Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

SWI/SNF complex subunit SMARCC1 (BRG1-associated factor 155) (BAF155) (SWI/SNF complex 155 kDa subunit) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1)

 SMRC1_HUMAN             Reviewed;        1105 AA.
Q92922; Q17RS0; Q6P172; Q8IWH2;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 3.
12-SEP-2018, entry version 186.
RecName: Full=SWI/SNF complex subunit SMARCC1;
AltName: Full=BRG1-associated factor 155;
Short=BAF155;
AltName: Full=SWI/SNF complex 155 kDa subunit;
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1;
Name=SMARCC1; Synonyms=BAF155;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8804307; DOI=10.1101/gad.10.17.2117;
Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.;
"Diversity and specialization of mammalian SWI/SNF complexes.";
Genes Dev. 10:2117-2130(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-32; 470-478; 483-491; 591-602; 653-663; 717-724
AND 894-905, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Mammary carcinoma;
Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[4]
PHOSPHORYLATION AT THE G2/M TRANSITION.
PubMed=9744861; DOI=10.1101/gad.12.18.2842;
Sif S., Stukenberg P.T., Kirschner M.W., Kingston R.E.;
"Mitotic inactivation of a human SWI/SNF chromatin remodeling
complex.";
Genes Dev. 12:2842-2851(1998).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330; THR-335
AND SER-357, 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-345; LYS-346; LYS-354;
LYS-359 AND LYS-948, 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).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-328; SER-330;
SER-357 AND SER-573, 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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330; THR-335;
SER-350; THR-398; SER-822 AND SER-825, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-328; SER-330
AND SER-573, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, 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).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-359, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-359 AND LYS-592, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-359; LYS-592;
LYS-739; LYS-796; LYS-829 AND LYS-856, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
STIMULATION OF THE CHROMATIN-REMODELING ACTIVITY OF SMARCA4.
PubMed=10078207; DOI=10.1016/S1097-2765(00)80315-9;
Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.;
"Reconstitution of a core chromatin remodeling complex from SWI/SNF
subunits.";
Mol. Cell 3:247-253(1999).
[22]
INTERACTION WITH CCNE1.
PubMed=9891079; DOI=10.1128/MCB.19.2.1460;
Shanahan F., Seghezzi W., Parry D., Mahony D., Lees E.;
"Cyclin E associates with BAF155 and BRG1, components of the mammalian
SWI-SNF complex, and alters the ability of BRG1 to induce growth
arrest.";
Mol. Cell. Biol. 19:1460-1469(1999).
[23]
FUNCTION.
PubMed=11018012; DOI=10.1101/gad.828000;
Kadam S., McAlpine G.S., Phelan M.L., Kingston R.E., Jones K.A.,
Emerson B.M.;
"Functional selectivity of recombinant mammalian SWI/SNF subunits.";
Genes Dev. 14:2441-2451(2000).
[24]
INTERACTION WITH SIN3A.
PubMed=11238380; DOI=10.1101/gad.872801;
Sif S., Saurin A.J., Imbalzano A.N., Kingston R.E.;
"Purification and characterization of mSin3A-containing Brg1 and hBrm
chromatin remodeling complexes.";
Genes Dev. 15:603-618(2001).
[25]
INTERACTION WITH NR3C1 AND SMARD1.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[26]
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).
[27]
INTERACTION WITH TRIP12.
PubMed=20829358; DOI=10.1074/jbc.M110.173997;
Keppler B.R., Archer T.K.;
"Ubiquitin-dependent and ubiquitin-independent control of subunit
stoichiometry in the SWI/SNF complex.";
J. Biol. Chem. 285:35665-35674(2010).
[28]
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).
[29]
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).
[30]
STRUCTURE BY NMR OF 607-676.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SANT domain of human SWI/SNF-related
matrix-associated actin-dependent regulator of chromatin subfamily C
member 1.";
Submitted (APR-2008) to the PDB data bank.
[31]
INTERACTION WITH MKKS, AND SUBCELLULAR LOCATION.
PubMed=28753627; DOI=10.1371/journal.pgen.1006936;
Scott C.A., Marsden A.N., Rebagliati M.R., Zhang Q., Chamling X.,
Searby C.C., Baye L.M., Sheffield V.C., Slusarski D.C.;
"Nuclear/cytoplasmic transport defects in BBS6 underlie congenital
heart disease through perturbation of a chromatin remodeling
protein.";
PLoS Genet. 13:E1006936-E1006936(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. May stimulate the ATPase activity of the
catalytic subunit of the complex (PubMed:10078207). 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:P97496, ECO:0000269|PubMed:10078207,
ECO:0000269|PubMed:11018012, 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,
ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A,
SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF
complex also contains DPF3 (PubMed:18765789). 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 (By similarity). Component of
the SWI/SNF-B (PBAF) chromatin remodeling complex, at least
composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240,
PubMed:26601204). May also interact with the SIN3A histone
deacetylase transcription repressor complex in conjunction with
SMARCA2 and SMARCA4 (PubMed:11238380). The minimal complex
composed of SMARCC1 and SMARCA4 seems to be able to associate with
cyclin such as CCNE1 or transcription factors such as KLF1 or
GATA1 (PubMed:9891079). Interacts with NR3C1 and SMARD1
(PubMed:12917342). Interacts with TRIP12; leading to disrupt
interaction between TRIP12 and SMARCE1 and prevent SMARCE1
ubiquitination (PubMed:20111005). Interacts with CEBPB (when not
methylated)(PubMed:20829358). Interacts with KDM6B (By
similarity). Interacts with MKKS; the interaction takes place
predominantly in the cytoplasm and may modulate SMARCC1 location
(PubMed:28753627). {ECO:0000250|UniProtKB:P97496,
ECO:0000269|PubMed:11238380, ECO:0000269|PubMed:12917342,
ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20111005,
ECO:0000269|PubMed:20829358, ECO:0000269|PubMed:28753627,
ECO:0000269|PubMed:9891079, ECO:0000303|PubMed:22952240,
ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=5; IntAct=EBI-355653, EBI-10173507;
Q86X55:CARM1; NbExp=4; IntAct=EBI-355653, EBI-2339854;
O60341:KDM1A; NbExp=3; IntAct=EBI-355653, EBI-710124;
P32242:OTX1; NbExp=3; IntAct=EBI-355653, EBI-740446;
O15162:PLSCR1; NbExp=3; IntAct=EBI-355653, EBI-740019;
P51532:SMARCA4; NbExp=26; IntAct=EBI-355653, EBI-302489;
Q96GM5:SMARCD1; NbExp=4; IntAct=EBI-355653, EBI-358489;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28753627}.
Cytoplasm {ECO:0000269|PubMed:28753627}.
-!- TISSUE SPECIFICITY: Expressed in brain, heart, muscle, placenta,
lung, liver, muscle, kidney and pancreas.
-!- PTM: Phosphorylated on undefined residues at the G2/M transition
by ERK1 and other kinases. This may contribute to cell cycle
specific inactivation of remodeling complexes containing the
phosphorylated protein. {ECO:0000269|PubMed:9744861}.
-!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH39843.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH65253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U66615; AAC50693.1; -; mRNA.
EMBL; BC039843; AAH39843.1; ALT_SEQ; mRNA.
EMBL; BC065253; AAH65253.1; ALT_SEQ; mRNA.
EMBL; BC113465; AAI13466.1; -; mRNA.
EMBL; BC117213; AAI17214.1; -; mRNA.
CCDS; CCDS2758.1; -.
RefSeq; NP_003065.3; NM_003074.3.
UniGene; Hs.476179; -.
PDB; 2YUS; NMR; -; A=610-675.
PDB; 5GJK; X-ray; 2.05 A; A=447-540.
PDBsum; 2YUS; -.
PDBsum; 5GJK; -.
ProteinModelPortal; Q92922; -.
SMR; Q92922; -.
BioGrid; 112483; 134.
ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
CORUM; Q92922; -.
DIP; DIP-27545N; -.
DIP; DIP-33044N; -.
IntAct; Q92922; 85.
MINT; Q92922; -.
STRING; 9606.ENSP00000254480; -.
iPTMnet; Q92922; -.
PhosphoSitePlus; Q92922; -.
BioMuta; SMARCC1; -.
DMDM; 209572723; -.
EPD; Q92922; -.
MaxQB; Q92922; -.
PaxDb; Q92922; -.
PeptideAtlas; Q92922; -.
PRIDE; Q92922; -.
ProteomicsDB; 75605; -.
DNASU; 6599; -.
Ensembl; ENST00000254480; ENSP00000254480; ENSG00000173473.
GeneID; 6599; -.
KEGG; hsa:6599; -.
UCSC; uc003crq.3; human.
CTD; 6599; -.
DisGeNET; 6599; -.
EuPathDB; HostDB:ENSG00000173473.10; -.
GeneCards; SMARCC1; -.
H-InvDB; HIX0030795; -.
HGNC; HGNC:11104; SMARCC1.
HPA; CAB011576; -.
HPA; CAB016336; -.
HPA; HPA024352; -.
HPA; HPA026853; -.
MIM; 601732; gene.
neXtProt; NX_Q92922; -.
OpenTargets; ENSG00000173473; -.
PharmGKB; PA35954; -.
eggNOG; KOG1279; Eukaryota.
eggNOG; COG5259; LUCA.
GeneTree; ENSGT00390000018166; -.
HOGENOM; HOG000047736; -.
HOVERGEN; HBG054849; -.
InParanoid; Q92922; -.
KO; K11649; -.
OMA; YKKYVHA; -.
OrthoDB; EOG091G06AJ; -.
PhylomeDB; Q92922; -.
TreeFam; TF314710; -.
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; Q92922; -.
ChiTaRS; SMARCC1; human.
EvolutionaryTrace; Q92922; -.
GeneWiki; SMARCC1; -.
GenomeRNAi; 6599; -.
PRO; PR:Q92922; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000173473; Expressed in 232 organ(s), highest expression level in kidney.
CleanEx; HS_SMARCC1; -.
ExpressionAtlas; Q92922; baseline and differential.
Genevisible; Q92922; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0001741; C:XY body; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; HDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR030087; BAF155.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR032451; SMARCC_C.
InterPro; IPR032450; SMARCC_N.
InterPro; IPR007526; SWIRM.
InterPro; IPR032448; SWIRM-assoc.
InterPro; IPR036388; WH-like_DNA-bd_sf.
PANTHER; PTHR12802:SF9; PTHR12802:SF9; 1.
Pfam; PF00249; Myb_DNA-binding; 1.
Pfam; PF04433; SWIRM; 1.
Pfam; PF16495; SWIRM-assoc_1; 1.
Pfam; PF16496; SWIRM-assoc_2; 1.
Pfam; PF16498; SWIRM-assoc_3; 1.
SMART; SM00298; CHROMO; 1.
SMART; SM00717; SANT; 1.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS51293; SANT; 1.
PROSITE; PS50934; SWIRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromatin regulator; Coiled coil;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.3}.
CHAIN 2 1105 SWI/SNF complex subunit SMARCC1.
/FTId=PRO_0000197115.
DOMAIN 449 546 SWIRM. {ECO:0000255|PROSITE-
ProRule:PRU00247}.
DOMAIN 618 669 SANT. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
COILED 914 946 {ECO:0000255}.
COMPBIAS 329 336 Poly-Pro.
COMPBIAS 769 863 Glu-rich.
COMPBIAS 867 878 Poly-Ala.
COMPBIAS 977 1105 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.3}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 335 335 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 345 345 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 346 346 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 354 354 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 359 359 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 398 398 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 948 948 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1064 1064 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P97496}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 359 359 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 592 592 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 739 739 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 796 796 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 829 829 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 856 856 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 1075 1075 P -> H (in dbSNP:rs3772406).
/FTId=VAR_020883.
CONFLICT 19 22 SGIA -> FGDS (in Ref. 1; AAC50693).
{ECO:0000305}.
CONFLICT 497 497 T -> S (in Ref. 1; AAC50693).
{ECO:0000305}.
CONFLICT 528 529 FL -> GG (in Ref. 1; AAC50693).
{ECO:0000305}.
CONFLICT 564 570 SGLVPLH -> LACASD (in Ref. 1; AAC50693).
{ECO:0000305}.
CONFLICT 622 622 E -> G (in Ref. 1; AAC50693).
{ECO:0000305}.
CONFLICT 842 843 TD -> SS (in Ref. 1; AAC50693).
{ECO:0000305}.
CONFLICT 916 916 E -> G (in Ref. 1; AAC50693).
{ECO:0000305}.
HELIX 453 455 {ECO:0000244|PDB:5GJK}.
HELIX 465 470 {ECO:0000244|PDB:5GJK}.
HELIX 472 474 {ECO:0000244|PDB:5GJK}.
HELIX 484 500 {ECO:0000244|PDB:5GJK}.
HELIX 508 512 {ECO:0000244|PDB:5GJK}.
HELIX 519 531 {ECO:0000244|PDB:5GJK}.
STRAND 534 536 {ECO:0000244|PDB:5GJK}.
HELIX 625 637 {ECO:0000244|PDB:2YUS}.
STRAND 638 640 {ECO:0000244|PDB:2YUS}.
HELIX 642 649 {ECO:0000244|PDB:2YUS}.
HELIX 654 661 {ECO:0000244|PDB:2YUS}.
SEQUENCE 1105 AA; 122867 MW; EDA6FF5B0472AEA9 CRC64;
MAAAAGGGGP GTAVGATGSG IAAAAAGLAV YRRKDGGPAT KFWESPETVS QLDSVRVWLG
KHYKKYVHAD APTNKTLAGL VVQLLQFQED AFGKHVTNPA FTKLPAKCFM DFKAGGALCH
ILGAAYKYKN EQGWRRFDLQ NPSRMDRNVE MFMNIEKTLV QNNCLTRPNI YLIPDIDLKL
ANKLKDIIKR HQGTFTDEKS KASHHIYPYS SSQDDEEWLR PVMRKEKQVL VHWGFYPDSY
DTWVHSNDVD AEIEDPPIPE KPWKVHVKWI LDTDIFNEWM NEEDYEVDEN RKPVSFRQRI
STKNEEPVRS PERRDRKASA NARKRKHSPS PPPPTPTESR KKSGKKGQAS LYGKRRSQKE
EDEQEDLTKD MEDPTPVPNI EEVVLPKNVN LKKDSENTPV KGGTVADLDE QDEETVTAGG
KEDEDPAKGD QSRSVDLGED NVTEQTNHII IPSYASWFDY NCIHVIERRA LPEFFNGKNK
SKTPEIYLAY RNFMIDTYRL NPQEYLTSTA CRRNLTGDVC AVMRVHAFLE QWGLVNYQVD
PESRPMAMGP PPTPHFNVLA DTPSGLVPLH LRSPQVPAAQ QMLNFPEKNK EKPVDLQNFG
LRTDIYSKKT LAKSKGASAG REWTEQETLL LLEALEMYKD DWNKVSEHVG SRTQDECILH
FLRLPIEDPY LENSDASLGP LAYQPVPFSQ SGNPVMSTVA FLASVVDPRV ASAAAKAALE
EFSRVREEVP LELVEAHVKK VQEAARASGK VDPTYGLESS CIAGTGPDEP EKLEGAEEEK
MEADPDGQQP EKAENKVENE TDEGDKAQDG ENEKNSEKEQ DSEVSEDTKS EEKETEENKE
LTDTCKERES DTGKKKVEHE ISEGNVATAA AAALASAATK AKHLAAVEER KIKSLVALLV
ETQMKKLEIK LRHFEELETI MDREKEALEQ QRQQLLTERQ NFHMEQLKYA ELRARQQMEQ
QQHGQNPQQA HQHSGGPGLA PLGAAGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP
GSMMPGQHMP GRMIPTVAAN IHPSGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ
QPPPPPPADG VPPPPAPGPP ASAAP


Related products :

Catalog number Product name Quantity
EIAAB38857 BAF155,BAF155,BRG1-associated factor 155,Homo sapiens,Human,SMARCC1,SWI_SNF complex 155 kDa subunit,SWI_SNF complex subunit SMARCC1,SWI_SNF-related matrix-associated actin-dependent regulator of chrom
EIAAB38856 BAF155,Baf155,BRG1-associated factor 155,Mouse,Mus musculus,Smarcc1,Srg3,SWI_SNF complex 155 kDa subunit,SWI_SNF complex subunit SMARCC1,SWI_SNF-related matrix-associated actin-dependent regulator of
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
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
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
SMARCC1 SMARCC1 Gene SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
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
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
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
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
EIAAB38858 BAF170,BAF170,BRG1-associated factor 170,Homo sapiens,Human,SMARCC2,SWI_SNF complex 170 kDa subunit,SWI_SNF complex subunit SMARCC2,SWI_SNF-related matrix-associated actin-dependent regulator of chrom
EIAAB38859 BAF170,Baf170,BRG1-associated factor 170,Mouse,Mus musculus,Smarcc2,SWI_SNF complex 170 kDa subunit,SWI_SNF complex subunit SMARCC2,SWI_SNF-related matrix-associated actin-dependent regulator of chrom
201-20-5443 SMARCC1{SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1}rabbit.pAb 0.2ml
H3836 SWI SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1(SMARCC1), Human, ELISA Kit 96T
CSB-E13574h Human SWI_SNF related, matrix associated,actin dependent regulator of chromatin, subfamily c,member 1 (SMARCC1) ELISA Kit 96T
CSB-E13574h Human SWI_SNF related, matrix associated,actin dependent regulator of chromatin, subfamily c,member 1 (SMARCC1) ELISA Kit SpeciesHuman 96T
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
EIAAB38784 BAF57,Baf57,BRG1-associated factor 57,Mouse,Mus musculus,Smarce1,SWI_SNF-related matrix-associated actin-dependent regulator chromatin subfamily E 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
EIAAB38869 60 kDa BRG-1_Brm-associated factor subunit C,BAF60C,Baf60c,BRG1-associated factor 60C,mBAF60c,Mouse,Mus musculus,Smarcd3,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfam
EIAAB38866 60 kDa BRG-1_Brm-associated factor subunit B,BAF60B,BAF60B,BRG1-associated factor 60B,Homo sapiens,Human,PRO2451,SMARCD2,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfam
CSB-EL021806MO Mouse SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1 (SMARCC1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021806HU Human SWI_SNF related, matrix associated,actin dependent regulator of chromatin, subfamily c,member 1 (SMARCC1) ELISA Kit, Species Human, Sample Type serum, plasma 96T
EIAAB38862 60 kDa BRG-1_Brm-associated factor subunit A,BAF60A,BAF60A,Bos taurus,Bovine,BRG1-associated factor 60A,SMARCD1,SWI_SNF complex 60 kDa subunit,SWI_SNF-related matrix-associated actin-dependent regulat
EIAAB38864 60 kDa BRG-1_Brm-associated factor subunit A,BAF60A,BAF60A,BRG1-associated factor 60A,Homo sapiens,Human,SMARCD1,SWI_SNF complex 60 kDa subunit,SWI_SNF-related matrix-associated actin-dependent regula


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur