SF3B1_MOUSE
ID SF3B1_MOUSE Reviewed; 1304 AA.
AC Q99NB9; Q9CSK5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Splicing factor 3B subunit 1;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 155 kDa subunit;
DE Short=SF3b155;
DE AltName: Full=Spliceosome-associated protein 155;
DE Short=SAP 155;
GN Name=Sf3b1; Synonyms=Sap155;
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 [MRNA].
RC TISSUE=Ovary;
RX PubMed=11252167; DOI=10.1007/s003350010258;
RA Isono K., Abe K., Tomaru Y., Okazaki Y., Hayashizaki Y., Koseki H.;
RT "Molecular cloning, genetic mapping, and expression of the mouse Sf3b1
RT (SAP155) gene for the U2 snRNP component of spliceosome.";
RL Mamm. Genome 12:192-198(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-211; THR-267 AND
RP THR-326, AND 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 [4]
RP PHOSPHORYLATION AT THR-434.
RX PubMed=18938227; DOI=10.1016/j.neuroscience.2008.09.034;
RA Sitz J.H., Baumgaertel K., Haemmerle B., Papadopoulos C., Hekerman P.,
RA Tejedor F.J., Becker W., Lutz B.;
RT "The Down syndrome candidate dual-specificity tyrosine phosphorylation-
RT regulated kinase 1A phosphorylates the neurodegeneration-related septin
RT 4.";
RL Neuroscience 157:596-605(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-142; THR-207;
RP THR-211; THR-223; THR-227; SER-229; THR-235; THR-244; THR-248; THR-257;
RP THR-261; THR-267; THR-273; THR-278; SER-287; THR-296; THR-303; THR-313;
RP THR-326; THR-328; SER-332; THR-341; SER-344; THR-350; SER-400; THR-434;
RP THR-436 AND SER-488, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, 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 [7]
RP CITRULLINATION AT ARG-157.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [8]
RP FUNCTION.
RX PubMed=26255770; DOI=10.1016/j.cell.2015.07.008;
RA Du P., Wang L., Sliz P., Gregory R.I.;
RT "A biogenesis step upstream of microprocessor controls miR-17~92
RT expression.";
RL Cell 162:885-899(2015).
RN [9]
RP INTERACTION WITH ZRSR1.
RX PubMed=29617656; DOI=10.1016/j.celrep.2018.03.028;
RA Horiuchi K., Perez-Cerezales S., Papasaikas P., Ramos-Ibeas P.,
RA Lopez-Cardona A.P., Laguna-Barraza R., Fonseca Balvis N., Pericuesta E.,
RA Fernandez-Gonzalez R., Planells B., Viera A., Suja J.A., Ross P.J.,
RA Alen F., Orio L., Rodriguez de Fonseca F., Pintado B., Valcarcel J.,
RA Gutierrez-Adan A.;
RT "Impaired spermatogenesis, muscle, and erythrocyte function in U12 intron
RT splicing-defective zrsr1 mutant mice.";
RL Cell Rep. 23:143-155(2018).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex. SF3B complex is required for 'A' complex assembly
CC formed by the stable binding of U2 snRNP to the branchpoint sequence
CC (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex
CC upstream of the branch site is essential, it may anchor U2 snRNP to the
CC pre-mRNA. Together with other U2 snRNP complex components may also play
CC a role in the selective processing of microRNAs (miRNAs) from the long
CC primary miRNA transcript, pri-miR-17-92 (PubMed:26255770). May also be
CC involved in the assembly of the 'E' complex. Belongs also to the minor
CC U12-dependent spliceosome, which is involved in the splicing of rare
CC class of nuclear pre-mRNA intron. {ECO:0000250|UniProtKB:O75533,
CC ECO:0000269|PubMed:26255770}.
CC -!- SUBUNIT: Component of the B-WICH complex, at least composed of
CC SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21.
CC Identified in the spliceosome C complex. Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome. Component of splicing
CC factor SF3B complex which is composed of at least eight subunits;
CC SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42. SF3B
CC associates with the splicing factor SF3A and a 12S RNA unit to form the
CC U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts
CC directly with the splicing factor U2AF. Within the SF3B complex
CC interacts directly (via HEAT domain) with SF3B3, SF3B5 and (via HEAT
CC domain) with PHF5A. Interacts directly with SF3B6. The SF3B complex
CC composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A
CC interacts with U2AF2. Phosphorylated form interacts with PPP1R8.
CC Interacts with PQBP1. Interacts with RBM17. Interacts with RBM39.
CC Interacts with SETX. Interacts with RBM15. Interacts with ZRSR1
CC (PubMed:29617656). Interacts with USH1G (By similarity).
CC {ECO:0000250|UniProtKB:O75533, ECO:0000269|PubMed:29617656}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75533}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O75533}. Note=During mitosis,
CC transiently dispersed from the nuclear speckles to the cytoplasm.
CC {ECO:0000250|UniProtKB:O75533}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated (By similarity). Phosphorylation occurs
CC concomitantly with the splicing catalytic steps (By similarity).
CC Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent
CC kinases promotes interaction with PPP1R8 during mitosis (By
CC similarity). {ECO:0000250|UniProtKB:O75533}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the SF3B1 family. {ECO:0000305}.
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DR EMBL; AB037890; BAB40140.1; -; mRNA.
DR EMBL; AK012632; BAB28369.1; -; mRNA.
DR AlphaFoldDB; Q99NB9; -.
DR BMRB; Q99NB9; -.
DR SMR; Q99NB9; -.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR IntAct; Q99NB9; 2.
DR MINT; Q99NB9; -.
DR STRING; 10090.ENSMUSP00000027127; -.
DR iPTMnet; Q99NB9; -.
DR PhosphoSitePlus; Q99NB9; -.
DR SwissPalm; Q99NB9; -.
DR EPD; Q99NB9; -.
DR jPOST; Q99NB9; -.
DR MaxQB; Q99NB9; -.
DR PaxDb; Q99NB9; -.
DR PRIDE; Q99NB9; -.
DR ProteomicsDB; 261176; -.
DR MGI; MGI:1932339; Sf3b1.
DR eggNOG; KOG0213; Eukaryota.
DR InParanoid; Q99NB9; -.
DR PhylomeDB; Q99NB9; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR ChiTaRS; Sf3b1; mouse.
DR PRO; PR:Q99NB9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99NB9; protein.
DR GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0034693; C:U11/U12 snRNP; ISO:MGI.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISO:MGI.
DR GO; GO:0005686; C:U2 snRNP; ISO:MGI.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISO:MGI.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0005684; C:U2-type spliceosomal complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:1990935; F:splicing factor binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015016; SF3b_su1.
DR InterPro; IPR038737; SF3b_su1-like.
DR PANTHER; PTHR12097; PTHR12097; 2.
DR Pfam; PF08920; SF3b1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Citrullination; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spliceosome; Ubl conjugation.
FT CHAIN 1..1304
FT /note="Splicing factor 3B subunit 1"
FT /id="PRO_0000174324"
FT REPEAT 529..568
FT /note="HEAT 1"
FT REPEAT 569..603
FT /note="HEAT 2"
FT REPEAT 604..641
FT /note="HEAT 3"
FT REPEAT 643..677
FT /note="HEAT 4"
FT REPEAT 680..718
FT /note="HEAT 5"
FT REPEAT 763..801
FT /note="HEAT 6"
FT REPEAT 843..881
FT /note="HEAT 7"
FT REPEAT 1010..1048
FT /note="HEAT 8"
FT REPEAT 1052..1090
FT /note="HEAT 9"
FT REPEAT 1122..1160
FT /note="HEAT 10"
FT REPEAT 1163..1201
FT /note="HEAT 11"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..491
FT /note="Interaction with PPP1R8"
FT /evidence="ECO:0000250"
FT REGION 547..550
FT /note="Interaction with PHF5A"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT REGION 1156..1157
FT /note="Interaction with PHF5A"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT REGION 1248..1304
FT /note="Interaction with SF3B3 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT COMPBIAS 104..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 469
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 587
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 592
FT /note="Interaction with PHF5A"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 602
FT /note="Interaction with SF3B3"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 677
FT /note="Interaction with SF3B3"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 1035
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 1049
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 1141
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT SITE 1205
FT /note="Interaction with SF3B3"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 125
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 214
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 434
FT /note="Phosphothreonine; by DYRK1A"
FT /evidence="ECO:0000269|PubMed:18938227,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 554
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT MOD_RES 562
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75533"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75533"
SQ SEQUENCE 1304 AA; 145816 MW; 12F051757D2A2DEE CRC64;
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA
TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK
KHRRTMIISP ERLDPFADGG KTPDPKMNAR TYMDVMREQH LTKEEREIRQ QLAEKAKAGE
LKVVNGAAAS QPPSKRKRRW DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK
GSETPGATPG SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE
RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST PVLTPGKTPI
GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS DEELDAMFPE GYKVLPPPAG
YVPIRTPARK LTATPTPLGG MTGFHMQTED RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV
DVDESTLSPE EQKERKIMKL LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM
SPTLEDQERH LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL
AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA VCKSKKSWQA
RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK VRTISALAIA ALAEAATPYG
IESFDSVLKP LWKGIRQHRG KGLAAFLKAI GYLIPLMDAE YANYYTREVM LILIREFQSP
DEEMKKIVLK VVKQCCGTDG VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL
ANKVGAAEII SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF
QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ AADLISRTAV
VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI VNVIGMHKMT PPIKDLLPRL
TPILKNRHEK VQENCIDLVG RIADRGAEYV SAREWMRICF ELLELLKAHK KAIRRATVNT
FGYIAKAIGP HDVLATLLNN LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE
LNVQNGVLKS LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY
GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC LQGLFHPARK
VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYDL DYIL
