Full text data of ACIN1
ACIN1
(ACINUS, KIAA0670)
[Confidence: low (only semi-automatic identification from reviews)]
Apoptotic chromatin condensation inducer in the nucleus; Acinus
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Apoptotic chromatin condensation inducer in the nucleus; Acinus
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UKV3
ID ACINU_HUMAN Reviewed; 1341 AA.
AC Q9UKV3; B2RTT4; D3DS45; O75158; Q9UG91; Q9UKV1; Q9UKV2;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 2.
DT 22-JAN-2014, entry version 132.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PARTIAL PROTEIN
RP SEQUENCE, 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
RT chromatin condensation.";
RL Nature 401:168-173(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP 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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP 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
RT project: 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
RP VARIANT 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.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT 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 MASS
RP 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243 AND
RP THR-254, AND MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-5, AND MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [13]
RP FUNCTION, PHOSPHORYLATION AT SER-1180 BY SRPK2, INTERACTION WITH
RP SRPK2, AND 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.,
RA Persson J.L., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-453; SER-895
RP AND SER-898, VARIANT [LARGE SCALE ANALYSIS] PRO-447, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-710 AND
RP SER-1004, AND MASS SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [16]
RP METHYLATION AT LYS-654, AND MASS SPECTROMETRY.
RX PubMed=18438403; DOI=10.1038/nchembio.88;
RA Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
RA Jurkowska R., 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 [17]
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;
RP SER-388; THR-393; SER-410; THR-414; SER-453; SER-490; TYR-512;
RP SER-561; SER-655; SER-657; THR-682; SER-710; THR-720; SER-838 AND
RP SER-1004, VARIANT [LARGE SCALE ANALYSIS] PRO-447, AND MASS
RP SPECTROMETRY.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
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 [21]
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 MASS
RP SPECTROMETRY.
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [23]
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 [24]
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;
RP SER-657; SER-710; SER-714; SER-729; SER-838 AND SER-1004, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
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.,
RA Buerckstuemmer T., 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 [26]
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;
RP THR-393; SER-410; SER-490; SER-655; SER-657; SER-710; SER-714;
RP SER-729; SER-825; SER-838; SER-987 AND SER-1004, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP FUNCTION.
RX PubMed=22203037; DOI=10.1128/MCB.06130-11;
RA Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P.,
RA Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H.,
RA Klinck R., 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 [28]
RP INTERACTION WITH RNPS1, COMPOSITION OF THE ASAP COMPLEX, AND FUNCTION
RP OF 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
RT Pinin-containing PSAP complex.";
RL Nat. Struct. Mol. Biol. 19:378-386(2012).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Auxiliary component of the splicing-dependent
CC multiprotein exon junction complex (EJC) deposited at splice
CC junction on mRNAs. The EJC is a dynamic structure consisting of
CC core proteins and several peripheral nuclear and cytoplasmic
CC associated factors that join the complex only transiently either
CC during EJC assembly or during subsequent mRNA metabolism.
CC Component of the ASAP complexes which bind RNA in a sequence-
CC independent manner and are proposed to be recruited to the EJC
CC prior to or during the splicing process and to regulate specific
CC excision of introns in specific transcription subsets; ACIN1
CC confers RNA-binding to the complex. The ASAP complex can inhibit
CC RNA processing during in vitro splicing reactions. The ASAP
CC complex promotes apoptosis and is disassembled after induction of
CC apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X
CC (and probably other apoptotic genes); specifically inhibits
CC formation of proapoptotic isoforms such as Bcl-X(S); the activity
CC is different from the established EJC assembly and function.
CC Induces apoptotic chromatin condensation after activation by
CC CASP3. Regulates cyclin A1, but not cyclin A2, expression in
CC leukemia cells.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Component of the heterotrimeric ASAP (apoptosis- and
CC splicing-associated protein) complexes consisting of RNPS1, SAP18
CC and different isoforms of ACIN1; the association of SAP18 seems to
CC require a preformed RNPS1:ACIN1 complex. Interacts with API5.
CC Interacts with SRPK2 in a phosphorylation-dependent manner.
CC -!- INTERACTION:
CC Q9BZZ5:API5; NbExp=2; IntAct=EBI-6976596, EBI-1048422;
CC P61457:PCBD1; NbExp=2; IntAct=EBI-396258, EBI-740475;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus,
CC nucleoplasm. Note=Phosphorylation on Ser-1180 by SRPK2
CC redistributes it from the 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
CC (by SRPK2) is highly expressed and phosphorylated in patients with
CC myeloid hematologic malignancies.
CC -!- PTM: Phosphorylation on Ser-1180 by SRPK2 up-regulates its
CC stimulatory effect on cyclin A1.
CC -!- PTM: Undergoes proteolytic cleavage; the processed form is active,
CC contrary to the uncleaved form.
CC -!- SIMILARITY: Contains 1 SAP domain.
CC -!- CAUTION: Structural and functional studies of the ASAP complex
CC have been conducted with a chimeric complex involving a conserved
CC fragment of Drosophila melanogaster Acinus/hkl (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 RefSeq; NP_001158286.1; NM_001164814.1.
DR RefSeq; NP_001158287.1; NM_001164815.1.
DR RefSeq; NP_001158288.1; NM_001164816.1.
DR RefSeq; NP_001158289.1; NM_001164817.1.
DR RefSeq; NP_055792.1; NM_014977.3.
DR RefSeq; XP_005267475.1; XM_005267418.1.
DR UniGene; Hs.124490; -.
DR ProteinModelPortal; Q9UKV3; -.
DR DIP; DIP-32963N; -.
DR IntAct; Q9UKV3; 20.
DR MINT; MINT-5006704; -.
DR STRING; 9606.ENSP00000262710; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR PhosphoSite; Q9UKV3; -.
DR DMDM; 308153407; -.
DR PaxDb; Q9UKV3; -.
DR PRIDE; Q9UKV3; -.
DR Ensembl; ENST00000262710; ENSP00000262710; ENSG00000100813.
DR Ensembl; ENST00000338631; ENSP00000345541; ENSG00000100813.
DR Ensembl; ENST00000357481; ENSP00000350073; ENSG00000100813.
DR Ensembl; ENST00000397341; ENSP00000380502; ENSG00000100813.
DR Ensembl; ENST00000555053; ENSP00000451328; ENSG00000100813.
DR GeneID; 22985; -.
DR KEGG; hsa:22985; -.
DR UCSC; uc001wis.4; human.
DR CTD; 22985; -.
DR GeneCards; GC14M023527; -.
DR HGNC; HGNC:17066; ACIN1.
DR HPA; HPA000657; -.
DR MIM; 604562; gene.
DR neXtProt; NX_Q9UKV3; -.
DR PharmGKB; PA134912489; -.
DR eggNOG; NOG291715; -.
DR HOGENOM; HOG000088615; -.
DR HOVERGEN; HBG050449; -.
DR InParanoid; Q9UKV3; -.
DR KO; K12875; -.
DR OMA; ADRNLKT; -.
DR PhylomeDB; Q9UKV3; -.
DR Reactome; REACT_578; Apoptosis.
DR ChiTaRS; ACIN1; human.
DR GeneWiki; ACIN1; -.
DR GenomeRNAi; 22985; -.
DR NextBio; 43823; -.
DR PMAP-CutDB; Q9UKV3; -.
DR PRO; PR:Q9UKV3; -.
DR ArrayExpress; Q9UKV3; -.
DR Bgee; Q9UKV3; -.
DR CleanEx; HS_ACIN1; -.
DR Genevestigator; Q9UKV3; -.
DR GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0016887; F:ATPase 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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Complete proteome;
KW Direct protein sequencing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1 1341 Apoptotic chromatin condensation inducer
FT in the nucleus.
FT /FTId=PRO_0000064436.
FT DOMAIN 72 106 SAP.
FT REGION 1210 1237 Sufficient for interaction with RNPS1 and
FT SAP18 and formation of th ASAP complex
FT (By similarity).
FT COMPBIAS 142 442 Glu-rich.
FT COMPBIAS 573 676 Ser-rich.
FT COMPBIAS 1114 1131 Pro-rich.
FT COMPBIAS 1132 1341 Arg/Asp/Glu/Lys-rich.
FT SITE 1093 1094 Cleavage; by caspase-3.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 169 169 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine.
FT MOD_RES 210 210 Phosphoserine.
FT MOD_RES 216 216 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 243 243 Phosphoserine.
FT MOD_RES 254 254 Phosphothreonine.
FT MOD_RES 269 269 Phosphothreonine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 326 326 Phosphothreonine.
FT MOD_RES 328 328 Phosphoserine.
FT MOD_RES 365 365 Phosphoserine.
FT MOD_RES 384 384 Phosphoserine.
FT MOD_RES 386 386 Phosphoserine.
FT MOD_RES 388 388 Phosphoserine.
FT MOD_RES 393 393 Phosphothreonine.
FT MOD_RES 400 400 Phosphoserine.
FT MOD_RES 410 410 Phosphoserine.
FT MOD_RES 414 414 Phosphothreonine.
FT MOD_RES 434 434 Phosphoserine.
FT MOD_RES 453 453 Phosphoserine.
FT MOD_RES 478 478 Phosphoserine.
FT MOD_RES 490 490 Phosphoserine.
FT MOD_RES 512 512 Phosphotyrosine.
FT MOD_RES 561 561 Phosphoserine.
FT MOD_RES 654 654 N6,N6,N6-trimethyllysine; by EHMT2;
FT alternate.
FT MOD_RES 654 654 N6,N6-dimethyllysine; by EHMT2;
FT alternate.
FT MOD_RES 655 655 Phosphoserine.
FT MOD_RES 657 657 Phosphoserine.
FT MOD_RES 682 682 Phosphothreonine.
FT MOD_RES 710 710 Phosphoserine.
FT MOD_RES 714 714 Phosphoserine.
FT MOD_RES 717 717 N6-acetyllysine.
FT MOD_RES 720 720 Phosphothreonine.
FT MOD_RES 729 729 Phosphoserine.
FT MOD_RES 825 825 Phosphoserine.
FT MOD_RES 838 838 Phosphoserine.
FT MOD_RES 895 895 Phosphoserine.
FT MOD_RES 898 898 Phosphoserine.
FT MOD_RES 987 987 Phosphoserine.
FT MOD_RES 990 990 Phosphoserine.
FT MOD_RES 1004 1004 Phosphoserine.
FT MOD_RES 1180 1180 Phosphoserine; by SRPK2 and PKB/AKT1.
FT CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 758 Missing (in isoform 3).
FT /FTId=VSP_004026.
FT VAR_SEQ 1 727 Missing (in isoform 2).
FT /FTId=VSP_004025.
FT VAR_SEQ 728 766 GSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTV
FT -> MSPADRCRSANTIEPATTSSLALFLLLQRDQSSRTRGL
FT P (in isoform 2).
FT /FTId=VSP_004028.
FT VAR_SEQ 759 766 SERIHHTV -> MLSESKEG (in isoform 3).
FT /FTId=VSP_004029.
FT VAR_SEQ 829 829 Missing (in isoform 4).
FT /FTId=VSP_042204.
FT VAR_SEQ 873 884 Missing (in isoform 4).
FT /FTId=VSP_042205.
FT VARIANT 257 257 R -> K (in dbSNP:rs11555803).
FT /FTId=VAR_050632.
FT VARIANT 311 311 I -> M (in dbSNP:rs3811182).
FT /FTId=VAR_022031.
FT VARIANT 447 447 A -> P (in dbSNP:rs941719).
FT /FTId=VAR_061547.
FT VARIANT 467 467 S -> P (in dbSNP:rs1885097).
FT /FTId=VAR_022032.
FT VARIANT 478 478 S -> F (in dbSNP:rs3751501).
FT /FTId=VAR_022033.
FT VARIANT 1160 1160 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035777.
FT MUTAGEN 1093 1093 D->A: Abolishes cleavage by CASP3 and
FT chromatin condensation activity.
FT CONFLICT 139 139 Q -> H (in Ref. 2; BAA31645).
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
//
ID ACINU_HUMAN Reviewed; 1341 AA.
AC Q9UKV3; B2RTT4; D3DS45; O75158; Q9UG91; Q9UKV1; Q9UKV2;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 2.
DT 22-JAN-2014, entry version 132.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PARTIAL PROTEIN
RP SEQUENCE, 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
RT chromatin condensation.";
RL Nature 401:168-173(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP 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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP 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
RT project: 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
RP VARIANT 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.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT 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 MASS
RP 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243 AND
RP THR-254, AND MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-5, AND MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [13]
RP FUNCTION, PHOSPHORYLATION AT SER-1180 BY SRPK2, INTERACTION WITH
RP SRPK2, AND 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.,
RA Persson J.L., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-453; SER-895
RP AND SER-898, VARIANT [LARGE SCALE ANALYSIS] PRO-447, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-710 AND
RP SER-1004, AND MASS SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [16]
RP METHYLATION AT LYS-654, AND MASS SPECTROMETRY.
RX PubMed=18438403; DOI=10.1038/nchembio.88;
RA Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
RA Jurkowska R., 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 [17]
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;
RP SER-388; THR-393; SER-410; THR-414; SER-453; SER-490; TYR-512;
RP SER-561; SER-655; SER-657; THR-682; SER-710; THR-720; SER-838 AND
RP SER-1004, VARIANT [LARGE SCALE ANALYSIS] PRO-447, AND MASS
RP SPECTROMETRY.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
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 [21]
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 MASS
RP SPECTROMETRY.
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [23]
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 [24]
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;
RP SER-657; SER-710; SER-714; SER-729; SER-838 AND SER-1004, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
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.,
RA Buerckstuemmer T., 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 [26]
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;
RP THR-393; SER-410; SER-490; SER-655; SER-657; SER-710; SER-714;
RP SER-729; SER-825; SER-838; SER-987 AND SER-1004, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP FUNCTION.
RX PubMed=22203037; DOI=10.1128/MCB.06130-11;
RA Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P.,
RA Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H.,
RA Klinck R., 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 [28]
RP INTERACTION WITH RNPS1, COMPOSITION OF THE ASAP COMPLEX, AND FUNCTION
RP OF 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
RT Pinin-containing PSAP complex.";
RL Nat. Struct. Mol. Biol. 19:378-386(2012).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Auxiliary component of the splicing-dependent
CC multiprotein exon junction complex (EJC) deposited at splice
CC junction on mRNAs. The EJC is a dynamic structure consisting of
CC core proteins and several peripheral nuclear and cytoplasmic
CC associated factors that join the complex only transiently either
CC during EJC assembly or during subsequent mRNA metabolism.
CC Component of the ASAP complexes which bind RNA in a sequence-
CC independent manner and are proposed to be recruited to the EJC
CC prior to or during the splicing process and to regulate specific
CC excision of introns in specific transcription subsets; ACIN1
CC confers RNA-binding to the complex. The ASAP complex can inhibit
CC RNA processing during in vitro splicing reactions. The ASAP
CC complex promotes apoptosis and is disassembled after induction of
CC apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X
CC (and probably other apoptotic genes); specifically inhibits
CC formation of proapoptotic isoforms such as Bcl-X(S); the activity
CC is different from the established EJC assembly and function.
CC Induces apoptotic chromatin condensation after activation by
CC CASP3. Regulates cyclin A1, but not cyclin A2, expression in
CC leukemia cells.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Component of the heterotrimeric ASAP (apoptosis- and
CC splicing-associated protein) complexes consisting of RNPS1, SAP18
CC and different isoforms of ACIN1; the association of SAP18 seems to
CC require a preformed RNPS1:ACIN1 complex. Interacts with API5.
CC Interacts with SRPK2 in a phosphorylation-dependent manner.
CC -!- INTERACTION:
CC Q9BZZ5:API5; NbExp=2; IntAct=EBI-6976596, EBI-1048422;
CC P61457:PCBD1; NbExp=2; IntAct=EBI-396258, EBI-740475;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus,
CC nucleoplasm. Note=Phosphorylation on Ser-1180 by SRPK2
CC redistributes it from the 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
CC (by SRPK2) is highly expressed and phosphorylated in patients with
CC myeloid hematologic malignancies.
CC -!- PTM: Phosphorylation on Ser-1180 by SRPK2 up-regulates its
CC stimulatory effect on cyclin A1.
CC -!- PTM: Undergoes proteolytic cleavage; the processed form is active,
CC contrary to the uncleaved form.
CC -!- SIMILARITY: Contains 1 SAP domain.
CC -!- CAUTION: Structural and functional studies of the ASAP complex
CC have been conducted with a chimeric complex involving a conserved
CC fragment of Drosophila melanogaster Acinus/hkl (PubMed:22388736).
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001158286.1; NM_001164814.1.
DR RefSeq; NP_001158287.1; NM_001164815.1.
DR RefSeq; NP_001158288.1; NM_001164816.1.
DR RefSeq; NP_001158289.1; NM_001164817.1.
DR RefSeq; NP_055792.1; NM_014977.3.
DR RefSeq; XP_005267475.1; XM_005267418.1.
DR UniGene; Hs.124490; -.
DR ProteinModelPortal; Q9UKV3; -.
DR DIP; DIP-32963N; -.
DR IntAct; Q9UKV3; 20.
DR MINT; MINT-5006704; -.
DR STRING; 9606.ENSP00000262710; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR PhosphoSite; Q9UKV3; -.
DR DMDM; 308153407; -.
DR PaxDb; Q9UKV3; -.
DR PRIDE; Q9UKV3; -.
DR Ensembl; ENST00000262710; ENSP00000262710; ENSG00000100813.
DR Ensembl; ENST00000338631; ENSP00000345541; ENSG00000100813.
DR Ensembl; ENST00000357481; ENSP00000350073; ENSG00000100813.
DR Ensembl; ENST00000397341; ENSP00000380502; ENSG00000100813.
DR Ensembl; ENST00000555053; ENSP00000451328; ENSG00000100813.
DR GeneID; 22985; -.
DR KEGG; hsa:22985; -.
DR UCSC; uc001wis.4; human.
DR CTD; 22985; -.
DR GeneCards; GC14M023527; -.
DR HGNC; HGNC:17066; ACIN1.
DR HPA; HPA000657; -.
DR MIM; 604562; gene.
DR neXtProt; NX_Q9UKV3; -.
DR PharmGKB; PA134912489; -.
DR eggNOG; NOG291715; -.
DR HOGENOM; HOG000088615; -.
DR HOVERGEN; HBG050449; -.
DR InParanoid; Q9UKV3; -.
DR KO; K12875; -.
DR OMA; ADRNLKT; -.
DR PhylomeDB; Q9UKV3; -.
DR Reactome; REACT_578; Apoptosis.
DR ChiTaRS; ACIN1; human.
DR GeneWiki; ACIN1; -.
DR GenomeRNAi; 22985; -.
DR NextBio; 43823; -.
DR PMAP-CutDB; Q9UKV3; -.
DR PRO; PR:Q9UKV3; -.
DR ArrayExpress; Q9UKV3; -.
DR Bgee; Q9UKV3; -.
DR CleanEx; HS_ACIN1; -.
DR Genevestigator; Q9UKV3; -.
DR GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0016887; F:ATPase 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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Complete proteome;
KW Direct protein sequencing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1 1341 Apoptotic chromatin condensation inducer
FT in the nucleus.
FT /FTId=PRO_0000064436.
FT DOMAIN 72 106 SAP.
FT REGION 1210 1237 Sufficient for interaction with RNPS1 and
FT SAP18 and formation of th ASAP complex
FT (By similarity).
FT COMPBIAS 142 442 Glu-rich.
FT COMPBIAS 573 676 Ser-rich.
FT COMPBIAS 1114 1131 Pro-rich.
FT COMPBIAS 1132 1341 Arg/Asp/Glu/Lys-rich.
FT SITE 1093 1094 Cleavage; by caspase-3.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 169 169 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine.
FT MOD_RES 210 210 Phosphoserine.
FT MOD_RES 216 216 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 243 243 Phosphoserine.
FT MOD_RES 254 254 Phosphothreonine.
FT MOD_RES 269 269 Phosphothreonine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 326 326 Phosphothreonine.
FT MOD_RES 328 328 Phosphoserine.
FT MOD_RES 365 365 Phosphoserine.
FT MOD_RES 384 384 Phosphoserine.
FT MOD_RES 386 386 Phosphoserine.
FT MOD_RES 388 388 Phosphoserine.
FT MOD_RES 393 393 Phosphothreonine.
FT MOD_RES 400 400 Phosphoserine.
FT MOD_RES 410 410 Phosphoserine.
FT MOD_RES 414 414 Phosphothreonine.
FT MOD_RES 434 434 Phosphoserine.
FT MOD_RES 453 453 Phosphoserine.
FT MOD_RES 478 478 Phosphoserine.
FT MOD_RES 490 490 Phosphoserine.
FT MOD_RES 512 512 Phosphotyrosine.
FT MOD_RES 561 561 Phosphoserine.
FT MOD_RES 654 654 N6,N6,N6-trimethyllysine; by EHMT2;
FT alternate.
FT MOD_RES 654 654 N6,N6-dimethyllysine; by EHMT2;
FT alternate.
FT MOD_RES 655 655 Phosphoserine.
FT MOD_RES 657 657 Phosphoserine.
FT MOD_RES 682 682 Phosphothreonine.
FT MOD_RES 710 710 Phosphoserine.
FT MOD_RES 714 714 Phosphoserine.
FT MOD_RES 717 717 N6-acetyllysine.
FT MOD_RES 720 720 Phosphothreonine.
FT MOD_RES 729 729 Phosphoserine.
FT MOD_RES 825 825 Phosphoserine.
FT MOD_RES 838 838 Phosphoserine.
FT MOD_RES 895 895 Phosphoserine.
FT MOD_RES 898 898 Phosphoserine.
FT MOD_RES 987 987 Phosphoserine.
FT MOD_RES 990 990 Phosphoserine.
FT MOD_RES 1004 1004 Phosphoserine.
FT MOD_RES 1180 1180 Phosphoserine; by SRPK2 and PKB/AKT1.
FT CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 758 Missing (in isoform 3).
FT /FTId=VSP_004026.
FT VAR_SEQ 1 727 Missing (in isoform 2).
FT /FTId=VSP_004025.
FT VAR_SEQ 728 766 GSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTV
FT -> MSPADRCRSANTIEPATTSSLALFLLLQRDQSSRTRGL
FT P (in isoform 2).
FT /FTId=VSP_004028.
FT VAR_SEQ 759 766 SERIHHTV -> MLSESKEG (in isoform 3).
FT /FTId=VSP_004029.
FT VAR_SEQ 829 829 Missing (in isoform 4).
FT /FTId=VSP_042204.
FT VAR_SEQ 873 884 Missing (in isoform 4).
FT /FTId=VSP_042205.
FT VARIANT 257 257 R -> K (in dbSNP:rs11555803).
FT /FTId=VAR_050632.
FT VARIANT 311 311 I -> M (in dbSNP:rs3811182).
FT /FTId=VAR_022031.
FT VARIANT 447 447 A -> P (in dbSNP:rs941719).
FT /FTId=VAR_061547.
FT VARIANT 467 467 S -> P (in dbSNP:rs1885097).
FT /FTId=VAR_022032.
FT VARIANT 478 478 S -> F (in dbSNP:rs3751501).
FT /FTId=VAR_022033.
FT VARIANT 1160 1160 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035777.
FT MUTAGEN 1093 1093 D->A: Abolishes cleavage by CASP3 and
FT chromatin condensation activity.
FT CONFLICT 139 139 Q -> H (in Ref. 2; BAA31645).
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
//
MIM
604562
*RECORD*
*FIELD* NO
604562
*FIELD* TI
*604562 ACINUS
;;APOPTOTIC CHROMATIN CONDENSATION INDUCER IN THE NUCLEUS
*FIELD* TX
read moreApoptosis is defined by several unique morphologic nuclear changes,
including chromatin condensation and nuclear fragmentation. These
changes are triggered by the activation of a family of cysteine
proteases called caspases (see 147678), and caspase-activated DNase
(CAD/DFF40; 601883) and lamin protease (see 150330) have been implicated
in some of these changes. CAD/DFF40 induces chromatin condensation in
purified nuclei, but distinct caspase-activated factor(s) may be
responsible for chromatin condensation. Sahara et al. (1999) used an in
vitro system to purify a nuclear factor which induces apoptotic
chromatin condensation after cleavage by caspase-3 (600636) without
inducing DNA fragmentation from bovine thymus lysate. The name of the
factor, 'acinus,' is both an acronym for 'apoptotic chromatin
condensation inducer in the nucleus' and the Latin word for 'grape' or
'berry,' denotive of the grape-like appearance of the condensed
chromatin. Immunodepletion experiments showed that acinus is essential
for apoptotic chromatin condensation in vitro, and an antisense study
revealed that acinus is also important in the induction of apoptotic
chromatin condensation in cells.
As part of a search for human brain cDNA clones with the potential to
encode large proteins in vitro, Ishikawa et al. (1998) independently
identified the human homolog of acinus as cDNA KIAA0670. Ishikawa et al.
(1998) found that KIAA0670 is ubiquitously expressed. Using the KIAA0670
clone, Sahara et al. (1999) obtained 3 isoforms of human acinus cDNA,
the L, S, and S-prime forms, which they stated had probably been
generated by alternative splicing. The acinus L, S, and S-prime cDNAs
contain open reading frames of 1,341, 583, and 568 amino acid residues,
respectively. Mouse and human S and S-prime acinus proteins share 94.5%
and 95.2% amino acid sequence identity, respectively. Ishikawa et al.
(1998) noted homology of acinus to U1 70-kD small nuclear
ribonucleoprotein (180740).
By analysis of a radiation hybrid mapping panel, Ishikawa et al. (1998)
mapped the human gene encoding acinus to chromosome 14.
*FIELD* RF
1. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
2. Sahara, S.; Aoto, M.; Eguchi, Y.; Imamoto, N.; Yoneda, Y.; Tsujimoto,
Y.: Acinus is a caspase-3-activated protein required for apoptotic
chromatin condensation. Nature 401: 168-173, 1999.
*FIELD* CD
Ada Hamosh: 2/18/2000
*FIELD* ED
carol: 12/26/2002
alopez: 2/18/2000
*RECORD*
*FIELD* NO
604562
*FIELD* TI
*604562 ACINUS
;;APOPTOTIC CHROMATIN CONDENSATION INDUCER IN THE NUCLEUS
*FIELD* TX
read moreApoptosis is defined by several unique morphologic nuclear changes,
including chromatin condensation and nuclear fragmentation. These
changes are triggered by the activation of a family of cysteine
proteases called caspases (see 147678), and caspase-activated DNase
(CAD/DFF40; 601883) and lamin protease (see 150330) have been implicated
in some of these changes. CAD/DFF40 induces chromatin condensation in
purified nuclei, but distinct caspase-activated factor(s) may be
responsible for chromatin condensation. Sahara et al. (1999) used an in
vitro system to purify a nuclear factor which induces apoptotic
chromatin condensation after cleavage by caspase-3 (600636) without
inducing DNA fragmentation from bovine thymus lysate. The name of the
factor, 'acinus,' is both an acronym for 'apoptotic chromatin
condensation inducer in the nucleus' and the Latin word for 'grape' or
'berry,' denotive of the grape-like appearance of the condensed
chromatin. Immunodepletion experiments showed that acinus is essential
for apoptotic chromatin condensation in vitro, and an antisense study
revealed that acinus is also important in the induction of apoptotic
chromatin condensation in cells.
As part of a search for human brain cDNA clones with the potential to
encode large proteins in vitro, Ishikawa et al. (1998) independently
identified the human homolog of acinus as cDNA KIAA0670. Ishikawa et al.
(1998) found that KIAA0670 is ubiquitously expressed. Using the KIAA0670
clone, Sahara et al. (1999) obtained 3 isoforms of human acinus cDNA,
the L, S, and S-prime forms, which they stated had probably been
generated by alternative splicing. The acinus L, S, and S-prime cDNAs
contain open reading frames of 1,341, 583, and 568 amino acid residues,
respectively. Mouse and human S and S-prime acinus proteins share 94.5%
and 95.2% amino acid sequence identity, respectively. Ishikawa et al.
(1998) noted homology of acinus to U1 70-kD small nuclear
ribonucleoprotein (180740).
By analysis of a radiation hybrid mapping panel, Ishikawa et al. (1998)
mapped the human gene encoding acinus to chromosome 14.
*FIELD* RF
1. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
2. Sahara, S.; Aoto, M.; Eguchi, Y.; Imamoto, N.; Yoneda, Y.; Tsujimoto,
Y.: Acinus is a caspase-3-activated protein required for apoptotic
chromatin condensation. Nature 401: 168-173, 1999.
*FIELD* CD
Ada Hamosh: 2/18/2000
*FIELD* ED
carol: 12/26/2002
alopez: 2/18/2000