PB1_MOUSE
ID PB1_MOUSE Reviewed; 1634 AA.
AC Q8BSQ9; E9QPW1; Q05C64; Q05CL6; Q7TMP1; Q7TNU2; Q9CV51;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein polybromo-1;
DE AltName: Full=BRG1-associated factor 180;
DE Short=BAF180;
GN Name=Pbrm1; Synonyms=Baf180, Pb1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-919 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 205-512 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHF10, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-355, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-353; SER-355; SER-498
RP AND SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-414, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [11]
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 [12]
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 [13]
RP STRUCTURE BY NMR OF 646-762.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fifth bromodomain from mouse polybromo-1.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Required for the stability of the SWI/SNF chromatin
CC remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of
CC cell proliferation. {ECO:0000250|UniProtKB:Q86U86,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin remodeling
CC complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5,
CC ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A,
CC SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
CC PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with PHF10/BAF45A (By
CC similarity). Interacts with acetylated 'Lys-14' of histone H3
CC (H3K14ac), and may also interact with other acetylated or methylated
CC Lys residues on histone H3 (By similarity).
CC {ECO:0000250|UniProtKB:Q86U86, ECO:0000269|PubMed:17640523,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BSQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BSQ9-2; Sequence=VSP_035471;
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the developing
CC spinal cord, brain and other embryonic tissues at 10.5 dpc-16.5 dpc.
CC {ECO:0000269|PubMed:17640523}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29037.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH55456.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=AAH55708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC154446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023452; AAH23452.1; -; mRNA.
DR EMBL; BC029037; AAH29037.1; ALT_TERM; mRNA.
DR EMBL; BC055456; AAH55456.1; ALT_TERM; mRNA.
DR EMBL; BC055708; AAH55708.1; ALT_INIT; mRNA.
DR EMBL; BF451491; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CN530699; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK009582; BAB26374.2; -; mRNA.
DR EMBL; AK030781; BAC27136.2; -; mRNA.
DR EMBL; AK030252; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK166588; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 2YQD; NMR; -; A=650-762.
DR PDBsum; 2YQD; -.
DR AlphaFoldDB; Q8BSQ9; -.
DR SMR; Q8BSQ9; -.
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 DIP; DIP-48885N; -.
DR IntAct; Q8BSQ9; 6.
DR MINT; Q8BSQ9; -.
DR STRING; 10090.ENSMUSP00000107727; -.
DR iPTMnet; Q8BSQ9; -.
DR PhosphoSitePlus; Q8BSQ9; -.
DR EPD; Q8BSQ9; -.
DR jPOST; Q8BSQ9; -.
DR MaxQB; Q8BSQ9; -.
DR PaxDb; Q8BSQ9; -.
DR PeptideAtlas; Q8BSQ9; -.
DR PRIDE; Q8BSQ9; -.
DR ProteomicsDB; 294334; -. [Q8BSQ9-1]
DR ProteomicsDB; 294335; -. [Q8BSQ9-2]
DR Antibodypedia; 2905; 188 antibodies from 29 providers.
DR Ensembl; ENSMUST00000112094; ENSMUSP00000107723; ENSMUSG00000042323. [Q8BSQ9-2]
DR Ensembl; ENSMUST00000112095; ENSMUSP00000107724; ENSMUSG00000042323. [Q8BSQ9-1]
DR UCSC; uc007swl.1; mouse. [Q8BSQ9-1]
DR UCSC; uc007swm.1; mouse. [Q8BSQ9-2]
DR MGI; MGI:1923998; Pbrm1.
DR VEuPathDB; HostDB:ENSMUSG00000042323; -.
DR eggNOG; KOG1827; Eukaryota.
DR GeneTree; ENSGT00390000003017; -.
DR InParanoid; Q8BSQ9; -.
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 ChiTaRS; Pbrm1; mouse.
DR EvolutionaryTrace; Q8BSQ9; -.
DR PRO; PR:Q8BSQ9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BSQ9; protein.
DR Bgee; ENSMUSG00000042323; Expressed in rostral migratory stream and 261 other tissues.
DR ExpressionAtlas; Q8BSQ9; baseline and differential.
DR Genevisible; Q8BSQ9; MM.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:MGI.
DR GO; GO:0016586; C:RSC-type complex; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; TAS:DFLAT.
DR GO; GO:0060948; P:cardiac vascular smooth muscle cell development; TAS:DFLAT.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0003349; P:epicardium-derived cardiac endothelial cell differentiation; TAS:DFLAT.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; TAS:DFLAT.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
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; TAS:DFLAT.
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; IC:ComplexPortal.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
DR CDD; cd05515; Bromo_polybromo_V; 1.
DR Gene3D; 1.20.920.10; -; 6.
DR Gene3D; 2.30.30.490; -; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037968; PBRM1_BD5.
DR InterPro; IPR037382; Rsc/polybromo.
DR PANTHER; PTHR16062; PTHR16062; 2.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 6.
DR Pfam; PF00505; HMG_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF47370; SSF47370; 6.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 5.
DR PROSITE; PS50014; BROMODOMAIN_2; 6.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..1634
FT /note="Protein polybromo-1"
FT /id="PRO_0000351134"
FT DOMAIN 64..134
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 200..270
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 400..470
FT /note="Bromo 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 538..608
FT /note="Bromo 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 676..746
FT /note="Bromo 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 792..862
FT /note="Bromo 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 956..1074
FT /note="BAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 1156..1272
FT /note="BAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DNA_BIND 1379..1447
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 134
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 414
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT MOD_RES 1289
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 653
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1398
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT CROSSLNK 1601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86U86"
FT VAR_SEQ 300..332
FT /note="RTASNLAAARLTGPSHNKSSLGEERNPTSKYYR -> S (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035471"
FT CONFLICT 417
FT /note="Y -> K (in Ref. 2; AAH23452)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="D -> E (in Ref. 3; BAC27136)"
FT /evidence="ECO:0000305"
FT HELIX 659..671
FT /evidence="ECO:0007829|PDB:2YQD"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:2YQD"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:2YQD"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:2YQD"
FT TURN 690..692
FT /evidence="ECO:0007829|PDB:2YQD"
FT HELIX 694..699
FT /evidence="ECO:0007829|PDB:2YQD"
FT HELIX 706..714
FT /evidence="ECO:0007829|PDB:2YQD"
FT HELIX 721..738
FT /evidence="ECO:0007829|PDB:2YQD"
FT HELIX 744..759
FT /evidence="ECO:0007829|PDB:2YQD"
SQ SEQUENCE 1634 AA; 187188 MW; A905963F22ECD75E CRC64;
MGSKRRRATS PSSSVSGDFD DGHHSVPTPG PSRKRRRLSN LPTVDPIAVC HELYNTIRDY
KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK LKMEEYDDVN LLTADFQLLF
NNAKAYYKPD SPEYKAACKL WDLYLRTRNE FVQKGEADDE DDDEDGQDNQ GTLADGSSPG
YLKEILEQLL EAIVVATNPS GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG
SYKSIHAMAK DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMTKSSLRIR
TASNLAAARL TGPSHNKSSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ YGSESEEDAA
LAAARYEEGE SEAESITSFM DVSNPFHQLY DTVRSCRNHQ GQLIAEPFFH LPSKKKYPDY
YQQIKMPISL QQIRTKLKNQ EYETLDHLEC DLNLMFENAK RYNVPNSAIY KRVLKLQQVM
QAKKKELARR DDIEDGDSMI SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR
RLCDLFMVKP SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMMEDM KLMFRNARHY
NEEGSQVYND AHILEKLLKD KRKELGPLPD DDDMASPKLK LSRKSGVSPK KSKYMTPMQQ
KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI KKPMDMEKIR SHMMANKYQD
IDSMVEDFVM MFNNACTYNE PESLIYKDAL VLHKVLLETR RDLEGDEDSH VPNVTLLIQE
LIHNLFVSVM SHQDDEGRCY SDSLAEIPAV DPNSPNKPPL TFDIIRKNVE SNRYRRLDLF
QEHMFEVLER ARRMNRTDSE IYEDAVELQQ FFIRIRDELC KNGEILLSPA LSYTTKHLHN
DVEKEKKEKL PKEIEEDKLK REEEKREAEK SEDSSGTTGL SGLHRTYSQD CSFKNSMYHV
GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR PNETFHLATR KFLEKEVFKS
DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI
SSVRFVPRDV PLPVVRVASV FANADKGDDE KNTDNSDDNR AEDNFNLEKE KEDVPVEMSN
GEPGCHYFEQ LRYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE
ETEHEPTKMF YKKEVFLSNL EETCPMSCIL GKCAVLSFKD FLSCRPTEIP ENDILLCESR
YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIIPQKE PSPLLEKKIQ LLEAKFAELE
GGDDDIEEMG EEDSEVIEAP SLPQLQTPLA NELDLMPYTP PQSTPKSAKG SAKKESSKRK
INMSGYILFS SEMRAVIKAQ HPDYSFGELS RLVGTEWRNL ETAKKAEYEG MMGGYPPGLP
PLQGPVDGLV SMGSMQPLHP GGPPPHHLPP GVPGLPGIPP PGVMNQGVAP MVGTPAPGGS
PYGQQVGVLG PPGQQAPPPY PGPHPAGPPV IQQPTTPMFV APPPKTQRLL HSEAYLKYIE
GLSAESNSIS KWDQTLAARR RDVHLSKEQE SRLPSHWLKS KGAHTTMADA LWRLRDLMLR
DTLNIRQAYN LENV
