O54941 (SMCE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Smarce1
Synonyms:	Baf57

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). 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.4 Ref.5 Ref.6
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/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. 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 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. Ref.6
Subcellular location	Nucleus By similarity.
Developmental stage	Expressed ubiquitously throughout the developing spinal cord, brain and other embryonic tissues at E10.5-E16.5. Ref.6
Domain	The HMG domain is essential for CD4 silencing and CD8 activation; mutation of this domain blocks thymus development.
Post-translational modification	Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ubiquitination is prevented upon interaction between TRIP12 and SMARCC1 By similarity.
Sequence similarities	Contains 1 HMG box DNA-binding domain.
Sequence caution	The sequence BAC36233.1 differs from that shown. Reason: Erroneous termination at position 408. Translated as Glu. The sequence BAC36233.1 differs from that shown. Reason: Frameshift at positions 184, 212, 255, 316 and 353. The sequence BAC36233.1 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
Biological process	Neurogenesis
Cellular component	Nucleus
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	Chromatin regulator
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara nervous system development Inferred from electronic annotation. Source: UniProtKB-KW nucleosome disassembly Inferred from electronic annotation. Source: Compara
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 16287714. Source: MGI nBAF complex Inferred from direct assay Ref.6. Source: UniProtKB npBAF complex Inferred from direct assay Ref.6. Source: UniProtKB transcriptional repressor complex Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyltransferase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 411	411	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1		PRO_0000048578
Regions
	DNA binding	66 – 134	69	HMG box
	Coiled coil	222 – 319	98	Potential
	Compositional bias	320 – 411	92	Glu-rich
Amino acid modifications
	Modified residue	265	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O54941 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 4099B333A0B63709	FASTA	411	46,638
	10 20 30 40 50 60 MSKRPSYAPP PTPAPATQMP STPGFVGYNP YSHLAYNNYR LGGNPGTNSR VTASSGITIP 70 80 90 100 110 120 KPPKPPDKPL MPYMRYSRKV WDQVKASNPD LKLWEIGKII GGMWRDLTDE EKQEYLNEYE 130 140 150 160 170 180 AEKIEYNESM KAYHNSPAYL AYINAKSRAE AALEEESRQR QSRMEKGEPY MSIQPAEDPD 190 200 210 220 230 240 DYDDGFSMKH TATARFQRNH RLISEILSES VVPDVRSVVT TARMQVLKRQ VQSLMVHQRK 250 260 270 280 290 300 LEAELLQIEE RHQEKKRKFL ESTDSFNNEL KRLCGLKVEV DMEKIAAEIA QAEEQARKRQ 310 320 330 340 350 360 EEREKEAAEQ AERSQSSMAP EEEQVANKAE EKKDEESIPM ETEETHLEDT AESQQNGEEG 370 380 390 400 410 TSTPEDKESG QEGVDSMEVE GTSDSNTGSE SNSATVEEPP TDPVPEDEKK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00119892.
RefSeq	NP_065643.1. NM_020618.4.
UniGene	Mm.379086. Mm.389717.
3D structure databases
ProteinModelPortal	O54941.
SMR	O54941. Positions 66-139.
ModBase	Search...
Protein-protein interaction databases
IntAct	O54941. 7 interactions.
PTM databases
PhosphoSite	O54941.
Proteomic databases
PaxDb	O54941.
PRIDE	O54941.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000103133; ENSMUSP00000099422; ENSMUSG00000037935.
GeneID	57376.
KEGG	mmu:57376.
Organism-specific databases
CTD	6605.
MGI	MGI:1927347. Smarce1.
Phylogenomic databases
eggNOG	NOG291422.
GeneTree	ENSGT00390000003628.
HOGENOM	HOG000230965.
HOVERGEN	HBG054558.
InParanoid	O54941.
KO	K11651.
OMA	EDESIPM.
OrthoDB	EOG4229K4.
Gene expression databases
ArrayExpress	O54941.
Bgee	O54941.
Genevestigator	O54941.
GermOnline	ENSMUSG00000037935. Mus musculus.
Family and domain databases
Gene3D	1.10.30.10. 1 hit.
InterPro	IPR009071. HMG_box_dom. [Graphical view]
Pfam	PF00505. HMG_box. 1 hit. [Graphical view]
SMART	SM00398. HMG. 1 hit. [Graphical view]
SUPFAM	SSF47095. HMG-box. 1 hit.
PROSITE	PS00353. HMG_BOX_1. False negative. PS50118. HMG_BOX_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SMARCE1. mouse.
NextBio	313752.
SOURCE	Search...

Entry information

Entry name

SMCE1_MOUSE

Accession

Primary (citable) accession number: O54941
Secondary accession number(s): Q8BPD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2004
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program