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Protein

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1

Gene

Smarce1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the coactivation of estrogen responsive promoters by Swi/Snf complexes and the SRC/p160 family of histone acetyltransferases (HATs). 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 similarity3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi66 – 13469HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: GO_Central
  2. ligand-dependent nuclear receptor binding Source: MGI
  3. N-acetyltransferase activity Source: MGI
  4. protein N-terminus binding Source: MGI
  5. RNA binding Source: MGI
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  7. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: MGI
  2. chromatin remodeling Source: MGI
  3. metabolic process Source: MGI
  4. negative regulation of transcription, DNA-templated Source: MGI
  5. nervous system development Source: UniProtKB-KW
  6. nucleosome disassembly Source: MGI
  7. regulation of transcription, DNA-templated Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_244207. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
Alternative name(s):
BRG1-associated factor 57
Short name:
BAF57
Gene namesi
Name:Smarce1
Synonyms:Baf57
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1927347. Smarce1.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. BAF-type complex Source: MGI
  2. nBAF complex Source: UniProtKB
  3. npBAF complex Source: UniProtKB
  4. nuclear chromatin Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: MGI
  7. protein complex Source: MGI
  8. SWI/SNF complex Source: MGI
  9. transcriptional repressor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1PRO_0000048578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ubiquitination is prevented upon interaction between TRIP12 and SMARCC1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO54941.
PaxDbiO54941.
PRIDEiO54941.

PTM databases

PhosphoSiteiO54941.

Expressioni

Developmental stagei

Expressed ubiquitously throughout the developing spinal cord, brain and other embryonic tissues at E10.5-E16.5.1 Publication

Gene expression databases

BgeeiO54941.
ExpressionAtlasiO54941. baseline and differential.
GenevestigatoriO54941.

Interactioni

Subunit structurei

Component of a number of multiprotein chromatin-remodeling complexes: Swi/Snf-A (BAF), Swi/Snf-B (PBAF), Brm, Brg1(I) and Brg1(II). Each of the complexes 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/INI1). 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/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. Also binds to the SRC/p160 family of histone acetyltransferases (HATs) composed of NCOA1, NCOA2, and NCOA3. NCOA3. Interacts with RCOR1/CoREST, NR3C1 and ZMIM2/ZIMP7. Interacts with BRDT (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.By similarity1 Publication

Protein-protein interaction databases

BioGridi208275. 19 interactions.
DIPiDIP-39985N.
IntActiO54941. 9 interactions.
MINTiMINT-1676035.

Structurei

3D structure databases

ProteinModelPortaliO54941.
SMRiO54941. Positions 66-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili222 – 31998Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi320 – 41192Glu-richAdd
BLAST

Domaini

The HMG domain is essential for CD4 silencing and CD8 activation; mutation of this domain blocks thymus development.

Sequence similaritiesi

Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG291422.
GeneTreeiENSGT00390000003628.
HOGENOMiHOG000230965.
HOVERGENiHBG054558.
InParanoidiO54941.
KOiK11651.
OMAiSSMVPEE.
OrthoDBiEOG7NKKKX.
PhylomeDBiO54941.
TreeFamiTF321146.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR030089. BAF57.
IPR009071. HMG_box_dom.
[Graphical view]
PANTHERiPTHR13711:SF150. PTHR13711:SF150. 1 hit.
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRPSYAPP PTPAPATQMP STPGFVGYNP YSHLAYNNYR LGGNPGTNSR
60 70 80 90 100
VTASSGITIP KPPKPPDKPL MPYMRYSRKV WDQVKASNPD LKLWEIGKII
110 120 130 140 150
GGMWRDLTDE EKQEYLNEYE AEKIEYNESM KAYHNSPAYL AYINAKSRAE
160 170 180 190 200
AALEEESRQR QSRMEKGEPY MSIQPAEDPD DYDDGFSMKH TATARFQRNH
210 220 230 240 250
RLISEILSES VVPDVRSVVT TARMQVLKRQ VQSLMVHQRK LEAELLQIEE
260 270 280 290 300
RHQEKKRKFL ESTDSFNNEL KRLCGLKVEV DMEKIAAEIA QAEEQARKRQ
310 320 330 340 350
EEREKEAAEQ AERSQSSMAP EEEQVANKAE EKKDEESIPM ETEETHLEDT
360 370 380 390 400
AESQQNGEEG TSTPEDKESG QEGVDSMEVE GTSDSNTGSE SNSATVEEPP
410
TDPVPEDEKK E
Length:411
Mass (Da):46,638
Last modified:June 1, 1998 - v1
Checksum:i4099B333A0B63709
GO

Sequence cautioni

The sequence BAC36233.1 differs from that shown.Sequencing errors.Curated
The sequence BAC36233.1 differs from that shown. Reason: Frameshift at positions 184, 212, 255, 316 and 353. Curated
The sequence BAC36233.1 differs from that shown. Reason: Erroneous termination at position 408. Translated as Glu.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035263 Genomic DNA. Translation: AAC04510.1.
AK076177 mRNA. Translation: BAC36233.1. Sequence problems.
BC047141 mRNA. Translation: AAH47141.1.
BC061498 mRNA. Translation: AAH61498.1.
BC065043 mRNA. Translation: AAH65043.1.
CCDSiCCDS25374.1.
RefSeqiNP_065643.1. NM_020618.4.
UniGeneiMm.379086.
Mm.389717.

Genome annotation databases

EnsembliENSMUST00000103133; ENSMUSP00000099422; ENSMUSG00000037935.
GeneIDi57376.
KEGGimmu:57376.
UCSCiuc007lii.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035263 Genomic DNA. Translation: AAC04510.1.
AK076177 mRNA. Translation: BAC36233.1. Sequence problems.
BC047141 mRNA. Translation: AAH47141.1.
BC061498 mRNA. Translation: AAH61498.1.
BC065043 mRNA. Translation: AAH65043.1.
CCDSiCCDS25374.1.
RefSeqiNP_065643.1. NM_020618.4.
UniGeneiMm.379086.
Mm.389717.

3D structure databases

ProteinModelPortaliO54941.
SMRiO54941. Positions 66-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208275. 19 interactions.
DIPiDIP-39985N.
IntActiO54941. 9 interactions.
MINTiMINT-1676035.

PTM databases

PhosphoSiteiO54941.

Proteomic databases

MaxQBiO54941.
PaxDbiO54941.
PRIDEiO54941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103133; ENSMUSP00000099422; ENSMUSG00000037935.
GeneIDi57376.
KEGGimmu:57376.
UCSCiuc007lii.1. mouse.

Organism-specific databases

CTDi6605.
MGIiMGI:1927347. Smarce1.

Phylogenomic databases

eggNOGiNOG291422.
GeneTreeiENSGT00390000003628.
HOGENOMiHOG000230965.
HOVERGENiHBG054558.
InParanoidiO54941.
KOiK11651.
OMAiSSMVPEE.
OrthoDBiEOG7NKKKX.
PhylomeDBiO54941.
TreeFamiTF321146.

Enzyme and pathway databases

ReactomeiREACT_244207. RMTs methylate histone arginines.

Miscellaneous databases

NextBioi313752.
PROiO54941.
SOURCEiSearch...

Gene expression databases

BgeeiO54941.
ExpressionAtlasiO54941. baseline and differential.
GenevestigatoriO54941.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR030089. BAF57.
IPR009071. HMG_box_dom.
[Graphical view]
PANTHERiPTHR13711:SF150. PTHR13711:SF150. 1 hit.
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Architectural DNA binding by a high-mobility-group/kinesin-like subunit in mammalian SWI/SNF-related complexes."
    Wang W., Chi T., Xue Y., Zhou S., Kuo A., Crabtree G.R.
    Proc. Natl. Acad. Sci. U.S.A. 95:492-498(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "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 and FVB/N.
    Tissue: Brain, Colon and Mammary tumor.
  4. "Targeting of SWI/SNF chromatin remodelling complexes to estrogen-responsive genes."
    Belandia B., Orford R.L., Hurst H.C., Parker M.G.
    EMBO J. 21:4094-4103(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF complexes."
    Chi T.H., Wan M., Zhao K., Taniuchi I., Chen L., Littman D.R., Crabtree G.R.
    Nature 418:195-199(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiSMCE1_MOUSE
AccessioniPrimary (citable) accession number: O54941
Secondary accession number(s): Q8BPD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: June 1, 1998
Last modified: March 4, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.