO:0006352; P:DNA-dependent transcription, initiation; IEA:Compara.
 GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
 GO:0009790; P:embryo development; IMP:MGI.
 GO:0006334; P:nucleosome assembly; IEA:Compara.
 GO:0016584; P:nucleosome positioning; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:MGI. 

Interpro

 IPR020838; DBINO.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR009057; Homeodomain-like.
 IPR015194; ISWI_HAND-dom.
 IPR027417; P-loop_NTPase.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR015195; SLIDE.
 IPR000330; SNF2_N. 

Pfam

 PF13892; DBINO
 PF09110; HAND
 PF00271; Helicase_C
 PF09111; SLIDE
 PF00176; SNF2_N 

SMART

 SM00487; DEXDc
 SM00490; HELICc
 SM00717; SANT 

PROSITE

 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51293; SANT 

PRINTS