NOP14_HUMAN
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 03-AUG-2022, entry version 170.
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; 158.
DR IntAct; P78316; 41.
DR MINT; P78316; -.
DR STRING; 9606.ENSP00000405068; -.
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; P78316; -.
DR PeptideAtlas; P78316; -.
DR PRIDE; P78316; -.
DR ProteomicsDB; 57560; -. [P78316-1]
DR ProteomicsDB; 57561; -. [P78316-2]
DR Antibodypedia; 22420; 74 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 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; KSKMHKY; -.
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; 722 hits in 1088 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 179 other tissues.
DR ExpressionAtlas; P78316; baseline and differential.
DR Genevisible; P78316; HS.
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; PTHR23183; 1.
DR Pfam; PF04147; Nop14; 1.
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
