SNUT2_MOUSE
ID SNUT2_MOUSE Reviewed; 564 AA.
AC Q3TIX9; Q3TI55; Q8BLI5; Q8BZZ5; Q9CQR1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein 2;
DE AltName: Full=Inactive ubiquitin-specific peptidase 39;
GN Name=Usp39;
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 STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Cecum, Colon, Placenta, Testis, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 pre-mRNA splicing as a component of the
CC U4/U6-U5 tri-snRNP, one of the building blocks of the precatalytic
CC spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in
CC cytokinesis and in the spindle checkpoint. Does not have ubiquitin-
CC specific peptidase activity. {ECO:0000250|UniProtKB:Q53GS9}.
CC -!- SUBUNIT: The U4/U6-U5 tri-snRNP complex is a building block of the
CC precatalytic spliceosome (spliceosome B 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 SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2,
CC PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5,
CC LSM6, LSM7 and LSM8. {ECO:0000250|UniProtKB:Q53GS9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53GS9}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved His and Cys residues that are essential
CC for the activity of de-ubiquitinating enzymes. Lacks ubiquitin C-
CC terminal hydrolase activity. {ECO:0000250|UniProtKB:Q53GS9,
CC ECO:0000305}.
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DR EMBL; AK010443; BAB26944.1; -; mRNA.
DR EMBL; AK018595; BAB31299.1; -; mRNA.
DR EMBL; AK033105; BAC28153.1; -; mRNA.
DR EMBL; AK045062; BAC32203.1; -; mRNA.
DR EMBL; AK167668; BAE39717.1; -; mRNA.
DR EMBL; AK165625; BAE38302.1; -; mRNA.
DR EMBL; AK168003; BAE39991.1; -; mRNA.
DR EMBL; AK088354; BAC40299.1; -; mRNA.
DR EMBL; BC026983; AAH26983.1; -; mRNA.
DR CCDS; CCDS20238.1; -.
DR RefSeq; NP_613058.1; NM_138592.4.
DR AlphaFoldDB; Q3TIX9; -.
DR SMR; Q3TIX9; -.
DR BioGRID; 205726; 3.
DR IntAct; Q3TIX9; 3.
DR MINT; Q3TIX9; -.
DR STRING; 10090.ENSMUSP00000064515; -.
DR MEROPS; C19.972; -.
DR iPTMnet; Q3TIX9; -.
DR PhosphoSitePlus; Q3TIX9; -.
DR EPD; Q3TIX9; -.
DR jPOST; Q3TIX9; -.
DR MaxQB; Q3TIX9; -.
DR PaxDb; Q3TIX9; -.
DR PeptideAtlas; Q3TIX9; -.
DR PRIDE; Q3TIX9; -.
DR ProteomicsDB; 261298; -.
DR Antibodypedia; 16981; 166 antibodies from 29 providers.
DR DNASU; 28035; -.
DR Ensembl; ENSMUST00000070345; ENSMUSP00000064515; ENSMUSG00000056305.
DR GeneID; 28035; -.
DR KEGG; mmu:28035; -.
DR UCSC; uc009cif.1; mouse.
DR CTD; 10713; -.
DR MGI; MGI:107622; Usp39.
DR VEuPathDB; HostDB:ENSMUSG00000056305; -.
DR eggNOG; KOG2026; Eukaryota.
DR GeneTree; ENSGT00390000007992; -.
DR HOGENOM; CLU_016848_4_0_1; -.
DR InParanoid; Q3TIX9; -.
DR OMA; HVYINLE; -.
DR OrthoDB; 931188at2759; -.
DR PhylomeDB; Q3TIX9; -.
DR TreeFam; TF300610; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 28035; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Usp39; mouse.
DR PRO; PR:Q3TIX9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3TIX9; protein.
DR Bgee; ENSMUSG00000056305; Expressed in epiblast (generic) and 80 other tissues.
DR ExpressionAtlas; Q3TIX9; baseline and differential.
DR Genevisible; Q3TIX9; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISS:UniProtKB.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; PTHR21646:SF16; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..564
FT /note="U4/U6.U5 tri-snRNP-associated protein 2"
FT /id="PRO_0000223963"
FT DOMAIN 224..554
FT /note="USP"
FT ZN_FING 102..199
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GS9"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GS9"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GS9"
FT CONFLICT 3
FT /note="S -> T (in Ref. 1; BAC32203)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="R -> S (in Ref. 1; BAE39991)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> V (in Ref. 1; BAC28153)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="K -> E (in Ref. 1; AAH26983/BAE39717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 65146 MW; 67A84B80FEE5AB71 CRC64;
MSSRSKRQSH GSTRGKRESE SRGSSGRIKK ERDREKEPEA ASSRGSPVRV KREAEPAARE
VPAPALPVVR VKREREADED SEPEREVRAK NGRVDSEDRR SRHCPYLDTI NRSVLDFDFE
KLCSISLSHI NAYACLVCGK YFQGRGLKSH AYIHSVQFSH HVFLNLHTLK FYCLPDNYEI
IDSSLEDITY VLKPTFTKQQ IANLDKQAKL SRAYDGTTYL PGIVGLNNIK ANDYANAVLQ
ALSNVPPLRN YFLEEDNYKN IKRPPGDIMF LLVQRFGELM RKLWNPRNFK AHVSPHEMLQ
AVVLCSKKTF QITKQGDGVD FLSWFLNALH SALGGTKKKK KTIVNDVFQG SMRIFTKKLP
HPDLPAEEKE QLLHNDEYQE TMVESTFMYL TLDLPTAPLY KDEKEQLIIP QVPLFNILAK
FNGITEKEYK TYKENFLKRF QLTKLPPYLI FCIKRFTKNN FFVEKNPTIV NFPITNVDLR
EYLSEEVQAV HKNTTYDLIA NIVHDGKPSE GSYRIHVLHH GTGKWYELQD LQVTDILPQM
ITLSEAYIQI WKRRDNDETN QQGA
