ID F2Z4A9_MOUSE Unreviewed; 1583 AA.
AC F2Z4A9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 {ECO:0000313|Ensembl:ENSMUSP00000025862.8};
GN Name=Smarca2 {ECO:0000313|Ensembl:ENSMUSP00000025862.8,
GN ECO:0000313|MGI:MGI:99603};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000025862.8, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000025862.8, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000025862.8,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000025862.8}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000025862.8};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR RefSeq; NP_035546.2; NM_011416.2.
DR RefSeq; XP_006527348.1; XM_006527285.2.
DR SMR; F2Z4A9; -.
DR jPOST; F2Z4A9; -.
DR MaxQB; F2Z4A9; -.
DR PeptideAtlas; F2Z4A9; -.
DR ProteomicsDB; 361795; -.
DR Antibodypedia; 9105; 282 antibodies from 31 providers.
DR DNASU; 67155; -.
DR Ensembl; ENSMUST00000025862.15; ENSMUSP00000025862.8; ENSMUSG00000024921.18.
DR GeneID; 67155; -.
DR KEGG; mmu:67155; -.
DR UCSC; uc008hbn.1; mouse.
DR AGR; MGI:99603; -.
DR CTD; 6595; -.
DR MGI; MGI:99603; Smarca2.
DR VEuPathDB; HostDB:ENSMUSG00000024921; -.
DR GeneTree; ENSGT00940000154821; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR OrthoDB; 5482994at2759; -.
DR TreeFam; TF300785; -.
DR BioGRID-ORCS; 67155; 4 hits in 81 CRISPR screens.
DR ChiTaRS; Smarca2; mouse.
DR Proteomes; UP000000589; Chromosome 19.
DR Bgee; ENSMUSG00000024921; Expressed in cortical plate and 265 other cell types or tissues.
DR ExpressionAtlas; F2Z4A9; baseline and differential.
DR Genevisible; F2Z4A9; MM.
DR GO; GO:0070603; C:SWI/SNF superfamily-type complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18063; DEXHc_SMARCA2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF541; GLOBAL TRANSCRIPTION ACTIVATOR SNF2L2-RELATED; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:F2Z4A9,
KW ECO:0007829|MaxQB:F2Z4A9};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 173..208
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 447..519
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 747..912
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1065..1227
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1412..1482
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1583 AA; 180722 MW; 11584802644C363E CRC64;
MSTPTDPAAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPLSTM
GSADFPQEGM HQLHKPMDGI HDKGIVEDVH CGSMKGTSMR PPHPGMGPPQ SPMDQHSQGY
MSPHPSPLGA PEHVSSPISG GGPTPPQMPP SQPGALIPGD PQAMNQPNRG PSPFSPVQLH
QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGMQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QPQQPQQQAQ AQPQQQQQQQ QQPALVSYNR PSGPGQELLL SGQSAPQKLS APAPSGRPSP
APQAAVQPTA TAVPGPSVQQ PAPGQPSPVL QLQQKQSRIS PIQKPQGLDP VEILQEREYR
LQARIAHRIQ ELESLPGSLP PDLRTKATVE LKALRLLNFQ RQLRQEVVAC MRRDTTLETA
LNSKAYKRSK RQTLREARMT EKLEKQQKIE QERKRRQKHQ EYLNSILQHA KDFKEYHRSV
AGKIQKLSKA VATWHANTER EQKKETERIE KERMRRLMAE DEEGYRKLID QKKDRRLAYL
LQQTDEYVAN LTNLVWEHKQ AQAAKEKKKR RRRKKKAEEN AEGGEPALGP DGEPIDESSQ
MSDLPVKVTH TETGKVLFGP EAPKASQLDA WLEMNPGYEV APRSDSEESE SDYEEEDEEE
ESSRQETEEK ILLDPNSEEV SEKDAKQIIE TAKQDVDDEY SMQYSARGSQ SYYTVAHAIS
ERVEKQSALL INGTLKHYQL QGLEWMVSLY NNNLNGILAD EMGLGKTIQT IALITYLMEH
KRLNGPYLII VPLSTLSNWT YEFDKWAPSV VKISYKGTPA MRRSLVPQLR SGKFNVLLTT
YEYIIKDKHI LAKIRWKYMI VDEGHRMKNH HCKLTQVLNT HYVAPRRILL TGTPLQNKLP
ELWALLNFLL PTIFKSCSTF EQWFNAPFAM TGERVDLNEE ETILIIRRLH KVLRPFLLRR
LKKEVESQLP EKVEYVIKCD MSALQKILYR HMQAKGILLT DGSEKDKKGK GGAKTLMNTI
MQLRKICNHP YMFQHIEESF AEHLGYSNGV INGAELYRAS GKFELLDRIL PKLRATNHRV
LLFCQMTSLM TIMEDYFAFR NFLYLRLDGT TKSEDRAALL KKFNEPGSQY FIFLLSTRAG
GLGLNLQAAD TVVIFDSDWN PHQDLQAQDR AHRIGQQNEV RVLRLCTVNS VEEKILAAAK
YKLNVDQKVI QAGMFDQKSS SHERRAFLQA ILEHEEENEE EDEVPDDETL NQMIARREEE
FDLFMRMDMD RRREDARNPK RKPRLMEEDE LPSWIIKDDA EVERLTCEEE EEKIFGRGSR
QRRDVDYSDA LTEKQWLRAI EDGNLEEMEE EVRLKKRKRR RNVDKDPVKE DVEKAKKRRG
RPPAEKLSPN PPKLTKQMNA IIDTVINYKD SSGRQLSEVF IQLPSRKDLP EYYELIRKPV
DFKKIKERIR NHKYRSLGDL EKDVMLLCHN AQTFNLEGSQ IYEDSIVLQS VFKSARQKIA
KEEESEEESN EEEEEDDEEE SESEAKSVKV KIKLNKKEEK GRDTGKGKKR PNRGKAKPVV
SDFDSDEEQE ENEQSEASGT DNE
//
