SMRD2_HUMAN
ID SMRD2_HUMAN Reviewed; 531 AA.
AC Q92925; A5PLL5; A6NNQ7; B4DV56; B4E1R6; Q7L2I6; Q9UHZ1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 177.
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; ORFNames=PRO2451;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=8804307; DOI=10.1101/gad.10.17.2117;
RA Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.;
RT "Diversity and specialization of mammalian SWI/SNF complexes.";
RL Genes Dev. 10:2117-2130(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Small intestine, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-531.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Liu M.,
RA He F.;
RT "Functional prediction of the coding sequences of 14 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP INTERACTION WITH UNKL, AND UBIQUITINATION.
RX PubMed=20148946; DOI=10.1111/j.1742-4658.2010.07575.x;
RA Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.;
RT "The SWI/SNF protein BAF60b is ubiquitinated through a signalling process
RT involving Rac GTPase and the RING finger protein Unkempt.";
RL FEBS J. 277:1453-1464(2010).
RN [13]
RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18765789; DOI=10.1101/gad.471408;
RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT "Regulation of muscle development by DPF3, a novel histone acetylation and
RT methylation reader of the BAF chromatin remodeling complex.";
RL Genes Dev. 22:2370-2384(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-81 AND ARG-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-226, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=22952240; DOI=10.1074/jbc.r111.309302;
RA Euskirchen G., Auerbach R.K., Snyder M.;
RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
RT functions.";
RL J. Biol. Chem. 287:30897-30905(2012).
RN [22]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=26601204; DOI=10.1126/sciadv.1500447;
RA Kadoch C., Crabtree G.R.;
RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic
RT insights gained from human genomics.";
RL Sci. Adv. 1:E1500447-E1500447(2015).
RN [23]
RP FUNCTION, INVOLVEMENT IN SGD2, AND INTERACTION WITH CEBPE.
RX PubMed=28369036; DOI=10.1038/ng.3833;
RA Witzel M., Petersheim D., Fan Y., Bahrami E., Racek T., Rohlfs M.,
RA Puchalka J., Mertes C., Gagneur J., Ziegenhain C., Enard W.,
RA Stray-Pedersen A., Arkwright P.D., Abboud M.R., Pazhakh V., Lieschke G.J.,
RA Krawitz P.M., Dahlhoff M., Schneider M.R., Wolf E., Horny H.P., Schmidt H.,
RA Schaeffer A.A., Klein C.;
RT "Chromatin-remodeling factor SMARCD2 regulates transcriptional networks
RT controlling differentiation of neutrophil granulocytes.";
RL Nat. Genet. 49:742-752(2017).
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 (PubMed:22952240, PubMed:26601204). Critical regulator of
CC myeloid differentiation, controlling granulocytopoiesis and the
CC expression of genes involved in neutrophil granule formation
CC (PubMed:28369036). {ECO:0000269|PubMed:28369036,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
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 (PubMed:22952240). Component of the BAF complex, which
CC includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B,
CC SMARCA2/BRM, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (PubMed:18765789). In
CC muscle cells, the BAF complex also contains DPF3. Component of the
CC SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of
CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C,
CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin
CC (ACTB) (PubMed:22952240, PubMed:26601204). Interacts with UNKL
CC (PubMed:20148946). Interacts with CEBPE (PubMed:28369036).
CC {ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20148946,
CC ECO:0000269|PubMed:28369036, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q92925; Q9H9P5: UNKL; NbExp=2; IntAct=EBI-358441, EBI-7797561;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92925-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92925-2; Sequence=VSP_040531, VSP_040532;
CC Name=3;
CC IsoId=Q92925-3; Sequence=VSP_040530;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in the pancreas.
CC {ECO:0000269|PubMed:8804307}.
CC -!- PTM: Ubiquitinated through a signaling process involving RAC1 and the
CC RING finger protein UNKL. {ECO:0000269|PubMed:20148946}.
CC -!- DISEASE: Specific granule deficiency 2 (SGD2) [MIM:617475]: A form of
CC specific granule deficiency, an autosomal recessive disorder
CC characterized by recurrent pyogenic infections, defective neutrophil
CC chemotaxis and bactericidal activity, and lack of neutrophil secondary
CC granule proteins. SGD2 is due to defective neutrophil development. Bone
CC marrow findings include hypercellularity, abnormal megakaryocytes, and
CC features of progressive myelofibrosis with blasts. Some patients may
CC have additional findings, including delayed development, mild
CC dysmorphic features, and distal skeletal anomalies.
CC {ECO:0000269|PubMed:28369036}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by aberrant splicing sites.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50696.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF20280.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U66618; AAC50696.1; ALT_INIT; mRNA.
DR EMBL; AK300939; BAG62568.1; -; mRNA.
DR EMBL; AK303951; BAG64878.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94267.1; -; Genomic_DNA.
DR EMBL; BC018953; AAH18953.2; -; mRNA.
DR EMBL; BC142963; AAI42964.1; -; mRNA.
DR EMBL; AF113019; AAF20280.1; ALT_INIT; mRNA.
DR CCDS; CCDS45756.1; -. [Q92925-1]
DR CCDS; CCDS82188.1; -. [Q92925-3]
DR RefSeq; NP_001091896.1; NM_001098426.1. [Q92925-1]
DR RefSeq; NP_001317369.1; NM_001330440.1. [Q92925-3]
DR AlphaFoldDB; Q92925; -.
DR SMR; Q92925; -.
DR BioGRID; 112487; 159.
DR ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1203; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1220; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR CORUM; Q92925; -.
DR DIP; DIP-31182N; -.
DR IntAct; Q92925; 83.
DR MINT; Q92925; -.
DR STRING; 9606.ENSP00000392617; -.
DR GlyGen; Q92925; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q92925; -.
DR PhosphoSitePlus; Q92925; -.
DR BioMuta; SMARCD2; -.
DR DMDM; 322510105; -.
DR EPD; Q92925; -.
DR jPOST; Q92925; -.
DR MassIVE; Q92925; -.
DR MaxQB; Q92925; -.
DR PaxDb; Q92925; -.
DR PeptideAtlas; Q92925; -.
DR PRIDE; Q92925; -.
DR ProteomicsDB; 75606; -. [Q92925-1]
DR ProteomicsDB; 75607; -. [Q92925-2]
DR ProteomicsDB; 75608; -. [Q92925-3]
DR Antibodypedia; 9431; 152 antibodies from 29 providers.
DR DNASU; 6603; -.
DR Ensembl; ENST00000323347.14; ENSP00000318451.10; ENSG00000108604.17. [Q92925-3]
DR Ensembl; ENST00000448276.7; ENSP00000392617.2; ENSG00000108604.17. [Q92925-1]
DR GeneID; 6603; -.
DR KEGG; hsa:6603; -.
DR MANE-Select; ENST00000448276.7; ENSP00000392617.2; NM_001098426.2; NP_001091896.1.
DR UCSC; uc010deb.2; human. [Q92925-1]
DR CTD; 6603; -.
DR DisGeNET; 6603; -.
DR GeneCards; SMARCD2; -.
DR HGNC; HGNC:11107; SMARCD2.
DR HPA; ENSG00000108604; Low tissue specificity.
DR MalaCards; SMARCD2; -.
DR MIM; 601736; gene.
DR MIM; 617475; phenotype.
DR neXtProt; NX_Q92925; -.
DR OpenTargets; ENSG00000108604; -.
DR Orphanet; 169142; Recurrent infection due to specific granule deficiency.
DR PharmGKB; PA35957; -.
DR VEuPathDB; HostDB:ENSG00000108604; -.
DR eggNOG; KOG2570; Eukaryota.
DR GeneTree; ENSGT00940000158654; -.
DR InParanoid; Q92925; -.
DR OMA; LMGIWEY; -.
DR OrthoDB; 1027566at2759; -.
DR PhylomeDB; Q92925; -.
DR TreeFam; TF106486; -.
DR PathwayCommons; Q92925; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; Q92925; -.
DR BioGRID-ORCS; 6603; 62 hits in 1088 CRISPR screens.
DR ChiTaRS; SMARCD2; human.
DR GeneWiki; SMARCD2; -.
DR GenomeRNAi; 6603; -.
DR Pharos; Q92925; Tbio.
DR PRO; PR:Q92925; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92925; protein.
DR Bgee; ENSG00000108604; Expressed in skin of abdomen and 167 other tissues.
DR ExpressionAtlas; Q92925; baseline and differential.
DR Genevisible; Q92925; HS.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
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_0000071985"
FT DOMAIN 306..383
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 205..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 104
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..71
FT /note="MSGRGAGGFPLPPLSPGGGAVAAALGAPPPPAGPGMLPGPALRGPGPAGGVG
FT GPGAAAFRPMGPAGPAAQY -> MGRRVGVEVTPRWAPQKCQGARP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040530"
FT VAR_SEQ 48..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8804307"
FT /id="VSP_040531"
FT VAR_SEQ 86..123
FT /note="GLQVGPPAGSPFGAAAPLRPGMPPTMMDPFRKRLLVPQ -> RLAGGTPCWL
FT PIWCSSSASTWHPTHHDGSIPKTPACAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8804307"
FT /id="VSP_040532"
FT CONFLICT 11
FT /note="L -> V (in Ref. 1; AAC50696)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="P -> Q (in Ref. 5; AAI42964)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="N -> G (in Ref. 1; AAC50696)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..276
FT /note="HR -> YW (in Ref. 1; AAC50696)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="M -> T (in Ref. 5; AAI42964)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="R -> S (in Ref. 5; AAI42964)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="E -> K (in Ref. 5; AAI42964)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="I -> T (in Ref. 1; AAC50696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 58921 MW; 8C92168AE7782814 CRC64;
MSGRGAGGFP LPPLSPGGGA VAAALGAPPP PAGPGMLPGP ALRGPGPAGG VGGPGAAAFR
PMGPAGPAAQ YQRPGMSPGN RMPMAGLQVG PPAGSPFGAA APLRPGMPPT MMDPFRKRLL
VPQAQPPMPA QRRGLKRRKM ADKVLPQRIR ELVPESQAYM DLLAFERKLD QTIARKRMEI
QEAIKKPLTQ KRKLRIYISN TFSPSKAEGD SAGTAGTPGG TPAGDKVASW ELRVEGKLLD
DPSKQKRKFS SFFKSLVIEL DKELYGPDNH LVEWHRMPTT QETDGFQVKR PGDLNVKCTL
LLMLDHQPPQ YKLDPRLARL LGVHTQTRAA IMQALWLYIK HNQLQDGHER EYINCNRYFR
QIFSCGRLRF SEIPMKLAGL LQHPDPIVIN HVISVDPNDQ KKTACYDIDV EVDDPLKAQM
SNFLASTTNQ QEIASLDVKI HETIESINQL KTQRDFMLSF STDPQDFIQE WLRSQRRDLK
IITDVIGNPE EERRAAFYHQ PWAQEAVGRH IFAKVQQRRQ ELEQVLGIRL T
