ID SNUT1_MOUSE Reviewed; 806 AA. AC Q9Z315; Q8K155; Q9R1I9; Q9R270; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein 1; DE AltName: Full=Hypoxia-associated factor; DE AltName: Full=Squamous cell carcinoma antigen recognized by T-cells 1; DE Short=SART-1; DE Short=mSART-1; GN Name=Sart1; Synonyms=Haf; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9765622; DOI=10.1111/j.1349-7006.1998.tb00639.x; RA Gotoh M., Shichijo S., Hoshino T., Imai Y., Imaizumi T., Inoue Y., RA Takasu H., Yamaoka T., Itoh K.; RT "Sequence analysis of genes encoding rodent homologues of the human tumor- RT rejection antigen SART-1."; RL Jpn. J. Cancer Res. 89:849-854(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP FUNCTION. RX PubMed=10887110; RA Gupta M., Mungai P.T., Goldwasser E.; RT "A new transacting factor that modulates hypoxia-induced expression of the RT erythropoietin gene."; RL Blood 96:491-497(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-742. RC STRAIN=C57BL/6J; RX PubMed=11410364; DOI=10.1016/s0378-1119(01)00504-2; RA Bolland D.J., Hewitt J.E.; RT "Intron loss in the SART1 genes of Fugu rubripes and Tetraodon RT nigroviridis."; RL Gene 271:43-49(2001). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189 AND SER-480, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Lung, Pancreas, 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). CC -!- FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5 CC tri-snRNP, one of the building blocks of the spliceosome. May also bind CC to DNA. {ECO:0000250|UniProtKB:O43290, ECO:0000269|PubMed:10887110}. CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Interacts with CC UBL5. {ECO:0000250|UniProtKB:O43290}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43290}. CC Note=Found in the nucleus of mitogen-activated peripheral blood CC mononuclear cells (PBMCs), tumor cells, or normal cell lines, but not CC in normal tissues except testis and fetal liver or in unstimulated CC PBMCs, suggesting preferential expression in proliferating cells. CC {ECO:0000250|UniProtKB:O43290}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Shows a high expression in CC fetal liver and a low expression in adult liver. CC {ECO:0000269|PubMed:10887110}. CC -!- DEVELOPMENTAL STAGE: Expressed at maximal level at 12 dpc. Declines CC progressively until birth. {ECO:0000269|PubMed:10887110}. CC -!- PTM: Sumoylated with SUMO2. {ECO:0000250|UniProtKB:O43290}. CC -!- SIMILARITY: Belongs to the SNU66/SART1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB014721; BAA36583.1; -; mRNA. DR EMBL; AF129931; AAD20645.1; -; mRNA. DR EMBL; BC028823; AAH28823.1; -; mRNA. DR EMBL; BC051394; AAH51394.1; -; mRNA. DR EMBL; AF105334; AAD38450.1; -; Genomic_DNA. DR CCDS; CCDS29460.1; -. DR RefSeq; NP_058578.3; NM_016882.3. DR AlphaFoldDB; Q9Z315; -. DR SMR; Q9Z315; -. DR BioGRID; 203075; 27. DR IntAct; Q9Z315; 25. DR MINT; Q9Z315; -. DR STRING; 10090.ENSMUSP00000047397; -. DR GlyGen; Q9Z315; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z315; -. DR PhosphoSitePlus; Q9Z315; -. DR SwissPalm; Q9Z315; -. DR EPD; Q9Z315; -. DR jPOST; Q9Z315; -. DR MaxQB; Q9Z315; -. DR PaxDb; 10090-ENSMUSP00000047397; -. DR PeptideAtlas; Q9Z315; -. DR ProteomicsDB; 261465; -. DR Pumba; Q9Z315; -. DR Antibodypedia; 30019; 231 antibodies from 36 providers. DR DNASU; 20227; -. DR Ensembl; ENSMUST00000044207.5; ENSMUSP00000047397.5; ENSMUSG00000039148.6. DR GeneID; 20227; -. DR KEGG; mmu:20227; -. DR UCSC; uc008gcu.1; mouse. DR AGR; MGI:1309453; -. DR CTD; 9092; -. DR MGI; MGI:1309453; Sart1. DR VEuPathDB; HostDB:ENSMUSG00000039148; -. DR eggNOG; KOG2217; Eukaryota. DR GeneTree; ENSGT00390000007071; -. DR HOGENOM; CLU_009379_3_0_1; -. DR InParanoid; Q9Z315; -. DR OMA; DTQMQKV; -. DR OrthoDB; 24344at2759; -. DR PhylomeDB; Q9Z315; -. DR TreeFam; TF318828; -. DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway. DR BioGRID-ORCS; 20227; 15 hits in 80 CRISPR screens. DR ChiTaRS; Sart1; mouse. DR PRO; PR:Q9Z315; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9Z315; Protein. DR Bgee; ENSMUSG00000039148; Expressed in retinal neural layer and 279 other cell types or tissues. DR ExpressionAtlas; Q9Z315; baseline and differential. DR GO; GO:0015030; C:Cajal body; ISO:MGI. DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0016607; C:nuclear speck; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISO:MGI. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI. DR GO; GO:0000481; P:maturation of 5S rRNA; IBA:GO_Central. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI. DR GO; GO:0045585; P:positive regulation of cytotoxic T cell differentiation; ISO:MGI. DR InterPro; IPR045347; HIND. DR InterPro; IPR005011; SNU66/SART1. DR PANTHER; PTHR14152; SQUAMOUS CELL CARCINOMA ANTIGEN RECOGNISED BY CYTOTOXIC T LYMPHOCYTES; 1. DR PANTHER; PTHR14152:SF5; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 1; 1. DR Pfam; PF19252; HIND; 1. DR Pfam; PF03343; SART-1; 1. DR Genevisible; Q9Z315; MM. PE 1: Evidence at protein level; KW Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation. FT CHAIN 1..806 FT /note="U4/U6.U5 tri-snRNP-associated protein 1" FT /id="PRO_0000223309" FT REGION 1..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 418..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 157..231 FT /evidence="ECO:0000255" FT COILED 494..540 FT /evidence="ECO:0000255" FT COMPBIAS 44..104 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 435..451 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 582..602 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 189 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 430 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 527 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 597 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 602 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 604 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 627 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 701 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 767 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 770 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT MOD_RES 795 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 125 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 133 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 147 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 188 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 277 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 329 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 336 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 400 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 414 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 554 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 654 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 663 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 690 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 705 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 715 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 729 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 755 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 764 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 781 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 786 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CROSSLNK 797 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43290" FT CONFLICT 70 FT /note="A -> T (in Ref. 2; AAD20645 and 3; FT AAH28823/AAH51394)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="C -> Y (in Ref. 2; AAD20645)" FT /evidence="ECO:0000305" SQ SEQUENCE 806 AA; 90885 MW; 1417E85C71BF380C CRC64; MGSSKKHRGE KEAAGTTAAA GTGGTTEQPP RHREHKKHKH RSSGGGSSGG ERRKRSRERG SERGSGRRGA EAEARSGAHG RERSQAEPSE RRVKREKRDD GYEAAASSKA SSGDASSLSI EETNKLRAKL GLKPLEVNAV KKEAGTKEEP VAADVINPMA LRQREELREK LAAAKEKRLL NQKLGKIKTL GEDDPWLDDT AAWIERSRQL QKEKDLAEKR AKLLEEMDQE FGVSTLVEEE FEQRRQDLYS ARDLQGLTVE HAIDSFREGE TVVLTLKDKG VLQDGEDVLV NVNMVDKERA DKNVELRKKK PDYLPYAEDE SVDDLAQQKP RSILAKYDEE LEGERPHSFR LEQGGMADGL RERELEEIRT KLRLQAQSLS SVGPRLASEY LSPEEMVTFK KTKRRVKKIR KKEKEVIMRA DDLLPLGDQT QDGDFGSRLR GRGRRRVPEV EEEALEDEEK DPVAQPPPSD DTRVENMDIS DEEDGGALPP GSPEGLEEDE AELELQKQLE KGRRLRQLQQ LQQLRDSGEK VLEIVKKLES RQRGWEEEED PERKGTIVFN ATSEFCRTLG EIPTYGLAGN REEQEELMDF ERDEERSANG GSESDGEENI GWSTVNLDEE KQHQDFSASS TTILDEEPIV NRGLAAALLL CQNKGLLETT VQKVARVKAP NKSLPSAVYC IEDKMAIDDK YSRREEYRGF TQDFKEKDGY KPDVKIEYVD ETGRKLTPKE AFRQLSHRFH GKGSGKMKTE RRMKKLDEEA LLKKMSSSDT PLGTVALLQE KQKAQKTPYI VLSGSGKSMN ANTITK //