ACINU_MOUSE
ID ACINU_MOUSE Reviewed; 1338 AA.
AC Q9JIX8; B8JJ87; Q9CSN7; Q9CSR9; Q9CSX7; Q9R046; Q9R047;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Apoptotic chromatin condensation inducer in the nucleus;
DE Short=Acinus;
GN Name=Acin1; Synonyms=Acinus;
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] (ISOFORMS 2 AND 3).
RX PubMed=10490026; DOI=10.1038/43678;
RA Sahara S., Aoto M., Eguchi Y., Imamoto N., Yoneda Y., Tsujimoto Y.;
RT "Acinus is a caspase-3-activated protein required for apoptotic chromatin
RT condensation.";
RL Nature 401:168-173(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Mamoru A., Setsuko S., Yoshihide T.;
RT "Molecular cloning of murine acinusL, a gene for apoptotic chromatin
RT condensation.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-1190 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 57-806 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Pancreatic islet;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-391; SER-479;
RP SER-491 AND SER-710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP INTERACTION WITH SRPK2.
RX PubMed=18559500; DOI=10.1158/0008-5472.can-08-0021;
RA Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J., Persson J.L.,
RA Ye K.;
RT "Serine/arginine protein-specific kinase 2 promotes leukemia cell
RT proliferation by phosphorylating acinus and regulating cyclin A1.";
RL Cancer Res. 68:4559-4570(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1003, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-710, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-491 AND SER-1003,
RP AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-387; SER-389;
RP SER-391; SER-413; THR-417; SER-454; SER-477; SER-479; SER-491; SER-497;
RP SER-710; SER-838; SER-898; SER-986 AND SER-1003, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-861, 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).
CC -!- FUNCTION: Auxiliary component of the splicing-dependent multiprotein
CC exon junction complex (EJC) deposited at splice junction on mRNAs. The
CC EJC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. Component of the ASAP complexes which bind
CC RNA in a sequence-independent manner and are proposed to be recruited
CC to the EJC prior to or during the splicing process and to regulate
CC specific excision of introns in specific transcription subsets; ACIN1
CC confers RNA-binding to the complex. The ASAP complex can inhibit RNA
CC processing during in vitro splicing reactions. The ASAP complex
CC promotes apoptosis and is disassembled after induction of apoptosis.
CC Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other
CC apoptotic genes); specifically inhibits formation of proapoptotic
CC isoforms such as Bcl-X(S); the activity is different from the
CC established EJC assembly and function. Induces apoptotic chromatin
CC condensation after activation by CASP3. Regulates cyclin A1, but not
CC cyclin A2, expression in leukemia cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-
CC associated protein) complexes consisting of RNPS1, SAP18 and different
CC isoforms of ACIN1; the association of SAP18 seems to require a
CC preformed RNPS1:ACIN1 complex. Interacts with API5. Interacts with
CC SRPK2 in a phosphorylation-dependent manner (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Phosphorylation
CC on Ser-1179 by SRPK2 redistributes it from the nuclear speckles to the
CC nucleoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=L;
CC IsoId=Q9JIX8-1; Sequence=Displayed;
CC Name=2; Synonyms=S;
CC IsoId=Q9JIX8-2; Sequence=VSP_004030, VSP_004033;
CC Name=3; Synonyms=S';
CC IsoId=Q9JIX8-3; Sequence=VSP_004031;
CC Name=4;
CC IsoId=Q9JIX8-4; Sequence=VSP_004032;
CC -!- PTM: Undergoes proteolytic cleavage; the processed form is active,
CC contrary to the uncleaved form. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-1179 by SRPK2 up-regulates its stimulatory
CC effect on cyclin A1. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF89661.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF124725; AAD56723.1; -; mRNA.
DR EMBL; AF124729; AAD56727.1; -; mRNA.
DR EMBL; AF168782; AAF89661.1; ALT_FRAME; mRNA.
DR EMBL; CT009512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK011698; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK012099; BAB28030.1; -; mRNA.
DR EMBL; AK012337; BAB28171.3; -; mRNA.
DR EMBL; AK050467; BAC34272.1; -; mRNA.
DR CCDS; CCDS27097.1; -. [Q9JIX8-1]
DR CCDS; CCDS49492.1; -. [Q9JIX8-2]
DR CCDS; CCDS56957.1; -. [Q9JIX8-3]
DR CCDS; CCDS88664.1; -. [Q9JIX8-4]
DR RefSeq; NP_001078942.2; NM_001085473.2.
DR RefSeq; NP_001229534.1; NM_001242605.1. [Q9JIX8-3]
DR RefSeq; NP_062513.3; NM_019567.3.
DR RefSeq; NP_075679.2; NM_023190.3. [Q9JIX8-1]
DR RefSeq; XP_006519361.1; XM_006519298.3.
DR RefSeq; XP_006519367.1; XM_006519304.3. [Q9JIX8-3]
DR AlphaFoldDB; Q9JIX8; -.
DR SMR; Q9JIX8; -.
DR BioGRID; 207849; 9.
DR IntAct; Q9JIX8; 8.
DR MINT; Q9JIX8; -.
DR STRING; 10090.ENSMUSP00000022793; -.
DR iPTMnet; Q9JIX8; -.
DR PhosphoSitePlus; Q9JIX8; -.
DR CPTAC; non-CPTAC-3629; -.
DR EPD; Q9JIX8; -.
DR jPOST; Q9JIX8; -.
DR MaxQB; Q9JIX8; -.
DR PaxDb; Q9JIX8; -.
DR PeptideAtlas; Q9JIX8; -.
DR PRIDE; Q9JIX8; -.
DR ProteomicsDB; 285927; -. [Q9JIX8-1]
DR ProteomicsDB; 285928; -. [Q9JIX8-2]
DR ProteomicsDB; 285929; -. [Q9JIX8-3]
DR ProteomicsDB; 285930; -. [Q9JIX8-4]
DR Antibodypedia; 63; 533 antibodies from 37 providers.
DR DNASU; 56215; -.
DR Ensembl; ENSMUST00000022793; ENSMUSP00000022793; ENSMUSG00000022185. [Q9JIX8-1]
DR Ensembl; ENSMUST00000111484; ENSMUSP00000107109; ENSMUSG00000022185. [Q9JIX8-4]
DR Ensembl; ENSMUST00000126166; ENSMUSP00000114546; ENSMUSG00000022185. [Q9JIX8-3]
DR Ensembl; ENSMUST00000148754; ENSMUSP00000122003; ENSMUSG00000022185. [Q9JIX8-2]
DR Ensembl; ENSMUST00000167015; ENSMUSP00000125776; ENSMUSG00000022185. [Q9JIX8-2]
DR GeneID; 56215; -.
DR KEGG; mmu:56215; -.
DR UCSC; uc007twr.2; mouse. [Q9JIX8-3]
DR UCSC; uc007twv.2; mouse. [Q9JIX8-1]
DR UCSC; uc007twx.2; mouse. [Q9JIX8-4]
DR UCSC; uc011zld.1; mouse. [Q9JIX8-2]
DR CTD; 22985; -.
DR MGI; MGI:1891824; Acin1.
DR VEuPathDB; HostDB:ENSMUSG00000022185; -.
DR eggNOG; KOG2416; Eukaryota.
DR GeneTree; ENSGT00710000106790; -.
DR HOGENOM; CLU_482284_0_0_1; -.
DR InParanoid; Q9JIX8; -.
DR OMA; DYHKGIR; -.
DR TreeFam; TF320727; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR BioGRID-ORCS; 56215; 12 hits in 76 CRISPR screens.
DR ChiTaRS; Acin1; mouse.
DR PRO; PR:Q9JIX8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JIX8; protein.
DR Bgee; ENSMUSG00000022185; Expressed in embryonic brain and 249 other tissues.
DR ExpressionAtlas; Q9JIX8; baseline and differential.
DR Genevisible; Q9JIX8; MM.
DR GO; GO:0061574; C:ASAP complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR CDD; cd12432; RRM_ACINU; 1.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034257; Acinus_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR032552; RSB_motif.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF16294; RSB_motif; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1338
FT /note="Apoptotic chromatin condensation inducer in the
FT nucleus"
FT /id="PRO_0000064437"
FT DOMAIN 72..106
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1236
FT /note="Sufficient for interaction with RNPS1 and SAP18 and
FT formation of th ASAP complex"
FT /evidence="ECO:0000250"
FT REGION 1226..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1191
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1093..1094
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 654
FT /note="N6,N6,N6-trimethyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 654
FT /note="N6,N6-dimethyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 861
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 975
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 1179
FT /note="Phosphoserine; by SRPK2 and PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 318
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 861
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 969
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 1046
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT CROSSLNK 1106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKV3"
FT VAR_SEQ 1..773
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10490026"
FT /id="VSP_004031"
FT VAR_SEQ 1..757
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10490026,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_004030"
FT VAR_SEQ 164..204
FT /note="EASAESEDEMTHPEGVASLLPPDFQSSLNRPELELSTHSPR -> G (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_004032"
FT VAR_SEQ 758..766
FT /note="ESERTHHTV -> MMFSDSRAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10490026,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_004033"
FT CONFLICT 244
FT /note="T -> A (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="T -> A (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="F -> L (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="G -> D (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="H -> Y (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="V -> A (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="S -> I (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="L -> P (in Ref. 2; AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="T -> A (in Ref. 1; AAD56723)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="Missing (in Ref. 4; BAB28030)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="R -> Q (in Ref. 1; AAD56723/AAD56727 and 2;
FT AAF89661)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="G -> R (in Ref. 4; BAB28030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1338 AA; 150719 MW; 683E56058723C9D8 CRC64;
MWGRKRPNSS GETRGILSGN RGVDYGSGRG QSGPFEGRWR KLPKMPEAVG TDPSTSRKMA
ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK RLKGALMLEN LQKHSTPHAA
FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ RLEREAREAA ELEEASAESE DEMTHPEGVA
SLLPPDFQSS LNRPELELST HSPRKSSSFS EEKGESDDEK PRKGERRSSR VRQAKSKLPE
YSQTAEEEED QETPSRNLRV RADRNLKIEE EEEEEEEEED DDDEEEEEVD EAQKSREAEA
PTLKQFEDEE GEERTRAKPE KVVDEKPLNI RSQEKGELEK GGRVTRSQEE ARRSHLARQQ
QEKETQIVSL PQEENEVKSS QSLEEKSQSP SPPPLPEDLE KAPVVLQPEQ IVSEEETPPP
LLTKEASSPP THIQLQEEME PVEGPAPPVL IQLSPPNTDA GAREPLASPH PAQLLRSLSP
LSGTTDTKAE SPAGRVSDES VLPLAQKSSL PECSTQKGVE SEREKSAPLP LTVEEFAPAK
GITEEPMKKQ SLEQKEGRRA SHALFPEHSG KQSADSSSSR SSSPSSSSSP SRSPSPDSVA
SRPQSSPGSK QRDGAQARVH ANPHERPKMG SRSTSESRSR SRSRSRSASS SSRKSLSPGV
SRDSNTSYTE TKDPSCGQEA AAPSGPQLQV LEPKEKAPTF SASVRGRHLS HPEPEQQHVI
QRLQPEQGSP KKCEAEEAEP PAATQPQTSE TQISHLLESE RTHHTVEEKE EVTMDTSENR
PENEVPEPPL PVADQVSNDE RPEGGAEEEE KKESSMPKSF KRKISVVSAT KGVQAGNSDT
EGGQPGRKRR WGASTAATQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED
ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE KEPEAELPAP PQVSVEVALP
PPVEHEVKKV TLGDTLTRRS ISQQKSGVSI TIDDPVRTAQ VPSPPRGKIS NIVHISNLVR
PFTLGQLKEL LGRTGTLVEE AFWIDKIKSH CFVTYSTVEE AVATRTALHG VKWPQSNPKF
LCADYAEQDE LDYHRGLLVD RPSETKAEEQ GAPRPLHPPP PPPVQPPPHP RAEQREQERA
VREQWAERER EMERRERTRS EREWDRDKVR EGPRSRSRSR DRRRKERAKS KEKKSEKKEK
AQEEPPAKLL DDLFRKTKAA PCIYWLPLTE SQIVQKEAEQ AERAKEREKR RKEREEEEQK
EREKEAERER NRQLEREKRR EHSRERERDR ERERDRGDRE RERERDRDRG RERDRRDTKR
HSRSRSRSTP VRDRGGRR
