Q3TKT4 (SMCA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription activator BRG1
EC=3.6.4.-

Alternative name(s):
ATP-dependent helicase SMARCA4
BRG1-associated factor 190A
Short name=BAF190A
Protein brahma homolog 1
SNF2-beta
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4

Gene names

Name:	Smarca4
Synonyms:	Baf190a, Brg1, Snf2b, Snf2l4

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	1613 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. 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. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP 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. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1 By similarity. Ref.5
Subunit structure	Interacts with NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7. 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, IKFZ1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. Interacts directly with IKFZ1 in the BAF complex. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Component of the CREST-BRG1 complex, at least composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1. Interacts with (via the bromodomain) with TERT; the interaction regulates Wnt-mediated signaling. 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 PHF10/BAF45A. Interacts with ZEB1 (via N-terminus) By similarity. Ref.5
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 bromo domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain. Contains 1 QLQ domain.

Ontologies

Keywords
Biological process	Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Chromatin regulator Helicase Hydrolase Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation on cytosine within a CG sequence Inferred from mutant phenotype PubMed 16287714. Source: MGI aortic smooth muscle cell differentiation Inferred from mutant phenotype PubMed 19342595. Source: MGI blastocyst growth Inferred from mutant phenotype PubMed 11163203. Source: MGI blastocyst hatching Inferred from mutant phenotype PubMed 11163203. Source: MGI cell morphogenesis Inferred from mutant phenotype PubMed 16287714. Source: MGI chromatin remodeling Inferred from mutant phenotype PubMed 16287714. Source: MGI definitive erythrocyte differentiation Inferred from mutant phenotype PubMed 16287714. Source: MGI embryonic hindlimb morphogenesis Inferred from mutant phenotype PubMed 16192310. Source: MGI embryonic organ morphogenesis Inferred from mutant phenotype PubMed 16287714. Source: MGI epidermis morphogenesis Inferred from mutant phenotype PubMed 16192310. Source: MGI extracellular matrix organization Inferred from mutant phenotype PubMed 18267097. Source: MGI forebrain development Inferred from mutant phenotype PubMed 16330018. Source: MGI glial cell fate determination Inferred from mutant phenotype PubMed 16330018. Source: MGI heart trabecula formation Inferred from genetic interaction PubMed 18267097. Source: MGI hindbrain development Inferred from mutant phenotype PubMed 16330018. Source: MGI histone H3 acetylation Inferred from mutant phenotype PubMed 16287714. Source: MGI keratinocyte differentiation Inferred from mutant phenotype PubMed 16192310. Source: MGI liver development Inferred from mutant phenotype PubMed 16287714. Source: MGI methylation-dependent chromatin silencing Inferred from direct assay PubMed 16322236. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16322236. Source: MGI nucleosome assembly Traceable author statement PubMed 11163203. Source: MGI positive regulation of DNA binding Inferred from genetic interaction PubMed 19342595. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 16287714. Source: MGI stem cell maintenance Inferred from mutant phenotype PubMed 20176728. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW vasculogenesis Inferred from mutant phenotype PubMed 18267097. Source: MGI
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 16287714. Source: MGI heterochromatin Inferred from direct assay PubMed 16322236. Source: MGI nBAF complex Inferred from direct assay Ref.5. Source: UniProtKB npBAF complex Inferred from direct assay Ref.5. Source: UniProtKB nuclear euchromatin Inferred from direct assay PubMed 10318760. Source: MGI perichromatin fibrils Inferred from direct assay PubMed 10318760. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from mutant phenotype PubMed 22513373. Source: MGI RNA polymerase II regulatory region sequence-specific DNA binding Inferred from direct assay PubMed 20176728. Source: MGI chromatin binding Inferred from direct assay PubMed 10318760PubMed 16287714PubMed 16322236PubMed 17074803PubMed 18267097. Source: MGI helicase activity Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RB1	P06400	4	EBI-1210244,EBI-491274	From a different organism.
Rb1	P13405	3	EBI-1210244,EBI-971782

Alternative products

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

Isoform 1 (identifier: Q3TKT4-1)

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: Q3TKT4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1441-1441: D → DS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1613	1613	Transcription activator BRG1		PRO_0000391343
Regions
	Domain	171 – 206	36	QLQ
	Domain	460 – 532	73	HSA
	Domain	766 – 931	166	Helicase ATP-binding
	Domain	1084 – 1246	163	Helicase C-terminal
	Domain	1443 – 1513	71	Bromo
	Nucleotide binding	779 – 786	8	ATP Potential
	Region	1 – 282	282	Necessary for interaction with SS18L1/CREST By similarity
	Motif	881 – 884	4	DEGH box By similarity
	Compositional bias	4 – 344	341	Pro-rich
	Compositional bias	663 – 672	10	Poly-Glu
	Compositional bias	1252 – 1370	119	Glu-rich
	Compositional bias	1531 – 1555	25	Glu-rich
Sites
	Site	1505 – 1506	2	Required for binding to 'Lys-15'-acetylated histone 3 By similarity
Amino acid modifications
	Modified residue	11	1	Phosphothreonine By similarity
	Modified residue	188	1	N6-acetyllysine By similarity
	Modified residue	353	1	Phosphothreonine By similarity
	Modified residue	609	1	Phosphothreonine By similarity
	Modified residue	610	1	Phosphoserine Ref.6
	Modified residue	613	1	Phosphoserine Ref.6
	Modified residue	695	1	Phosphoserine Ref.4 Ref.7
	Modified residue	699	1	Phosphoserine By similarity
	Modified residue	1349	1	Phosphoserine By similarity
	Modified residue	1419	1	Phosphoserine Ref.8
	Modified residue	1536	1	Phosphoserine By similarity
	Modified residue	1541	1	Phosphoserine By similarity
	Modified residue	1552	1	Phosphoserine By similarity
	Modified residue	1593	1	Phosphoserine By similarity
	Modified residue	1597	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1441	1	D → DS in isoform 2.		VSP_038696
Experimental info
	Sequence conflict	1355	1	W → WLKT in BAE36034. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: C23804ED858F98FE	FASTA	1,613	181,427
	10 20 30 40 50 60 MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG 70 80 90 100 110 120 PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMAPPP SPMDQHSQGY 130 140 150 160 170 180 PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL 190 200 210 220 230 240 RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP 250 260 270 280 290 300 GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ 310 320 330 340 350 360 KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG 370 380 390 400 410 420 LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV 430 440 450 460 470 480 VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL 490 500 510 520 530 540 QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK 550 560 570 580 590 600 LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG 610 620 630 640 650 660 PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES 670 680 690 700 710 720 GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV 730 740 750 760 770 780 SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE 790 800 810 820 830 840 MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA 850 860 870 880 890 900 RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH 910 920 930 940 950 960 YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE 970 980 990 1000 1010 1020 TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD 1030 1040 1050 1060 1070 1080 GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG 1090 1100 1110 1120 1130 1140 KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK 1150 1160 1170 1180 1190 1200 TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR 1210 1220 1230 1240 1250 1260 VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE 1270 1280 1290 1300 1310 1320 DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE 1330 1340 1350 1360 1370 1380 VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR 1390 1400 1410 1420 1430 1440 KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK 1450 1460 1470 1480 1490 1500 DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ 1510 1520 1530 1540 1550 1560 NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK 1570 1580 1590 1600 1610 VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSEEE QEEDRSGSGS EED
	Isoform 2 [UniParc]. Checksum: 1DC02672488F3BA5	FASTA	1,614	181,514
	10 20 30 40 50 60 MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG 70 80 90 100 110 120 PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMAPPP SPMDQHSQGY 130 140 150 160 170 180 PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL 190 200 210 220 230 240 RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP 250 260 270 280 290 300 GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ 310 320 330 340 350 360 KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG 370 380 390 400 410 420 LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV 430 440 450 460 470 480 VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL 490 500 510 520 530 540 QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK 550 560 570 580 590 600 LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG 610 620 630 640 650 660 PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES 670 680 690 700 710 720 GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV 730 740 750 760 770 780 SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE 790 800 810 820 830 840 MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA 850 860 870 880 890 900 RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH 910 920 930 940 950 960 YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE 970 980 990 1000 1010 1020 TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD 1030 1040 1050 1060 1070 1080 GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG 1090 1100 1110 1120 1130 1140 KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK 1150 1160 1170 1180 1190 1200 TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR 1210 1220 1230 1240 1250 1260 VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE 1270 1280 1290 1300 1310 1320 DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE 1330 1340 1350 1360 1370 1380 VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR 1390 1400 1410 1420 1430 1440 KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK 1450 1460 1470 1480 1490 1500 DSSSGRQLSE VFIQLPSRKE LPEYYELIRK PVDFKKIKER IRNHKYRSLN DLEKDVMLLC 1510 1520 1530 1540 1550 1560 QNAQTFNLEG SLIYEDSIVL QSVFTSVRQK IEKEDDSEGE ESEEEEEGEE EGSESESRSV 1570 1580 1590 1600 1610 KVKIKLGRKE KAQDRLKGGR RRPSRGSRAK PVVSDDDSEE EQEEDRSGSG SEED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Placenta.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 2). Strain: C57BL/6. Tissue: Brain.
[4]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, MASS SPECTROMETRY. Tissue: Liver.
[5]	"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, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, INTERACTION WITH PHF10.
[6]	"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-610 AND SER-613, MASS SPECTROMETRY. Tissue: Liver.
[7]	"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-695, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"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-1419, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK147285 mRNA. Translation: BAE27821.1. AK160825 mRNA. Translation: BAE36034.1. AK166837 mRNA. Translation: BAE39059.1. BC079560 mRNA. Translation: AAH79560.1. CH466522 Genomic DNA. Translation: EDL25209.1.
IPI	IPI00875789. IPI00955124.
RefSeq	NP_001167549.1. NM_001174078.1. NP_001167550.1. NM_001174079.1. NP_035547.2. NM_011417.3.
UniGene	Mm.286593.
3D structure databases
ProteinModelPortal	Q3TKT4.
SMR	Q3TKT4. Positions 749-1221, 1416-1535.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-40650N. DIP-59249N.
IntAct	Q3TKT4. 11 interactions.
MINT	MINT-1958721.
STRING	10090.ENSMUSP00000096547.
PTM databases
PhosphoSite	Q3TKT4.
Proteomic databases
PaxDb	Q3TKT4.
PRIDE	Q3TKT4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034707; ENSMUSP00000034707; ENSMUSG00000032187. ENSMUST00000098948; ENSMUSP00000096547; ENSMUSG00000032187. ENSMUST00000174008; ENSMUSP00000133922; ENSMUSG00000032187.
GeneID	20586.
KEGG	mmu:20586.
UCSC	uc009omd.2. mouse. uc009ome.2. mouse.
Organism-specific databases
CTD	6597.
MGI	MGI:88192. Smarca4.
Phylogenomic databases
eggNOG	COG0553.
GeneTree	ENSGT00550000074659.
HOGENOM	HOG000172363.
HOVERGEN	HBG056636.
InParanoid	Q3TUD7.
KO	K11647.
OrthoDB	EOG418BMJ.
Gene expression databases
ArrayExpress	Q3TKT4.
Bgee	Q3TKT4.
Genevestigator	Q3TKT4.
Family and domain databases
Gene3D	1.20.920.10. 1 hit.
InterPro	IPR006576. BRK_domain. IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR014978. Gln-Leu-Gln_QLQ. IPR013999. HAS_subgr. IPR014012. Helicase/SANT-assoc_DNA-bd. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR006562. HSA. IPR000330. SNF2_N. [Graphical view]
Pfam	PF07533. BRK. 1 hit. PF00439. Bromodomain. 1 hit. PF00271. Helicase_C. 1 hit. PF07529. HSA. 1 hit. PF08880. QLQ. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00592. BRK. 1 hit. SM00297. BROMO. 1 hit. SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00573. HSA. 1 hit. SM00951. QLQ. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51204. HSA. 1 hit. PS51666. QLQ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	298883.
SOURCE	Search...

Entry information

Entry name

SMCA4_MOUSE

Accession

Primary (citable) accession number: Q3TKT4
Secondary accession number(s): Q3TUD7, Q6AXG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 9, 2010
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program