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SMRD2_MOUSE
ID   SMRD2_MOUSE             Reviewed;         531 AA.
AC   Q99JR8; B1ARI7; B1ARJ6;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;
DE   AltName: Full=60 kDa BRG-1/Brm-associated factor subunit B;
DE   AltName: Full=BRG1-associated factor 60B;
DE            Short=BAF60B;
GN   Name=Smarcd2; Synonyms=Baf60b;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Spleen, and Testis;
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).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). Component of SWI/SNF chromatin remodeling complexes that
CC       carry out key enzymatic activities, changing chromatin structure by
CC       altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC       manner. Critical regulator of myeloid differentiation, controlling
CC       granulocytopoiesis and the expression of genes involved in neutrophil
CC       granule formation. {ECO:0000250|UniProtKB:Q92925}.
CC   -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC       SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC       canonical complex contains a catalytic subunit (either
CC       SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1,
CC       ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC       Other subunits specific to each of the complexes may also be present
CC       permitting several possible combinations developmentally and tissue
CC       specific. Component of the BAF complex, which includes at least actin
CC       (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1,
CC       ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
CC       SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A,
CC       SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex
CC       also contains DPF3. Component of the SWI/SNF-B (PBAF) chromatin
CC       remodeling complex, at least composed of SMARCA4/BRG1,
CC       SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57,
CC       SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155,
CC       SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin (ACTB). Interacts
CC       with UNKL. Interacts with CEBPE. {ECO:0000250|UniProtKB:Q92925}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92925}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99JR8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99JR8-2; Sequence=VSP_040533;
CC   -!- PTM: Ubiquitinated through a signaling process involving RAC1 and the
CC       RING finger protein UNKL. {ECO:0000250|UniProtKB:Q92925}.
CC   -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05732.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL604045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005732; AAH05732.1; ALT_INIT; mRNA.
DR   CCDS; CCDS48957.1; -. [Q99JR8-2]
DR   CCDS; CCDS48958.1; -. [Q99JR8-1]
DR   RefSeq; NP_001123659.1; NM_001130187.1. [Q99JR8-1]
DR   AlphaFoldDB; Q99JR8; -.
DR   SMR; Q99JR8; -.
DR   BioGRID; 219976; 6.
DR   ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR   ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR   ComplexPortal; CPX-1261; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1263; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   CORUM; Q99JR8; -.
DR   DIP; DIP-58950N; -.
DR   IntAct; Q99JR8; 5.
DR   MINT; Q99JR8; -.
DR   STRING; 10090.ENSMUSP00000021052; -.
DR   iPTMnet; Q99JR8; -.
DR   PhosphoSitePlus; Q99JR8; -.
DR   EPD; Q99JR8; -.
DR   jPOST; Q99JR8; -.
DR   MaxQB; Q99JR8; -.
DR   PaxDb; Q99JR8; -.
DR   PeptideAtlas; Q99JR8; -.
DR   PRIDE; Q99JR8; -.
DR   ProteomicsDB; 258705; -. [Q99JR8-1]
DR   ProteomicsDB; 258706; -. [Q99JR8-2]
DR   Antibodypedia; 9431; 152 antibodies from 29 providers.
DR   DNASU; 83796; -.
DR   Ensembl; ENSMUST00000021052; ENSMUSP00000021052; ENSMUSG00000078619. [Q99JR8-1]
DR   Ensembl; ENSMUST00000106843; ENSMUSP00000102456; ENSMUSG00000078619. [Q99JR8-2]
DR   GeneID; 83796; -.
DR   KEGG; mmu:83796; -.
DR   UCSC; uc007lyo.2; mouse. [Q99JR8-2]
DR   UCSC; uc007lyp.2; mouse. [Q99JR8-1]
DR   CTD; 6603; -.
DR   MGI; MGI:1933621; Smarcd2.
DR   VEuPathDB; HostDB:ENSMUSG00000078619; -.
DR   eggNOG; KOG2570; Eukaryota.
DR   GeneTree; ENSGT00940000158654; -.
DR   HOGENOM; CLU_023529_0_2_1; -.
DR   InParanoid; Q99JR8; -.
DR   OMA; LMGIWEY; -.
DR   OrthoDB; 1027566at2759; -.
DR   PhylomeDB; Q99JR8; -.
DR   TreeFam; TF106486; -.
DR   Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR   Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   BioGRID-ORCS; 83796; 4 hits in 81 CRISPR screens.
DR   ChiTaRS; Smarcd2; mouse.
DR   PRO; PR:Q99JR8; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q99JR8; protein.
DR   Bgee; ENSMUSG00000078619; Expressed in ileal epithelium and 262 other tissues.
DR   ExpressionAtlas; Q99JR8; baseline and differential.
DR   Genevisible; Q99JR8; MM.
DR   GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR   GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR   GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR   GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR   GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR   GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR   GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR   GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.245.10; -; 1.
DR   InterPro; IPR030090; BAF60B.
DR   InterPro; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR13844:SF2; PTHR13844:SF2; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   SMART; SM00151; SWIB; 1.
DR   SUPFAM; SSF47592; SSF47592; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Isopeptide bond; Methylation;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..531
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily D member 2"
FT                   /id="PRO_0000071986"
FT   DOMAIN          306..383
FT                   /note="SWIB/MDM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT   REGION          20..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         81
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   MOD_RES         104
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   MOD_RES         217
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        226
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92925"
FT   VAR_SEQ         1..71
FT                   /note="MSGRGAGGFPLPPLSPGGGAVAAALGAPPPPAGPGMLPSPALRGPGPSGGMG
FT                   VPGAAAFRPMGPAGPAAQY -> MEGMGYGPRRAPPLTCVPPLFHFP (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040533"
SQ   SEQUENCE   531 AA;  59085 MW;  B6C9D8CDC88477B5 CRC64;
     MSGRGAGGFP LPPLSPGGGA VAAALGAPPP PAGPGMLPSP ALRGPGPSGG MGVPGAAAFR
     PMGPAGPAAQ YQRPGMSPGS RMPMAGLQVG PPAGSPFGTA APLRPGMPPT MMDPFRKRLL
     VPQAQPPMPA QRRGLKRRKM ADKVLPQRIR ELVPESQAYM DLLAFERKLD QTIARKRMEI
     QEAIKKPLTQ KRKLRIYISN TFSPSKADGD NAGTAGTPGG TPAADKVASW ELRVEGKLLD
     DPSKQKRKFS SFFKSLVIEL DKELYGPDNH LVEWHRMPTT QETDGFQVKR PGDLNVKCTL
     LLMLDHQPPQ YKLDPRLARL LGVHTQTRAA IMQALWLYIK HNQLQDGHER EYINCNRYFR
     QIFSCGRLRF SEIPMKLAGL LQHPDPIVIN HVISVDPNDQ KKTACYDIDV EVDDPLKAQM
     SNFLASTTNQ QEIASLDVKI HETIESINQL KTQRDFMLSF STEPQDFIQE WLRSQRRDLK
     IITDVIGNPE EERRAAFYHQ PWAQEAVGRH IFAKVQQRRQ ELEQVLGIRL T
 
 
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