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SNUT1_MOUSE
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   03-AUG-2022, entry version 133.
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. Appears to play a role in hypoxia-induced regulation of EPO
CC       gene expression. {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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the SNU66/SART1 family. {ECO:0000305}.
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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; 26.
DR   IntAct; Q9Z315; 25.
DR   MINT; Q9Z315; -.
DR   STRING; 10090.ENSMUSP00000047397; -.
DR   iPTMnet; Q9Z315; -.
DR   PhosphoSitePlus; Q9Z315; -.
DR   EPD; Q9Z315; -.
DR   jPOST; Q9Z315; -.
DR   MaxQB; Q9Z315; -.
DR   PaxDb; Q9Z315; -.
DR   PeptideAtlas; Q9Z315; -.
DR   PRIDE; Q9Z315; -.
DR   ProteomicsDB; 261465; -.
DR   Antibodypedia; 30019; 219 antibodies from 36 providers.
DR   DNASU; 20227; -.
DR   Ensembl; ENSMUST00000044207; ENSMUSP00000047397; ENSMUSG00000039148.
DR   GeneID; 20227; -.
DR   KEGG; mmu:20227; -.
DR   UCSC; uc008gcu.1; mouse.
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; EYARWEN; -.
DR   OrthoDB; 1068640at2759; -.
DR   PhylomeDB; Q9Z315; -.
DR   TreeFam; TF318828; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 20227; 15 hits in 75 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 276 other tissues.
DR   ExpressionAtlas; Q9Z315; baseline and differential.
DR   Genevisible; Q9Z315; MM.
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; PTHR14152; 1.
DR   Pfam; PF19252; HIND; 1.
DR   Pfam; PF03343; SART-1; 1.
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; AAH28823/
FT                   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
 
 
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