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 SMARCC2 (BRG1-associated factor 170) (BAF170) (SWI/SNF complex 170 kDa subunit) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2)

 SMRC2_HUMAN             Reviewed;        1214 AA.
Q8TAQ2; F8VTJ5; Q59GV3; Q92923; Q96E12; Q96GY4;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
18-JUL-2018, entry version 163.
RecName: Full=SWI/SNF complex subunit SMARCC2;
AltName: Full=BRG1-associated factor 170;
Short=BAF170;
AltName: Full=SWI/SNF complex 170 kDa subunit;
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2;
Name=SMARCC2; Synonyms=BAF170;
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 1).
TISSUE=T-cell;
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] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Colon, and Duodenum;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, 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-283; SER-286; SER-302;
SER-304 AND SER-347, 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-347, 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-326, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-304; SER-306;
SER-347; THR-548 AND SER-813, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302; SER-304
AND SER-347, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302; SER-347;
THR-548 AND SER-813, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-347, 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).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-848, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-566 AND LYS-704, 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).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-564; LYS-566; LYS-568;
LYS-592; LYS-704; LYS-787 AND LYS-848, 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).
[18]
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).
[19]
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).
[20]
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).
[21]
INTERACTION WITH RCOR1.
PubMed=12192000; DOI=10.1074/jbc.M205691200;
Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G.,
Rosenfeld M.G., Anderson M.E., Mandel G.;
"REST repression of neuronal genes requires components of the hSWI.SNF
complex.";
J. Biol. Chem. 277:41038-41045(2002).
[22]
INTERACTION WITH 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).
[23]
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).
[24]
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).
[25]
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).
-!- 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 (PubMed:11018012). Can stimulate the
ATPase activity of the catalytic subunit of these complexes
(PubMed:10078207). May be required for CoREST dependent repression
of neuronal specific gene promoters in non-neuronal cells
(PubMed:12192000). 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). Critical regulator of myeloid
differentiation, controlling granulocytopoiesis and the expression
of genes involved in neutrophil granule formation (By similarity).
{ECO:0000250|UniProtKB:Q6PDG5, ECO:0000269|PubMed:10078207,
ECO:0000269|PubMed:11018012, ECO:0000269|PubMed:12192000,
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. 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). Interacts with SMARD1 (PubMed:12917342).
Interacts with KDM6B (By similarity). Interaction with RCOR1
(PubMed:12192000). {ECO:0000250|UniProtKB:Q6PDG5,
ECO:0000269|PubMed:11238380, ECO:0000269|PubMed:12192000,
ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:18765789,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
Q9P2D1:CHD7; NbExp=4; IntAct=EBI-357418, EBI-3951683;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-357418, EBI-750109;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=SMARCC2a;
IsoId=Q8TAQ2-1; Sequence=Displayed;
Name=2; Synonyms=SMARCC2b;
IsoId=Q8TAQ2-2; Sequence=VSP_012490, VSP_012491;
Name=3;
IsoId=Q8TAQ2-3; Sequence=VSP_012490, VSP_044647;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92243.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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; U66616; AAC50694.1; -; mRNA.
EMBL; BT009924; AAP88926.1; -; mRNA.
EMBL; AB209006; BAD92243.1; ALT_INIT; mRNA.
EMBL; AC073896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009067; AAH09067.1; -; mRNA.
EMBL; BC013045; AAH13045.1; -; mRNA.
EMBL; BC026222; AAH26222.1; -; mRNA.
CCDS; CCDS55835.1; -. [Q8TAQ2-3]
CCDS; CCDS8907.1; -. [Q8TAQ2-1]
CCDS; CCDS8908.1; -. [Q8TAQ2-2]
RefSeq; NP_001123892.1; NM_001130420.2. [Q8TAQ2-3]
RefSeq; NP_001317217.1; NM_001330288.1.
RefSeq; NP_003066.2; NM_003075.4. [Q8TAQ2-1]
RefSeq; NP_620706.1; NM_139067.3. [Q8TAQ2-2]
UniGene; Hs.236030; -.
UniGene; Hs.632717; -.
ProteinModelPortal; Q8TAQ2; -.
SMR; Q8TAQ2; -.
BioGrid; 112485; 149.
CORUM; Q8TAQ2; -.
DIP; DIP-27611N; -.
IntAct; Q8TAQ2; 63.
MINT; Q8TAQ2; -.
STRING; 9606.ENSP00000267064; -.
iPTMnet; Q8TAQ2; -.
PhosphoSitePlus; Q8TAQ2; -.
BioMuta; SMARCC2; -.
DMDM; 57012959; -.
EPD; Q8TAQ2; -.
MaxQB; Q8TAQ2; -.
PaxDb; Q8TAQ2; -.
PeptideAtlas; Q8TAQ2; -.
PRIDE; Q8TAQ2; -.
ProteomicsDB; 73906; -.
ProteomicsDB; 73907; -. [Q8TAQ2-2]
DNASU; 6601; -.
Ensembl; ENST00000267064; ENSP00000267064; ENSG00000139613. [Q8TAQ2-1]
Ensembl; ENST00000347471; ENSP00000302919; ENSG00000139613. [Q8TAQ2-2]
Ensembl; ENST00000394023; ENSP00000377591; ENSG00000139613. [Q8TAQ2-3]
GeneID; 6601; -.
KEGG; hsa:6601; -.
UCSC; uc001ska.4; human. [Q8TAQ2-1]
CTD; 6601; -.
DisGeNET; 6601; -.
EuPathDB; HostDB:ENSG00000139613.11; -.
GeneCards; SMARCC2; -.
HGNC; HGNC:11105; SMARCC2.
HPA; CAB004321; -.
HPA; HPA021213; -.
HPA; HPA061788; -.
MIM; 601734; gene.
neXtProt; NX_Q8TAQ2; -.
OpenTargets; ENSG00000139613; -.
PharmGKB; PA35955; -.
eggNOG; KOG1279; Eukaryota.
eggNOG; COG5259; LUCA.
GeneTree; ENSGT00390000018166; -.
HOGENOM; HOG000047736; -.
HOVERGEN; HBG054849; -.
InParanoid; Q8TAQ2; -.
KO; K11649; -.
PhylomeDB; Q8TAQ2; -.
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; Q8TAQ2; -.
ChiTaRS; SMARCC2; human.
GeneWiki; SMARCC2; -.
GenomeRNAi; 6601; -.
PRO; PR:Q8TAQ2; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139613; -.
CleanEx; HS_SMARCC2; -.
ExpressionAtlas; Q8TAQ2; baseline and differential.
Genevisible; Q8TAQ2; HS.
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:0032991; C:protein-containing complex; HDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:0043044; P:ATP-dependent chromatin remodeling; HDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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.
CDD; cd00167; SANT; 1.
Gene3D; 1.10.10.10; -; 1.
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; IPR038044; SMARCC2.
InterPro; IPR032451; SMARCC_C.
InterPro; IPR032450; SMARCC_N.
InterPro; IPR007526; SWIRM.
InterPro; IPR032448; SWIRM-assoc.
InterPro; IPR036388; WH-like_DNA-bd_sf.
PANTHER; PTHR12802:SF38; PTHR12802:SF38; 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;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Isopeptide bond; Neurogenesis; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 1214 SWI/SNF complex subunit SMARCC2.
/FTId=PRO_0000197117.
DOMAIN 424 521 SWIRM. {ECO:0000255|PROSITE-
ProRule:PRU00247}.
DOMAIN 596 647 SANT. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
COILED 907 934 {ECO:0000255}.
COMPBIAS 186 189 Poly-Glu.
COMPBIAS 747 855 Glu-rich.
COMPBIAS 861 870 Poly-Ala.
COMPBIAS 956 960 Poly-Gln.
COMPBIAS 961 1213 Pro-rich.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 326 326 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000244|PubMed:17081983,
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 387 387 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PDG5}.
MOD_RES 548 548 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 813 813 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 564 564 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 566 566 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 568 568 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 592 592 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 704 704 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 787 787 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 848 848 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 550 550 Q -> QGRQVDADTKAGRKGKELDDLVPETAKGKPEL (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2, ECO:0000303|Ref.3}.
/FTId=VSP_012490.
VAR_SEQ 1075 1189 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_012491.
VAR_SEQ 1075 1167 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_044647.
CONFLICT 311 316 AKKKNA -> VKEEKC (in Ref. 1; AAC50694).
{ECO:0000305}.
CONFLICT 498 498 M -> S (in Ref. 1; AAC50694).
{ECO:0000305}.
CONFLICT 587 587 V -> A (in Ref. 1; AAC50694).
{ECO:0000305}.
CONFLICT 876 876 L -> F (in Ref. 2; AAP88926 and 5;
AAH13045). {ECO:0000305}.
CONFLICT 942 942 A -> P (in Ref. 1; AAC50694).
{ECO:0000305}.
CONFLICT 1020 1020 A -> R (in Ref. 1; AAC50694).
{ECO:0000305}.
CONFLICT 1117 1126 HGHHHHLPFA -> MGSPPSPVR (in Ref. 1;
AAC50694). {ECO:0000305}.
SEQUENCE 1214 AA; 132879 MW; EEFC1042A9296320 CRC64;
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ
EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN
VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDII KRHQGTVTED KNNASHVVYP
VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK
WILDTDTFNE WMNEEDYEVN DDKNPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK
RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT
VNTKKDSESA PVKGGTMTDL DEQEDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ
THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY
LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG
LVPLQPKTPQ QTSASQQMLN FPDKGKEKPT DMQNFGLRTD MYTKKNVPSK SKAAASATRE
WTEQETLLLL EALEMYKDDW NKVSEHVGSR TQDECILHFL RLPIEDPYLE DSEASLGPLA
YQPIPFSQSG NPVMSTVAFL ASVVDPRVAS AAAKSALEEF SKMKEEVPTA LVEAHVRKVE
EAAKVTGKAD PAFGLESSGI AGTTSDEPER IEESGNDEAR VEGQATDEKK EPKEPREGGG
AIEEEAKEKT SEAPKKDEEK GKEGDSEKES EKSDGDPIVD PEKEKEPKEG QEEVLKEVVE
SEGERKTKVE RDIGEGNLST AAAAALAAAA VKAKHLAAVE ERKIKSLVAL LVETQMKKLE
IKLRHFEELE TIMDREREAL EYQRQQLLAD RQAFHMEQLK YAEMRARQQH FQQMHQQQQQ
PPPALPPGSQ PIPPTGAAGP PAVHGLAVAP ASVVPAPAGS GAPPGSLGPS EQIGQAGSTA
GPQQQQPAGA PQPGAVPPGV PPPGPHGPSP FPNQQTPPSM MPGAVPGSGH PGVAGNAPLG
LPFGMPPPPP PPAPSIIPFG SLADSISINL PAPPNLHGHH HHLPFAPGTL PPPNLPVSMA
NPLHPNLPAT TTMPSSLPLG PGLGSAAAQS PAIVAAVQGN LLPSASPLPD PGTPLPPDPT
APSPGTVTPV PPPQ


Related products :

Catalog number Product name Quantity
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
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
SMARCC2 SMARCC2 Gene SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
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
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
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
201-20-5444 SMARCC2{SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2}rabbit.pAb 0.2ml
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-EL021807MO Mouse SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 (SMARCC2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021807HU Human SWI_SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 (SMARCC2) 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
H3862 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (HMG20B), Mouse, ELISA Kit 96T
H3861 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (HMG20B), Human, ELISA Kit 96T
H3860 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (HMG20B), Bovine, ELISA Kit 96T


 

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