ACINU_HUMAN
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 03-AUG-2022, entry version 201.
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; 231.
DR CORUM; Q9UKV3; -.
DR DIP; DIP-32963N; -.
DR IntAct; Q9UKV3; 71.
DR MINT; Q9UKV3; -.
DR STRING; 9606.ENSP00000262710; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; Q9UKV3; 3 sites, 1 O-linked glycan (3 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; Q9UKV3; -.
DR PeptideAtlas; Q9UKV3; -.
DR PRIDE; Q9UKV3; -.
DR ProteomicsDB; 84889; -. [Q9UKV3-1]
DR ProteomicsDB; 84890; -. [Q9UKV3-2]
DR ProteomicsDB; 84891; -. [Q9UKV3-3]
DR ProteomicsDB; 84892; -. [Q9UKV3-5]
DR Antibodypedia; 63; 533 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 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; 828911at2759; -.
DR PhylomeDB; Q9UKV3; -.
DR TreeFam; TF320727; -.
DR PathwayCommons; Q9UKV3; -.
DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
DR SignaLink; Q9UKV3; -.
DR SIGNOR; Q9UKV3; -.
DR BioGRID-ORCS; 22985; 513 hits in 1084 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 201 other tissues.
DR ExpressionAtlas; Q9UKV3; baseline and differential.
DR Genevisible; Q9UKV3; HS.
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; 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 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 th 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
