ID   ACINU_HUMAN             Reviewed;        1341 AA.
AC   Q9UKV3; B2RTT4; D3DS45; O75158; Q9UG91; Q9UKV1; Q9UKV2;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Apoptotic chromatin condensation inducer in the nucleus;
DE            Short=Acinus;
GN   Name=ACIN1; Synonyms=ACINUS, KIAA0670;
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] (ISOFORMS 1; 2 AND 3), PARTIAL PROTEIN SEQUENCE,
RP   FUNCTION, MUTAGENESIS OF ASP-1093, AND VARIANT PRO-447.
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 [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-447.
RC   TISSUE=Fetal brain;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-447.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT PRO-447.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-1341 (ISOFORM 1), AND VARIANT
RP   PRO-447.
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 798-813.
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   IDENTIFICATION IN THE ASAP COMPLEX, AND FUNCTION OF THE ASAP COMPLEX.
RX   PubMed=12665594; DOI=10.1128/mcb.23.8.2981-2990.2003;
RA   Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E.,
RA   Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.;
RT   "ASAP, a novel protein complex involved in RNA processing and apoptosis.";
RL   Mol. Cell. Biol. 23:2981-2990(2003).
RN   [9]
RP   IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX,
RP   INTERACTION WITH RNPS1 AND SAP18, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=16314458; DOI=10.1261/rna.2155905;
RA   Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
RT   "Biochemical analysis of the EJC reveals two new factors and a stable
RT   tetrameric protein core.";
RL   RNA 11:1869-1883(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-328; SER-490;
RP   SER-710 AND SER-1004, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243 AND THR-254, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [12]
RP   FUNCTION, PHOSPHORYLATION AT SER-1180 BY SRPK2, INTERACTION WITH SRPK2, AND
RP   SUBCELLULAR LOCATION.
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-453; SER-895 AND
RP   SER-898, VARIANT [LARGE SCALE ANALYSIS] PRO-447, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-710 AND SER-1004,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=T-cell;
RX   PubMed=19367720; DOI=10.1021/pr800500r;
RA   Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT   "Phosphorylation analysis of primary human T lymphocytes using sequential
RT   IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [15]
RP   METHYLATION AT LYS-654, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18438403; DOI=10.1038/nchembio.88;
RA   Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R.,
RA   Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
RT   "Protein lysine methyltransferase G9a acts on non-histone targets.";
RL   Nat. Chem. Biol. 4:344-346(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-169; SER-216;
RP   SER-240; SER-243; THR-254; SER-295; SER-365; SER-384; SER-386; SER-388;
RP   THR-393; SER-410; THR-414; SER-453; SER-490; TYR-512; SER-561; SER-655;
RP   SER-657; THR-682; SER-710; THR-720; SER-838 AND SER-1004, VARIANT [LARGE
RP   SCALE ANALYSIS] PRO-447, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [19]
RP   INTERACTION WITH API5.
RX   PubMed=19387494; DOI=10.1038/emboj.2009.106;
RA   Rigou P., Piddubnyak V., Faye A., Rain J.-C., Michel L., Calvo F.,
RA   Poyet J.-L.;
RT   "The antiapoptotic protein AAC-11 interacts with and regulates Acinus-
RT   mediated DNA fragmentation.";
RL   EMBO J. 28:1576-1588(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; THR-269; SER-400;
RP   SER-410; THR-414; SER-478; SER-490; SER-838 AND SER-990, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, 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   [22]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SAP18 AND RNPS1.
RX   PubMed=20966198; DOI=10.1261/rna.2304410;
RA   Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A.,
RA   Schulze-Osthoff K., Schaal H., Schwerk C.;
RT   "Human SAP18 mediates assembly of a splicing regulatory multiprotein
RT   complex via its ubiquitin-like fold.";
RL   RNA 16:2442-2454(2010).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-240; SER-243;
RP   THR-254; SER-365; SER-410; THR-414; SER-490; SER-561; SER-655; SER-657;
RP   SER-710; SER-714; SER-729; SER-838 AND SER-1004, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [24]
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   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-210; SER-216;
RP   SER-240; SER-243; THR-326; SER-328; SER-365; SER-384; SER-386; THR-393;
RP   SER-410; SER-490; SER-655; SER-657; SER-710; SER-714; SER-729; SER-825;
RP   SER-838; SER-987 AND SER-1004, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [26]
RP   FUNCTION.
RX   PubMed=22203037; DOI=10.1128/mcb.06130-11;
RA   Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M.,
RA   Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R.,
RA   Elela S.A., Prinos P., Chabot B.;
RT   "Proteins associated with the exon junction complex also control the
RT   alternative splicing of apoptotic regulators.";
RL   Mol. Cell. Biol. 32:954-967(2012).
RN   [27]
RP   INTERACTION WITH RNPS1, COMPOSITION OF THE ASAP COMPLEX, AND FUNCTION OF
RP   THE ASAP COMPLEX.
RX   PubMed=22388736; DOI=10.1038/nsmb.2242;
RA   Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.;
RT   "The structure of the ASAP core complex reveals the existence of a Pinin-
RT   containing PSAP complex.";
RL   Nat. Struct. Mol. Biol. 19:378-386(2012).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-216; SER-240;
RP   SER-243; THR-254; SER-328; SER-365; SER-386; SER-388; SER-400; SER-410;
RP   THR-414; THR-420; SER-490; SER-522; SER-561; SER-655; SER-657; THR-682;
RP   SER-710; SER-714; SER-825; SER-838; THR-976; SER-987; SER-990 AND SER-1004,
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-447, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-169; SER-216;
RP   SER-365; SER-400; SER-410; THR-414; SER-453; SER-478; SER-490; SER-561;
RP   SER-710; SER-825; SER-838; SER-898 AND SER-1004, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-825 (ISOFORM 4), VARIANT [LARGE SCALE ANALYSIS]
RP   PRO-447, AND 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   [30]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-315 AND LYS-532, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [31]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268 AND LYS-532, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [32]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-315 AND LYS-532, AND
RP   IDENTIFICATION BY MASS 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   [33]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-305 AND LYS-532, 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   [34]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-305; LYS-315; LYS-375; LYS-532;
RP   LYS-732; LYS-861; LYS-879; LYS-970; LYS-1047 AND LYS-1107, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [35]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-1160.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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. {ECO:0000269|PubMed:10490026,
CC       ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:18559500,
CC       ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22388736}.
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.
CC       {ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:16314458,
CC       ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19387494,
CC       ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:22388736}.
CC   -!- INTERACTION:
CC       Q9UKV3; P61457: PCBD1; NbExp=2; IntAct=EBI-396258, EBI-740475;
CC       Q9UKV3; Q9H307: PNN; NbExp=2; IntAct=EBI-396258, EBI-681904;
CC       Q9UKV3-2; Q15287-1: RNPS1; NbExp=4; IntAct=EBI-5279966, EBI-15972541;
CC       Q9UKV3-3; Q9BZZ5: API5; NbExp=2; IntAct=EBI-6976596, EBI-1048422;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm.
CC       Note=Phosphorylation on Ser-1180 by SRPK2 redistributes it from the
CC       nuclear speckles to the nucleoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=L;
CC         IsoId=Q9UKV3-1; Sequence=Displayed;
CC       Name=2; Synonyms=S';
CC         IsoId=Q9UKV3-2; Sequence=VSP_004025, VSP_004028;
CC       Name=3; Synonyms=S;
CC         IsoId=Q9UKV3-3; Sequence=VSP_004026, VSP_004029;
CC       Name=4;
CC         IsoId=Q9UKV3-5; Sequence=VSP_042204, VSP_042205;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. The Ser-1180 phosphorylated form (by
CC       SRPK2) is highly expressed and phosphorylated in patients with myeloid
CC       hematologic malignancies.
CC   -!- PTM: Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory
CC       effect on cyclin A1. {ECO:0000269|PubMed:18559500}.
CC   -!- PTM: Undergoes proteolytic cleavage; the processed form is active,
CC       contrary to the uncleaved form.
CC   -!- CAUTION: Structural and functional studies of the ASAP complex have
CC       been conducted with a chimeric complex involving a conserved fragment
CC       of Drosophila melanogaster Acinus/hkl. {ECO:0000305|PubMed:22388736}.
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DR   EMBL; AF124726; AAD56724.1; -; mRNA.
DR   EMBL; AF124727; AAD56725.1; -; mRNA.
DR   EMBL; AF124728; AAD56726.1; -; mRNA.
DR   EMBL; BX247975; CAD62309.1; -; mRNA.
DR   EMBL; AL117258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471078; EAW66187.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66188.1; -; Genomic_DNA.
DR   EMBL; BC140805; AAI40806.1; -; mRNA.
DR   EMBL; AB014570; BAA31645.2; -; mRNA.
DR   EMBL; AL050382; CAB43681.2; -; mRNA.
DR   CCDS; CCDS53887.1; -. [Q9UKV3-3]
DR   CCDS; CCDS53888.1; -. [Q9UKV3-2]
DR   CCDS; CCDS55905.1; -. [Q9UKV3-5]
DR   CCDS; CCDS9587.1; -. [Q9UKV3-1]
DR   RefSeq; NP_001158286.1; NM_001164814.1.
DR   RefSeq; NP_001158287.1; NM_001164815.1.
DR   RefSeq; NP_001158288.1; NM_001164816.1. [Q9UKV3-2]
DR   RefSeq; NP_001158289.1; NM_001164817.1. [Q9UKV3-3]
DR   RefSeq; NP_055792.1; NM_014977.3.
DR   RefSeq; XP_005267475.1; XM_005267418.1. [Q9UKV3-3]
DR   PDB; 6G6S; X-ray; 1.65 A; A/B=1008-1100.
DR   PDBsum; 6G6S; -.
DR   AlphaFoldDB; Q9UKV3; -.
DR   SMR; Q9UKV3; -.
DR   BioGRID; 116634; 304.
DR   ComplexPortal; CPX-2256; ASAP splicing-associated complex.
DR   CORUM; Q9UKV3; -.
DR   DIP; DIP-32963N; -.
DR   IntAct; Q9UKV3; 79.
DR   MINT; Q9UKV3; -.
DR   STRING; 9606.ENSP00000262710; -.
DR   TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR   GlyCosmos; Q9UKV3; 3 sites, 1 glycan.
DR   GlyGen; Q9UKV3; 10 sites, 1 O-linked glycan (10 sites).
DR   iPTMnet; Q9UKV3; -.
DR   MetOSite; Q9UKV3; -.
DR   PhosphoSitePlus; Q9UKV3; -.
DR   SwissPalm; Q9UKV3; -.
DR   BioMuta; ACIN1; -.
DR   DMDM; 308153407; -.
DR   CPTAC; CPTAC-1342; -.
DR   EPD; Q9UKV3; -.
DR   jPOST; Q9UKV3; -.
DR   MassIVE; Q9UKV3; -.
DR   MaxQB; Q9UKV3; -.
DR   PaxDb; 9606-ENSP00000262710; -.
DR   PeptideAtlas; Q9UKV3; -.
DR   ProteomicsDB; 84889; -. [Q9UKV3-1]
DR   ProteomicsDB; 84890; -. [Q9UKV3-2]
DR   ProteomicsDB; 84891; -. [Q9UKV3-3]
DR   ProteomicsDB; 84892; -. [Q9UKV3-5]
DR   Pumba; Q9UKV3; -.
DR   Antibodypedia; 63; 579 antibodies from 37 providers.
DR   DNASU; 22985; -.
DR   Ensembl; ENST00000262710.5; ENSP00000262710.1; ENSG00000100813.15. [Q9UKV3-1]
DR   Ensembl; ENST00000338631.10; ENSP00000345541.6; ENSG00000100813.15. [Q9UKV3-2]
DR   Ensembl; ENST00000357481.6; ENSP00000350073.2; ENSG00000100813.15. [Q9UKV3-3]
DR   Ensembl; ENST00000397341.7; ENSP00000380502.3; ENSG00000100813.15. [Q9UKV3-3]
DR   Ensembl; ENST00000555053.5; ENSP00000451328.1; ENSG00000100813.15. [Q9UKV3-5]
DR   GeneID; 22985; -.
DR   KEGG; hsa:22985; -.
DR   UCSC; uc001wip.5; human. [Q9UKV3-1]
DR   AGR; HGNC:17066; -.
DR   CTD; 22985; -.
DR   DisGeNET; 22985; -.
DR   GeneCards; ACIN1; -.
DR   HGNC; HGNC:17066; ACIN1.
DR   HPA; ENSG00000100813; Low tissue specificity.
DR   MIM; 604562; gene.
DR   neXtProt; NX_Q9UKV3; -.
DR   OpenTargets; ENSG00000100813; -.
DR   PharmGKB; PA134912489; -.
DR   VEuPathDB; HostDB:ENSG00000100813; -.
DR   eggNOG; KOG2416; Eukaryota.
DR   GeneTree; ENSGT00710000106790; -.
DR   HOGENOM; CLU_482284_0_0_1; -.
DR   InParanoid; Q9UKV3; -.
DR   OMA; DYHKGIR; -.
DR   OrthoDB; 1411884at2759; -.
DR   PhylomeDB; Q9UKV3; -.
DR   TreeFam; TF320727; -.
DR   PathwayCommons; Q9UKV3; -.
DR   Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q9UKV3; -.
DR   SIGNOR; Q9UKV3; -.
DR   BioGRID-ORCS; 22985; 520 hits in 1164 CRISPR screens.
DR   ChiTaRS; ACIN1; human.
DR   GeneWiki; ACIN1; -.
DR   GenomeRNAi; 22985; -.
DR   Pharos; Q9UKV3; Tbio.
DR   PRO; PR:Q9UKV3; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9UKV3; Protein.
DR   Bgee; ENSG00000100813; Expressed in right uterine tube and 203 other cell types or tissues.
DR   ExpressionAtlas; Q9UKV3; baseline and differential.
DR   GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0016887; F:ATP hydrolysis activity; NAS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; NAS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0030263; P:apoptotic chromosome condensation; IDA:UniProtKB.
DR   GO; GO:0030218; P:erythrocyte differentiation; IEP:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045657; P:positive regulation of monocyte differentiation; IEP:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR   CDD; cd12432; RRM_ACINU; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 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   PANTHER; PTHR46589; APOPTOTIC CHROMATIN CONDENSATION INDUCER IN THE NUCLEUS; 1.
DR   PANTHER; PTHR46589:SF1; APOPTOTIC CHROMATIN CONDENSATION INDUCER IN THE NUCLEUS; 1.
DR   Pfam; PF16294; RSB_motif; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   Genevisible; Q9UKV3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   Direct protein sequencing; Isopeptide bond; Methylation; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN           1..1341
FT                   /note="Apoptotic chromatin condensation inducer in the
FT                   nucleus"
FT                   /id="PRO_0000064436"
FT   DOMAIN          72..106
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1098..1341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1210..1237
FT                   /note="Sufficient for interaction with RNPS1 and SAP18 and
FT                   formation of the ASAP complex"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        159..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..291
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..738
FT                   /note="Basic and acidic 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        851..865
FT                   /note="Polar 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        1098..1112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1192
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1236..1322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            1093..1094
FT                   /note="Cleavage; by caspase-3"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         254
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         269
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         326
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         393
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         414
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         420
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         490
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         512
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         561
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         654
FT                   /note="N6,N6,N6-trimethyllysine; by EHMT2; alternate"
FT                   /evidence="ECO:0000269|PubMed:18438403"
FT   MOD_RES         654
FT                   /note="N6,N6-dimethyllysine; by EHMT2; alternate"
FT                   /evidence="ECO:0000269|PubMed:18438403"
FT   MOD_RES         655
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         657
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         682
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         717
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         720
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         861
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIX8"
FT   MOD_RES         895
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336"
FT   MOD_RES         898
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         976
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         987
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         990
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1004
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         1180
FT                   /note="Phosphoserine; by SRPK2 and PKB/AKT1"
FT                   /evidence="ECO:0000269|PubMed:18559500"
FT   CROSSLNK        268
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        305
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        315
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        375
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        532
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25114211,
FT                   ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        732
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        861
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        879
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        970
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1047
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1107
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..758
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10490026, ECO:0000303|Ref.2"
FT                   /id="VSP_004026"
FT   VAR_SEQ         1..727
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10490026"
FT                   /id="VSP_004025"
FT   VAR_SEQ         728..766
FT                   /note="GSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTV -> MSPADRCRS
FT                   ANTIEPATTSSLALFLLLQRDQSSRTRGLP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10490026"
FT                   /id="VSP_004028"
FT   VAR_SEQ         759..766
FT                   /note="SERIHHTV -> MLSESKEG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10490026, ECO:0000303|Ref.2"
FT                   /id="VSP_004029"
FT   VAR_SEQ         829
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042204"
FT   VAR_SEQ         873..884
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042205"
FT   VARIANT         257
FT                   /note="R -> K (in dbSNP:rs11555803)"
FT                   /id="VAR_050632"
FT   VARIANT         311
FT                   /note="I -> M (in dbSNP:rs3811182)"
FT                   /id="VAR_022031"
FT   VARIANT         447
FT                   /note="A -> P (in dbSNP:rs941719)"
FT                   /evidence="ECO:0000269|PubMed:10490026,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.4,
FT                   ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT                   /id="VAR_061547"
FT   VARIANT         467
FT                   /note="S -> P (in dbSNP:rs1885097)"
FT                   /id="VAR_022032"
FT   VARIANT         478
FT                   /note="S -> F (in dbSNP:rs3751501)"
FT                   /id="VAR_022033"
FT   VARIANT         1160
FT                   /note="R -> Q (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs754494408)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035777"
FT   MUTAGEN         1093
FT                   /note="D->A: Abolishes cleavage by CASP3 and chromatin
FT                   condensation activity."
FT                   /evidence="ECO:0000269|PubMed:10490026"
FT   CONFLICT        139
FT                   /note="Q -> H (in Ref. 2; BAA31645)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1012..1017
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   HELIX           1025..1032
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   HELIX           1040..1042
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   STRAND          1049..1058
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   HELIX           1059..1069
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   STRAND          1083..1087
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   HELIX           1089..1095
FT                   /evidence="ECO:0007829|PDB:6G6S"
FT   MOD_RES         Q9UKV3-5:825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
SQ   SEQUENCE   1341 AA;  151862 MW;  DCCBF310A4680691 CRC64;
     MWRRKHPRTS GGTRGVLSGN RGVEYGSGRG HLGTFEGRWR KLPKMPEAVG TDPSTSRKMA
     ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK RLKGALMLEN LQKHSTPHAA
     FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ RLEREAREAA ELEEASAESE DEMIHPEGVA
     SLLPPDFQSS LERPELELSR HSPRKSSSIS EEKGDSDDEK PRKGERRSSR VRQARAAKLS
     EGSQPAEEEE DQETPSRNLR VRADRNLKTE EEEEEEEEEE EDDEEEEGDD EGQKSREAPI
     LKEFKEEGEE IPRVKPEEMM DERPKTRSQE QEVLERGGRF TRSQEEARKS HLARQQQEKE
     MKTTSPLEEE EREIKSSQGL KEKSKSPSPP RLTEDRKKAS LVALPEQTAS EEETPPPLLT
     KEASSPPPHP QLHSEEEIEP MEGPAPAVLI QLSPPNTDAD TRELLVSQHT VQLVGGLSPL
     SSPSDTKAES PAEKVPEESV LPLVQKSTLA DYSAQKDLEP ESDRSAQPLP LKIEELALAK
     GITEECLKQP SLEQKEGRRA SHTLLPSHRL KQSADSSSSR SSSSSSSSSR SRSRSPDSSG
     SRSHSPLRSK QRDVAQARTH ANPRGRPKMG SRSTSESRSR SRSRSRSASS NSRKSLSPGV
     SRDSSTSYTE TKDPSSGQEV ATPPVPQLQV CEPKERTSTS SSSVQARRLS QPESAEKHVT
     QRLQPERGSP KKCEAEEAEP PAATQPQTSE TQTSHLPESE RIHHTVEEKE EVTMDTSENR
     PENDVPEPPM PIADQVSNDD RPEGSVEDEE KKESSLPKSF KRKISVVSAT KGVPAGNSDT
     EGGQPGRKRR WGASTATTQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED
     ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE EKEPEAEPPV PPQVSVEVAL
     PPPAEHEVKK VTLGDTLTRR SISQQKSGVS ITIDDPVRTA QVPSPPRGKI SNIVHISNLV
     RPFTLGQLKE LLGRTGTLVE EAFWIDKIKS HCFVTYSTVE EAVATRTALH GVKWPQSNPK
     FLCADYAEQD ELDYHRGLLV DRPSETKTEE QGIPRPLHPP PPPPVQPPQH PRAEQREQER
     AVREQWAERE REMERRERTR SEREWDRDKV REGPRSRSRS RDRRRKERAK SKEKKSEKKE
     KAQEEPPAKL LDDLFRKTKA APCIYWLPLT DSQIVQKEAE RAERAKEREK RRKEQEEEEQ
     KEREKEAERE RNRQLEREKR REHSRERDRE RERERERDRG DRDRDRERDR ERGRERDRRD
     TKRHSRSRSR STPVRDRGGR R
//