NOL9_MOUSE
ID NOL9_MOUSE Reviewed; 714 AA.
AC Q3TZX8; A0PJC7; B1AS65; Q05A31; Q8BQE1; Q8C8L5; Q8C9A8; Q9D678;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase NOL9;
DE EC=2.7.1.-;
DE AltName: Full=Nucleolar protein 9 {ECO:0000312|EMBL:AAI25433.1};
GN Name=Nol9 {ECO:0000312|MGI:MGI:1921285};
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] {ECO:0000305, ECO:0000312|EMBL:BAE34079.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29433.1}, and
RC NOD {ECO:0000312|EMBL:BAE34079.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC31300.1},
RC Embryo {ECO:0000312|EMBL:BAC34472.1},
RC Neonatal skin {ECO:0000312|EMBL:BAB29433.1},
RC Spleen {ECO:0000312|EMBL:BAE34079.1}, and
RC Thymus {ECO:0000312|EMBL:BAC32857.1};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:CAM24580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI25433.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-524 (ISOFORMS 1/2/3).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH24877.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH24877.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
RN [6]
RP INTERACTION WITH PELP1; WDR18 AND SENP3, AND SUBCELLULAR LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. The
CC kinase activity is required for the processing of the 32S precursor
CC into 5.8S and 28S rRNAs, more specifically for the generation of the
CC major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase
CC activities. Probably binds RNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PELP1, WDR18 and SENP3.
CC {ECO:0000269|PubMed:22872859}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q5SY16}. Nucleus {ECO:0000269|PubMed:22872859}.
CC Note=Colocalizes with pre-60S rRNP particles. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3TZX8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q3TZX8-2; Sequence=VSP_053056, VSP_053057;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3TZX8-3; Sequence=VSP_053058, VSP_053059;
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24877.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK014568; BAB29433.1; -; mRNA.
DR EMBL; AK042581; BAC31300.1; -; mRNA.
DR EMBL; AK046761; BAC32857.1; -; mRNA.
DR EMBL; AK050948; BAC34472.1; -; mRNA.
DR EMBL; AK157398; BAE34079.1; -; mRNA.
DR EMBL; AL611927; CAM24579.1; -; Genomic_DNA.
DR EMBL; AL611927; CAM24580.1; -; Genomic_DNA.
DR EMBL; CH466594; EDL14922.1; -; Genomic_DNA.
DR EMBL; BC024877; AAH24877.1; ALT_SEQ; mRNA.
DR EMBL; BC125432; AAI25433.1; -; mRNA.
DR EMBL; BC132099; AAI32100.1; -; mRNA.
DR CCDS; CCDS18986.1; -. [Q3TZX8-2]
DR CCDS; CCDS51389.1; -. [Q3TZX8-1]
DR RefSeq; NP_001153071.1; NM_001159599.2. [Q3TZX8-1]
DR RefSeq; NP_083003.2; NM_028727.3. [Q3TZX8-2]
DR AlphaFoldDB; Q3TZX8; -.
DR SMR; Q3TZX8; -.
DR BioGRID; 216440; 4.
DR IntAct; Q3TZX8; 2.
DR STRING; 10090.ENSMUSP00000099486; -.
DR iPTMnet; Q3TZX8; -.
DR PhosphoSitePlus; Q3TZX8; -.
DR EPD; Q3TZX8; -.
DR jPOST; Q3TZX8; -.
DR MaxQB; Q3TZX8; -.
DR PaxDb; Q3TZX8; -.
DR PeptideAtlas; Q3TZX8; -.
DR PRIDE; Q3TZX8; -.
DR ProteomicsDB; 252919; -. [Q3TZX8-1]
DR ProteomicsDB; 252920; -. [Q3TZX8-2]
DR ProteomicsDB; 252921; -. [Q3TZX8-3]
DR Antibodypedia; 53093; 59 antibodies from 24 providers.
DR DNASU; 74035; -.
DR Ensembl; ENSMUST00000084116; ENSMUSP00000081133; ENSMUSG00000028948. [Q3TZX8-1]
DR Ensembl; ENSMUST00000103197; ENSMUSP00000099486; ENSMUSG00000028948. [Q3TZX8-2]
DR GeneID; 74035; -.
DR KEGG; mmu:74035; -.
DR UCSC; uc008vzc.3; mouse. [Q3TZX8-3]
DR UCSC; uc008vzd.3; mouse. [Q3TZX8-1]
DR UCSC; uc008vzf.3; mouse. [Q3TZX8-2]
DR CTD; 79707; -.
DR MGI; MGI:1921285; Nol9.
DR VEuPathDB; HostDB:ENSMUSG00000028948; -.
DR eggNOG; KOG2750; Eukaryota.
DR GeneTree; ENSGT00940000153668; -.
DR HOGENOM; CLU_021128_2_0_1; -.
DR InParanoid; Q3TZX8; -.
DR OMA; CLYGQVE; -.
DR OrthoDB; 1217334at2759; -.
DR PhylomeDB; Q3TZX8; -.
DR TreeFam; TF313802; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 74035; 25 hits in 60 CRISPR screens.
DR ChiTaRS; Nol9; mouse.
DR PRO; PR:Q3TZX8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3TZX8; protein.
DR Bgee; ENSMUSG00000028948; Expressed in cleaving embryo and 215 other tissues.
DR ExpressionAtlas; Q3TZX8; baseline and differential.
DR Genevisible; Q3TZX8; MM.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; PTHR12755; 1.
DR Pfam; PF16575; CLP1_P; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Isopeptide bond; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; rRNA processing; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5SY16"
FT CHAIN 2..714
FT /note="Polynucleotide 5'-hydroxyl-kinase NOL9"
FT /id="PRO_0000367432"
FT REGION 80..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5SY16"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SY16"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5SY16"
FT VAR_SEQ 627
FT /note="I -> E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053058"
FT VAR_SEQ 628..714
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053059"
FT VAR_SEQ 671
FT /note="P -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053056"
FT VAR_SEQ 672..714
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053057"
FT CONFLICT 101
FT /note="A -> G (in Ref. 1; BAC31300)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="D -> E (in Ref. 1; BAB29433 and 2; CAM24579)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="A -> S (in Ref. 1; BAC34472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 80840 MW; E2FFC860BD488F5C CRC64;
MAESEVLHRR APSRSSWLRV RKARPHLLLS RRGRRRFGVL TRVELRRLRR RLLRAHALGG
DWKQVAPAGA HVAVKCKLRA RSRPAPRSPP TPSVPPAPCT ASATCSLLNP RNHSTPQSRA
GRPVRKVSPN VTQPVRDLGS GRVLMMLPPG EGFTFSGICR VTCVYGQLEV YGHIINQGQP
PQDVFSVYTH SYLTINGVPY AEPEKSEKAI RREIRALLKP YTKLDDRNWV VRYFPPLGSI
MILERMQSRF VDFLKTYKCS SYVLLQENAP VRVNSEFTTL KKIGIRRQKR KKAICLSESG
LCALEELVSV SCDGCPVILL CGACDIGKST FNRILINQLL NSIPGVDYLE CDLGQTEFTP
PGCVALLTIT EPLLGPPYTH QRKPQRMVYY GKMNCYNDYE NYIDIVKYVF RDYKREFPLI
INTMGWVSDN GLRLLVDLIR VLSPNYVVQL YSDRCKFTPT LTSEYVELTD GLYTKSKIKR
YRGFEIPEFG DNLEFTYEEK ESSPLPVFTG HVLLSVHSEF LSSKNEKNRA KYNRIFRDLA
VLGYLSQLML PVPESLSPLH SLTPYQVPFS AVAIRVLHAD VAPTHILYAV NASWVGLCRI
VDDMKGYTRG PILLAQNPIC DCLGFGICRG IDMDKRTYHI LTPLPPEELK TVNCLLVGSI
SIPHCIFQNQ PGPEGSVPYV TTDYNLNIPG ATEKIGEREY GKAFPRHKLR QRRK
