UTP25_HUMAN
ID UTP25_HUMAN Reviewed; 756 AA.
AC Q68CQ4; O75992; Q4VY00; Q63HL9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=U3 small nucleolar RNA-associated protein 25 homolog {ECO:0000305};
DE AltName: Full=Digestive organ expansion factor homolog;
DE AltName: Full=UTP25 small subunit processor component {ECO:0000312|HGNC:HGNC:28440};
GN Name=UTP25 {ECO:0000312|HGNC:HGNC:28440};
GN Synonyms=C1orf107, DEF {ECO:0000303|PubMed:23357851},
GN DIEXF {ECO:0000303|PubMed:25007945};
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 [LARGE SCALE MRNA], AND VARIANTS GLU-67 AND ASP-111.
RC TISSUE=Endometrial adenocarcinoma, and Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY MIR195.
RX PubMed=25007945; DOI=10.1186/1471-230x-14-123;
RA Lei H., Tang J., Li H., Zhang H., Lu C., Chen H., Li W., Xia Y., Tang W.;
RT "MiR-195 affects cell migration and cell proliferation by down-regulating
RT DIEXF in Hirschsprung's disease.";
RL BMC Gastroenterol. 14:123-123(2014).
RN [9]
RP FUNCTION, INTERACTION WITH CAPN3, AND PHOSPHORYLATION AT SER-50; SER-58 AND
RP SER-62.
RX PubMed=27657329; DOI=10.1371/journal.pbio.1002555;
RA Guan Y., Huang D., Chen F., Gao C., Tao T., Shi H., Zhao S., Liao Z.,
RA Lo L.J., Wang Y., Chen J., Peng J.;
RT "Phosphorylation of Def Regulates Nucleolar p53 Turnover and Cell Cycle
RT Progression through Def Recruitment of Calpain3.";
RL PLoS Biol. 14:e1002555-e1002555(2016).
RN [10]
RP VARIANTS GLU-67 AND ASP-111, CHARACTERIZATION OF VARIANTS GLU-67 AND
RP ASP-111, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAPN3.
RX PubMed=23357851; DOI=10.1038/cr.2013.16;
RA Tao T., Shi H., Guan Y., Huang D., Chen Y., Lane D.P., Chen J., Peng J.;
RT "Def defines a conserved nucleolar pathway that leads p53 to proteasome-
RT independent degradation.";
RL Cell Res. 23:620-634(2013).
CC -!- FUNCTION: Component of the ribosomal small subunit processome for the
CC biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA)
CC processing (By similarity). Essential for embryonic development in part
CC through the regulation of p53 pathway. Controls the expansion growth of
CC digestive organs and liver (PubMed:25007945, PubMed:27657329,
CC PubMed:23357851). Also involved in the sympathetic neuronal development
CC (By similarity). Mediates, with CAPN3, the proteasome-independent
CC degradation of p53/TP53 (PubMed:23357851, PubMed:27657329).
CC {ECO:0000250|UniProtKB:Q6PEH4, ECO:0000269|PubMed:23357851,
CC ECO:0000269|PubMed:25007945, ECO:0000269|PubMed:27657329}.
CC -!- SUBUNIT: Interacts with CAPN3; the interaction is required for CAPN3
CC translocation to the nucleolus. {ECO:0000269|PubMed:23357851,
CC ECO:0000269|PubMed:27657329}.
CC -!- INTERACTION:
CC Q68CQ4; Q96CW1: AP2M1; NbExp=5; IntAct=EBI-747711, EBI-297683;
CC Q68CQ4; Q8NHQ1: CEP70; NbExp=8; IntAct=EBI-747711, EBI-739624;
CC Q68CQ4; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-747711, EBI-10178634;
CC Q68CQ4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-747711, EBI-16439278;
CC Q68CQ4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-747711, EBI-10172526;
CC Q68CQ4; Q8TD10: MIPOL1; NbExp=4; IntAct=EBI-747711, EBI-2548751;
CC Q68CQ4; Q96T51: RUFY1; NbExp=5; IntAct=EBI-747711, EBI-3941207;
CC Q68CQ4; Q96T51-2: RUFY1; NbExp=6; IntAct=EBI-747711, EBI-12192715;
CC Q68CQ4; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-747711, EBI-6929619;
CC Q68CQ4; Q9C026: TRIM9; NbExp=3; IntAct=EBI-747711, EBI-720828;
CC Q68CQ4; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-747711, EBI-12017160;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:22002106,
CC ECO:0000269|PubMed:27657329}.
CC -!- TISSUE SPECIFICITY: Expressed in colon. {ECO:0000269|PubMed:25007945}.
CC -!- INDUCTION: Down-regulated by the miRNA MIR195.
CC {ECO:0000269|PubMed:25007945}.
CC -!- PTM: Phosphorylated. Phosphorylation is required to promote p53/TP53
CC degradation in the nucleolus which promotes cell cycle progression and
CC liver development. {ECO:0000269|PubMed:27657329}.
CC -!- SIMILARITY: Belongs to the UTP25 family. {ECO:0000305}.
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DR EMBL; CR749825; CAH18684.1; -; mRNA.
DR EMBL; BX648514; CAH56170.1; -; mRNA.
DR EMBL; AL022398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022964; AAH22964.1; -; mRNA.
DR CCDS; CCDS1493.1; -.
DR RefSeq; NP_055203.4; NM_014388.6.
DR AlphaFoldDB; Q68CQ4; -.
DR BioGRID; 117972; 94.
DR IntAct; Q68CQ4; 21.
DR MINT; Q68CQ4; -.
DR STRING; 9606.ENSP00000419005; -.
DR GlyGen; Q68CQ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q68CQ4; -.
DR PhosphoSitePlus; Q68CQ4; -.
DR BioMuta; DIEXF; -.
DR DMDM; 117949399; -.
DR EPD; Q68CQ4; -.
DR jPOST; Q68CQ4; -.
DR MassIVE; Q68CQ4; -.
DR MaxQB; Q68CQ4; -.
DR PaxDb; Q68CQ4; -.
DR PeptideAtlas; Q68CQ4; -.
DR PRIDE; Q68CQ4; -.
DR ProteomicsDB; 66020; -.
DR Antibodypedia; 20703; 83 antibodies from 20 providers.
DR DNASU; 27042; -.
DR Ensembl; ENST00000491415.7; ENSP00000419005.1; ENSG00000117597.18.
DR GeneID; 27042; -.
DR KEGG; hsa:27042; -.
DR MANE-Select; ENST00000491415.7; ENSP00000419005.1; NM_014388.7; NP_055203.4.
DR UCSC; uc001hhr.3; human.
DR CTD; 27042; -.
DR DisGeNET; 27042; -.
DR GeneCards; UTP25; -.
DR HGNC; HGNC:28440; UTP25.
DR HPA; ENSG00000117597; Low tissue specificity.
DR MIM; 619663; gene.
DR neXtProt; NX_Q68CQ4; -.
DR OpenTargets; ENSG00000117597; -.
DR PharmGKB; PA142672491; -.
DR VEuPathDB; HostDB:ENSG00000117597; -.
DR eggNOG; KOG2340; Eukaryota.
DR GeneTree; ENSGT00390000000709; -.
DR HOGENOM; CLU_018705_1_1_1; -.
DR InParanoid; Q68CQ4; -.
DR OMA; KYFRQTI; -.
DR OrthoDB; 257318at2759; -.
DR PhylomeDB; Q68CQ4; -.
DR TreeFam; TF105930; -.
DR PathwayCommons; Q68CQ4; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q68CQ4; -.
DR BioGRID-ORCS; 27042; 651 hits in 1075 CRISPR screens.
DR ChiTaRS; DIEXF; human.
DR GenomeRNAi; 27042; -.
DR Pharos; Q68CQ4; Tbio.
DR PRO; PR:Q68CQ4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q68CQ4; protein.
DR Bgee; ENSG00000117597; Expressed in endothelial cell and 208 other tissues.
DR ExpressionAtlas; Q68CQ4; baseline and differential.
DR Genevisible; Q68CQ4; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; IMP:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010678; UTP25.
DR PANTHER; PTHR12933; PTHR12933; 1.
DR Pfam; PF06862; UTP25; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..756
FT /note="U3 small nucleolar RNA-associated protein 25
FT homolog"
FT /id="PRO_0000254149"
FT REGION 1..185
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..635
FT /note="Promotes p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT REGION 636..697
FT /note="Represses p53/TP53 degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27657329"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27657329"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27657329"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEH4"
FT VARIANT 67
FT /note="Q -> E (decreases degradation of p53/TP53;
FT dbSNP:rs585627)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:23357851"
FT /id="VAR_028827"
FT VARIANT 111
FT /note="G -> D (decreases degradation of p53/TP53;
FT dbSNP:rs61747285)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:23357851"
FT /id="VAR_084648"
FT CONFLICT 258
FT /note="T -> A (in Ref. 1; CAH56170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 87055 MW; A8821B0AC4BF4067 CRC64;
MGKRGSRSQS QLLNTLTKKQ KKHLRDFGEE HPFYDRVSRK EAKPQICQLS ESSDSSDSES
DSESEPQQVS GYHRLLATLK NVSEEEEEDE EEEEEEDSIV DDAEMNDEDG GSDVSVEEEM
AAESTESPEN VALSADPEGK EDGEEPPGTS QTSPEEFTDA KHESLFSLET NFLEEESGDN
SSLKASQDPF LQHVNKELKE KAIQAVATNP KTTHELKWPI LGQLFFSSKF QKLETFKPPK
DIDLKSLHLQ KPLESTWTKT NSQFLSGPQK SSSPFTPLQK ELFLIMNSYR DLFYPERTAL
KNGEEIRHVY CLHVINHILK ANAQVLGNNS RRRSQKFGVG DDDDFRDQGL TRPKVLIVVP
FREAALRVVQ LFISLLEGDS KKKIIVSNKK RFQGEYGSDP EERPPNLKRP EDYEAVFVGN
IDDHFRIGVA ILQRSIRLYA PFYSSDILIA SPLGLRTIIG GEGEKKRDFD FLSSIELLII
DQADIYLMQN WEHVLHLMNH MNLLPLDSHG VDFSRVRMWS LNNWSKYYRQ TLLFGALQDA
QINSVFNKYC VNMQGQVAVR NVPMTGSISH VLVQLPHVFQ RMEAENLASV IDARFNFFVN
KILPQYRDAV MSHTLIYIPS YFDFVRLRNY FKKEELNFTH ICEYTQKSGV SRARHFFLQG
EKQFLLFTER FHFYKRYTIK GIRNLIFYEL PTYPHFYSEI CNMLRATNRG EEATWTCTVL
YSKYDAQRLA AVVGVERAAQ MLQSNKNVHL FITGEK
