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Q8TAQ2 (SMRC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SWI/SNF complex subunit SMARCC2
Alternative name(s):
BRG1-associated factor 170
Short name=BAF170
SWI/SNF complex 170 kDa subunit
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2
Gene names
Name:SMARCC2
Synonyms:BAF170
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth By similarity. Ref.6 Ref.15

Subunit structure

Component of 6 multiprotein chromatin-remodeling complexes: Swi/Snf-A (BAF), Swi/Snf-B (PBAF), Brm, Brg1(I), WINAC and Brg1(II). Each of the five complexes contains a catalytic subunit (either SMARCA4 or SMARCA2), and at least SMARCE1, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCC1 and SMARCB1. Other subunits specific to each of the complexes may also be present. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. May also interact with the SIN3A histone deacetylase transcription repressor complex in conjunction with SMARCA2 and SMARCA4. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with SMARD1. 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. Ref.6 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Nucleus.

Tissue specificity

Ubiquitously expressed.

Sequence similarities

Belongs to the SMARCC family.

Contains 1 SANT domain.

Contains 1 SWIRM domain.

Sequence caution

The sequence BAD92243.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processNeurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin remodeling

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

negative regulation of transcription, DNA-dependent

Inferred from direct assay Ref.17. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome disassembly

Inferred from direct assay PubMed 8895581. Source: BHF-UCL

positive regulation of transcription, DNA-dependent

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Non-traceable author statement Ref.1. Source: BHF-UCL

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSWI/SNF complex

Inferred from direct assay Ref.14PubMed 11078522. Source: UniProtKB

nBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

npBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

chromatin binding

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Non-traceable author statement Ref.1. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TAQ2-1)

Also known as: SMARCC2a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8TAQ2-2)

Also known as: SMARCC2b;

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: Q → QGRQVDADTKAGRKGKELDDLVPETAKGKPEL
     1075-1189: Missing.
Isoform 3 (identifier: Q8TAQ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: Q → QGRQVDADTKAGRKGKELDDLVPETAKGKPEL
     1075-1167: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12141214SWI/SNF complex subunit SMARCC2
PRO_0000197117

Regions

Domain424 – 52198SWIRM
Domain596 – 64752SANT
Coiled coil907 – 93428 Potential
Compositional bias186 – 1894Poly-Glu
Compositional bias747 – 855109Glu-rich
Compositional bias861 – 87010Poly-Ala
Compositional bias956 – 9605Poly-Gln
Compositional bias961 – 1213253Pro-rich

Amino acid modifications

Modified residue2831Phosphoserine Ref.8 Ref.13
Modified residue2861Phosphoserine Ref.8
Modified residue3021Phosphoserine Ref.8 Ref.11 Ref.13
Modified residue3041Phosphoserine Ref.8 Ref.11 Ref.13
Modified residue3061Phosphoserine Ref.11
Modified residue3261N6-acetyllysine Ref.10
Modified residue3471Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11 Ref.13
Modified residue5481Phosphothreonine Ref.11
Modified residue8061Phosphoserine By similarity
Modified residue8101Phosphoserine By similarity
Modified residue8131Phosphoserine Ref.11

Natural variations

Alternative sequence5501Q → QGRQVDADTKAGRKGKELDD LVPETAKGKPEL in isoform 2 and isoform 3.
VSP_012490
Alternative sequence1075 – 1189115Missing in isoform 2.
VSP_012491
Alternative sequence1075 – 116793Missing in isoform 3.
VSP_044647

Experimental info

Sequence conflict311 – 3166AKKKNA → VKEEKC in AAC50694. Ref.1
Sequence conflict4981M → S in AAC50694. Ref.1
Sequence conflict5871V → A in AAC50694. Ref.1
Sequence conflict8761L → F in AAP88926. Ref.2
Sequence conflict8761L → F in AAH13045. Ref.5
Sequence conflict9421A → P in AAC50694. Ref.1
Sequence conflict10201A → R in AAC50694. Ref.1
Sequence conflict1117 – 112610HGHHHHLPFA → MGSPPSPVR in AAC50694. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SMARCC2a) [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: EEFC1042A9296320

FASTA1,214132,879
        10         20         30         40         50         60 
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ 

        70         80         90        100        110        120 
EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN 

       130        140        150        160        170        180 
VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDII KRHQGTVTED KNNASHVVYP 

       190        200        210        220        230        240 
VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK 

       250        260        270        280        290        300 
WILDTDTFNE WMNEEDYEVN DDKNPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK 

       310        320        330        340        350        360 
RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT 

       370        380        390        400        410        420 
VNTKKDSESA PVKGGTMTDL DEQEDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ 

       430        440        450        460        470        480 
THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY 

       490        500        510        520        530        540 
LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG 

       550        560        570        580        590        600 
LVPLQPKTPQ QTSASQQMLN FPDKGKEKPT DMQNFGLRTD MYTKKNVPSK SKAAASATRE 

       610        620        630        640        650        660 
WTEQETLLLL EALEMYKDDW NKVSEHVGSR TQDECILHFL RLPIEDPYLE DSEASLGPLA 

       670        680        690        700        710        720 
YQPIPFSQSG NPVMSTVAFL ASVVDPRVAS AAAKSALEEF SKMKEEVPTA LVEAHVRKVE 

       730        740        750        760        770        780 
EAAKVTGKAD PAFGLESSGI AGTTSDEPER IEESGNDEAR VEGQATDEKK EPKEPREGGG 

       790        800        810        820        830        840 
AIEEEAKEKT SEAPKKDEEK GKEGDSEKES EKSDGDPIVD PEKEKEPKEG QEEVLKEVVE 

       850        860        870        880        890        900 
SEGERKTKVE RDIGEGNLST AAAAALAAAA VKAKHLAAVE ERKIKSLVAL LVETQMKKLE 

       910        920        930        940        950        960 
IKLRHFEELE TIMDREREAL EYQRQQLLAD RQAFHMEQLK YAEMRARQQH FQQMHQQQQQ 

       970        980        990       1000       1010       1020 
PPPALPPGSQ PIPPTGAAGP PAVHGLAVAP ASVVPAPAGS GAPPGSLGPS EQIGQAGSTA 

      1030       1040       1050       1060       1070       1080 
GPQQQQPAGA PQPGAVPPGV PPPGPHGPSP FPNQQTPPSM MPGAVPGSGH PGVAGNAPLG 

      1090       1100       1110       1120       1130       1140 
LPFGMPPPPP PPAPSIIPFG SLADSISINL PAPPNLHGHH HHLPFAPGTL PPPNLPVSMA 

      1150       1160       1170       1180       1190       1200 
NPLHPNLPAT TTMPSSLPLG PGLGSAAAQS PAIVAAVQGN LLPSASPLPD PGTPLPPDPT 

      1210 
APSPGTVTPV PPPQ

« Hide

Isoform 2 (SMARCC2b) [UniParc].

Checksum: 30107786CB04BC1E
Show »

FASTA1,130124,841
Isoform 3 [UniParc].

Checksum: 70504763A7CA887C
Show »

FASTA1,152126,924

References

« Hide 'large scale' references
[1]"Diversity and specialization of mammalian SWI/SNF complexes."
Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.
Genes Dev. 10:2117-2130(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: T-cell.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"The finished DNA sequence of human chromosome 12."
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. expand/collapse author list , 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.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain, Colon and Duodenum.
[6]"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-286; SER-302; SER-304 AND SER-347, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, MASS SPECTROMETRY.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-304; SER-306; SER-347; THR-548 AND SER-813, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302; SER-304 AND SER-347, MASS SPECTROMETRY.
[14]"Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits."
Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.
Mol. Cell 3:247-253(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STIMULATION OF THE CHROMATIN-REMODELING ACTIVITY OF SMARCA4.
[15]"Functional selectivity of recombinant mammalian SWI/SNF subunits."
Kadam S., McAlpine G.S., Phelan M.L., Kingston R.E., Jones K.A., Emerson B.M.
Genes Dev. 14:2441-2451(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes."
Sif S., Saurin A.J., Imbalzano A.N., Kingston R.E.
Genes Dev. 15:603-618(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIN3A.
[17]"REST repression of neuronal genes requires components of the hSWI.SNF complex."
Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G., Rosenfeld M.G., Anderson M.E., Mandel G.
J. Biol. Chem. 277:41038-41045(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE COREST REPRESSOR.
[18]"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARD1.
[19]"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U66616 mRNA. Translation: AAC50694.1.
BT009924 mRNA. Translation: AAP88926.1.
AB209006 mRNA. Translation: BAD92243.1. Different initiation.
AC073896 Genomic DNA. No translation available.
BC009067 mRNA. Translation: AAH09067.1.
BC013045 mRNA. Translation: AAH13045.1.
BC026222 mRNA. Translation: AAH26222.1.
IPIIPI00150057.
IPI00216047.
IPI00793163.
RefSeqNP_001123892.1. NM_001130420.1.
NP_003066.2. NM_003075.3.
NP_620706.1. NM_139067.2.
UniGeneHs.236030.
Hs.632717.

3D structure databases

ProteinModelPortalQ8TAQ2.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27611N.
IntActQ8TAQ2. 34 interactions.
MINTMINT-1151033.
STRING9606.ENSP00000267064.

PTM databases

PhosphoSiteQ8TAQ2.

Polymorphism databases

DMDM57012959.

Proteomic databases

PaxDbQ8TAQ2.
PeptideAtlasQ8TAQ2.
PRIDEQ8TAQ2.

Protocols and materials databases

DNASU6601.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267064; ENSP00000267064; ENSG00000139613.
ENST00000347471; ENSP00000302919; ENSG00000139613.
ENST00000394023; ENSP00000377591; ENSG00000139613.
GeneID6601.
KEGGhsa:6601.
UCSCuc001ska.3. human.
uc001skb.3. human.

Organism-specific databases

CTD6601.
GeneCardsGC12M056555.
HGNCHGNC:11105. SMARCC2.
HPACAB004321.
HPA021213.
MIM601734. gene.
neXtProtNX_Q8TAQ2.
PharmGKBPA35955.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5259.
HOGENOMHOG000047736.
HOVERGENHBG054849.
InParanoidQ8TAQ2.
KOK11649.
PhylomeDBQ8TAQ2.

Gene expression databases

ArrayExpressQ8TAQ2.
BgeeQ8TAQ2.
CleanExHS_SMARCC2.
GenevestigatorQ8TAQ2.
GermOnlineENSG00000139613. Homo sapiens.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProIPR001357. BRCT_dom.
IPR000953. Chromo_domain/shadow.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
SSF46689. Homeodomain_like. 2 hits.
PROSITEPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMARCC2. human.
GenomeRNAi6601.
NextBio25677.
SOURCESearch...

Entry information

Entry nameSMRC2_HUMAN
AccessionPrimary (citable) accession number: Q8TAQ2
Secondary accession number(s): F8VTJ5 expand/collapse secondary AC list , Q59GV3, Q92923, Q96E12, Q96GY4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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