UniProt Accession

 SMCA5_HUMAN; O60264 

Genbank Protein ID

 AB010882; BC023144 

Genbank Nucleotide ID

 BAA25173.1; AAH23144.1 

Protein Name

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

Protein Synonyms/Alias

 SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5; Sucrose nonfermenting protein 2 homolog; hSNF2H 

Gene Name

 SMARCA5 

Gene Synonyms/Alias

 SNF2H; WCRF135 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
83	PDPTYEEKMQTDRAN	ubiquitination	[1, 2]
97	NRFEYLLKQTELFAH	ubiquitination	[3]
132	PRIKKDEKQNLLSVG	ubiquitination	[4]
160	ELLTESSKATNVCTR	ubiquitination	[1, 2, 5]
176	EDSPSYVKWGKLRDY	ubiquitination	[1, 2, 4, 6, 7]
264	SVCLIGDKEQRAAFV	acetylation	[7]
264	SVCLIGDKEQRAAFV	ubiquitination	[2, 7]
418	KIYVGLSKMQREWYT	ubiquitination	[2, 4, 6]
430	WYTRILMKDIDILNS	ubiquitination	[2, 4]
440	DILNSAGKMDKMRLL	acetylation	[7, 8, 9, 10]
440	DILNSAGKMDKMRLL	ubiquitination	[2]
455	NILMQLRKCCNHPYL	ubiquitination	[3]
490	GKMVVLDKLLPKLKE	ubiquitination	[2]
600	AHRIGQTKTVRVFRF	acetylation	[7]
644	LVDQNLNKIGKDEML	ubiquitination	[2]
647	QNLNKIGKDEMLQMI	acetylation	[9]
647	QNLNKIGKDEMLQMI	ubiquitination	[2, 4, 6, 7]
665	ATHVFASKESEITDE	ubiquitination	[3]
691	KTAEMNEKLSKMGES	ubiquitination	[2]
694	EMNEKLSKMGESSLR	ubiquitination	[2]
722	EGEDYREKQKIAFTE	ubiquitination	[3]
724	EDYREKQKIAFTEWI	ubiquitination	[2, 4]
735	TEWIEPPKRERKANY	ubiquitination	[2, 7]
739	EPPKRERKANYAVDA	ubiquitination	[6]
814	PNAAQAQKEEQLKID	ubiquitination	[1, 3]
834	NDEELEEKEKLLTQG	ubiquitination	[1]
836	EELEEKEKLLTQGFT	ubiquitination	[4, 6]
847	QGFTNWNKRDFNQFI	ubiquitination	[4]
929	DTKIGRYKAPFHQLR	ubiquitination	[3, 6]
1018	ENMELEEKEKAEKKK	ubiquitination	[7]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [10] 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] 

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 192 357 Helicase ATP-binding.
 DOMAIN 487 638 Helicase C-terminal.
 DOMAIN 840 892 SANT 1.
 DOMAIN 943 1007 SANT 2.
 NP_BIND 205 212 ATP (Probable).
 MOTIF 308 311 DEAH box.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 113 113 Phosphothreonine.
 MOD_RES 116 116 Phosphoserine.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 440 440 N6-acetyllysine.
 MOD_RES 825 825 Phosphoserine.  

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

 1052 AA 

Protein Sequence

Gene Ontology

 GO:0005677; C:chromatin silencing complex; IEA:Compara.
 GO:0000793; C:condensed chromosome; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0016589; C:NURF complex; IDA:UniProtKB.
 GO:0031213; C:RSF complex; IPI:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0016887; F:ATPase activity; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0004386; F:helicase activity; TAS:ProtInc.
 GO:0031491; F:nucleosome binding; IEA:InterPro.
 GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
 GO:0000183; P:chromatin silencing at rDNA; IEA:Compara.
 GO:0006352; P:DNA-dependent transcription, initiation; IDA:UniProtKB.
 GO:0006302; P:double-strand break repair; IEA:Compara.
 GO:0009790; P:embryo development; IEA:Compara.
 GO:0016584; P:nucleosome positioning; IDA:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc. 

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