Q969G3 (SMCE1_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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). 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. Required for the coactivation of estrogen responsive promoters by Swi/Snf complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells. 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. Ref.9
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. 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. 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 BRDT By similarity. Ref.6 Ref.9 Ref.14 Ref.15 Ref.16
Subcellular location	Nucleus Ref.6.
Domain	The HMG domain is essential for CD4 silencing and CD8 activation; mutation of this domain blocks thymus development By similarity.
Post-translational modification	Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ubiquitination is prevented upon interaction between TRIP12 and SMARCC1. Ref.17
Involvement in disease	Defects in SMARCE1 may be a cause of Coffin-Siris syndrome, a highly variable disease characterized by mental retardation associated with a broad spectrum of different clinical features.
Sequence similarities	Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
Biological process	Neurogenesis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Mental retardation
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 direct assay PubMed 11726552. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW nucleosome disassembly Inferred from direct assay PubMed 8895581. Source: BHF-UCL regulation of transcription from RNA polymerase II promoter Non-traceable author statement PubMed 8804307. Source: BHF-UCL
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 11078522. Source: UniProtKB nBAF complex Inferred from sequence or structural similarity. Source: UniProtKB npBAF complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear chromosome Traceable author statement Ref.1. Source: ProtInc transcriptional repressor complex Inferred from physical interaction Ref.6. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyltransferase activity Inferred from direct assay Ref.6. Source: UniProtKB chromatin binding Traceable author statement Ref.1. Source: ProtInc transcription coactivator activity Non-traceable author statement PubMed 8804307. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARID2	Q68CP9	4	EBI-455078,EBI-637818
BRMS1	Q9HCU9	2	EBI-455078,EBI-714781
RCOR1	Q9UKL0	4	EBI-455096,EBI-926563

Alternative products

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

Isoform 1 (identifier: Q969G3-1)

Also known as: BAF57;

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: Q969G3-2)

Also known as: BAF57v;

The sequence of this isoform differs from the canonical sequence as follows:
     344-363: ETHLEETTESQQNGEEGTST → KNCQLCPRKTLTSRYTDFPD
     364-411: Missing.

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_0000048577
Regions
	DNA binding	66 – 134	69	HMG box
	Coiled coil	220 – 319	100	Potential
	Compositional bias	5 – 65	61	Pro-rich
	Compositional bias	320 – 411	92	Glu-rich
Amino acid modifications
	Modified residue	265	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	344 – 363	20	ETHLE…EGTST → KNCQLCPRKTLTSRYTDFPD in isoform 2.		VSP_011801
	Alternative sequence	364 – 411	48	Missing in isoform 2.		VSP_011802
	Natural variant	73	1	Y → C Probable disease-associated mutation found in one patient diagnosed with Coffin-Siris syndrome. Ref.18		VAR_068215
Experimental info
	Sequence conflict	46	1	G → S in AAP35840. Ref.2
	Sequence conflict	46	1	G → S in AAH07082. Ref.5
	Sequence conflict	46	1	G → S in AAH11017. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (BAF57) [UniParc]. Last modified October 25, 2004. Version 2. Checksum: 6F1C1B7917BAD506	FASTA	411	46,649
	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 AERSQSSIVP EEEQAANKGE EKKDDENIPM ETEETHLEET TESQQNGEEG 370 380 390 400 410 TSTPEDKESG QEGVDSMAEE GTSDSNTGSE SNSATVEEPP TDPIPEDEKK E
	Isoform 2 (BAF57v) [UniParc]. Checksum: CAADA4121B64578D	FASTA	363	41,780
	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 AERSQSSIVP EEEQAANKGE EKKDDENIPM ETEKNCQLCP RKTLTSRYTD FPD

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], ALTERNATIVE SPLICING (ISOFORM 1).
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hippocampus.
[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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 1). Tissue: Brain and Testis.
[6]	"REST repression of neuronal genes requires components of the hSWI.SNF complex." Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G., Rosenfeld M.G., Anderson M.E., Mandel G. J. Biol. Chem. 277:41038-41045(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH RCOR1.
[7]	"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: CHARACTERIZATION.
[8]	"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: CHARACTERIZATION.
[9]	"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.
[10]	"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-265, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"Recent advances in understanding chromatin remodeling by SWI/SNF complexes." Martens J.A., Winston F. Curr. Opin. Genet. Dev. 13:136-142(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SWI/SNF CHROMATIN REMODELING COMPLEXES.
[14]	"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation." Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K. Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR3C1.
[15]	"hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated transcription and interacts with SWI/SNF-like BAF complexes." Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z. Mol. Endocrinol. 19:2915-2929(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZMIM2.
[16]	"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.
[17]	"Ubiquitin-dependent and ubiquitin-independent control of subunit stoichiometry in the SWI/SNF complex." Keppler B.R., Archer T.K. J. Biol. Chem. 285:35665-35674(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[18]	"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. , 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: VARIANT CYS-73, POSSIBLE INVOLVEMENT IN COFFIN-SIRIS SYNDROME.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF035262 Genomic DNA. Translation: AAC04509.1. BT007176 mRNA. Translation: AAP35840.1. AK001532 mRNA. Translation: BAG50933.1. AK095047 mRNA. Translation: BAG52975.1. CH471152 Genomic DNA. Translation: EAW60670.1. BC007082 mRNA. Translation: AAH07082.1. BC011017 mRNA. Translation: AAH11017.1. BC063700 mRNA. Translation: AAH63700.1.
IPI	IPI00017669. IPI01018063.
RefSeq	NP_003070.3. NM_003079.4.
UniGene	Hs.740388.
3D structure databases
ProteinModelPortal	Q969G3.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27614N. DIP-33041N.
IntAct	Q969G3. 19 interactions.
MINT	MINT-1137973.
STRING	9606.ENSP00000323967.
PTM databases
PhosphoSite	Q969G3.
Polymorphism databases
DMDM	61247587.
Proteomic databases
PaxDb	Q969G3.
PRIDE	Q969G3.
Protocols and materials databases
DNASU	6605.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000348513; ENSP00000323967; ENSG00000073584.
GeneID	6605.
KEGG	hsa:6605.
UCSC	uc002hux.2. human.
Organism-specific databases
CTD	6605.
GeneCards	GC17M038781.
HGNC	HGNC:11109. SMARCE1.
HPA	HPA003916.
MIM	603111. gene.
neXtProt	NX_Q969G3.
PharmGKB	PA35959.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG291422.
HOGENOM	HOG000230965.
HOVERGEN	HBG054558.
InParanoid	Q969G3.
KO	K11651.
OMA	EDESIPM.
OrthoDB	EOG4229K4.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_tf_pathway. Regulation of Androgen receptor activity.
Gene expression databases
ArrayExpress	Q969G3.
Bgee	Q969G3.
CleanEx	HS_SMARCE1.
Genevestigator	Q969G3.
GermOnline	ENSG00000073584. Homo sapiens.
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
GenomeRNAi	6605.
NextBio	25703.
SOURCE	Search...

Entry information

Entry name

SMCE1_HUMAN

Accession

Primary (citable) accession number: Q969G3
Secondary accession number(s): B3KMC1, O43539

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2004
Last sequence update:	October 25, 2004
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.