ISY1_MOUSE
ID ISY1_MOUSE Reviewed; 285 AA.
AC Q69ZQ2; Q8VDX4; Q9D3E2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Pre-mRNA-splicing factor ISY1 homolog;
GN Name=Isy1; Synonyms=Kiaa1160;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH CPSF3;
RP DGCR8 AND DROSHA, AND DEVELOPMENTAL STAGE.
RX PubMed=26255770; DOI=10.1016/j.cell.2015.07.008;
RA Du P., Wang L., Sliz P., Gregory R.I.;
RT "A biogenesis step upstream of microprocessor controls miR-17~92
RT expression.";
RL Cell 162:885-899(2015).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=29804889; DOI=10.1016/j.stem.2018.04.021;
RA Du P., Pirouz M., Choi J., Huebner A.J., Clement K., Meissner A.,
RA Hochedlinger K., Gregory R.I.;
RT "An intermediate pluripotent state controlled by microRNAs is required for
RT the naive-to-primed stem cell transition.";
RL Cell Stem Cell 22:851-864(2018).
RN [7]
RP STRUCTURE BY NMR OF 24-102.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ISY1 domain in hypothetical protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Component of the spliceosome C complex required for the
CC selective processing of microRNAs (miRNAs) during embryonic stem cell
CC differentiation (PubMed:26255770, PubMed:29804889). Required for the
CC biogenesis of all miRNAs from the pri-miR-17-92 primary transcript
CC except miR-92a (PubMed:26255770). Only required for the biogenesis of
CC miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary
CC transcripts, respectively (PubMed:29804889). Required during the
CC transition of embryonic stem cells (ESCs) from the naive to primed
CC state (PubMed:29804889). By enhancing miRNA biogenesis, promotes exit
CC of ESCs from the naive state to an intermediate state of poised
CC pluripotency, which precedes the transition to the primed state
CC (PubMed:29804889). Involved in pre-mRNA splicing as component of the
CC spliceosome. {ECO:0000250|UniProtKB:Q9ULR0,
CC ECO:0000269|PubMed:26255770, ECO:0000269|PubMed:29804889}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the XAB2
CC complex, a multimeric protein complex composed of XAB2, PRPF19, AQR,
CC ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB)
CC complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is
CC incorporated into the spliceosome as a preassembled complex. The IB
CC complex does not contain PRPF19. Interacts with CPSF3; this interaction
CC is in an RNA independent manner (PubMed:26255770). Interacts with the
CC microprocessor complex subunits DGCR8 and DROSHA; this interaction is
CC in an RNA dependent manner (PubMed:26255770).
CC {ECO:0000250|UniProtKB:Q9ULR0, ECO:0000269|PubMed:26255770}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR0}.
CC -!- DEVELOPMENTAL STAGE: During embryoid body (EB) formation, expression
CC peaks at day 1 of EB differentiation (at protein level)
CC (PubMed:29804889). Expressed during embryonic stem cell differentiation
CC in vitro, with high expression during the earliest time point of
CC differentiation during a 'poised' pluripotency phase that occurs in
CC between embryonic day 4.5 and embryonic day 5.5 (PubMed:26255770,
CC PubMed:29804889). {ECO:0000269|PubMed:26255770,
CC ECO:0000269|PubMed:29804889}.
CC -!- SIMILARITY: Belongs to the ISY1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32394.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173116; BAD32394.1; ALT_INIT; mRNA.
DR EMBL; AK017996; BAB31028.1; -; mRNA.
DR EMBL; BC020103; AAH20103.1; -; mRNA.
DR EMBL; BC037695; AAH37695.1; -; mRNA.
DR CCDS; CCDS39548.1; -.
DR RefSeq; NP_598695.1; NM_133934.4.
DR PDB; 1X4T; NMR; -; A=24-102.
DR PDBsum; 1X4T; -.
DR AlphaFoldDB; Q69ZQ2; -.
DR SMR; Q69ZQ2; -.
DR BioGRID; 208359; 19.
DR IntAct; Q69ZQ2; 18.
DR STRING; 10090.ENSMUSP00000086923; -.
DR iPTMnet; Q69ZQ2; -.
DR PhosphoSitePlus; Q69ZQ2; -.
DR EPD; Q69ZQ2; -.
DR MaxQB; Q69ZQ2; -.
DR PaxDb; Q69ZQ2; -.
DR PeptideAtlas; Q69ZQ2; -.
DR PRIDE; Q69ZQ2; -.
DR ProteomicsDB; 269003; -.
DR DNASU; 57905; -.
DR Ensembl; ENSMUST00000089497; ENSMUSP00000086923; ENSMUSG00000030056.
DR GeneID; 57905; -.
DR KEGG; mmu:57905; -.
DR UCSC; uc009cub.1; mouse.
DR CTD; 57461; -.
DR MGI; MGI:1923310; Isy1.
DR VEuPathDB; HostDB:ENSMUSG00000030056; -.
DR eggNOG; KOG3068; Eukaryota.
DR GeneTree; ENSGT00390000014109; -.
DR HOGENOM; CLU_043453_0_0_1; -.
DR InParanoid; Q69ZQ2; -.
DR OMA; MARSQEK; -.
DR OrthoDB; 1513531at2759; -.
DR PhylomeDB; Q69ZQ2; -.
DR TreeFam; TF105841; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 57905; 22 hits in 70 CRISPR screens.
DR ChiTaRS; Isy1; mouse.
DR EvolutionaryTrace; Q69ZQ2; -.
DR PRO; PR:Q69ZQ2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q69ZQ2; protein.
DR Bgee; ENSMUSG00000030056; Expressed in embryonic post-anal tail and 230 other tissues.
DR ExpressionAtlas; Q69ZQ2; baseline and differential.
DR Genevisible; Q69ZQ2; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071020; C:post-spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IBA:GO_Central.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR Gene3D; 1.10.287.660; -; 1.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009360; Isy1.
DR InterPro; IPR037200; Isy1_sf.
DR PANTHER; PTHR13021; PTHR13021; 1.
DR Pfam; PF06246; Isy1; 1.
DR SUPFAM; SSF140102; SSF140102; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..285
FT /note="Pre-mRNA-splicing factor ISY1 homolog"
FT /id="PRO_0000235814"
FT REGION 197..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR0"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR0"
FT CONFLICT 133
FT /note="R -> K (in Ref. 2; BAB31028)"
FT /evidence="ECO:0000305"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1X4T"
FT HELIX 39..62
FT /evidence="ECO:0007829|PDB:1X4T"
FT HELIX 67..94
FT /evidence="ECO:0007829|PDB:1X4T"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1X4T"
SQ SEQUENCE 285 AA; 32989 MW; 4A456045660F29D6 CRC64;
MARNAEKAMT ALARFRQAQL EEGKVKERRP FLASECTELP KAEKWRRQII GEISKKVAQI
QNAGLGEFRI RDLNDEINKL LREKGHWEVR IKELGGPDYG KVGPKMLDHE GKEVPGNRGY
KYFGAAKDLP GVRELFEKEP LPPPRKTRAE LMKAIDFEYY GYLDEDDGVI VPLEQEYEKK
LRAELVEKWK AEREARLARG EKEEEEEEEE EINIYAVTEE ESDEEGNQEK AGEDGQQKFI
AHVPVPSQQE IEEALVRRKK MELLQKYASE TLQAQSEEAK RLLGY
