SNUT1_RAT
ID SNUT1_RAT Reviewed; 806 AA.
AC Q5XIW8; Q9Z314;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein 1;
DE AltName: Full=Squamous cell carcinoma antigen recognized by T-cells 1;
DE Short=SART-1;
DE Short=rSART-1;
GN Name=Sart1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; SER-597; SER-602 AND
RP SER-604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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 -!- PTM: Sumoylated with SUMO2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNU66/SART1 family. {ECO:0000305}.
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DR EMBL; AB014722; BAA36584.1; -; mRNA.
DR EMBL; BC083551; AAH83551.1; -; mRNA.
DR RefSeq; NP_113784.1; NM_031596.1.
DR AlphaFoldDB; Q5XIW8; -.
DR SMR; Q5XIW8; -.
DR STRING; 10116.ENSRNOP00000027812; -.
DR iPTMnet; Q5XIW8; -.
DR PhosphoSitePlus; Q5XIW8; -.
DR jPOST; Q5XIW8; -.
DR PaxDb; Q5XIW8; -.
DR PRIDE; Q5XIW8; -.
DR Ensembl; ENSRNOT00000027811; ENSRNOP00000027812; ENSRNOG00000020475.
DR GeneID; 29678; -.
DR KEGG; rno:29678; -.
DR UCSC; RGD:61930; rat.
DR CTD; 9092; -.
DR RGD; 61930; Sart1.
DR eggNOG; KOG2217; Eukaryota.
DR GeneTree; ENSGT00390000007071; -.
DR HOGENOM; CLU_009379_3_0_1; -.
DR InParanoid; Q5XIW8; -.
DR OMA; EYARWEN; -.
DR OrthoDB; 1068640at2759; -.
DR PhylomeDB; Q5XIW8; -.
DR TreeFam; TF318828; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q5XIW8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020475; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5XIW8; RN.
DR GO; GO:0015030; C:Cajal body; ISO:RGD.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISO:RGD.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
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:RGD.
DR GO; GO:0045585; P:positive regulation of cytotoxic T cell differentiation; ISO:RGD.
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_0000223310"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..505
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 495..540
FT /evidence="ECO:0000255"
FT COMPBIAS 44..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..452
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:0000250|UniProtKB:Q9Z315"
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 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43290"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43290"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 317
FT /note="A -> V (in Ref. 1; BAA36584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 91011 MW; C8A1BCADC07544E9 CRC64;
MGSSKKHRGE KEAAGTTAAA GTGGTTEQPP RHREHKKHKH RSSGGGSSGG ERRKRSRERG
AERGSGRRGA EAEARSGAHG RERSQAEPSE RRVKREKRDE GYEAAASSKA SSGDASSLSI
EETNKLRAKL GLKPLEVNAV KKEAGTKEEP VAADVINPMA LRQREELREK LAAAKEKRLL
NQKLGKIKTL GEDDPWLDDT AAWIERSRQL QKEKDLAEKR AKLLEEMDQE FGVSTLVEEE
FEQRRQDLYS ARDLQGLTVE HAIDSFREGE TVVLTLKDKG VLQEGEDVLV NVNMVDKERA
DKNVELRKKK PDYLPYAEDE SVDDLAQQKP RSILAKYDEE LEGERPHSFR LEQGGMADGL
RERELEEIRT KLRLQAQSLN TVGPRLASEY LSPEEMVTFK KTKRRVKKIR KKEKEVIMRA
DDLLPLGEDQ TQDGDFGSRL RGRGRRRVPE VEEEALEDEE KDPVAQPPPS DDTRVENMDI
SDEEDGGALP SGPPELEEDE 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
