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Q3TKT4 (SMCA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1613 AA.
Sequence statusComplete.
Protein existenceEvidence 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.4

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 ZEB1 (via N-terminus) By similarity. Interacts with PHF10/BAF45A. Interacts with MYOG. Ref.4 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 processNeurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Chromatin regulator
Helicase
Hydrolase
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from mutant phenotype PubMed 22513373. Source: GOC

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 development

Inferred from mutant phenotype PubMed 18267097. 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

in utero embryonic development

Inferred from mutant phenotype PubMed 16287714. Source: MGI

keratinocyte differentiation

Inferred from mutant phenotype PubMed 16192310. Source: MGI

lens fiber cell development

Inferred from mutant phenotype PubMed 21118511. 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 androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16322236. Source: MGI

nervous system development

Inferred from mutant phenotype Ref.4. Source: UniProtKB

neural retina development

Inferred from electronic annotation. Source: Ensembl

neurogenesis

Inferred from direct assay PubMed 22513373. Source: MGI

nucleosome assembly

Traceable author statement PubMed 11163203. Source: MGI

nucleosome disassembly

Inferred from electronic annotation. Source: Ensembl

positive regulation by host of viral transcription

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA binding

Inferred from genetic interaction PubMed 19342595. Source: MGI

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

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

vasculogenesis

Inferred from mutant phenotype PubMed 18267097. Source: MGI

   Cellular_componentSWI/SNF complex

Inferred from direct assay PubMed 16287714. Source: MGI

WINAC complex

Inferred from electronic annotation. Source: Ensembl

heterochromatin

Inferred from direct assay PubMed 16322236. Source: MGI

nBAF complex

Inferred from direct assay Ref.4. Source: UniProtKB

npBAF complex

Inferred from direct assay Ref.4. Source: UniProtKB

nuclear euchromatin

Inferred from direct assay PubMed 10318760. Source: MGI

nucleus

Inferred from direct assay PubMed 10318760PubMed 15565649PubMed 16192310PubMed 16787967PubMed 16880268PubMed 18267097PubMed 9603422. Source: MGI

perichromatin fibrils

Inferred from direct assay PubMed 10318760. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from mutant phenotype PubMed 22513373. Source: MGI

DNA-dependent ATPase activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 20176728. Source: MGI

RNA polymerase II transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay PubMed 10318760PubMed 16287714PubMed 16322236PubMed 17074803PubMed 18267097. Source: MGI

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 15767674. Source: MGI

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16131613Transcription activator BRG1
PRO_0000391343

Regions

Domain171 – 20636QLQ
Domain460 – 53273HSA
Domain766 – 931166Helicase ATP-binding
Domain1084 – 1246163Helicase C-terminal
Domain1443 – 151371Bromo
Nucleotide binding779 – 7868ATP Potential
Region1 – 282282Necessary for interaction with SS18L1/CREST By similarity
Motif881 – 8844DEGH box By similarity
Compositional bias4 – 344341Pro-rich
Compositional bias663 – 67210Poly-Glu
Compositional bias1252 – 1370119Glu-rich
Compositional bias1531 – 155525Glu-rich

Sites

Site1505 – 15062Required for binding to 'Lys-15'-acetylated histone 3 By similarity

Amino acid modifications

Modified residue111Phosphothreonine By similarity
Modified residue1881N6-acetyllysine By similarity
Modified residue3531Phosphothreonine By similarity
Modified residue6091Phosphothreonine By similarity
Modified residue6101Phosphoserine Ref.6
Modified residue6131Phosphoserine Ref.6
Modified residue6951Phosphoserine By similarity
Modified residue6991Phosphoserine By similarity
Modified residue13491Phosphoserine By similarity
Modified residue14191Phosphoserine By similarity
Modified residue15361Phosphoserine By similarity
Modified residue15411Phosphoserine By similarity
Modified residue15521Phosphoserine By similarity
Modified residue15931Phosphoserine By similarity
Modified residue15971Phosphoserine By similarity

Natural variations

Alternative sequence14411D → DS in isoform 2.
VSP_038696

Experimental info

Sequence conflict13551W → WLKT in BAE36034. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: C23804ED858F98FE

FASTA1,613181,427
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 1DC02672488F3BA5
Show »

FASTA1,614181,514

References

« Hide '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. expand/collapse author list , 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]"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.
[5]"Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase Brg1."
Ohkawa Y., Marfella C.G., Imbalzano A.N.
EMBO J. 25:490-501(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYOG.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS22909.1. [Q3TKT4-2]
CCDS57662.1. [Q3TKT4-1]
RefSeqNP_001167549.1. NM_001174078.1.
NP_001167550.1. NM_001174079.1. [Q3TKT4-1]
NP_035547.2. NM_011417.3. [Q3TKT4-2]
UniGeneMm.286593.

3D structure databases

ProteinModelPortalQ3TKT4.
SMRQ3TKT4. Positions 749-1221, 1416-1535.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203336. 72 interactions.
DIPDIP-40650N.
DIP-59249N.
IntActQ3TKT4. 28 interactions.
MINTMINT-1958721.
STRING10090.ENSMUSP00000096547.

PTM databases

PhosphoSiteQ3TKT4.

Proteomic databases

MaxQBQ3TKT4.
PaxDbQ3TKT4.
PRIDEQ3TKT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034707; ENSMUSP00000034707; ENSMUSG00000032187. [Q3TKT4-2]
ENSMUST00000098948; ENSMUSP00000096547; ENSMUSG00000032187.
ENSMUST00000174008; ENSMUSP00000133922; ENSMUSG00000032187. [Q3TKT4-1]
GeneID20586.
KEGGmmu:20586.
UCSCuc009omd.2. mouse. [Q3TKT4-2]
uc009ome.2. mouse. [Q3TKT4-1]

Organism-specific databases

CTD6597.
MGIMGI:88192. Smarca4.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00550000074659.
HOGENOMHOG000172363.
HOVERGENHBG056636.
InParanoidQ3TUD7.
KOK11647.
OrthoDBEOG771265.
PhylomeDBQ3TKT4.
TreeFamTF300785.

Gene expression databases

ArrayExpressQ3TKT4.
BgeeQ3TKT4.
GenevestigatorQ3TKT4.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR006576. 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.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00592. 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]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

NextBio298883.
PROQ3TKT4.
SOURCESearch...

Entry information

Entry nameSMCA4_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot