SMRC2_HUMAN
ID SMRC2_HUMAN Reviewed; 1214 AA.
AC Q8TAQ2; F8VTJ5; Q59GV3; Q92923; Q96E12; Q96GY4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=SWI/SNF complex subunit SMARCC2;
DE AltName: Full=BRG1-associated factor 170;
DE Short=BAF170;
DE AltName: Full=SWI/SNF complex 170 kDa subunit;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2;
GN Name=SMARCC2; Synonyms=BAF170;
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 1).
RC TISSUE=T-cell;
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] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Colon, and Duodenum;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-286; SER-302;
RP SER-304 AND SER-347, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, AND IDENTIFICATION BY MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-304; SER-306;
RP SER-347; THR-548 AND SER-813, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302; SER-304 AND
RP SER-347, AND IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302; SER-347;
RP THR-548 AND SER-813, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-347, AND
RP IDENTIFICATION BY 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-848, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-566 AND LYS-704, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-564; LYS-566; LYS-568; LYS-592;
RP LYS-704; LYS-787 AND LYS-848, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP STIMULATION OF THE CHROMATIN-REMODELING ACTIVITY OF SMARCA4.
RX PubMed=10078207; DOI=10.1016/s1097-2765(00)80315-9;
RA Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.;
RT "Reconstitution of a core chromatin remodeling complex from SWI/SNF
RT subunits.";
RL Mol. Cell 3:247-253(1999).
RN [19]
RP FUNCTION.
RX PubMed=11018012; DOI=10.1101/gad.828000;
RA Kadam S., McAlpine G.S., Phelan M.L., Kingston R.E., Jones K.A.,
RA Emerson B.M.;
RT "Functional selectivity of recombinant mammalian SWI/SNF subunits.";
RL Genes Dev. 14:2441-2451(2000).
RN [20]
RP INTERACTION WITH SIN3A.
RX PubMed=11238380; DOI=10.1101/gad.872801;
RA Sif S., Saurin A.J., Imbalzano A.N., Kingston R.E.;
RT "Purification and characterization of mSin3A-containing Brg1 and hBrm
RT chromatin remodeling complexes.";
RL Genes Dev. 15:603-618(2001).
RN [21]
RP INTERACTION WITH RCOR1.
RX PubMed=12192000; DOI=10.1074/jbc.m205691200;
RA Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G., Rosenfeld M.G.,
RA Anderson M.E., Mandel G.;
RT "REST repression of neuronal genes requires components of the hSWI.SNF
RT complex.";
RL J. Biol. Chem. 277:41038-41045(2002).
RN [22]
RP INTERACTION WITH SMARD1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [23]
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 [24]
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 [25]
RP INTERACTION WITH ERCC6.
RX PubMed=24874740; DOI=10.1038/cddis.2014.228;
RA Ciaffardini F., Nicolai S., Caputo M., Canu G., Paccosi E., Costantino M.,
RA Frontini M., Balajee A.S., Proietti-De-Santis L.;
RT "The cockayne syndrome B protein is essential for neuronal differentiation
RT and neuritogenesis.";
RL Cell Death Dis. 5:E1268-E1268(2014).
RN [26]
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 [27]
RP INTERACTION WITH DPF2.
RX PubMed=28533407; DOI=10.1073/pnas.1700328114;
RA Huber F.M., Greenblatt S.M., Davenport A.M., Martinez C., Xu Y., Vu L.P.,
RA Nimer S.D., Hoelz A.;
RT "Histone-binding of DPF2 mediates its repressive role in myeloid
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6016-6021(2017).
RN [28]
RP INVOLVEMENT IN CSS8, AND VARIANTS CSS8 ASP-134; 241-TRP--GLN-1214 DEL;
RP PRO-609; PRO-610; PRO-613; ARG-635; VAL-896 AND GLY-900.
RX PubMed=30580808; DOI=10.1016/j.ajhg.2018.11.007;
RG Undiagnosed Diseases Network;
RA Machol K., Rousseau J., Ehresmann S., Garcia T., Nguyen T.T.M.,
RA Spillmann R.C., Sullivan J.A., Shashi V., Jiang Y.H., Stong N., Fiala E.,
RA Willing M., Pfundt R., Kleefstra T., Cho M.T., McLaughlin H.,
RA Rosello Piera M., Orellana C., Martinez F., Caro-Llopis A., Monfort S.,
RA Roscioli T., Nixon C.Y., Buckley M.F., Turner A., Jones W.D.,
RA van Hasselt P.M., Hofstede F.C., van Gassen K.L.I., Brooks A.S.,
RA van Slegtenhorst M.A., Lachlan K., Sebastian J., Madan-Khetarpal S.,
RA Sonal D., Sakkubai N., Thevenon J., Faivre L., Maurel A., Petrovski S.,
RA Krantz I.D., Tarpinian J.M., Rosenfeld J.A., Lee B.H., Campeau P.M.;
RT "Expanding the Spectrum of BAF-Related Disorders: De Novo Variants in
RT SMARCC2 Cause a Syndrome with Intellectual Disability and Developmental
RT Delay.";
RL Am. J. Hum. Genet. 104:164-178(2019).
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:11018012). Can stimulate the ATPase activity of the
CC catalytic subunit of these complexes (PubMed:10078207). May be required
CC for CoREST dependent repression of neuronal specific gene promoters in
CC non-neuronal cells (PubMed:12192000). Belongs to the neural
CC progenitors-specific chromatin remodeling complex (npBAF complex) and
CC the neuron-specific chromatin remodeling complex (nBAF complex). During
CC neural development a switch from a stem/progenitor to a postmitotic
CC chromatin remodeling mechanism occurs as neurons exit the cell cycle
CC and become committed to their adult state. The transition from
CC proliferating neural stem/progenitor cells to postmitotic neurons
CC requires a switch in subunit composition of the npBAF and nBAF
CC complexes. As neural progenitors exit mitosis and differentiate into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth
CC (By similarity). Critical regulator of myeloid differentiation,
CC controlling granulocytopoiesis and the expression of genes involved in
CC neutrophil granule formation (By similarity).
CC {ECO:0000250|UniProtKB:Q6PDG5, ECO:0000269|PubMed:10078207,
CC ECO:0000269|PubMed:11018012, ECO:0000269|PubMed:12192000,
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 (Probable). Component of the BAF complex, which includes at
CC least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC 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. In muscle cells, the
CC BAF complex also contains DPF3 (PubMed:18765789). Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC DPF3/BAF45C, ACTL6B/BAF53B and actin. Component of the SWI/SNF-B (PBAF)
CC chromatin 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 (PubMed:22952240,
CC PubMed:26601204). May also interact with the SIN3A histone deacetylase
CC transcription repressor complex in conjunction with SMARCA2 and SMARCA4
CC (PubMed:11238380). Interacts with SMARD1 (PubMed:12917342). Interacts
CC with KDM6B (By similarity). Interaction with RCOR1 (PubMed:12192000).
CC Interacts with DPF2 (PubMed:28533407). Interacts with ERCC6
CC (PubMed:24874740). Interacts with FOS (By similarity).
CC {ECO:0000250|UniProtKB:Q6PDG5, ECO:0000269|PubMed:11238380,
CC ECO:0000269|PubMed:12192000, ECO:0000269|PubMed:12917342,
CC ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:24874740,
CC ECO:0000269|PubMed:28533407, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q8TAQ2; Q9P2D1: CHD7; NbExp=4; IntAct=EBI-357418, EBI-3951683;
CC Q8TAQ2; P51531: SMARCA2; NbExp=2; IntAct=EBI-357418, EBI-679562;
CC Q8TAQ2; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-357418, EBI-750109;
CC Q8TAQ2-2; P42858: HTT; NbExp=3; IntAct=EBI-11990400, EBI-466029;
CC Q8TAQ2-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-11990400, EBI-3044087;
CC Q8TAQ2-2; Q12824-2: SMARCB1; NbExp=4; IntAct=EBI-11990400, EBI-358436;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SMARCC2a;
CC IsoId=Q8TAQ2-1; Sequence=Displayed;
CC Name=2; Synonyms=SMARCC2b;
CC IsoId=Q8TAQ2-2; Sequence=VSP_012490, VSP_012491;
CC Name=3;
CC IsoId=Q8TAQ2-3; Sequence=VSP_012490, VSP_044647;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Mono-ADP-ribosylation at Lys-312 by SIRT6 promotes recruitment to
CC the enhancer region of the Heme oxygenase-1 (HO-1) locus, leading to
CC transcription activation of the locus. {ECO:0000250|UniProtKB:Q6PDG5}.
CC -!- DISEASE: Coffin-Siris syndrome 8 (CSS8) [MIM:618362]: A form of Coffin-
CC Siris syndrome, a congenital multiple malformation syndrome with broad
CC phenotypic and genetic variability. Cardinal features are intellectual
CC disability, coarse facial features, hypertrichosis, and hypoplastic or
CC absent fifth digit nails or phalanges. Additional features include
CC malformations of the cardiac, gastrointestinal, genitourinary, and/or
CC central nervous systems. Sucking/feeding difficulties, poor growth,
CC ophthalmologic abnormalities, hearing impairment, and spinal anomalies
CC are common findings. CSS8 patients manifest prominent speech
CC impairment, hypotonia, feeding difficulties, behavioral abnormalities,
CC and dysmorphic features such as hypertrichosis, thick eyebrows, thin
CC upper lip vermilion, and upturned nose. CSS8 inheritance is autosomal
CC dominant. {ECO:0000269|PubMed:30580808}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92243.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; U66616; AAC50694.1; -; mRNA.
DR EMBL; BT009924; AAP88926.1; -; mRNA.
DR EMBL; AB209006; BAD92243.1; ALT_INIT; mRNA.
DR EMBL; AC073896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009067; AAH09067.1; -; mRNA.
DR EMBL; BC013045; AAH13045.1; -; mRNA.
DR EMBL; BC026222; AAH26222.1; -; mRNA.
DR CCDS; CCDS55835.1; -. [Q8TAQ2-3]
DR CCDS; CCDS8907.1; -. [Q8TAQ2-1]
DR CCDS; CCDS8908.1; -. [Q8TAQ2-2]
DR RefSeq; NP_001123892.1; NM_001130420.2. [Q8TAQ2-3]
DR RefSeq; NP_001317217.1; NM_001330288.1.
DR RefSeq; NP_003066.2; NM_003075.4. [Q8TAQ2-1]
DR RefSeq; NP_620706.1; NM_139067.3. [Q8TAQ2-2]
DR PDB; 6KAG; X-ray; 2.60 A; B/C=325-518.
DR PDB; 6LTH; EM; 3.00 A; N/O=1-1214.
DR PDB; 6LTJ; EM; 3.70 A; N/O=1-1214.
DR PDBsum; 6KAG; -.
DR PDBsum; 6LTH; -.
DR PDBsum; 6LTJ; -.
DR AlphaFoldDB; Q8TAQ2; -.
DR SMR; Q8TAQ2; -.
DR BioGRID; 112485; 235.
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-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 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-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, 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; Q8TAQ2; -.
DR DIP; DIP-27611N; -.
DR IntAct; Q8TAQ2; 113.
DR MINT; Q8TAQ2; -.
DR STRING; 9606.ENSP00000267064; -.
DR GlyGen; Q8TAQ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TAQ2; -.
DR PhosphoSitePlus; Q8TAQ2; -.
DR BioMuta; SMARCC2; -.
DR DMDM; 57012959; -.
DR EPD; Q8TAQ2; -.
DR jPOST; Q8TAQ2; -.
DR MassIVE; Q8TAQ2; -.
DR MaxQB; Q8TAQ2; -.
DR PaxDb; Q8TAQ2; -.
DR PeptideAtlas; Q8TAQ2; -.
DR PRIDE; Q8TAQ2; -.
DR ProteomicsDB; 28640; -.
DR ProteomicsDB; 73906; -. [Q8TAQ2-1]
DR ProteomicsDB; 73907; -. [Q8TAQ2-2]
DR ABCD; Q8TAQ2; 1 sequenced antibody.
DR Antibodypedia; 3811; 263 antibodies from 31 providers.
DR DNASU; 6601; -.
DR Ensembl; ENST00000267064.8; ENSP00000267064.4; ENSG00000139613.12. [Q8TAQ2-1]
DR Ensembl; ENST00000347471.8; ENSP00000302919.4; ENSG00000139613.12. [Q8TAQ2-2]
DR Ensembl; ENST00000394023.7; ENSP00000377591.3; ENSG00000139613.12. [Q8TAQ2-3]
DR GeneID; 6601; -.
DR KEGG; hsa:6601; -.
DR UCSC; uc001ska.4; human. [Q8TAQ2-1]
DR CTD; 6601; -.
DR DisGeNET; 6601; -.
DR GeneCards; SMARCC2; -.
DR GeneReviews; SMARCC2; -.
DR HGNC; HGNC:11105; SMARCC2.
DR HPA; ENSG00000139613; Low tissue specificity.
DR MalaCards; SMARCC2; -.
DR MIM; 601734; gene.
DR MIM; 618362; phenotype.
DR neXtProt; NX_Q8TAQ2; -.
DR OpenTargets; ENSG00000139613; -.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR PharmGKB; PA35955; -.
DR VEuPathDB; HostDB:ENSG00000139613; -.
DR eggNOG; KOG1279; Eukaryota.
DR GeneTree; ENSGT00940000155746; -.
DR HOGENOM; CLU_004447_0_1_1; -.
DR InParanoid; Q8TAQ2; -.
DR OrthoDB; 683891at2759; -.
DR PhylomeDB; Q8TAQ2; -.
DR TreeFam; TF314710; -.
DR PathwayCommons; Q8TAQ2; -.
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; Q8TAQ2; -.
DR SIGNOR; Q8TAQ2; -.
DR BioGRID-ORCS; 6601; 31 hits in 1084 CRISPR screens.
DR ChiTaRS; SMARCC2; human.
DR GeneWiki; SMARCC2; -.
DR GenomeRNAi; 6601; -.
DR Pharos; Q8TAQ2; Tbio.
DR PRO; PR:Q8TAQ2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TAQ2; protein.
DR Bgee; ENSG00000139613; Expressed in ventricular zone and 209 other tissues.
DR ExpressionAtlas; Q8TAQ2; baseline and differential.
DR Genevisible; Q8TAQ2; 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:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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; NAS:BHF-UCL.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR038044; SMARCC2.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR032450; SMARCC_N.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR032448; SWIRM-assoc.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12802:SF105; PTHR12802:SF105; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR Pfam; PF16496; SWIRM-assoc_2; 1.
DR Pfam; PF16498; SWIRM-assoc_3; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Chromatin regulator; Coiled coil; Disease variant; Intellectual disability;
KW Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1214
FT /note="SWI/SNF complex subunit SMARCC2"
FT /id="PRO_0000197117"
FT DOMAIN 424..521
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 596..647
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 257..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 907..934
FT /evidence="ECO:0000255"
FT COMPBIAS 258..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 312
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDG5"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDG5"
FT MOD_RES 548
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 564
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 566
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 568
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 787
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 848
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 550
FT /note="Q -> QGRQVDADTKAGRKGKELDDLVPETAKGKPEL (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_012490"
FT VAR_SEQ 1075..1189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_012491"
FT VAR_SEQ 1075..1167
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044647"
FT VARIANT 134
FT /note="N -> D (in CSS8)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082077"
FT VARIANT 241..1214
FT /note="Missing (in CSS8)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082078"
FT VARIANT 609
FT /note="L -> P (in CSS8)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082079"
FT VARIANT 610
FT /note="L -> P (in CSS8; dbSNP:rs1565903367)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082080"
FT VARIANT 613
FT /note="L -> P (in CSS8)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082081"
FT VARIANT 635
FT /note="C -> R (in CSS8; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082082"
FT VARIANT 896
FT /note="M -> V (in CSS8; unknown pathological significance;
FT dbSNP:rs1565896447)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082083"
FT VARIANT 900
FT /note="E -> G (in CSS8; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30580808"
FT /id="VAR_082084"
FT CONFLICT 311..316
FT /note="AKKKNA -> VKEEKC (in Ref. 1; AAC50694)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="M -> S (in Ref. 1; AAC50694)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="V -> A (in Ref. 1; AAC50694)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="L -> F (in Ref. 2; AAP88926 and 5; AAH13045)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="A -> P (in Ref. 1; AAC50694)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="A -> R (in Ref. 1; AAC50694)"
FT /evidence="ECO:0000305"
FT CONFLICT 1117..1126
FT /note="HGHHHHLPFA -> MGSPPSPVR (in Ref. 1; AAC50694)"
FT /evidence="ECO:0000305"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:6KAG"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 440..445
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 459..475
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 483..487
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 494..506
FT /evidence="ECO:0007829|PDB:6KAG"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6KAG"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 603..615
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 621..627
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 632..640
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 646..649
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 672..681
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 686..701
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 712..715
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 859..948
FT /evidence="ECO:0007829|PDB:6LTH"
SQ SEQUENCE 1214 AA; 132879 MW; EEFC1042A9296320 CRC64;
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ
EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN
VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDII KRHQGTVTED KNNASHVVYP
VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK
WILDTDTFNE WMNEEDYEVN DDKNPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK
RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT
VNTKKDSESA PVKGGTMTDL DEQEDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ
THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY
LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG
LVPLQPKTPQ QTSASQQMLN FPDKGKEKPT DMQNFGLRTD MYTKKNVPSK SKAAASATRE
WTEQETLLLL EALEMYKDDW NKVSEHVGSR TQDECILHFL RLPIEDPYLE DSEASLGPLA
YQPIPFSQSG NPVMSTVAFL ASVVDPRVAS AAAKSALEEF SKMKEEVPTA LVEAHVRKVE
EAAKVTGKAD PAFGLESSGI AGTTSDEPER IEESGNDEAR VEGQATDEKK EPKEPREGGG
AIEEEAKEKT SEAPKKDEEK GKEGDSEKES EKSDGDPIVD PEKEKEPKEG QEEVLKEVVE
SEGERKTKVE RDIGEGNLST AAAAALAAAA VKAKHLAAVE ERKIKSLVAL LVETQMKKLE
IKLRHFEELE TIMDREREAL EYQRQQLLAD RQAFHMEQLK YAEMRARQQH FQQMHQQQQQ
PPPALPPGSQ PIPPTGAAGP PAVHGLAVAP ASVVPAPAGS GAPPGSLGPS EQIGQAGSTA
GPQQQQPAGA PQPGAVPPGV PPPGPHGPSP FPNQQTPPSM MPGAVPGSGH PGVAGNAPLG
LPFGMPPPPP PPAPSIIPFG SLADSISINL PAPPNLHGHH HHLPFAPGTL PPPNLPVSMA
NPLHPNLPAT TTMPSSLPLG PGLGSAAAQS PAIVAAVQGN LLPSASPLPD PGTPLPPDPT
APSPGTVTPV PPPQ
