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Q6DIC0 (SMCA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable global transcription activator SNF2L2

EC=3.6.4.-
Alternative name(s):
ATP-dependent helicase SMARCA2
BRG1-associated factor 190B
Short name=BAF190B
Protein brahma homolog
SNF2-alpha
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
Gene names
Name:Smarca2
Synonyms:Baf190b, Brm, Snf2a, Snf2l2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene By similarity. 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. Ref.2

Subunit structure

Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Binds TOPBP1 By similarity. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. Interacts with PHF10/BAF45A. Ref.2

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in the cortex and the hippocampus. Expressed in the cortical plate in the embryo. Ref.4

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 bromo domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HSA domain.

Contains 1 QLQ domain.

Ontologies

Keywords
   Biological processNeurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionActivator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaortic smooth muscle cell differentiation

Inferred from mutant phenotype PubMed 19342595. Source: MGI

chromatin organization

Traceable author statement PubMed 11318604. Source: MGI

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 9843504. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome assembly

Traceable author statement PubMed 11163203. Source: MGI

   Cellular_componentSWI/SNF complex

Traceable author statement PubMed 11163203PubMed 11318604. Source: MGI

WINAC complex

Inferred from electronic annotation. Source: Ensembl

intermediate filament cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nBAF complex

Inferred from direct assay Ref.2. Source: UniProtKB

npBAF complex

Inferred from direct assay Ref.2. Source: UniProtKB

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 9603422. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.2. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15771577Probable global transcription activator SNF2L2
PRO_0000391618

Regions

Domain167 – 20236QLQ
Domain441 – 51373HSA
Domain741 – 906166Helicase ATP-binding
Domain1059 – 1221163Helicase C-terminal
Domain1406 – 147671Bromo
Nucleotide binding754 – 7618ATP By similarity
Motif856 – 8594DEGH box
Compositional bias4 – 170167Pro-rich
Compositional bias172 – 340169Gln-rich
Compositional bias648 – 6558Poly-Glu
Compositional bias1302 – 13065Poly-Glu
Compositional bias1496 – 151823Glu-rich

Amino acid modifications

Modified residue1691Phosphoserine By similarity
Modified residue3341Phosphoserine Ref.3
Modified residue6091N6-acetyllysine Ref.5
Modified residue10021N6-acetyllysine By similarity
Modified residue10041N6-acetyllysine By similarity
Modified residue14991Phosphoserine Ref.3
Modified residue15031Phosphoserine Ref.3
Modified residue15151Phosphoserine By similarity
Modified residue15551Phosphoserine By similarity
Modified residue15591Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6DIC0 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 5D79E8FFC66085BE

FASTA1,577180,253
        10         20         30         40         50         60 
MSTPTDPAAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPLSTM 

        70         80         90        100        110        120 
GSADFPQEGM HQLHKPMDGI HDKGIVEDVH CGSMKGTSMR PPHPGMGPPQ SPMDQHSQGY 

       130        140        150        160        170        180 
MSPHPSPLGA PEHVSSPTPP QMPPSQPGAL IPGDPQAMNQ PNRGPSPFSP VQLHQLRAQI 

       190        200        210        220        230        240 
LAYKMLARGQ PLPETLQLAV QGKRTLPGMQ QQQQQQQQQQ QQQQQQQQQQ QQQQQPQQPQ 

       250        260        270        280        290        300 
QQAQAQPQQQ QQQQQQPALV SYNRPSGPGQ ELLLSGQSAP QKLSAPAPSG RPSPAPQAAV 

       310        320        330        340        350        360 
QPTATAVPGP SVQQPAPGQP SPVLQLQQKQ SRISPIQKPQ GLDPVEILQE REYRLQARIA 

       370        380        390        400        410        420 
HRIQELESLP GSLPPDLRTK ATVELKALRL LNFQRQLRQE VVACMRRDTT LETALNSKAY 

       430        440        450        460        470        480 
KRSKRQTLRE ARMTEKLEKQ QKIEQERKRR QKHQEYLNSI LQHAKDFKEY HRSVAGKIQK 

       490        500        510        520        530        540 
LSKAVATWHA NTEREQKKET ERIEKERMRR LMAEDEEGYR KLIDQKKDRR LAYLLQQTDE 

       550        560        570        580        590        600 
YVANLTNLVW EHKQAQAAKE KKKRRRRKKK AEENAEGGEP ALGPDGEPID ESSQMSDLPV 

       610        620        630        640        650        660 
KVTHTETGKV LFGPEAPKAS QLDAWLEMNP GYEVAPRSDS EESESDYEEE DEEEESSRQE 

       670        680        690        700        710        720 
TEEKILLDPN SEEVSEKDAK QIIETAKQDV DDEYSMQYSA RGSQSYYTVA HAISERVEKQ 

       730        740        750        760        770        780 
SALLINGTLK HYQLQGLEWM VSLYNNNLNG ILADEMGLGK TIQTIALITY LMEHKRLNGP 

       790        800        810        820        830        840 
YLIIVPLSTL SNWTYEFDKW APSVVKISYK GTPAMRRSLV PQLRSGKFNV LLTTYEYIIK 

       850        860        870        880        890        900 
DKHILAKIRW KYMIVDEGHR MKNHHCKLTQ VLNTHYVAPR RILLTGTPLQ NKLPELWALL 

       910        920        930        940        950        960 
NFLLPTIFKS CSTFEQWFNA PFAMTGERVD LNEEETILII RRLHKVLRPF LLRRLKKEVE 

       970        980        990       1000       1010       1020 
SQLPEKVEYV IKCDMSALQK ILYRHMQAKG ILLTDGSEKD KKGKGGAKTL MNTIMQLRKI 

      1030       1040       1050       1060       1070       1080 
CNHPYMFQHI EESFAEHLGY SNGVINGAEL YRASGKFELL DRILPKLRAT NHRVLLFCQM 

      1090       1100       1110       1120       1130       1140 
TSLMTIMEDY FAFRNFLYLR LDGTTKSEDR AALLKKFNEP GSQYFIFLLS TRAGGLGLNL 

      1150       1160       1170       1180       1190       1200 
QAADTVVIFD SDWNPHQDLQ AQDRAHRIGQ QNEVRVLRLC TVNSVEEKIL AAAKYKLNVD 

      1210       1220       1230       1240       1250       1260 
QKVIQAGMFD QKSSSHERRA FLQAILEHEE ENEEEDEVPD DETLNQMIAR REEEFDLFMR 

      1270       1280       1290       1300       1310       1320 
MDMDRRREDA RNPKRKPRLM EEDELPSWII KDDAEVERLT CEEEEEKIFG RGSRQRRDVD 

      1330       1340       1350       1360       1370       1380 
YSDALTEKQW LRAIEDGNLE EMEEEVRLKK RKRRRNVDKD PVKEDVEKAK KRRGRPPAEK 

      1390       1400       1410       1420       1430       1440 
LSPNPPKLTK QMNAIIDTVI NYKDSSGRQL SEVFIQLPSR KDLPEYYELI RKPVDFKKIK 

      1450       1460       1470       1480       1490       1500 
ERIRNHKYRS LGDLEKDVML LCHNAQTFNL EGSQIYEDSI VLQSVFKSAR QKIAKEEESE 

      1510       1520       1530       1540       1550       1560 
EESNEEEEED DEEESESEAK SVKVKIKLNK KEEKGRDTGK GKKRPNRGKA KPVVSDFDSD 

      1570 
EEQEENEQSE ASGTDNE 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: C57BL/6.
Tissue: Brain.
[2]"An essential switch in subunit composition of a chromatin remodeling complex during neural development."
Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H., Aebersold R., Graef I.A., Crabtree G.R.
Neuron 55:201-215(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, INTERACTION WITH PHF10.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-1499 AND SER-1503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Heterozygous missense mutations in SMARCA2 cause Nicolaides-Baraitser syndrome."
Van Houdt J.K., Nowakowska B.A., Sousa S.B., van Schaik B.D., Seuntjens E., Avonce N., Sifrim A., Abdul-Rahman O.A., van den Boogaard M.J., Bottani A., Castori M., Cormier-Daire V., Deardorff M.A., Filges I., Fryer A., Fryns J.P., Gana S., Garavelli L. expand/collapse author list , Gillessen-Kaesbach G., Hall B.D., Horn D., Huylebroeck D., Klapecki J., Krajewska-Walasek M., Kuechler A., Lines M.A., Maas S., Macdermot K.D., McKee S., Magee A., de Man S.A., Moreau Y., Morice-Picard F., Obersztyn E., Pilch J., Rosser E., Shannon N., Stolte-Dijkstra I., Van Dijck P., Vilain C., Vogels A., Wakeling E., Wieczorek D., Wilson L., Zuffardi O., van Kampen A.H., Devriendt K., Hennekam R., Vermeesch J.R.
Nat. Genet. 44:445-449(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC075641 mRNA. Translation: AAH75641.1.
RefSeqNP_035546.2. NM_011416.2.
UniGeneMm.491146.

3D structure databases

ProteinModelPortalQ6DIC0.
SMRQ6DIC0. Positions 670-1207, 1383-1491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211982. 34 interactions.
DIPDIP-48888N.

PTM databases

PhosphoSiteQ6DIC0.

Proteomic databases

MaxQBQ6DIC0.
PaxDbQ6DIC0.
PRIDEQ6DIC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID67155.
KEGGmmu:67155.
UCSCuc012bjw.1. mouse.

Organism-specific databases

CTD6595.
MGIMGI:99603. Smarca2.

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000172363.
HOVERGENHBG056636.
InParanoidQ6DIC0.
KOK11647.
PhylomeDBQ6DIC0.

Gene expression databases

ArrayExpressQ6DIC0.
BgeeQ6DIC0.
GenevestigatorQ6DIC0.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
SM00951. QLQ. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS51666. QLQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMARCA2. mouse.
NextBio323746.
PROQ6DIC0.
SOURCESearch...

Entry information

Entry nameSMCA2_MOUSE
AccessionPrimary (citable) accession number: Q6DIC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: August 16, 2004
Last modified: June 11, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot