ID   NOL12_HUMAN             Reviewed;         213 AA.
AC   Q9UGY1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Nucleolar protein 12;
GN   Name=NOL12;
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].
RX   PubMed=12529303; DOI=10.1101/gr.695703;
RA   Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA   Bye J.M., Beare D.M., Dunham I.;
RT   "Reevaluating human gene annotation: a second-generation analysis of
RT   chromosome 22.";
RL   Genome Res. 13:27-36(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
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   INTERACTION WITH KIAA1191.
RX   PubMed=21153684; DOI=10.1007/s11010-010-0690-4;
RA   Mishra M., Inoue N., Heese K.;
RT   "Characterizing the novel protein p33MONOX.";
RL   Mol. Cell. Biochem. 350:127-134(2011).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-21 AND ASP-23.
RX   PubMed=29069457; DOI=10.1093/nar/gkx963;
RA   Scott D.D., Trahan C., Zindy P.J., Aguilar L.C., Delubac M.Y.,
RA   Van Nostrand E.L., Adivarahan S., Wei K.E., Yeo G.W., Zenklusen D.,
RA   Oeffinger M.;
RT   "Nol12 is a multifunctional RNA binding protein at the nexus of RNA and DNA
RT   metabolism.";
RL   Nucleic Acids Res. 45:12509-12528(2017).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=30988155; DOI=10.1128/mcb.00099-19;
RA   Pinho M., Macedo J.C., Logarinho E., Pereira P.S.;
RT   "NOL12 Repression Induces Nucleolar Stress-Driven Cellular Senescence and
RT   Is Associated with Normative Aging.";
RL   Mol. Cell. Biol. 39:0-0(2019).
CC   -!- FUNCTION: Multifunctional RNA binding protein that plays a role in RNA
CC       metabolism and DNA maintenance. Participates in the resolution of DNA
CC       stress and the maintenance of genome integrity by localizing to sites
CC       of DNA insults (PubMed:29069457). Plays also a role in proper nucleolar
CC       organization by limiting nucleolar size and regulating nucleolar
CC       number. Mechanistically, regulates the nucleolar levels of fibrillarin
CC       and nucleolin, two key players in pre-rRNA processing and ribosome
CC       assembly (PubMed:30988155). {ECO:0000269|PubMed:29069457,
CC       ECO:0000269|PubMed:30988155}.
CC   -!- SUBUNIT: Interacts with KIAA1191. {ECO:0000269|PubMed:21153684}.
CC   -!- INTERACTION:
CC       Q9UGY1; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-716098, EBI-10181188;
CC       Q9UGY1; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-716098, EBI-5278764;
CC       Q9UGY1; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-716098, EBI-739624;
CC       Q9UGY1; Q92997: DVL3; NbExp=3; IntAct=EBI-716098, EBI-739789;
CC       Q9UGY1; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-716098, EBI-12012928;
CC       Q9UGY1; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-716098, EBI-10172290;
CC       Q9UGY1; P23508: MCC; NbExp=3; IntAct=EBI-716098, EBI-307531;
CC       Q9UGY1; Q9UGY1: NOL12; NbExp=3; IntAct=EBI-716098, EBI-716098;
CC       Q9UGY1; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-716098, EBI-12023934;
CC       Q9UGY1; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-716098, EBI-2212028;
CC       Q9UGY1; P54274: TERF1; NbExp=2; IntAct=EBI-716098, EBI-710997;
CC       Q9UGY1; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-716098, EBI-947459;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:29069457,
CC       ECO:0000269|PubMed:30988155}. Nucleus {ECO:0000269|PubMed:29069457}.
CC       Cytoplasm {ECO:0000269|PubMed:29069457}.
CC   -!- SIMILARITY: Belongs to the RRP17 family. {ECO:0000305}.
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DR   EMBL; AL160132; CAB77148.1; -; mRNA.
DR   EMBL; CR456463; CAG30349.1; -; mRNA.
DR   EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002808; AAH02808.1; -; mRNA.
DR   CCDS; CCDS13955.1; -.
DR   RefSeq; NP_077289.1; NM_024313.2.
DR   AlphaFoldDB; Q9UGY1; -.
DR   SMR; Q9UGY1; -.
DR   BioGRID; 122577; 224.
DR   IntAct; Q9UGY1; 67.
DR   MINT; Q9UGY1; -.
DR   STRING; 9606.ENSP00000352021; -.
DR   iPTMnet; Q9UGY1; -.
DR   PhosphoSitePlus; Q9UGY1; -.
DR   BioMuta; NOL12; -.
DR   DMDM; 74761951; -.
DR   EPD; Q9UGY1; -.
DR   jPOST; Q9UGY1; -.
DR   MassIVE; Q9UGY1; -.
DR   MaxQB; Q9UGY1; -.
DR   PaxDb; 9606-ENSP00000352021; -.
DR   PeptideAtlas; Q9UGY1; -.
DR   ProteomicsDB; 84270; -.
DR   Pumba; Q9UGY1; -.
DR   Antibodypedia; 73215; 89 antibodies from 22 providers.
DR   DNASU; 79159; -.
DR   Ensembl; ENST00000359114.9; ENSP00000352021.4; ENSG00000273899.5.
DR   Ensembl; ENST00000438329.5; ENSP00000403059.1; ENSG00000273899.5.
DR   Ensembl; ENST00000611699.1; ENSP00000482349.1; ENSG00000273899.5.
DR   GeneID; 79159; -.
DR   KEGG; hsa:79159; -.
DR   MANE-Select; ENST00000359114.9; ENSP00000352021.4; NM_024313.3; NP_077289.1.
DR   UCSC; uc003ato.2; human.
DR   AGR; HGNC:28585; -.
DR   CTD; 79159; -.
DR   GeneCards; NOL12; -.
DR   HGNC; HGNC:28585; NOL12.
DR   HPA; ENSG00000273899; Low tissue specificity.
DR   neXtProt; NX_Q9UGY1; -.
DR   OpenTargets; ENSG00000273899; -.
DR   PharmGKB; PA145148362; -.
DR   VEuPathDB; HostDB:ENSG00000273899; -.
DR   eggNOG; KOG4709; Eukaryota.
DR   GeneTree; ENSGT00390000015973; -.
DR   HOGENOM; CLU_111183_0_0_1; -.
DR   InParanoid; Q9UGY1; -.
DR   OMA; HMHSRKK; -.
DR   OrthoDB; 5404493at2759; -.
DR   PhylomeDB; Q9UGY1; -.
DR   TreeFam; TF323855; -.
DR   PathwayCommons; Q9UGY1; -.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   SignaLink; Q9UGY1; -.
DR   BioGRID-ORCS; 79159; 681 hits in 1164 CRISPR screens.
DR   ChiTaRS; NOL12; human.
DR   GeneWiki; NOL12; -.
DR   GenomeRNAi; 79159; -.
DR   Pharos; Q9UGY1; Tbio.
DR   PRO; PR:Q9UGY1; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9UGY1; Protein.
DR   Bgee; ENSG00000273899; Expressed in sural nerve and 119 other cell types or tissues.
DR   ExpressionAtlas; Q9UGY1; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR   InterPro; IPR019186; Nucleolar_protein_12.
DR   PANTHER; PTHR14577; NUCLEOLAR PROTEIN 12; 1.
DR   PANTHER; PTHR14577:SF0; NUCLEOLAR PROTEIN 12; 1.
DR   Pfam; PF09805; Nop25; 1.
DR   Genevisible; Q9UGY1; HS.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Nucleus; Reference proteome; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..213
FT                   /note="Nucleolar protein 12"
FT                   /id="PRO_0000271207"
FT   REGION          118..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          33..96
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        130..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..186
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         21
FT                   /note="S->A: Loss of DNA damage response pathway
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:29069457"
FT   MUTAGEN         23
FT                   /note="D->L: Loss of DNA damage response pathway
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:29069457"
SQ   SEQUENCE   213 AA;  24663 MW;  86A4DFBD363179CA CRC64;
     MGRNKKKKRD GDDRRPRLVL SFDEEKRREY LTGFHKRKVE RKKAAIEEIK QRLKEEQRKL
     REERHQEYLK MLAEREEALE EADELDRLVT AKTESVQYDH PNHTVTVTTI SDLDLSGARL
     LGLTPPEGGA GDRSEEEASS TEKPTKALPR KSRDPLLSQR ISSLTASLHA HSRKKVKRKH
     PRRAQDSKKP PRAPRTSKAQ RRRLTGKARH SGE
//