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Reviewed, UniProtKB/Swiss-Prot P51531 (SMCA2_HUMAN)

Last modified November 25, 2008. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable global transcription activator SNF2L2
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent helicase SMARCA2
    SNF2-alpha
    SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
      Short name=hBRM
Gene names
Name: SMARCA2
Synonyms: BRM, SNF2A, SNF2L2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1590 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation.

Subunit structure

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. Binds TOPBP1.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

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.

Ontologies

Keywords

   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processregulation of transcription from RNA polymerase II promoter Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentSWI/SNF complex

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: InterPro

helicase activity Ref.1

Traceable author statement. Source: ProtInc

transcription coactivator activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P51531-1)

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 Short (identifier: P51531-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1400-1417: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15901590Probable global transcription activator SNF2L2
PRO_0000074352

Regions

Domain436 – 50873HSA
Domain736 – 901166Helicase ATP-binding
Domain1054 – 1216163Helicase C-terminal
Domain1419 – 148971Bromo
Nucleotide binding749 – 7568ATP Potential
Motif851 – 8544DEGH box
Compositional bias216 – 23823Poly-Gln
Compositional bias245 – 2539Poly-Gln
Compositional bias559 – 5624Poly-Arg
Compositional bias643 – 6508Poly-Glu
Compositional bias1297 – 13015Poly-Glu
Compositional bias1518 – 152912Poly-Glu

Amino acid modifications

Modified residue3291Phosphoserine
Modified residue5911Phosphoserine
Modified residue9561Phosphoserine
Modified residue13771Phosphoserine
Modified residue14101Phosphoserine
Modified residue14181Phosphoserine
Modified residue14191Phosphoserine
Modified residue15511N6-acetyllysine
Modified residue15531N6-acetyllysine
Modified residue15551N6-acetyllysine
Modified residue15681Phosphoserine
Modified residue15721Phosphoserine

Natural variations

Alternative sequence1400 – 141718Missing in isoform Short.
VSP_000577

Experimental info

Sequence conflict237 – 2404Missing in CAA51407. Ref.1
Sequence conflict3941Q → E in BAA05142. Ref.2
Sequence conflict5131G → S in BAA05142. Ref.2
Sequence conflict7111R → W in CAA51407. Ref.1
Sequence conflict11391D → H in BAA05142. Ref.2
Sequence conflict13941V → C in CAA51407. Ref.1
Sequence conflict14001R → S in CAA51407. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: CE69BBB287D35AB5

FASTA1,590181,279
        10         20         30         40         50         60 
MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM 

        70         80         90        100        110        120 
GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY 

       130        140        150        160        170        180 
MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH 

       190        200        210        220        230        240 
QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ 

       250        260        270        280        290        300 
QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA 

       310        320        330        340        350        360 
AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE 

       370        380        390        400        410        420 
LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR 

       430        440        450        460        470        480 
QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV 

       490        500        510        520        530        540 
ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL 

       550        560        570        580        590        600 
TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT 

       610        620        630        640        650        660 
ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI 

       670        680        690        700        710        720 
LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI 

       730        740        750        760        770        780 
NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV 

       790        800        810        820        830        840 
PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL 

       850        860        870        880        890        900 
AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP 

       910        920        930        940        950        960 
TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE 

       970        980        990       1000       1010       1020 
KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY 

      1030       1040       1050       1060       1070       1080 
MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT 

      1090       1100       1110       1120       1130       1140 
IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT 

      1150       1160       1170       1180       1190       1200 
VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ 

      1210       1220       1230       1240       1250       1260 
AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR 

      1270       1280       1290       1300       1310       1320 
RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL 

      1330       1340       1350       1360       1370       1380 
TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP 

      1390       1400       1410       1420       1430       1440 
PKLTKQMNAI IDTVINYKDR CNVEKVPSNS QLEIEGNSSG RQLSEVFIQL PSRKELPEYY 

      1450       1460       1470       1480       1490       1500 
ELIRKPVDFK KIKERIRNHK YRSLGDLEKD VMLLCHNAQT FNLEGSQIYE DSIVLQSVFK 

      1510       1520       1530       1540       1550       1560 
SARQKIAKEE ESEDESNEEE EEEDEEESES EAKSVKVKIK LNKKDDKGRD KGKGKKRPNR 

      1570       1580       1590 
GKAKPVVSDF DSDEEQDERE QSEGSGTDDE 

« Hide

Isoform Short [UniParc].

Checksum: BBD4488C2861C270
Show »

1,572179,281

References

« Hide 'large scale' references
[1]"A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor."
Muchardt C., Yaniv M.
EMBO J. 12:4279-4290(1993) [PubMed: 8223438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Liver.
[2]"Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor."
Chiba H., Muramatsu M., Nomoto A., Kato H.
Nucleic Acids Res. 22:1815-1820(1994) [PubMed: 8208605] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Brain.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival."
Liu K., Luo Y., Lin F.-T., Lin W.-C.
Genes Dev. 18:673-686(2004) [PubMed: 15075294] [Abstract]
Cited for: INTERACTION WITH TOPBP1.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, MASS SPECTROMETRY.
Tissue: Hepatocyte.
[8]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-956; SER-1377; SER-1418; SER-1419; SER-1568 AND SER-1572, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1551; LYS-1553 AND LYS-1555, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1410, MASS SPECTROMETRY.
[11]"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: 18765789] [Abstract]
Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

X72889 mRNA. Translation: CAA51407.1.
D26155 mRNA. Translation: BAA05142.1.
AL359076, AL138755 Genomic DNA. Translation: CAI12967.1.
AL359076, AL138755 Genomic DNA. Translation: CAI12968.1.
AL138755, AL359076 Genomic DNA. Translation: CAI14599.1.
AL138755, AL359076 Genomic DNA. Translation: CAI14600.1.
CH471071 Genomic DNA. Translation: EAW58811.1.
CH471071 Genomic DNA. Translation: EAW58813.1.
PIRS39580.
S45251.
RefSeqNP_003061.3.
UniGeneHs.298990

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2DATNMR-A1377-1486[»]
SMRP51531. Positions 1384-1500.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29005N.
IntActP51531.

PTM databases

PhosphoSiteP51531.