Q12824 (SNF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1

Alternative name(s):
BRG1-associated factor 47
Short name=BAF47
Integrase interactor 1 protein
SNF5 homolog
Short name=hSNF5

Gene names

Name:	SMARCB1
Synonyms:	BAF47, INI1, SNF5L1

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	385 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. 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. Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. 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.12 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26
Subunit structure	Component of the BAF (hSWI/SNF) 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 to double-stranded DNA. Interacts with MYK and MAEL. Interacts with PPP1R15A. Binds tightly to the human immunodeficiency virus-type 1 (HIV-1) integrase in vitro and stimulates its DNA-joining activity. Interacts with human papillomavirus 18 E1 protein to stimulate its viral replication. Interacts with Epstein-Barr virus protein EBNA-2. 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 similarity. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 Ref.27
Subcellular location	Nucleus.
Involvement in disease	Rhabdoid tumor predisposition syndrome 1 (RTPS1) [MIM:609322]: A familial cancer syndrome predisposing to renal or extrarenal malignant rhabdoid tumors and to a variety of tumors of the central nervous system, including choroid plexus carcinoma, medulloblastoma, and central primitive neuroectodermal tumors. Rhabdoid tumors are the most aggressive and lethal malignancies occurring in early childhood. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.23 Schwannomatosis (SCHWA) [MIM:162091]: Schwannomas are benign tumors of the peripheral nerve sheath that usually occur singly in otherwise normal individuals. Multiple schwannomas in the same individual suggest an underlying tumor-predisposition syndrome. The most common such syndrome is NF2. The hallmark of NF2 is the development of bilateral vestibular-nerve schwannomas; but two-thirds or more of all NF2-affected individuals develop schwannomas in other locations, and dermal schwannomas may precede vestibular tumors in NF2-affected children. There have been several reports of individuals with multiple schwannomas who do not show evidence of vestibular schwannoma. Clinical report suggests that schwannomatosis is a clinical entity distinct from other forms of neurofibromatosis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.23 Ref.28 Ref.29 Mental retardation, autosomal dominant 15 (MRD15) [MIM:614608]: A disease characterized by multiple congenital anomalies and mental retardation. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRD15 patients manifest developmental delay, hypotonia, absent or hypoplastic fifth finger or toenails, a coarse facial appearance, sparse scalp hair, thick eyebrows, and long eyelashes. Additional variable features include microcephaly, small cerebellum, seizures, hearing loss, abnormal delayed dentition, hirsutism. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.23 Ref.30
Sequence similarities	Belongs to the SNF5 family.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Mental retardation Tumor suppressor
Domain	Repeat
Molecular function	Activator Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA integration Traceable author statement Ref.1. Source: ProtInc blastocyst hatching Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: Compara chromatin remodeling Inferred from direct assay PubMed 11726552. Source: BHF-UCL negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara nervous system development Inferred from electronic annotation. Source: UniProtKB-KW nucleosome disassembly Inferred from direct assay Ref.10. Source: BHF-UCL positive regulation by host of viral transcription Inferred from mutant phenotype PubMed 16687403. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 11950834. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 11950834. Source: BHF-UCL retroviral genome replication Inferred from direct assay PubMed 14963118. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 11078522. Source: UniProtKB XY body Inferred from electronic annotation. Source: Compara nBAF complex Inferred from sequence or structural similarity. Source: UniProtKB npBAF complex Inferred from sequence or structural similarity. Source: UniProtKB nuclear chromosome Inferred from electronic annotation. Source: InterPro nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement Ref.1. Source: ProtInc
Molecular_function	transcription coactivator activity Inferred from mutant phenotype PubMed 16687403. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARID2	Q68CP9	3	EBI-358419,EBI-637818

Alternative products

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

Isoform A (identifier: Q12824-1)

Also known as: INI1A;

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 B (identifier: Q12824-2)

Also known as: INI1B;

The sequence of this isoform differs from the canonical sequence as follows:
     69-77: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 385	385	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1		PRO_0000205948
Regions
	Repeat	186 – 245	60	1
	Repeat	259 – 319	61	2
	Region	106 – 183	78	DNA-binding Potential
	Region	183 – 243	61	HIV-1 integrase-binding
	Region	186 – 319	134	2 X approximate tandem repeats
	Region	186 – 245	60	MYC-binding
	Region	304 – 318	15	Interaction with PPP1R15A
Amino acid modifications
	Modified residue	129	1	Phosphoserine Ref.24
Natural variations
	Alternative sequence	69 – 77	9	Missing in isoform B.		VSP_004399
	Natural variant	364	1	Missing in MRD15. Ref.30		VAR_068178
	Natural variant	377	1	R → H in MRD15. Ref.30		VAR_068179
Experimental info
	Sequence conflict	136	1	P → S Ref.1
	Sequence conflict	136	1	P → S in CAA76639. Ref.2
	Sequence conflict	378	1	L → E in CAA76639. Ref.2
	Sequence conflict	382	1	A → G Ref.1
	Sequence conflict	382	1	A → G in CAA76639. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (INI1A) [UniParc]. Last modified August 16, 2004. Version 2. Checksum: B7BCA26875BD943D	FASTA	385	44,141
	10 20 30 40 50 60 MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER 70 80 90 100 110 120 KKIVASSHGK KTKPNTKDHG YTTLATSVTL LKASEVEEIL DGNDEKYKAV SISTEPPTYL 130 140 150 160 170 180 REQKAKRNSQ WVPTLPNSSH HLDAVPCSTT INRNRMGRDK KRTFPLCFDD HDPAVIHENA 190 200 210 220 230 240 SQPEVLVPIR LDMEIDGQKL RDAFTWNMNE KLMTPEMFSE ILCDDLDLNP LTFVPAIASA 250 260 270 280 290 300 IRQQIESYPT DSILEDQSDQ RVIIKLNIHV GNISLVDQFE WDMSEKENSP EKFALKLCSE 310 320 330 340 350 360 LGLGGEFVTT IAYSIRGQLS WHQKTYAFSE NPLPTVEIAI RNTGDADQWC PLLETLTDAE 370 380 MEKKIRDQDR NTRRMRRLAN TAPAW
	Isoform B (INI1B) [UniParc]. Checksum: 6C7233EAFBC389A9	FASTA	376	43,158
	10 20 30 40 50 60 MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER 70 80 90 100 110 120 KKIVASSHDH GYTTLATSVT LLKASEVEEI LDGNDEKYKA VSISTEPPTY LREQKAKRNS 130 140 150 160 170 180 QWVPTLPNSS HHLDAVPCST TINRNRMGRD KKRTFPLCFD DHDPAVIHEN ASQPEVLVPI 190 200 210 220 230 240 RLDMEIDGQK LRDAFTWNMN EKLMTPEMFS EILCDDLDLN PLTFVPAIAS AIRQQIESYP 250 260 270 280 290 300 TDSILEDQSD QRVIIKLNIH VGNISLVDQF EWDMSEKENS PEKFALKLCS ELGLGGEFVT 310 320 330 340 350 360 TIAYSIRGQL SWHQKTYAFS ENPLPTVEIA IRNTGDADQW CPLLETLTDA EMEKKIRDQD 370 RNTRRMRRLA NTAPAW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5." Kalpana G.V., Marmon S., Wang W., Crabtree G.R., Goff S.P. Science 266:2002-2006(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]	"Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer." Versteege I., Sevenet N., Lange J., Rousseau-Merck M.-F., Ambros P., Handgretinger R., Aurias A., Delattre O. Nature 394:203-206(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN RDT.
[3]	"The mouse ortholog of the human SMARCB1 gene encodes two splice forms." Bruder C.E., Dumanski J.P., Kedra D. Biochem. Biophys. Res. Commun. 257:886-890(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
[4]	"Human Ini1 27bp deletion form." Tozaki H., Yasuda J., Iwakura Y. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[5]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[6]	"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 B). Tissue: Embryo.
[7]	NIEHS SNPs program Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton 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].
[9]	"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 B). Tissue: Brain.
[10]	"Purification and biochemical heterogeneity of the mammalian SWI-SNF complex." Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R., Muchardt C., Kalpana G.V., Goff S.P., Yaniv M., Workman J.L., Crabtree G.R. EMBO J. 15:5370-5382(1996) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN BAF COMPLEX.
[11]	"Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1." Wu D.Y., Kalpana G.V., Goff S.P., Schubach W.H. J. Virol. 70:6020-6028(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2.
[12]	"Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region." Morozov A., Yung E., Kalpana G.V. Proc. Natl. Acad. Sci. U.S.A. 95:1120-1125(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins." Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M., Fornace A.J. Jr., Tkachuk D.C. Mol. Cell. Biol. 19:7050-7060(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R15A.
[14]	"c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function." Cheng S.-W., Davies K.P., Yung E., Beltran R.J., Yu J., Kalpana G.V. Nat. Genet. 22:102-105(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYC.
[15]	"Interaction of E1 and hSNF5 proteins stimulates replication of human papillomavirus DNA." Lee D., Sohn H., Kalpana G.V., Choe J. Nature 399:487-491(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN PAPILLOMAVIRUS-18 E1 PROTEIN.
[16]	"Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits." Phelan M.L., Sif S., Narlikar G.J., Kingston R.E. Mol. Cell 3:247-253(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Germ-line and acquired mutations of INI1 in atypical teratoid and rhabdoid tumors." Biegel J.A., Zhou J.-Y., Rorke L.B., Stenstrom C., Wainwright L.M., Fogelgren B. Cancer Res. 59:74-79(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[18]	"The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity." Wu D.Y., Tkachuck D.C., Roberson R.S., Schubach W.H. J. Biol. Chem. 277:27706-27715(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R15A.
[19]	"A key role of the hSNF5/INI1 tumour suppressor in the control of the G1-S transition of the cell cycle." Versteege I., Medjkane S., Rouillard D., Delattre O. Oncogene 21:6403-6412(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL CYCLE.
[20]	"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.
[21]	"P16INK4a is required for hSNF5 chromatin remodeler-induced cellular senescence in malignant rhabdoid tumor cells." Oruetxebarria I., Venturini F., Kekarainen T., Houweling A., Zuijderduijn L.M.P., Mohd-Sarip A., Vries R.G.J., Hoeben R.C., Verrijzer C.P. J. Biol. Chem. 279:3807-3816(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL CYCLE.
[22]	"Chromatin-remodeling factor INI1/hSNF5/BAF47 is involved in activation of the colony stimulating factor 1 promoter." Pan X., Song Z., Zhai L., Li X., Zeng X. Mol. Cells 20:183-188(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF COLONY STIMULATING FACTOR 1 PROMOTER.
[23]	"SMARCB1/INI1 tumor suppressor gene is frequently inactivated in epithelioid sarcomas." Modena P., Lualdi E., Facchinetti F., Galli L., Teixeira M.R., Pilotti S., Sozzi G. Cancer Res. 65:4012-4019(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[24]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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].
[26]	"Human SWI/SNF generates abundant, structurally altered dinucleosomes on polynucleosomal templates." Ulyanova N.P., Schnitzler G.R. Mol. Cell. Biol. 25:11156-11170(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF BAF COMPLEX IN CHROMATIN REMODELING.
[27]	"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.
[28]	"Germline mutation of INI1/SMARCB1 in familial schwannomatosis." Hulsebos T.J.M., Plomp A.S., Wolterman R.A., Robanus-Maandag E.C., Baas F., Wesseling P. Am. J. Hum. Genet. 80:805-810(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SCHWA.
[29]	"Evidence of a four-hit mechanism involving SMARCB1 and NF2 in schwannomatosis-associated schwannomas." Sestini R., Bacci C., Provenzano A., Genuardi M., Papi L. Hum. Mutat. 29:227-231(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SCHWA.
[30]	"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: VARIANTS MRD15 LYS-364 DEL AND HIS-377.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	U04847 mRNA. Translation: AAA81905.1. Y17118 , Y17119, Y17120, Y17121, Y17122, Y17123, Y17124, Y17125, Y17126 Genomic DNA. Translation: CAA76639.1. Sequence problems. AJ011738 mRNA. Translation: CAA09759.1. AJ011737 mRNA. Translation: CAA09758.1. AB017523 mRNA. Translation: BAC77068.1. CR456581 mRNA. Translation: CAG30467.1. AK021419 mRNA. Translation: BAG51033.1. DQ230988 Genomic DNA. Translation: ABB02184.1. CH471095 Genomic DNA. Translation: EAW59606.1. BC117114 mRNA. Translation: AAI17115.1. BC143667 mRNA. Translation: AAI43668.1.
IPI	IPI00029695. IPI00745019.
PIR	S54705.
RefSeq	NP_001007469.1. NM_001007468.1. NP_003064.2. NM_003073.3.
UniGene	Hs.534350.
3D structure databases
ProteinModelPortal	Q12824.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27550N.
IntAct	Q12824. 12 interactions.
MINT	MINT-94943.
STRING	9606.ENSP00000263121.
PTM databases
PhosphoSite	Q12824.
Polymorphism databases
DMDM	51338799.
Proteomic databases
PaxDb	Q12824.
PRIDE	Q12824.
Protocols and materials databases
DNASU	6598.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263121; ENSP00000263121; ENSG00000099956. ENST00000407422; ENSP00000383984; ENSG00000099956.
GeneID	6598.
KEGG	hsa:6598.
UCSC	uc002zya.3. human.
Organism-specific databases
CTD	6598.
GeneCards	GC22P024129.
HGNC	HGNC:11103. SMARCB1.
HPA	CAB009196. HPA018248. HPA019127.
MIM	162091. phenotype. 601607. gene. 609322. phenotype. 614608. phenotype.
neXtProt	NX_Q12824.
Orphanet	1465. Coffin-Siris syndrome. 263662. Familial multiple meningioma. 231108. Familial rhabdoid tumor. 93921. Neurofibromatosis type 3. 69077. Rhabdoid tumor.
PharmGKB	PA35953.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG291299.
HOGENOM	HOG000015760.
HOVERGEN	HBG011709.
KO	K11648.
OrthoDB	EOG4BK53X.
Gene expression databases
ArrayExpress	Q12824.
Bgee	Q12824.
CleanEx	HS_SMARCB1.
Genevestigator	Q12824.
GermOnline	ENSG00000099956. Homo sapiens.
Family and domain databases
InterPro	IPR006939. SNF5. IPR017393. SWI_SNF_chromatin_remodel_cplx. [Graphical view]
PANTHER	PTHR10019. PTHR10019. 1 hit.
Pfam	PF04855. SNF5. 2 hits. [Graphical view]
PIRSF	PIRSF038126. SWI_SNF. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SMARCB1. human.
GenomeRNAi	6598.
NextBio	25665.
SOURCE	Search...

Entry information

Entry name

SNF5_HUMAN

Accession

Primary (citable) accession number: Q12824
Secondary accession number(s): O75784 , O95474, Q17S11, Q38GA1, Q76N08, Q9UBH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 131 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.