Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51531 (SMCA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Short name=hBRM
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1590 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. 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.5

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. 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 By similarity. Ref.5 Ref.6 Ref.9

Subcellular location

Nucleus.

Involvement in disease

Nicolaides-Baraitser syndrome (NCBRS) [MIM:601358]: A rare disorder characterized by severe mental retardation with absent or limited speech, seizures, short stature, sparse hair, typical facial characteristics, brachydactyly, prominent finger joints and broad distal phalanges. Some of the features are progressive with time.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.18

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
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hypotrichosis
Mental retardation
   DomainBromodomain
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionActivator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement PubMed 17938176. Source: GOC

aortic smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Traceable author statement PubMed 17938176. Source: BHF-UCL

negative regulation of cell growth

Inferred from mutant phenotype PubMed 12065415. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 17938176. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12065415. Source: BHF-UCL

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15774904. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17984088. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription, DNA-templated

Traceable author statement PubMed 8670841. Source: ProtInc

   Cellular_componentSWI/SNF complex

Inferred from direct assay PubMed 11078522. Source: UniProtKB

WINAC complex

Inferred from direct assay Ref.5. Source: BHF-UCL

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

npBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 12065415. Source: BHF-UCL

nucleoplasm

Traceable author statement PubMed 8670841. Source: ProtInc

nucleus

Inferred from direct assay PubMed 17984088. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Traceable author statement PubMed 17938176. Source: BHF-UCL

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 17984088. Source: UniProtKB

helicase activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17984088. Source: UniProtKB

Complete GO annotation...

Binary interactions

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

Domain173 – 20836QLQ
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 residue1751Phosphoserine Ref.10 Ref.14
Modified residue3291Phosphoserine Ref.7 Ref.14
Modified residue6041N6-acetyllysine By similarity
Modified residue9971N6-acetyllysine Ref.13
Modified residue9991N6-acetyllysine Ref.13
Modified residue15121Phosphoserine Ref.10 Ref.12
Modified residue15161Phosphoserine Ref.10 Ref.12
Modified residue15281Phosphoserine Ref.10
Modified residue15681Phosphoserine Ref.7 Ref.11 Ref.14
Modified residue15721Phosphoserine Ref.7 Ref.11 Ref.14

Natural variations

Alternative sequence1400 – 141718Missing in isoform Short.
VSP_000577
Natural variant7521G → A in NCBRS. Ref.18
Corresponds to variant rs281875198 [ dbSNP | Ensembl ].
VAR_068180
Natural variant7551K → R in NCBRS. Ref.18
Corresponds to variant rs281875203 [ dbSNP | Ensembl ].
VAR_068181
Natural variant7561T → I in NCBRS. Ref.18
Corresponds to variant rs281875191 [ dbSNP | Ensembl ].
VAR_068182
Natural variant8511D → H in NCBRS. Ref.18
Corresponds to variant rs281875206 [ dbSNP | Ensembl ].
VAR_068183
Natural variant8521E → D in NCBRS. Ref.18
Corresponds to variant rs281875193 [ dbSNP | Ensembl ].
VAR_068184
Natural variant8521E → K in NCBRS. Ref.18
Corresponds to variant rs281875199 [ dbSNP | Ensembl ].
VAR_068185
Natural variant8541H → N in NCBRS. Ref.18
VAR_068186
Natural variant8541H → R in NCBRS. Ref.18
Corresponds to variant rs281875202 [ dbSNP | Ensembl ].
VAR_068187
Natural variant8551R → G in NCBRS. Ref.18
Corresponds to variant rs281875207 [ dbSNP | Ensembl ].
VAR_068188
Natural variant8811G → R in NCBRS. Ref.18
Corresponds to variant rs281875194 [ dbSNP | Ensembl ].
VAR_068189
Natural variant8811G → V in NCBRS. Ref.18
Corresponds to variant rs281875185 [ dbSNP | Ensembl ].
VAR_068190
Natural variant8831P → L in NCBRS. Ref.18
Corresponds to variant rs281875188 [ dbSNP | Ensembl ].
VAR_068191
Natural variant9391H → Y in NCBRS. Ref.18
Corresponds to variant rs281875190 [ dbSNP | Ensembl ].
VAR_068192
Natural variant9461L → F in NCBRS. Ref.18
Corresponds to variant rs281875205 [ dbSNP | Ensembl ].
VAR_068193
Natural variant9461L → S in NCBRS. Ref.18
Corresponds to variant rs281875200 [ dbSNP | Ensembl ].
VAR_068194
Natural variant11051R → C in NCBRS. Ref.18
Corresponds to variant rs281875192 [ dbSNP | Ensembl ].
VAR_068195
Natural variant11051R → P in NCBRS. Ref.18
Corresponds to variant rs281875197 [ dbSNP | Ensembl ].
VAR_068196
Natural variant11351L → P in NCBRS. Ref.18
Corresponds to variant rs281875195 [ dbSNP | Ensembl ].
VAR_068197
Natural variant11461S → R in NCBRS. Ref.18
Corresponds to variant rs281875204 [ dbSNP | Ensembl ].
VAR_068198
Natural variant11581D → V in NCBRS. Ref.18
Corresponds to variant rs281875240 [ dbSNP | Ensembl ].
VAR_068199
Natural variant11591R → G in NCBRS. Ref.18
Corresponds to variant rs281875184 [ dbSNP | Ensembl ].
VAR_068200
Natural variant11591R → L in NCBRS. Ref.18
Corresponds to variant rs281875187 [ dbSNP | Ensembl ].
VAR_068201
Natural variant11591R → Q in NCBRS. Ref.18
Corresponds to variant rs281875187 [ dbSNP | Ensembl ].
VAR_068202
Natural variant11621R → H in NCBRS. Ref.18
Corresponds to variant rs281875186 [ dbSNP | Ensembl ].
VAR_068203
Natural variant11881A → P in NCBRS. Ref.18
Corresponds to variant rs281875196 [ dbSNP | Ensembl ].
VAR_068204
Natural variant12011A → V in NCBRS. Ref.18
Corresponds to variant rs281875189 [ dbSNP | Ensembl ].
VAR_068205
Natural variant12021G → C in NCBRS. Ref.18
Corresponds to variant rs281875239 [ dbSNP | Ensembl ].
VAR_068206
Natural variant12051D → G in NCBRS. Ref.18
Corresponds to variant rs281875201 [ dbSNP | Ensembl ].
VAR_068207
Natural variant12131R → W in NCBRS. Ref.18
Corresponds to variant rs281875238 [ dbSNP | Ensembl ].
VAR_068208
Natural variant14161G → A.
Corresponds to variant rs3793510 [ dbSNP | Ensembl ].
VAR_049501
Natural variant15461D → E.
Corresponds to variant rs2296212 [ dbSNP | Ensembl ].
VAR_049502

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

Secondary structure

.................. 1590
Helix Strand Turn

Details...

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 »

FASTA1,572179,281

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"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.
[6]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOPBP1.
[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-329; SER-1568 AND SER-1572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"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.
[10]"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-175; SER-1512; SER-1516 AND SER-1528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"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-1512 AND SER-1516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-997 AND LYS-999, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-175; SER-329; SER-1568 AND SER-1572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"Mutations affecting components of the SWI/SNF complex cause Coffin-Siris syndrome."
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S. expand/collapse author list , Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.
Nat. Genet. 44:376-378(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN NCBRS.
[17]"Solution structure of the bromodomain of human SWI/SNF related matrix associated actin dependent regulator of chromatin subfamily A member 2."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1377-1486.
[18]"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: VARIANTS NCBRS ALA-752; ARG-755; ILE-756; HIS-851; ASP-852; LYS-852; ARG-854; ASN-854; GLY-855; ARG-881; VAL-881; LEU-883; TYR-939; SER-946; PHE-946; CYS-1105; PRO-1105; PRO-1135; ARG-1146; VAL-1158; GLY-1159; LEU-1159; GLN-1159; HIS-1162; PRO-1188; VAL-1201; CYS-1202; GLY-1205 AND TRP-1213.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CH471071 Genomic DNA. Translation: EAW58814.1.
CH471071 Genomic DNA. Translation: EAW58815.1.
PIRS39580.
S45251.
RefSeqNP_003061.3. NM_003070.4.
NP_620614.2. NM_139045.3.
UniGeneHs.298990.
Hs.644901.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DATNMR-A1377-1504[»]
ProteinModelPortalP51531.
SMRP51531. Positions 441-507, 665-1249, 1378-1504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112479. 94 interactions.
DIPDIP-29005N.
IntActP51531. 23 interactions.
MINTMINT-1898892.
STRING9606.ENSP00000265773.

Chemistry

ChEMBLCHEMBL2362979.

PTM databases

PhosphoSiteP51531.

Polymorphism databases

DMDM212276472.

Proteomic databases

PaxDbP51531.
PRIDEP51531.

Protocols and materials databases

DNASU6595.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349721; ENSP00000265773; ENSG00000080503. [P51531-1]
ENST00000357248; ENSP00000349788; ENSG00000080503. [P51531-2]
ENST00000382194; ENSP00000371629; ENSG00000080503. [P51531-2]
ENST00000382203; ENSP00000371638; ENSG00000080503. [P51531-1]
GeneID6595.
KEGGhsa:6595.
UCSCuc003zhc.3. human. [P51531-1]
uc003zhd.3. human. [P51531-2]

Organism-specific databases

CTD6595.
GeneCardsGC09P002005.
HGNCHGNC:11098. SMARCA2.
HPACAB037276.
HPA029981.
MIM600014. gene.
601358. phenotype.
neXtProtNX_P51531.
Orphanet3051. Intellectual deficit - sparse hair - brachydactyly.
PharmGKBPA35948.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000172363.
HOVERGENHBG056636.
InParanoidP51531.
KOK11647.
OMAINYKDRC.
PhylomeDBP51531.
TreeFamTF300785.

Gene expression databases

ArrayExpressP51531.
BgeeP51531.
CleanExHS_SMARCA2.
GenevestigatorP51531.

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.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 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. human.
EvolutionaryTraceP51531.
GeneWikiSMARCA2.
GenomeRNAi6595.
NextBio25649.
PMAP-CutDBP51531.
PROP51531.
SOURCESearch...

Entry information

Entry nameSMCA2_HUMAN
AccessionPrimary (citable) accession number: P51531
Secondary accession number(s): B1ALG3 expand/collapse secondary AC list , B1ALG4, D3DRH4, D3DRH5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 151 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM