SNUT2_HUMAN
ID SNUT2_HUMAN Reviewed; 565 AA.
AC Q53GS9; A8K086; B3KM40; B4DHT4; D6W5L4; G5E9H0; Q6NX47; Q96RK9; Q9BV89;
AC Q9H381; Q9P050; Q9Y310;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=U4/U6.U5 tri-snRNP-associated protein 2;
DE AltName: Full=Inactive ubiquitin-specific peptidase 39 {ECO:0000303|PubMed:18728397};
DE AltName: Full=SAD1 homolog {ECO:0000303|PubMed:11350945};
DE AltName: Full=U4/U6.U5 tri-snRNP-associated 65 kDa protein {ECO:0000303|PubMed:11350945};
DE Short=65K {ECO:0000303|PubMed:11350945};
GN Name=USP39; ORFNames=CGI-21, HSPC332, PRO2855;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=11350945; DOI=10.1093/emboj/20.10.2553;
RA Makarova O.V., Makarov E.M., Luehrmann R.;
RT "The 65 and 110 kDa SR-related proteins of the U4/U6*U5 tri-snRNP are
RT essential for the assembly of mature spliceosomes.";
RL EMBO J. 20:2553-2563(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Caudate nucleus, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-565.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA Gao F., Liu M., He F.;
RT "Functional prediction of the coding sequences of 75 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-565.
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP SUBUNIT.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5 tri-
RT snRNP.";
RL RNA 12:1418-1430(2006).
RN [12]
RP FUNCTION, AND ABSENCE OF UBIQUITIN-SPECIFIC PEPTIDASE ACTIVITY.
RX PubMed=18728397; DOI=10.4161/cc.7.17.6553;
RA van Leuken R.J., Luna-Vargas M.P., Sixma T.K., Wolthuis R.M., Medema R.H.;
RT "Usp39 is essential for mitotic spindle checkpoint integrity and controls
RT mRNA-levels of aurora B.";
RL Cell Cycle 7:2710-2719(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-82, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
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 (PubMed:11350945, PubMed:26912367). Regulates AURKB mRNA
CC levels, and thereby plays a role in cytokinesis and in the spindle
CC checkpoint. Does not have ubiquitin-specific peptidase activity
CC (PubMed:18728397). {ECO:0000269|PubMed:11350945,
CC ECO:0000269|PubMed:18728397, ECO:0000269|PubMed:26912367}.
CC -!- SUBUNIT: The U4/U6-U5 tri-snRNP complex is a building block of the
CC precatalytic spliceosome (spliceosome B complex) (PubMed:11350945,
CC PubMed:26912367). Component of the U4/U6-U5 tri-snRNP complex composed
CC of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8,
CC PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and
CC USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8
CC (PubMed:16723661, PubMed:26912367). {ECO:0000269|PubMed:11350945,
CC ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:26912367}.
CC -!- INTERACTION:
CC Q53GS9; Q5S007: LRRK2; NbExp=3; IntAct=EBI-1044822, EBI-5323863;
CC Q53GS9; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-1044822, EBI-539478;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350945,
CC ECO:0000269|PubMed:26912367}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q53GS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53GS9-2; Sequence=VSP_045167, VSP_045168;
CC Name=3;
CC IsoId=Q53GS9-3; Sequence=VSP_046822;
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 (PubMed:18728397).
CC {ECO:0000269|PubMed:18728397, ECO:0000305|PubMed:11350945}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27730.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG35521.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF353989; AAK49524.1; -; mRNA.
DR EMBL; AF132955; AAD27730.1; ALT_FRAME; mRNA.
DR EMBL; AK289451; BAF82140.1; -; mRNA.
DR EMBL; AK001047; BAG50852.1; -; mRNA.
DR EMBL; AK295257; BAG58246.1; -; mRNA.
DR EMBL; AK222852; BAD96572.1; -; mRNA.
DR EMBL; AC012454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99490.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99492.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99493.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99494.1; -; Genomic_DNA.
DR EMBL; BC001384; AAH01384.2; -; mRNA.
DR EMBL; BC067273; AAH67273.1; -; mRNA.
DR EMBL; AF130096; AAG35521.1; ALT_INIT; mRNA.
DR EMBL; AF161450; AAF29010.1; -; mRNA.
DR CCDS; CCDS33234.1; -. [Q53GS9-1]
DR CCDS; CCDS58716.1; -. [Q53GS9-2]
DR CCDS; CCDS58717.1; -. [Q53GS9-3]
DR RefSeq; NP_001243654.1; NM_001256725.1. [Q53GS9-1]
DR RefSeq; NP_001243655.1; NM_001256726.1. [Q53GS9-3]
DR RefSeq; NP_001243656.1; NM_001256727.1.
DR RefSeq; NP_001243657.1; NM_001256728.1. [Q53GS9-2]
DR RefSeq; NP_006581.2; NM_006590.3. [Q53GS9-1]
DR RefSeq; XP_006711985.1; XM_006711922.1.
DR RefSeq; XP_006711986.1; XM_006711923.2.
DR RefSeq; XP_011530789.1; XM_011532487.1.
DR RefSeq; XP_011530790.1; XM_011532488.1.
DR RefSeq; XP_016858671.1; XM_017003182.1.
DR PDB; 3JCR; EM; 7.00 A; V=1-565.
DR PDB; 6AH0; EM; 5.70 A; W=1-565.
DR PDB; 6QW6; EM; 2.92 A; U=1-555.
DR PDB; 6QX9; EM; 3.28 A; U=1-555.
DR PDBsum; 3JCR; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; Q53GS9; -.
DR SMR; Q53GS9; -.
DR BioGRID; 115939; 160.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q53GS9; -.
DR IntAct; Q53GS9; 56.
DR MINT; Q53GS9; -.
DR STRING; 9606.ENSP00000312981; -.
DR MEROPS; C19.972; -.
DR GlyGen; Q53GS9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q53GS9; -.
DR MetOSite; Q53GS9; -.
DR PhosphoSitePlus; Q53GS9; -.
DR SwissPalm; Q53GS9; -.
DR BioMuta; USP39; -.
DR DMDM; 88909655; -.
DR EPD; Q53GS9; -.
DR jPOST; Q53GS9; -.
DR MassIVE; Q53GS9; -.
DR MaxQB; Q53GS9; -.
DR PaxDb; Q53GS9; -.
DR PeptideAtlas; Q53GS9; -.
DR PRIDE; Q53GS9; -.
DR ProteomicsDB; 33936; -.
DR ProteomicsDB; 4246; -.
DR ProteomicsDB; 62489; -. [Q53GS9-1]
DR Antibodypedia; 16981; 166 antibodies from 29 providers.
DR DNASU; 10713; -.
DR Ensembl; ENST00000323701.11; ENSP00000312981.6; ENSG00000168883.20. [Q53GS9-1]
DR Ensembl; ENST00000409470.5; ENSP00000386864.1; ENSG00000168883.20. [Q53GS9-1]
DR Ensembl; ENST00000409766.7; ENSP00000386803.3; ENSG00000168883.20. [Q53GS9-3]
DR Ensembl; ENST00000450066.6; ENSP00000396133.2; ENSG00000168883.20. [Q53GS9-2]
DR GeneID; 10713; -.
DR KEGG; hsa:10713; -.
DR MANE-Select; ENST00000323701.11; ENSP00000312981.6; NM_006590.4; NP_006581.2.
DR UCSC; uc002sqe.5; human. [Q53GS9-1]
DR CTD; 10713; -.
DR DisGeNET; 10713; -.
DR GeneCards; USP39; -.
DR HGNC; HGNC:20071; USP39.
DR HPA; ENSG00000168883; Low tissue specificity.
DR MIM; 611594; gene.
DR neXtProt; NX_Q53GS9; -.
DR OpenTargets; ENSG00000168883; -.
DR PharmGKB; PA134905136; -.
DR VEuPathDB; HostDB:ENSG00000168883; -.
DR eggNOG; KOG2026; Eukaryota.
DR GeneTree; ENSGT00390000007992; -.
DR InParanoid; Q53GS9; -.
DR OMA; HVYINLE; -.
DR OrthoDB; 931188at2759; -.
DR PhylomeDB; Q53GS9; -.
DR TreeFam; TF300610; -.
DR PathwayCommons; Q53GS9; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q53GS9; -.
DR BioGRID-ORCS; 10713; 691 hits in 1093 CRISPR screens.
DR ChiTaRS; USP39; human.
DR GeneWiki; USP39; -.
DR GenomeRNAi; 10713; -.
DR Pharos; Q53GS9; Tbio.
DR PRO; PR:Q53GS9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53GS9; protein.
DR Bgee; ENSG00000168883; Expressed in ventricular zone and 192 other tissues.
DR ExpressionAtlas; Q53GS9; baseline and differential.
DR Genevisible; Q53GS9; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
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:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000245; P:spliceosomal complex assembly; IMP: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 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..565
FT /note="U4/U6.U5 tri-snRNP-associated protein 2"
FT /id="PRO_0000223962"
FT DOMAIN 225..555
FT /note="USP"
FT ZN_FING 103..200
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 161
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:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..89
FT /note="MSGRSKRESRGSTRGKRESESRGSSGRVKRERDREREPEAASSRGSPVRVKR
FT EFEPASAREAPASVVPFVRVKREREVDEDSEPEREVR -> MLTAVPSHLFS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045167"
FT VAR_SEQ 113..144
FT /note="RSVLDFDFEKLCSISLSHINAYACLVCGKYFQ -> SFSPFPT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045168"
FT VAR_SEQ 477..565
FT /note="NVDLREYLSEEVQAVHKNTTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYE
FT LQDLQVTDILPQMITLSEAYIQIWKRRDNDETNQQGA -> GQANGMNYKTSR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046822"
FT CONFLICT 13
FT /note="T -> I (in Ref. 4; BAD96572)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> V (in Ref. 4; BAD96572)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="F -> S (in Ref. 3; BAG50852)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> P (in Ref. 3; BAG50852)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="V -> A (in Ref. 3; BAG50852)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> F (in Ref. 1; AAK49524)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="R -> I (in Ref. 2; AAD27730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 65381 MW; 8946FD5DCDEFD0B0 CRC64;
MSGRSKRESR GSTRGKRESE SRGSSGRVKR ERDREREPEA ASSRGSPVRV KREFEPASAR
EAPASVVPFV RVKREREVDE DSEPEREVRA KNGRVDSEDR RSRHCPYLDT INRSVLDFDF
EKLCSISLSH INAYACLVCG KYFQGRGLKS HAYIHSVQFS HHVFLNLHTL KFYCLPDNYE
IIDSSLEDIT YVLKPTFTKQ QIANLDKQAK LSRAYDGTTY LPGIVGLNNI KANDYANAVL
QALSNVPPLR NYFLEEDNYK NIKRPPGDIM FLLVQRFGEL MRKLWNPRNF KAHVSPHEML
QAVVLCSKKT FQITKQGDGV DFLSWFLNAL HSALGGTKKK KKTIVTDVFQ GSMRIFTKKL
PHPDLPAEEK EQLLHNDEYQ ETMVESTFMY LTLDLPTAPL YKDEKEQLII PQVPLFNILA
KFNGITEKEY KTYKENFLKR FQLTKLPPYL IFCIKRFTKN NFFVEKNPTI VNFPITNVDL
REYLSEEVQA VHKNTTYDLI ANIVHDGKPS EGSYRIHVLH HGTGKWYELQ DLQVTDILPQ
MITLSEAYIQ IWKRRDNDET NQQGA
