P51531 (SMCA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable global transcription activator SNF2L2
EC=3.6.4.-

Alternative name(s):
ATP-dependent helicase SMARCA2
BRG1-associated factor 190B
Short name=BAF190B
Protein brahma homolog
Short name=hBRM
SNF2-alpha
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2

Gene names

Name:	SMARCA2
Synonyms:	BAF190B, BRM, SNF2A, SNF2L2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1590 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth By similarity. Ref.5
Subunit structure	Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Binds TOPBP1. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. Interacts with PHF10/BAF45A By similarity. Ref.5 Ref.6 Ref.9
Subcellular location	Nucleus.
Involvement in disease	Nicolaides-Baraitser syndrome (NCBRS) [MIM:601358]: A rare disorder characterized by severe mental retardation with absent or limited speech, seizures, short stature, sparse hair, typical facial characteristics, brachydactyly, prominent finger joints and broad distal phalanges. Some of the features are progressive with time. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.18
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 bromo domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain. Contains 1 QLQ domain.

Ontologies

Keywords
Biological process	Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hypotrichosis Mental retardation
Domain	Bromodomain
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aortic smooth muscle cell differentiation Inferred from electronic annotation. Source: Compara chromatin remodeling Traceable author statement PubMed 17938176. Source: BHF-UCL negative regulation of cell growth Inferred from mutant phenotype PubMed 12065415. Source: BHF-UCL negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 17938176. Source: BHF-UCL nervous system development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 11078522. Source: UniProtKB WINAC complex Inferred from direct assay Ref.5. Source: BHF-UCL intermediate filament cytoskeleton Inferred from direct assay. Source: HPA nBAF complex Inferred from sequence or structural similarity. Source: UniProtKB npBAF complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear chromatin Inferred from direct assay PubMed 12065415. Source: BHF-UCL nucleoplasm Traceable author statement PubMed 8670841. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-dependent ATPase activity Traceable author statement PubMed 17938176. Source: BHF-UCL RNA polymerase II transcription coactivator activity Inferred from direct assay PubMed 17984088. Source: UniProtKB helicase activity Traceable author statement Ref.1. Source: ProtInc transcription regulatory region DNA binding Inferred from direct assay PubMed 17984088. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARID1A	O14497	3	EBI-679562,EBI-637887
ARID1B	Q8NFD5	3	EBI-679562,EBI-679921
KHDRBS1	Q07666	2	EBI-679562,EBI-1364
MECP2	P51608	4	EBI-679562,EBI-1189067

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P51531-1)

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.

Isoform Short (identifier: P51531-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1400-1417: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1590

1590

Probable global transcription activator SNF2L2

PRO_0000074352

Regions

Domain

173 – 208

36

QLQ

Domain

436 – 508

73

HSA

Domain

736 – 901

166

Helicase ATP-binding

Domain

1054 – 1216

163

Helicase C-terminal

Domain

1419 – 1489

71

Bromo

Nucleotide binding

749 – 756

8

ATP Potential

Motif

851 – 854

4

DEGH box

Compositional bias

216 – 238

23

Poly-Gln

Compositional bias

245 – 253

9

Poly-Gln

Compositional bias

559 – 562

4

Poly-Arg

Compositional bias

643 – 650

8

Poly-Glu

Compositional bias

1297 – 1301

5

Poly-Glu

Compositional bias

1518 – 1529

12

Poly-Glu

Amino acid modifications

Modified residue

175

1

Phosphoserine Ref.10 Ref.14

Modified residue

329

1

Phosphoserine Ref.7 Ref.14

Modified residue

997

1

N6-acetyllysine Ref.13

Modified residue

999

1

N6-acetyllysine Ref.13

Modified residue

1512

1

Phosphoserine Ref.10 Ref.12

Modified residue

1516

1

Phosphoserine Ref.10 Ref.12

Modified residue

1528

1

Phosphoserine Ref.10

Modified residue

1568

1

Phosphoserine Ref.7 Ref.11 Ref.14

Modified residue

1572

1

Phosphoserine Ref.7 Ref.11 Ref.14

Natural variations

Alternative sequence

1400 – 1417

18

Missing in isoform Short.

VSP_000577

Natural variant

752

1

G → A in NCBRS. Ref.18

VAR_068180

Natural variant

755

1

K → R in NCBRS. Ref.18

VAR_068181

Natural variant

756

1

T → I in NCBRS. Ref.18

VAR_068182

Natural variant

851

1

D → H in NCBRS. Ref.18

VAR_068183

Natural variant

852

1

E → D in NCBRS. Ref.18

VAR_068184

Natural variant

852

1

E → K in NCBRS. Ref.18

VAR_068185

Natural variant

854

1

H → N in NCBRS. Ref.18

VAR_068186

Natural variant

854

1

H → R in NCBRS. Ref.18

VAR_068187

Natural variant

855

1

R → G in NCBRS. Ref.18

VAR_068188

Natural variant

881

1

G → R in NCBRS. Ref.18

VAR_068189

Natural variant

881

1

G → V in NCBRS. Ref.18

VAR_068190

Natural variant

883

1

P → L in NCBRS. Ref.18

VAR_068191

Natural variant

939

1

H → Y in NCBRS. Ref.18

VAR_068192

Natural variant

946

1

L → F in NCBRS. Ref.18

VAR_068193

Natural variant

946

1

L → S in NCBRS. Ref.18

VAR_068194

Natural variant

1105

1

R → C in NCBRS. Ref.18

VAR_068195

Natural variant

1105

1

R → P in NCBRS. Ref.18

VAR_068196

Natural variant

1135

1

L → P in NCBRS. Ref.18

VAR_068197

Natural variant

1146

1

S → R in NCBRS. Ref.18

VAR_068198

Natural variant

1158

1

D → V in NCBRS. Ref.18

VAR_068199

Natural variant

1159

1

R → G in NCBRS. Ref.18

VAR_068200

Natural variant

1159

1

R → L in NCBRS. Ref.18

VAR_068201

Natural variant

1159

1

R → Q in NCBRS. Ref.18

VAR_068202

Natural variant

1162

1

R → H in NCBRS. Ref.18

VAR_068203

Natural variant

1188

1

A → P in NCBRS. Ref.18

VAR_068204

Natural variant

1201

1

A → V in NCBRS. Ref.18

VAR_068205

Natural variant

1202

1

G → C in NCBRS. Ref.18

VAR_068206

Natural variant

1205

1

D → G in NCBRS. Ref.18

VAR_068207

Natural variant

1213

1

R → W in NCBRS. Ref.18

VAR_068208

Natural variant

1416

1

G → A.
Corresponds to variant rs3793510 [ dbSNP | Ensembl ].

VAR_049501

Natural variant

1546

1

D → E.
Corresponds to variant rs2296212 [ dbSNP | Ensembl ].

VAR_049502

Experimental info

Sequence conflict

237 – 240

4

Missing in CAA51407. Ref.1

Sequence conflict

394

1

Q → E in BAA05142. Ref.2

Sequence conflict

513

1

G → S in BAA05142. Ref.2

Sequence conflict

711

1

R → W in CAA51407. Ref.1

Sequence conflict

1139

1

D → H in BAA05142. Ref.2

Sequence conflict

1394

1

V → C in CAA51407. Ref.1

Sequence conflict

1400

1

R → S in CAA51407. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1590

Helix Strand Turn

Details...

Helix

1381 – 1396

16

Beta strand

1418 – 1420

3

Helix

1424 – 1427

4

Turn

1433 – 1435

3

Helix

1438 – 1442

5

Helix

1449 – 1456

8

Turn

1457 – 1459

3

Helix

1464 – 1481

18

Helix

1487 – 1504

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified November 4, 2008. Version 2. Checksum: CE69BBB287D35AB5	FASTA	1,590	181,279
	10 20 30 40 50 60 MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM 70 80 90 100 110 120 GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY 130 140 150 160 170 180 MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH 190 200 210 220 230 240 QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ 250 260 270 280 290 300 QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA 310 320 330 340 350 360 AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE 370 380 390 400 410 420 LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR 430 440 450 460 470 480 QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV 490 500 510 520 530 540 ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL 550 560 570 580 590 600 TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT 610 620 630 640 650 660 ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI 670 680 690 700 710 720 LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI 730 740 750 760 770 780 NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV 790 800 810 820 830 840 PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL 850 860 870 880 890 900 AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP 910 920 930 940 950 960 TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE 970 980 990 1000 1010 1020 KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY 1030 1040 1050 1060 1070 1080 MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT 1090 1100 1110 1120 1130 1140 IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT 1150 1160 1170 1180 1190 1200 VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ 1210 1220 1230 1240 1250 1260 AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR 1270 1280 1290 1300 1310 1320 RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL 1330 1340 1350 1360 1370 1380 TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP 1390 1400 1410 1420 1430 1440 PKLTKQMNAI IDTVINYKDR CNVEKVPSNS QLEIEGNSSG RQLSEVFIQL PSRKELPEYY 1450 1460 1470 1480 1490 1500 ELIRKPVDFK KIKERIRNHK YRSLGDLEKD VMLLCHNAQT FNLEGSQIYE DSIVLQSVFK 1510 1520 1530 1540 1550 1560 SARQKIAKEE ESEDESNEEE EEEDEEESES EAKSVKVKIK LNKKDDKGRD KGKGKKRPNR 1570 1580 1590 GKAKPVVSDF DSDEEQDERE QSEGSGTDDE
	Isoform Short [UniParc]. Checksum: BBD4488C2861C270	FASTA	1,572	179,281
	10 20 30 40 50 60 MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM 70 80 90 100 110 120 GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY 130 140 150 160 170 180 MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH 190 200 210 220 230 240 QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ 250 260 270 280 290 300 QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA 310 320 330 340 350 360 AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE 370 380 390 400 410 420 LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR 430 440 450 460 470 480 QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV 490 500 510 520 530 540 ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL 550 560 570 580 590 600 TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT 610 620 630 640 650 660 ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI 670 680 690 700 710 720 LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI 730 740 750 760 770 780 NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV 790 800 810 820 830 840 PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL 850 860 870 880 890 900 AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP 910 920 930 940 950 960 TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE 970 980 990 1000 1010 1020 KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY 1030 1040 1050 1060 1070 1080 MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT 1090 1100 1110 1120 1130 1140 IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT 1150 1160 1170 1180 1190 1200 VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ 1210 1220 1230 1240 1250 1260 AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR 1270 1280 1290 1300 1310 1320 RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL 1330 1340 1350 1360 1370 1380 TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP 1390 1400 1410 1420 1430 1440 PKLTKQMNAI IDTVINYKDS SGRQLSEVFI QLPSRKELPE YYELIRKPVD FKKIKERIRN 1450 1460 1470 1480 1490 1500 HKYRSLGDLE KDVMLLCHNA QTFNLEGSQI YEDSIVLQSV FKSARQKIAK EEESEDESNE 1510 1520 1530 1540 1550 1560 EEEEEDEEES ESEAKSVKVK IKLNKKDDKG RDKGKGKKRP NRGKAKPVVS DFDSDEEQDE 1570 REQSEGSGTD DE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor." Muchardt C., Yaniv M. EMBO J. 12:4279-4290(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). Tissue: Liver.
[2]	"Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor." Chiba H., Muramatsu M., Nomoto A., Kato H. Nucleic Acids Res. 22:1815-1820(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). Tissue: Brain.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome." Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S. Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[6]	"TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival." Liu K., Luo Y., Lin F.-T., Lin W.-C. Genes Dev. 18:673-686(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOPBP1.
[7]	"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 SER-329; SER-1568 AND SER-1572, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[9]	"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex." Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S. Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-1512; SER-1516 AND SER-1528, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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-1512 AND SER-1516, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-997 AND LYS-999, MASS SPECTROMETRY.
[14]	"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-175; SER-329; SER-1568 AND SER-1572, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Mutations affecting components of the SWI/SNF complex cause Coffin-Siris syndrome." Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S. , Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N. Nat. Genet. 44:376-378(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN NCBRS.
[17]	"Solution structure of the bromodomain of human SWI/SNF related matrix associated actin dependent regulator of chromatin subfamily A member 2." RIKEN structural genomics initiative (RSGI) Submitted (JAN-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1377-1486.
[18]	"Heterozygous missense mutations in SMARCA2 cause Nicolaides-Baraitser syndrome." Van Houdt J.K., Nowakowska B.A., Sousa S.B., van Schaik B.D., Seuntjens E., Avonce N., Sifrim A., Abdul-Rahman O.A., van den Boogaard M.J., Bottani A., Castori M., Cormier-Daire V., Deardorff M.A., Filges I., Fryer A., Fryns J.P., Gana S., Garavelli L. , Gillessen-Kaesbach G., Hall B.D., Horn D., Huylebroeck D., Klapecki J., Krajewska-Walasek M., Kuechler A., Lines M.A., Maas S., Macdermot K.D., McKee S., Magee A., de Man S.A., Moreau Y., Morice-Picard F., Obersztyn E., Pilch J., Rosser E., Shannon N., Stolte-Dijkstra I., Van Dijck P., Vilain C., Vogels A., Wakeling E., Wieczorek D., Wilson L., Zuffardi O., van Kampen A.H., Devriendt K., Hennekam R., Vermeesch J.R. Nat. Genet. 44:445-449(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS NCBRS ALA-752; ARG-755; ILE-756; HIS-851; ASP-852; LYS-852; ARG-854; ASN-854; GLY-855; ARG-881; VAL-881; LEU-883; TYR-939; SER-946; PHE-946; CYS-1105; PRO-1105; PRO-1135; ARG-1146; VAL-1158; GLY-1159; LEU-1159; GLN-1159; HIS-1162; PRO-1188; VAL-1201; CYS-1202; GLY-1205 AND TRP-1213.
+	Additional computationally mapped references.

Web resources

SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X72889 mRNA. Translation: CAA51407.1.
D26155 mRNA. Translation: BAA05142.1.
AL359076, AL138755 Genomic DNA. Translation: CAI12967.1.
AL359076, AL138755 Genomic DNA. Translation: CAI12968.1.
AL138755, AL359076 Genomic DNA. Translation: CAI14599.1.
AL138755, AL359076 Genomic DNA. Translation: CAI14600.1.
CH471071 Genomic DNA. Translation: EAW58811.1.
CH471071 Genomic DNA. Translation: EAW58813.1.
CH471071 Genomic DNA. Translation: EAW58814.1.
CH471071 Genomic DNA. Translation: EAW58815.1.

IPI

IPI00386718.
IPI00514648.

PIR

S39580.
S45251.

RefSeq

NP_003061.3. NM_003070.3.
NP_620614.2. NM_139045.2.

UniGene

Hs.298990.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DAT	NMR	-	A	1377-1504	[»]

ProteinModelPortal

P51531.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29005N.

IntAct

P51531. 18 interactions.

MINT

MINT-1898892.

STRING

9606.ENSP00000265773.

PTM databases

PhosphoSite

P51531.

Polymorphism databases

DMDM

212276472.

Proteomic databases

PaxDb

P51531.

PRIDE

P51531.

Protocols and materials databases

DNASU

6595.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000349721; ENSP00000265773; ENSG00000080503.
ENST00000357248; ENSP00000349788; ENSG00000080503.
ENST00000382194; ENSP00000371629; ENSG00000080503.
ENST00000382203; ENSP00000371638; ENSG00000080503.

GeneID

6595.

KEGG

hsa:6595.

UCSC

uc003zhc.3. human.
uc003zhd.3. human.

Organism-specific databases

CTD

6595.

GeneCards

GC09P002005.

HGNC

HGNC:11098. SMARCA2.

HPA

HPA029981.

MIM

600014. gene.
601358. phenotype.

neXtProt

NX_P51531.

Orphanet

3051. Intellectual deficit - sparse hair - brachydactyly.

PharmGKB

PA35948.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0553.

HOGENOM

HOG000172363.

HOVERGEN

HBG056636.

InParanoid

P51531.

KO

K11647.

OMA

PQEGMHQ.

PhylomeDB

P51531.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

P51531.

Bgee

P51531.

CleanEx

HS_SMARCA2.

Genevestigator

P51531.

GermOnline

ENSG00000080503. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.

InterPro

IPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR006562. HSA.
IPR000330. SNF2_N.
[Graphical view]

Pfam

PF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
SM00951. QLQ. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS51666. QLQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SMARCA2. human.

EvolutionaryTrace

P51531.

GenomeRNAi

6595.

NextBio

25649.

PMAP-CutDB

P51531.

SOURCE

Search...

Entry information

Entry name

SMCA2_HUMAN

Accession

Primary (citable) accession number: P51531
Secondary accession number(s): B1ALG3 , B1ALG4, D3DRH4, D3DRH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 4, 2008
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.