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Probable global transcription activator SNF2L2 (EC 3.6.4.-) (ATP-dependent helicase SMARCA2) (BRG1-associated factor 190B) (BAF190B) (Protein brahma homolog) (hBRM) (SNF2-alpha) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2)

 SMCA2_HUMAN             Reviewed;        1590 AA.
P51531; B1ALG3; B1ALG4; D3DRH4; D3DRH5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
31-JAN-2018, entry version 192.
RecName: Full=Probable global transcription activator SNF2L2;
EC=3.6.4.-;
AltName: Full=ATP-dependent helicase SMARCA2;
AltName: Full=BRG1-associated factor 190B;
Short=BAF190B;
AltName: Full=Protein brahma homolog;
Short=hBRM;
AltName: Full=SNF2-alpha;
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 {ECO:0000312|HGNC:HGNC:11098};
Name=SMARCA2 {ECO:0000312|HGNC:HGNC:11098};
Synonyms=BAF190B, BRM, SNF2A, SNF2L2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Liver;
PubMed=8223438;
Muchardt C., Yaniv M.;
"A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and
Drosophila brm genes potentiates transcriptional activation by the
glucocorticoid receptor.";
EMBO J. 12:4279-4290(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Brain;
PubMed=8208605; DOI=10.1093/nar/22.10.1815;
Chiba H., Muramatsu M., Nomoto A., Kato H.;
"Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
Drosophila brahma are transcriptional coactivators cooperating with
the estrogen receptor and the retinoic acid receptor.";
Nucleic Acids Res. 22:1815-1820(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
INTERACTION WITH TOPBP1.
PubMed=15075294; DOI=10.1101/gad.1180204;
Liu K., Luo Y., Lin F.-T., Lin W.-C.;
"TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel
pRb-independent and E2F1-specific control for cell survival.";
Genes Dev. 18:673-686(2004).
[6]
INTERACTION WITH CEBPA.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-1568 AND
SER-1572, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
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.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-1512; SER-1516
AND SER-1528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[12]
PROBABLE INVOLVEMENT IN SCZD, VARIANT GLU-1546, AND CHARACTERIZATION
OF VARIANT GLU-1546.
PubMed=19363039; DOI=10.1093/hmg/ddp166;
Koga M., Ishiguro H., Yazaki S., Horiuchi Y., Arai M., Niizato K.,
Iritani S., Itokawa M., Inada T., Iwata N., Ozaki N., Ujike H.,
Kunugi H., Sasaki T., Takahashi M., Watanabe Y., Someya T., Kakita A.,
Takahashi H., Nawa H., Muchardt C., Yaniv M., Arinami T.;
"Involvement of SMARCA2/BRM in the SWI/SNF chromatin-remodeling
complex in schizophrenia.";
Hum. Mol. Genet. 18:2483-2494(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512 AND SER-1516, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-997 AND LYS-999, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
INTERACTION WITH CEBPB.
PubMed=20111005; DOI=10.1038/emboj.2010.3;
Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
"Crosstalk between C/EBPbeta phosphorylation, arginine methylation,
and SWI/SNF/Mediator implies an indexing transcription factor code.";
EMBO J. 29:1105-1115(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-329; SER-1568
AND SER-1572, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INVOLVEMENT IN NCBRS.
PubMed=22426308; DOI=10.1038/ng.2219;
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.;
"Mutations affecting components of the SWI/SNF complex cause Coffin-
Siris syndrome.";
Nat. Genet. 44:376-378(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-329; SER-591;
SER-666 AND SER-1377, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-591; SER-1377
AND SER-1572, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=22952240; DOI=10.1074/jbc.R111.309302;
Euskirchen G., Auerbach R.K., Snyder M.;
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
functions.";
J. Biol. Chem. 287:30897-30905(2012).
[22]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=26601204; DOI=10.1126/sciadv.1500447;
Kadoch C., Crabtree G.R.;
"Mammalian SWI/SNF chromatin remodeling complexes and cancer:
Mechanistic insights gained from human genomics.";
Sci. Adv. 1:E1500447-E1500447(2015).
[23]
VARIANTS NCBRS LYS-852; GLN-855 AND ILE-880.
PubMed=23906836; DOI=10.1093/hmg/ddt366;
Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S.,
Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J.,
Alanay Y., Kayserili H., Klein-Hitpass L., Boehringer S.,
Wollstein A., Albrecht B., Boduroglu K., Caliebe A., Chrzanowska K.,
Cogulu O., Cristofoli F., Czeschik J.C., Devriendt K., Dotti M.T.,
Elcioglu N., Gener B., Goecke T.O., Krajewska-Walasek M.,
Guillen-Navarro E., Hayek J., Houge G., Kilic E., Simsek-Kiper P.O.,
Lopez-Gonzalez V., Kuechler A., Lyonnet S., Mari F., Marozza A.,
Mathieu Dramard M., Mikat B., Morin G., Morice-Picard F., Ozkinay F.,
Rauch A., Renieri A., Tinschert S., Utine G.E., Vilain C.,
Vivarelli R., Zweier C., Nuernberg P., Rahmann S., Vermeesch J.,
Luedecke H.J., Zeschnigk M., Wollnik B.;
"A comprehensive molecular study on Coffin-Siris and Nicolaides-
Baraitser syndromes identifies a broad molecular and clinical spectrum
converging on altered chromatin remodeling.";
Hum. Mol. Genet. 22:5121-5135(2013).
[24]
STRUCTURE BY NMR OF 1377-1486.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the bromodomain of human SWI/SNF related matrix
associated actin dependent regulator of chromatin subfamily A member
2.";
Submitted (JAN-2007) to the PDB data bank.
[25]
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.
PubMed=22366787; DOI=10.1038/ng.1105;
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.;
"Heterozygous missense mutations in SMARCA2 cause Nicolaides-Baraitser
syndrome.";
Nat. Genet. 44:445-449(2012).
[26]
VARIANT NCBRS GLU-1241.
PubMed=27665729; DOI=10.1002/ajmg.a.37935;
EuroEPINOMICS RES myoclonic astatic epilepsy working group;
Tang S., Hughes E., Lascelles K., Simpson M.A., Pal D.K.;
"New SMARCA2 mutation in a patient with Nicolaides-Baraitser syndrome
and myoclonic astatic epilepsy.";
Am. J. Med. Genet. A 173:195-199(2017).
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Component of SWI/SNF chromatin remodeling complexes
that carry out key enzymatic activities, changing chromatin
structure by altering DNA-histone contacts within a nucleosome in
an ATP-dependent manner. Binds DNA non-specifically
(PubMed:22952240, PubMed:26601204). 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 postmitotic 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 postmitotic 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).
{ECO:0000250|UniProtKB:Q6DIC0, ECO:0000303|PubMed:22952240,
ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of the multiprotein chromatin-remodeling
complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
complexes. The canonical complex contains a catalytic subunit
(either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific (Probable).
Component of the BAF complex, which includes at least actin
(ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C
(PubMed:18765789). In muscle cells, the BAF complex also contains
DPF3. 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). Interacts with CEBPB (when not
methylated)(PubMed:20111005). Interacts with TOPBP1
(PubMed:15075294). Interacts with CEBPA (when phosphorylated)
(PubMed:15107404). {ECO:0000250|UniProtKB:Q6DIC0,
ECO:0000269|PubMed:15075294, ECO:0000269|PubMed:15107404,
ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20111005,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
O14497:ARID1A; NbExp=3; IntAct=EBI-679562, EBI-637887;
Q8NFD5:ARID1B; NbExp=3; IntAct=EBI-679562, EBI-679921;
Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-10212306, EBI-10181188;
Q07666:KHDRBS1; NbExp=2; IntAct=EBI-679562, EBI-1364;
P51608:MECP2; NbExp=4; IntAct=EBI-679562, EBI-1189067;
O00560:SDCBP; NbExp=3; IntAct=EBI-10212306, EBI-727004;
P04326:tat (xeno); NbExp=8; IntAct=EBI-679562, EBI-7333987;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P51531-1; Sequence=Displayed;
Name=Short;
IsoId=P51531-2; Sequence=VSP_000577;
-!- 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. {ECO:0000269|PubMed:22366787,
ECO:0000269|PubMed:22426308, ECO:0000269|PubMed:23906836,
ECO:0000269|PubMed:27665729}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex,
multifactorial psychotic disorder or group of disorders
characterized by disturbances in the form and content of thought
(e.g. delusions, hallucinations), in mood (e.g. inappropriate
affect), in sense of self and relationship to the external world
(e.g. loss of ego boundaries, withdrawal), and in behavior (e.g
bizarre or apparently purposeless behavior). Although it affects
emotions, it is distinguished from mood disorders in which such
disturbances are primary. Similarly, there may be mild impairment
of cognitive function, and it is distinguished from the dementias
in which disturbed cognitive function is considered primary. Some
patients manifest schizophrenic as well as bipolar disorder
symptoms and are often given the diagnosis of schizoaffective
disorder. {ECO:0000269|PubMed:19363039}. Note=Disease
susceptibility may be associated with variations affecting the
gene represented in this entry.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SWI/SNF related, matrix associated, actin
dependent regulator of chromatin, subfamily a, member 2 (SMARCA2);
Note=Leiden Open Variation Database (LOVD);
URL="https://databases.lovd.nl/shared/genes/SMARCA2";
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EMBL; X72889; CAA51407.1; -; mRNA.
EMBL; D26155; BAA05142.1; -; mRNA.
EMBL; AL359076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58811.1; -; Genomic_DNA.
EMBL; CH471071; EAW58813.1; -; Genomic_DNA.
EMBL; CH471071; EAW58814.1; -; Genomic_DNA.
EMBL; CH471071; EAW58815.1; -; Genomic_DNA.
CCDS; CCDS34977.1; -. [P51531-1]
CCDS; CCDS34978.1; -. [P51531-2]
PIR; S39580; S39580.
PIR; S45251; S45251.
RefSeq; NP_001276325.1; NM_001289396.1. [P51531-1]
RefSeq; NP_001276326.1; NM_001289397.1.
RefSeq; NP_003061.3; NM_003070.4. [P51531-1]
RefSeq; NP_620614.2; NM_139045.3. [P51531-2]
UniGene; Hs.298990; -.
UniGene; Hs.644901; -.
PDB; 2DAT; NMR; -; A=1377-1504.
PDB; 4QY4; X-ray; 1.97 A; A/B/C=1373-1511.
PDB; 5DKC; X-ray; 1.60 A; A=1373-1511.
PDB; 5DKH; X-ray; 1.70 A; A/B/C=1373-1511.
PDBsum; 2DAT; -.
PDBsum; 4QY4; -.
PDBsum; 5DKC; -.
PDBsum; 5DKH; -.
ProteinModelPortal; P51531; -.
SMR; P51531; -.
BioGrid; 112479; 115.
CORUM; P51531; -.
DIP; DIP-29005N; -.
IntAct; P51531; 34.
MINT; MINT-1898892; -.
STRING; 9606.ENSP00000265773; -.
BindingDB; P51531; -.
ChEMBL; CHEMBL2362979; -.
iPTMnet; P51531; -.
PhosphoSitePlus; P51531; -.
BioMuta; SMARCA2; -.
DMDM; 212276472; -.
EPD; P51531; -.
MaxQB; P51531; -.
PaxDb; P51531; -.
PeptideAtlas; P51531; -.
PRIDE; P51531; -.
DNASU; 6595; -.
Ensembl; ENST00000349721; ENSP00000265773; ENSG00000080503. [P51531-1]
Ensembl; ENST00000357248; ENSP00000349788; ENSG00000080503. [P51531-2]
Ensembl; ENST00000382194; ENSP00000371629; ENSG00000080503. [P51531-2]
Ensembl; ENST00000382203; ENSP00000371638; ENSG00000080503. [P51531-1]
GeneID; 6595; -.
KEGG; hsa:6595; -.
UCSC; uc003zhc.5; human. [P51531-1]
CTD; 6595; -.
DisGeNET; 6595; -.
EuPathDB; HostDB:ENSG00000080503.20; -.
GeneCards; SMARCA2; -.
HGNC; HGNC:11098; SMARCA2.
HPA; CAB037276; -.
HPA; HPA029981; -.
MalaCards; SMARCA2; -.
MIM; 181500; phenotype.
MIM; 600014; gene.
MIM; 601358; phenotype.
neXtProt; NX_P51531; -.
OpenTargets; ENSG00000080503; -.
Orphanet; 3051; intellectual disability - sparse hair - brachydactyly.
PharmGKB; PA35948; -.
eggNOG; KOG0386; Eukaryota.
eggNOG; COG0553; LUCA.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00550000074659; -.
HOGENOM; HOG000172363; -.
HOVERGEN; HBG056636; -.
InParanoid; P51531; -.
KO; K11647; -.
OMA; GWDWIDD; -.
OrthoDB; EOG091G01R9; -.
PhylomeDB; P51531; -.
TreeFam; TF300785; -.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SIGNOR; P51531; -.
ChiTaRS; SMARCA2; human.
EvolutionaryTrace; P51531; -.
GeneWiki; SMARCA2; -.
GenomeRNAi; 6595; -.
PMAP-CutDB; P51531; -.
PRO; PR:P51531; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000080503; -.
CleanEx; HS_SMARCA2; -.
ExpressionAtlas; P51531; baseline and differential.
Genevisible; P51531; HS.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0008094; F:DNA-dependent ATPase activity; TAS:BHF-UCL.
GO; GO:0004386; F:helicase activity; TAS:ProtInc.
GO; GO:0042393; F:histone binding; IEA:InterPro.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
CDD; cd00079; HELICc; 1.
Gene3D; 1.20.920.10; -; 2.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR006576; BRK_domain.
InterPro; IPR037259; BRK_sf.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR014978; Gln-Leu-Gln_QLQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014012; HSA_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR030088; SMARCA2.
InterPro; IPR029295; SnAC.
InterPro; IPR000330; SNF2_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR10799:SF541; PTHR10799:SF541; 1.
Pfam; PF07533; BRK; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF07529; HSA; 1.
Pfam; PF08880; QLQ; 1.
Pfam; PF14619; SnAC; 1.
Pfam; PF00176; SNF2_N; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00592; BRK; 1.
SMART; SM00297; BROMO; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00573; HSA; 1.
SMART; SM00951; QLQ; 1.
SMART; SM01314; SnAC; 1.
SUPFAM; SSF160481; SSF160481; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51204; HSA; 1.
PROSITE; PS51666; QLQ; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Bromodomain; Complete proteome; Disease mutation;
DNA-binding; Helicase; Hydrolase; Hypotrichosis; Mental retardation;
Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Schizophrenia; Transcription;
Transcription regulation.
CHAIN 1 1590 Probable global transcription activator
SNF2L2.
/FTId=PRO_0000074352.
DOMAIN 173 208 QLQ. {ECO:0000255|PROSITE-
ProRule:PRU01001}.
DOMAIN 436 508 HSA. {ECO:0000255|PROSITE-
ProRule:PRU00549}.
DOMAIN 736 901 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1054 1216 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 1419 1489 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
NP_BIND 749 756 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 851 854 DEGH box.
COMPBIAS 216 238 Poly-Gln.
COMPBIAS 245 253 Poly-Gln.
COMPBIAS 559 562 Poly-Arg.
COMPBIAS 643 650 Poly-Glu.
COMPBIAS 1297 1301 Poly-Glu.
COMPBIAS 1518 1529 Poly-Glu.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000250|UniProtKB:Q6DIC0}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 604 604 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q6DIC0}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 997 997 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 999 999 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1377 1377 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1512 1512 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1516 1516 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1528 1528 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1568 1568 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:20068231}.
MOD_RES 1572 1572 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1400 1417 Missing (in isoform Short).
{ECO:0000303|PubMed:8208605}.
/FTId=VSP_000577.
VARIANT 752 752 G -> A (in NCBRS; dbSNP:rs281875198).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068180.
VARIANT 755 755 K -> R (in NCBRS; dbSNP:rs281875203).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068181.
VARIANT 756 756 T -> I (in NCBRS; dbSNP:rs281875191).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068182.
VARIANT 851 851 D -> H (in NCBRS; dbSNP:rs281875206).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068183.
VARIANT 852 852 E -> D (in NCBRS; dbSNP:rs281875193).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068184.
VARIANT 852 852 E -> K (in NCBRS; dbSNP:rs281875199).
{ECO:0000269|PubMed:22366787,
ECO:0000269|PubMed:23906836}.
/FTId=VAR_068185.
VARIANT 854 854 H -> N (in NCBRS).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068186.
VARIANT 854 854 H -> R (in NCBRS; dbSNP:rs281875202).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068187.
VARIANT 855 855 R -> G (in NCBRS; dbSNP:rs281875207).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068188.
VARIANT 855 855 R -> Q (in NCBRS).
{ECO:0000269|PubMed:23906836}.
/FTId=VAR_076936.
VARIANT 880 880 T -> I (in NCBRS).
{ECO:0000269|PubMed:23906836}.
/FTId=VAR_076937.
VARIANT 881 881 G -> R (in NCBRS; dbSNP:rs281875194).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068189.
VARIANT 881 881 G -> V (in NCBRS; dbSNP:rs281875185).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068190.
VARIANT 883 883 P -> L (in NCBRS; dbSNP:rs281875188).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068191.
VARIANT 939 939 H -> Y (in NCBRS; dbSNP:rs281875190).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068192.
VARIANT 946 946 L -> F (in NCBRS; dbSNP:rs281875205).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068193.
VARIANT 946 946 L -> S (in NCBRS; dbSNP:rs281875200).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068194.
VARIANT 1105 1105 R -> C (in NCBRS; dbSNP:rs281875192).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068195.
VARIANT 1105 1105 R -> P (in NCBRS; dbSNP:rs281875197).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068196.
VARIANT 1135 1135 L -> P (in NCBRS; dbSNP:rs281875195).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068197.
VARIANT 1146 1146 S -> R (in NCBRS; dbSNP:rs281875204).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068198.
VARIANT 1158 1158 D -> V (in NCBRS; dbSNP:rs281875240).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068199.
VARIANT 1159 1159 R -> G (in NCBRS; dbSNP:rs281875184).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068200.
VARIANT 1159 1159 R -> L (in NCBRS; dbSNP:rs281875187).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068201.
VARIANT 1159 1159 R -> Q (in NCBRS; dbSNP:rs281875187).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068202.
VARIANT 1162 1162 R -> H (in NCBRS; dbSNP:rs281875186).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068203.
VARIANT 1188 1188 A -> P (in NCBRS; dbSNP:rs281875196).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068204.
VARIANT 1201 1201 A -> V (in NCBRS; dbSNP:rs281875189).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068205.
VARIANT 1202 1202 G -> C (in NCBRS; dbSNP:rs281875239).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068206.
VARIANT 1205 1205 D -> G (in NCBRS; dbSNP:rs281875201).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068207.
VARIANT 1213 1213 R -> W (in NCBRS; dbSNP:rs281875238).
{ECO:0000269|PubMed:22366787}.
/FTId=VAR_068208.
VARIANT 1241 1241 Q -> E (in NCBRS).
{ECO:0000269|PubMed:27665729}.
/FTId=VAR_078815.
VARIANT 1416 1416 G -> A (in dbSNP:rs3793510).
/FTId=VAR_049501.
VARIANT 1546 1546 D -> E (polymorphism; associated with
schizophrenia in some populations;
results in reduced localization to the
nucleus; decreased interaction with
chromatin; dbSNP:rs2296212).
{ECO:0000269|PubMed:19363039}.
/FTId=VAR_049502.
CONFLICT 237 240 Missing (in Ref. 1; CAA51407).
{ECO:0000305}.
CONFLICT 394 394 Q -> E (in Ref. 2; BAA05142).
{ECO:0000305}.
CONFLICT 513 513 G -> S (in Ref. 2; BAA05142).
{ECO:0000305}.
CONFLICT 711 711 R -> W (in Ref. 1; CAA51407).
{ECO:0000305}.
CONFLICT 1139 1139 D -> H (in Ref. 2; BAA05142).
{ECO:0000305}.
CONFLICT 1394 1394 V -> C (in Ref. 1; CAA51407).
{ECO:0000305}.
CONFLICT 1400 1400 R -> S (in Ref. 1; CAA51407).
{ECO:0000305}.
HELIX 1382 1396 {ECO:0000244|PDB:5DKC}.
STRAND 1418 1420 {ECO:0000244|PDB:2DAT}.
HELIX 1425 1427 {ECO:0000244|PDB:5DKC}.
TURN 1433 1435 {ECO:0000244|PDB:5DKC}.
HELIX 1437 1442 {ECO:0000244|PDB:5DKC}.
HELIX 1449 1457 {ECO:0000244|PDB:5DKC}.
HELIX 1464 1481 {ECO:0000244|PDB:5DKC}.
HELIX 1487 1507 {ECO:0000244|PDB:5DKC}.
SEQUENCE 1590 AA; 181279 MW; CE69BBB287D35AB5 CRC64;
MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM
GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY
MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH
QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ
QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA
AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE
LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR
QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV
ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL
TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT
ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI
LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI
NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV
PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL
AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP
TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE
KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY
MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT
IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT
VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ
AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR
RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL
TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP
PKLTKQMNAI IDTVINYKDR CNVEKVPSNS QLEIEGNSSG RQLSEVFIQL PSRKELPEYY
ELIRKPVDFK KIKERIRNHK YRSLGDLEKD VMLLCHNAQT FNLEGSQIYE DSIVLQSVFK
SARQKIAKEE ESEDESNEEE EEEDEEESES EAKSVKVKIK LNKKDDKGRD KGKGKKRPNR
GKAKPVVSDF DSDEEQDERE QSEGSGTDDE


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EIAAB38780 ATP-dependent helicase SMARCA4,BAF190A,BAF190A,BRG1,BRG1-associated factor 190A,Homo sapiens,Human,Mitotic growth and transcription activator,Protein brahma homolog 1,Protein BRG-1,SMARCA4,SNF2B,SNF2-
18-003-43477 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 - BRG1-associated factor 57 Polyclonal 0.05 mg Aff Pur
18-003-43476 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2 - 60 kDa BRG-1_Brm-associated factor subunit B; BRG1-associated factor 60B Polyclonal 0.05 mg Aff Pur
18-003-43138 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 - 60 kDa BRG-1_Brm-associated factor subunit C; BRG1-associated factor 60C Polyclonal 0.05 mg Aff Pur
EIAAB38867 60 kDa BRG-1_Brm-associated factor subunit B,BAF60B,Bos taurus,Bovine,BRG1-associated factor 60B,SMARCD2,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
EIAAB38784 BAF57,Baf57,BRG1-associated factor 57,Mouse,Mus musculus,Smarce1,SWI_SNF-related matrix-associated actin-dependent regulator chromatin subfamily E member 1
EIAAB38951 BAF47,BAF47,Bos taurus,Bovine,BRG1-associated factor 47,SMARCB1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
EIAAB38785 BAF57,BAF57,BRG1-associated factor 57,Homo sapiens,Human,SMARCE1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
EIAAB38860 ATP-dependent helicase SMARCAD1,Enhancer trap locus homolog 1,Etl1,Etl-1,Kiaa1122,Mouse,Mus musculus,Smarcad1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A conta
20-372-60078 SWI_SNF related. matrix associated. actin dependent regulator of chromatin. subfamily a. member 4 (SMARCA4) - Mouse monoclonal anti-human SMARCA4 antibody; EC 3.6.1.-; ATP-dependent helicase SMARCA4; 0.1 mg
EIAAB38861 ATP-dependent helicase 1,hHEL1,Homo sapiens,Human,KIAA1122,SMARCAD1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD_H box 1
CSB-EL021799HU Human SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL021799MO Mouse SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB38782 Mouse,mSnf2h,Mus musculus,Smarca5,Snf2h,Sucrose nonfermenting protein 2 homolog,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
EIAAB38868 60 kDa BRG-1_Brm-associated factor subunit B,BAF60B,Baf60b,BRG1-associated factor 60B,Mouse,Mus musculus,Smarcd2,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D me
EIAAB38865 60 kDa BRG-1_Brm-associated factor subunit B,BAF60B,Baf60b,BRG1-associated factor 60B,Rat,Rattus norvegicus,Smarcd2,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D
EIAAB38870 60 kDa BRG-1_Brm-associated factor subunit C,BAF60C,BAF60C,BRG1-associated factor 60C,Homo sapiens,Human,SMARCD3,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D me


 

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