P97496 (SMRC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SWI/SNF complex subunit SMARCC1

Alternative name(s):
BRG1-associated factor 155
SWI/SNF complex 155 kDa subunit
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1
SWI3-related protein
Short name=BAF155

Gene names

Name:	Smarcc1
Synonyms:	Baf155, Srg3

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	1104 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). May stimulate the ATPase activity of the catalytic subunit of the complex. 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.3 Ref.4
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 or SMARCA2), and at least SMARCE1, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCC2 and SMARCB1. 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, 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. May also interact with the SIN3A histone deacetylase transcription repressor complex in conjunction with SMARCA2 and SMARCA4. The minimal complex composed of SMARCC1 and SMARCA4 seems to be able to associate with cyclin such as CCNE1 or transcription factors such as KLF1 or GATA1. 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 NR3C1 and SMARD1. Interacts with TRIP12; leading to disrupt interaction between TRIP12 and SMARCE1 and prevent SMARCE1 ubiquitination 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.4
Subcellular location	Nucleus.
Tissue specificity	Highly expressed in adult brain, testis and thymus.
Developmental stage	Highly expressed in all organs except heart and liver (E12.5 and E14.5). The level of expression gradually diminishes as embryos develop, with expression restricted mostly to the CNS and thymus at E18.5. Expressed ubiquitously throughout the developing spinal cord, brain and other embryonic tissues at E10.5-E16.5. Ref.4
Sequence similarities	Belongs to the SMARCC family. Contains 1 SANT domain. Contains 1 SWIRM domain.
Sequence caution	The sequence AAB42085.1 differs from that shown. Reason: Frameshift at positions 5, 32, 48, 563, 565, 679 and 682.

Ontologies

Keywords
Biological process	Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA packaging Traceable author statement Ref.3. Source: MGI chromatin remodeling Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Inferred from direct assay PubMed 17074803. Source: MGI nervous system development Inferred from electronic annotation. Source: UniProtKB-KW nucleosome disassembly Inferred from electronic annotation. Source: Compara organ morphogenesis Inferred from mutant phenotype Ref.3. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 17074803. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 16287714. Source: MGI WINAC complex Inferred from electronic annotation. Source: Compara XY body Inferred from direct assay PubMed 16787967. Source: UniProtKB nBAF complex Inferred from direct assay Ref.4. Source: UniProtKB npBAF complex Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from direct assay PubMed 17074803. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Smarcb1	Q9Z0H3	5	EBI-648047,EBI-689365

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P97496-1)

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 2 (identifier: P97496-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1074-1104: YPPPPQQQQPPPPADGVPPPPAPGPPASATP → CK

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1104	1104	SWI/SNF complex subunit SMARCC1		PRO_0000197116
Regions
	Domain	448 – 545	98	SWIRM
	Domain	617 – 668	52	SANT
	Coiled coil	909 – 945	37	Potential
	Compositional bias	326 – 333	8	Poly-Pro
	Compositional bias	768 – 862	95	Glu-rich
	Compositional bias	866 – 877	12	Poly-Ala
	Compositional bias	977 – 1104	128	Pro-rich
Amino acid modifications
	Modified residue	300	1	Phosphoserine Ref.7
	Modified residue	309	1	Phosphoserine Ref.6
	Modified residue	327	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	329	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	334	1	Phosphothreonine By similarity
	Modified residue	336	1	Phosphothreonine Ref.6
	Modified residue	344	1	N6-acetyllysine By similarity
	Modified residue	345	1	N6-acetyllysine By similarity
	Modified residue	349	1	Phosphoserine By similarity
	Modified residue	353	1	N6-acetyllysine By similarity
	Modified residue	356	1	Phosphoserine By similarity
	Modified residue	358	1	N6-acetyllysine By similarity
	Modified residue	397	1	Phosphothreonine By similarity
	Modified residue	572	1	Phosphoserine By similarity
	Modified residue	821	1	Phosphoserine By similarity
	Modified residue	824	1	Phosphoserine By similarity
	Modified residue	947	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1074 – 1104	31	YPPPP…ASATP → CK in isoform 2.		VSP_012489
Experimental info
	Sequence conflict	132	1	G → S in AAB42085. Ref.1
	Sequence conflict	468	1	R → G in AAB42085. Ref.1
	Sequence conflict	498	1	R → C in AAB42085. Ref.1
	Sequence conflict	512	1	R → L in AAB42085. Ref.1
	Sequence conflict	883	1	L → P in AAB42085. Ref.1
	Sequence conflict	891	1	I → K in AAH53064. Ref.2
	Sequence conflict	952	1	R → L in AAH52423. Ref.2
	Sequence conflict	984	1	A → R in AAB42085. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 9030545104B90CAF	FASTA	1,104	122,890
	10 20 30 40 50 60 MAATAGGGPG AAAGAVGAGG AAAASGLAVY RRKDGGPASK FWESPDTVSQ LDSVRVWLGK 70 80 90 100 110 120 HYKKYVHADA PTNKTLAGLV VQLLQFQEDA FGKHVTNPAF TKLPAKCFMD FKAGGTLCHI 130 140 150 160 170 180 LGAAYKYKNE QGWRRFDLQN PSRMDRNVEM FMNIEKTLVQ NNCLTRPNIY LIPDIDLKLA 190 200 210 220 230 240 NKLKDIIKRH QGTFTDEKSK ASHHIYPYPS SQEDEEWLRP VMRRDKQVLV HWGFYPDSYD 250 260 270 280 290 300 TWVHSNDVDA EIEDAPIPEK PWKVHVKWIL DTDVFNEWMN EEDYEVDENR KPVSFRQRIS 310 320 330 340 350 360 TKNEEPVRSP ERRDRKASAN SRKRKPSPSP PPPTATESRK KSGKKGQASL YGKRRSQKEE 370 380 390 400 410 420 DEQEDLTKDM EDPTPVPNIE EVVLPKNVNP KKDSENTPVK GGTVADLDEQ DEEAVTTGGK 430 440 450 460 470 480 EDEDPSKGDP SRSVDPGEDN VTEQTNHIII PSYASWFDYN CIHVIERRAL PEFFNGKNKS 490 500 510 520 530 540 KTPEIYLAYR NFMIDTYRLN PQEYLTSTAC RRNLTGDVCA VMRVHAFLEQ WGLVNYQVDP 550 560 570 580 590 600 ESRPMAMGPP PTPHFNVLAD TPSGLVPLHL RSPQVPAAQQ MLNFPEKNKE KPIDLQNFGL 610 620 630 640 650 660 RTDIYSKKTL AKSKGASAGR EWTEQETLLL LEALEMYKDD WNKVSEHVGS RTQDECILHF 670 680 690 700 710 720 LRLPIEDPYL ENSDASLGPL AYQPVPFSQS GNPVMSTVAF LASVVDPRVA SAAAKAALEE 730 740 750 760 770 780 FSRVREEVPL ELVEAHVKKV QEAARASGKV DPTYGLESSC IAGTGPDEPE KLEGSEEEKM 790 800 810 820 830 840 ETDPDGQQPE KAENKVENES DEGDKIQDRE NEKNTEKEQD SDVSEDVKPE EKENEENKEL 850 860 870 880 890 900 TDTCKERESD AGKKKVEHEI SEGNVATAAA AALASAATKA KHLAAVEERK IKSLVALLVE 910 920 930 940 950 960 TQMKKLEIKL RHFEELETIM DREKEALEQQ RQQLLTERQN FHMEQLKYAE LRARQQMEQQ 970 980 990 1000 1010 1020 QQHGQTPQQA HQHTGGPGMA PLGATGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP 1030 1040 1050 1060 1070 1080 GSMMPGQPMP GRMIPAVAAN IHPTGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ 1090 1100 QQPPPPADGV PPPPAPGPPA SATP
	Isoform 2 [UniParc]. Checksum: DC6BDB5CD4C9A296	FASTA	1,075	120,091
	10 20 30 40 50 60 MAATAGGGPG AAAGAVGAGG AAAASGLAVY RRKDGGPASK FWESPDTVSQ LDSVRVWLGK 70 80 90 100 110 120 HYKKYVHADA PTNKTLAGLV VQLLQFQEDA FGKHVTNPAF TKLPAKCFMD FKAGGTLCHI 130 140 150 160 170 180 LGAAYKYKNE QGWRRFDLQN PSRMDRNVEM FMNIEKTLVQ NNCLTRPNIY LIPDIDLKLA 190 200 210 220 230 240 NKLKDIIKRH QGTFTDEKSK ASHHIYPYPS SQEDEEWLRP VMRRDKQVLV HWGFYPDSYD 250 260 270 280 290 300 TWVHSNDVDA EIEDAPIPEK PWKVHVKWIL DTDVFNEWMN EEDYEVDENR KPVSFRQRIS 310 320 330 340 350 360 TKNEEPVRSP ERRDRKASAN SRKRKPSPSP PPPTATESRK KSGKKGQASL YGKRRSQKEE 370 380 390 400 410 420 DEQEDLTKDM EDPTPVPNIE EVVLPKNVNP KKDSENTPVK GGTVADLDEQ DEEAVTTGGK 430 440 450 460 470 480 EDEDPSKGDP SRSVDPGEDN VTEQTNHIII PSYASWFDYN CIHVIERRAL PEFFNGKNKS 490 500 510 520 530 540 KTPEIYLAYR NFMIDTYRLN PQEYLTSTAC RRNLTGDVCA VMRVHAFLEQ WGLVNYQVDP 550 560 570 580 590 600 ESRPMAMGPP PTPHFNVLAD TPSGLVPLHL RSPQVPAAQQ MLNFPEKNKE KPIDLQNFGL 610 620 630 640 650 660 RTDIYSKKTL AKSKGASAGR EWTEQETLLL LEALEMYKDD WNKVSEHVGS RTQDECILHF 670 680 690 700 710 720 LRLPIEDPYL ENSDASLGPL AYQPVPFSQS GNPVMSTVAF LASVVDPRVA SAAAKAALEE 730 740 750 760 770 780 FSRVREEVPL ELVEAHVKKV QEAARASGKV DPTYGLESSC IAGTGPDEPE KLEGSEEEKM 790 800 810 820 830 840 ETDPDGQQPE KAENKVENES DEGDKIQDRE NEKNTEKEQD SDVSEDVKPE EKENEENKEL 850 860 870 880 890 900 TDTCKERESD AGKKKVEHEI SEGNVATAAA AALASAATKA KHLAAVEERK IKSLVALLVE 910 920 930 940 950 960 TQMKKLEIKL RHFEELETIM DREKEALEQQ RQQLLTERQN FHMEQLKYAE LRARQQMEQQ 970 980 990 1000 1010 1020 QQHGQTPQQA HQHTGGPGMA PLGATGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP 1030 1040 1050 1060 1070 GSMMPGQPMP GRMIPAVAAN IHPTGSGPTP PGMPPMPGNI LGPRVPLTAP NGMCK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new mouse gene, SRG3, related to the SWI3 of Saccharomyces cerevisiae, is required for apoptosis induced by glucocorticoids in a thymoma cell line." Jeon S.H., Kang M.G., Kim Y.H., Jin Y.H., Lee C., Chung H.-Y., Kwon H., Park S.D., Seong R.H. J. Exp. Med. 185:1827-1836(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6J.
[2]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-892 (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[3]	"Srg3, a mouse homolog of yeast SWI3, is essential for early embryogenesis and involved in brain development." Kim J.K., Huh S.-O., Choi H., Lee K.-S., Shin D., Lee C., Nam J.-S., Kim H., Chung H., Lee H.W., Park S.D., Seong R.H. Mol. Cell. Biol. 21:7787-7795(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"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.
[5]	"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-327 AND SER-329, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-327; SER-329 AND THR-336, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-327 AND SER-329, MASS SPECTROMETRY. Tissue: Macrophage.
[8]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U85614 mRNA. Translation: AAB42085.1. Frameshift. BC052423 mRNA. Translation: AAH52423.1. BC053064 mRNA. Translation: AAH53064.1.
IPI	IPI00125662. IPI00515361.
PIR	T30967.
RefSeq	NP_033237.2. NM_009211.2.
UniGene	Mm.85410.
3D structure databases
ProteinModelPortal	P97496.
SMR	P97496. Positions 454-538, 606-675.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39986N.
IntAct	P97496. 10 interactions.
MINT	MINT-4084777.
PTM databases
PhosphoSite	P97496.
Proteomic databases
PaxDb	P97496.
PRIDE	P97496.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000088716; ENSMUSP00000086094; ENSMUSG00000032481. ENSMUST00000111969; ENSMUSP00000107600; ENSMUSG00000032481.
GeneID	20588.
KEGG	mmu:20588.
UCSC	uc009rto.1. mouse. uc009rtp.1. mouse.
Organism-specific databases
CTD	6599.
MGI	MGI:1203524. Smarcc1.
Phylogenomic databases
eggNOG	COG5259.
GeneTree	ENSGT00390000018166.
HOGENOM	HOG000047736.
HOVERGEN	HBG054849.
InParanoid	P97496.
KO	K11649.
OMA	YKKYVHA.
OrthoDB	EOG4JHCF5.
Gene expression databases
ArrayExpress	P97496.
Bgee	P97496.
Genevestigator	P97496.
GermOnline	ENSMUSG00000032481. Mus musculus.
Family and domain databases
Gene3D	1.10.10.10. 1 hit. 1.10.10.60. 1 hit.
InterPro	IPR001357. BRCT_dom. IPR000953. Chromo_domain/shadow. IPR009057. Homeodomain-like. IPR001005. SANT/Myb. IPR017884. SANT_dom. IPR007526. SWIRM. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00249. Myb_DNA-binding. 1 hit. PF04433. SWIRM. 1 hit. [Graphical view]
SMART	SM00298. CHROMO. 1 hit. SM00717. SANT. 1 hit. [Graphical view]
SUPFAM	SSF52113. BRCT. 1 hit. SSF46689. Homeodomain_like. 2 hits.
PROSITE	PS51293. SANT. 1 hit. PS50934. SWIRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	298891.
SOURCE	Search...

Entry information

Entry name

SMRC1_MOUSE

Accession

Primary (citable) accession number: P97496
Secondary accession number(s): Q7TS80, Q7TT29

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program