ID   NOP14_HUMAN             Reviewed;         857 AA.
AC   P78316; D3DVR6; Q7LGI5; Q7Z6K0; Q8TBR6;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 3.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Nucleolar protein 14;
DE   AltName: Full=Nucleolar complex protein 14;
GN   Name=NOP14; Synonyms=C4orf9, NOL14; ORFNames=RES4-25;
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).
RX   PubMed=9661704; DOI=10.1007/bf02673751;
RA   Pribill I., Barnes G.T., Chen J., Church D., Buckler A., Baxendale S.,
RA   Bates G.P., Lehrach H., Gusella M.J., Duyao M.P., Ambrose C.M.,
RA   Gusella J.F., MacDonald M.E.;
RT   "Exon trapping and sequence-based methods of gene finding in transcript
RT   mapping of human 4p16.3.";
RL   Somat. Cell Mol. Genet. 23:413-427(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-380.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cervix, and Colon;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 140-857 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9734812; DOI=10.1093/dnares/5.3.177;
RA   Hadano S., Ishida Y., Ikeda J.-E.;
RT   "The primary structure and genomic organization of five novel transcripts
RT   located close to the Huntington's disease gene on human chromosome
RT   4p16.3.";
RL   DNA Res. 5:177-186(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-148, AND
RP   IDENTIFICATION BY 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-148, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-146, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-146 AND SER-148, AND
RP   IDENTIFICATION BY 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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-146 AND SER-349, AND
RP   IDENTIFICATION BY 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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-148, AND
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       Has a role in the nuclear export of 40S pre-ribosomal subunit to the
CC       cytoplasm (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P78316-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P78316-2; Sequence=VSP_018021, VSP_018022;
CC   -!- SIMILARITY: Belongs to the NOP14 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB97011.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF040965; AAB97011.1; ALT_INIT; mRNA.
DR   EMBL; CH471131; EAW82489.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82491.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82492.1; -; Genomic_DNA.
DR   EMBL; BC026035; AAH26035.1; -; mRNA.
DR   EMBL; BC053635; AAH53635.1; -; mRNA.
DR   EMBL; AB000467; BAA19121.1; -; mRNA.
DR   CCDS; CCDS33945.1; -. [P78316-1]
DR   CCDS; CCDS77893.1; -. [P78316-2]
DR   PIR; JE0188; JE0188.
DR   RefSeq; NP_001278907.1; NM_001291978.1. [P78316-1]
DR   RefSeq; NP_001278908.1; NM_001291979.1. [P78316-2]
DR   RefSeq; NP_003694.1; NM_003703.2. [P78316-1]
DR   AlphaFoldDB; P78316; -.
DR   SMR; P78316; -.
DR   BioGRID; 114162; 194.
DR   ComplexPortal; CPX-2511; Small ribosomal subunit processome.
DR   IntAct; P78316; 41.
DR   MINT; P78316; -.
DR   STRING; 9606.ENSP00000405068; -.
DR   GlyGen; P78316; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; P78316; -.
DR   MetOSite; P78316; -.
DR   PhosphoSitePlus; P78316; -.
DR   SwissPalm; P78316; -.
DR   BioMuta; NOP14; -.
DR   DMDM; 56404449; -.
DR   EPD; P78316; -.
DR   jPOST; P78316; -.
DR   MassIVE; P78316; -.
DR   MaxQB; P78316; -.
DR   PaxDb; 9606-ENSP00000405068; -.
DR   PeptideAtlas; P78316; -.
DR   ProteomicsDB; 57560; -. [P78316-1]
DR   ProteomicsDB; 57561; -. [P78316-2]
DR   Pumba; P78316; -.
DR   Antibodypedia; 22420; 95 antibodies from 19 providers.
DR   DNASU; 8602; -.
DR   Ensembl; ENST00000314262.10; ENSP00000315674.6; ENSG00000087269.16. [P78316-1]
DR   Ensembl; ENST00000398071.4; ENSP00000381146.4; ENSG00000087269.16. [P78316-2]
DR   Ensembl; ENST00000416614.7; ENSP00000405068.2; ENSG00000087269.16. [P78316-1]
DR   GeneID; 8602; -.
DR   KEGG; hsa:8602; -.
DR   MANE-Select; ENST00000416614.7; ENSP00000405068.2; NM_001291978.2; NP_001278907.1.
DR   UCSC; uc003ggj.2; human. [P78316-1]
DR   AGR; HGNC:16821; -.
DR   CTD; 8602; -.
DR   DisGeNET; 8602; -.
DR   GeneCards; NOP14; -.
DR   HGNC; HGNC:16821; NOP14.
DR   HPA; ENSG00000087269; Low tissue specificity.
DR   MIM; 611526; gene.
DR   neXtProt; NX_P78316; -.
DR   OpenTargets; ENSG00000087269; -.
DR   PharmGKB; PA164723982; -.
DR   VEuPathDB; HostDB:ENSG00000087269; -.
DR   eggNOG; KOG2147; Eukaryota.
DR   GeneTree; ENSGT00390000017459; -.
DR   HOGENOM; CLU_008874_1_1_1; -.
DR   InParanoid; P78316; -.
DR   OMA; FTFPCPQ; -.
DR   OrthoDB; 132327at2759; -.
DR   PhylomeDB; P78316; -.
DR   TreeFam; TF105698; -.
DR   PathwayCommons; P78316; -.
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; P78316; -.
DR   BioGRID-ORCS; 8602; 753 hits in 1164 CRISPR screens.
DR   ChiTaRS; NOP14; human.
DR   GenomeRNAi; 8602; -.
DR   Pharos; P78316; Tbio.
DR   PRO; PR:P78316; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P78316; Protein.
DR   Bgee; ENSG00000087269; Expressed in sural nerve and 180 other cell types or tissues.
DR   ExpressionAtlas; P78316; baseline and differential.
DR   GO; GO:0030686; C:90S preribosome; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030692; C:Noc4p-Nop14p complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR   InterPro; IPR007276; Nop14.
DR   PANTHER; PTHR23183; NOP14; 1.
DR   PANTHER; PTHR23183:SF0; NUCLEOLAR PROTEIN 14; 1.
DR   Pfam; PF04147; Nop14; 1.
DR   Genevisible; P78316; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..857
FT                   /note="Nucleolar protein 14"
FT                   /id="PRO_0000137155"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..376
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VAR_SEQ         772..819
FT                   /note="KVLEFGRKQGSSKEEQERKRLIHKHKREFKGAVREIRKDNQFLARMQL ->
FT                   SNSRPQVIHLPWPPNYRCEPQHPAKKVIFFRVIML (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018021"
FT   VAR_SEQ         820..857
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018022"
FT   VARIANT         380
FT                   /note="L -> S (in dbSNP:rs2515960)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_053540"
FT   VARIANT         716
FT                   /note="Q -> R (in dbSNP:rs1054090)"
FT                   /id="VAR_060075"
SQ   SEQUENCE   857 AA;  97668 MW;  CDADFB91083DBB75 CRC64;
     MAKAKKVGAR RKASGAPAGA RGGPAKANSN PFEVKVNRQK FQILGRKTRH DVGLPGVSRA
     RALRKRTQTL LKEYKERDKS NVFRDKRFGE YNSNMSPEEK MMKRFALEQQ RHHEKKSIYN
     LNEDEELTHY GQSLADIEKH NDIVDSDSDA EDRGTLSAEL TAAHFGGGGG LLHKKTQQEG
     EEREKPKSRK ELIEELIAKS KQEKRERQAQ REDALELTEK LDQDWKEIQT LLSHKTPKSE
     NRDKKEKPKP DAYDMMVREL GFEMKAQPSN RMKTEAELAK EEQEHLRKLE AERLRRMLGK
     DEDENVKKPK HMSADDLNDG FVLDKDDRRL LSYKDGKMNV EEDVQEEQSK EASDPESNEE
     EGDSSGGEDT EESDSPDSHL DLESNVESEE ENEKPAKEQR QTPGKGLISG KERAGKATRD
     ELPYTFAAPE SYEELRSLLL GRSMEEQLLV VERIQKCNHP SLAEGNKAKL EKLFGFLLEY
     VGDLATDDPP DLTVIDKLVV HLYHLCQMFP ESASDAIKFV LRDAMHEMEE MIETKGRAAL
     PGLDVLIYLK ITGLLFPTSD FWHPVVTPAL VCLSQLLTKC PILSLQDVVK GLFVCCLFLE
     YVALSQRFIP ELINFLLGIL YIATPNKASQ GSTLVHPFRA LGKNSELLVV SAREDVATWQ
     QSSLSLRWAS RLRAPTSTEA NHIRLSCLAV GLALLKRCVL MYGSLPSFHA IMGPLQALLT
     DHLADCSHPQ ELQELCQSTL TEMESQKQLC RPLTCEKSKP VPLKLFTPRL VKVLEFGRKQ
     GSSKEEQERK RLIHKHKREF KGAVREIRKD NQFLARMQLS EIMERDAERK RKVKQLFNSL
     ATQEGEWKAL KRKKFKK
//