NOP14_YEAST
ID NOP14_YEAST Reviewed; 810 AA.
AC Q99207; D6VRK0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Nucleolar complex protein 14;
DE AltName: Full=U three protein 2;
DE AltName: Full=U3 small nucleolar RNA-associated protein 2;
DE Short=U3 snoRNA-associated protein 2;
GN Name=NOP14; Synonyms=UTP2; OrderedLocusNames=YDL148C; ORFNames=D1566;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL Yeast 12:1587-1592(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH EMG1.
RX PubMed=11694595; DOI=10.1091/mbc.12.11.3644;
RA Liu P.C., Thiele D.J.;
RT "Novel stress-responsive genes EMG1 and NOP14 encode conserved, interacting
RT proteins required for 40S ribosome biogenesis.";
RL Mol. Biol. Cell 12:3644-3657(2001).
RN [5]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [6]
RP FUNCTION, INTERACTION WITH NOC4, AND SUBCELLULAR LOCATION.
RX PubMed=12446671; DOI=10.1074/jbc.m208898200;
RA Milkereit P., Strauss D., Bassler J., Gadal O., Kuhn H., Schutz S., Gas N.,
RA Lechner J., Hurt E., Tschochner H.;
RT "A Noc complex specifically involved in the formation and nuclear export of
RT ribosomal 40 S subunits.";
RL J. Biol. Chem. 278:4072-4081(2003).
RN [7]
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).
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. {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:12446671}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with EMG1, MPP10 and NOC4.
CC Component of the ribosomal small subunit (SSU) processome composed of
CC at least 40 protein subunits and snoRNA U3.
CC {ECO:0000269|PubMed:11694595, ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:12446671}.
CC -!- INTERACTION:
CC Q99207; Q06287: EMG1; NbExp=7; IntAct=EBI-35157, EBI-11979;
CC Q99207; P38333: ENP1; NbExp=10; IntAct=EBI-35157, EBI-6482;
CC Q99207; P47083: MPP10; NbExp=6; IntAct=EBI-35157, EBI-11168;
CC Q99207; Q06512: NOC4; NbExp=7; IntAct=EBI-35157, EBI-36459;
CC Q99207; Q12136: SAS10; NbExp=3; IntAct=EBI-35157, EBI-36084;
CC Q99207; P53254: UTP22; NbExp=7; IntAct=EBI-35157, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:12446671}.
CC -!- SIMILARITY: Belongs to the NOP14 family. {ECO:0000305}.
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DR EMBL; X97751; CAA66343.1; -; Genomic_DNA.
DR EMBL; Z74196; CAA98722.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11710.1; -; Genomic_DNA.
DR PIR; S67696; S67696.
DR RefSeq; NP_010133.1; NM_001180208.1.
DR PDB; 5WLC; EM; 3.80 A; ST=1-810.
DR PDB; 6KE6; EM; 3.40 A; RN=1-810.
DR PDB; 6LQP; EM; 3.20 A; RN=1-810.
DR PDB; 6LQQ; EM; 4.10 A; RN=1-810.
DR PDB; 6LQR; EM; 8.60 A; RN=1-810.
DR PDB; 6LQS; EM; 3.80 A; RN=1-810.
DR PDB; 6LQT; EM; 4.90 A; RN=1-810.
DR PDB; 6LQU; EM; 3.70 A; RN=1-810.
DR PDB; 6LQV; EM; 4.80 A; RN=1-810.
DR PDB; 6ZQA; EM; 4.40 A; UB=1-810.
DR PDB; 6ZQB; EM; 3.90 A; UB=1-810.
DR PDB; 6ZQC; EM; 3.80 A; UB=1-810.
DR PDB; 6ZQD; EM; 3.80 A; UB=1-810.
DR PDB; 6ZQE; EM; 7.10 A; UB=1-810.
DR PDB; 6ZQF; EM; 4.90 A; UB=1-810.
DR PDB; 6ZQG; EM; 3.50 A; UB=1-810.
DR PDB; 7AJT; EM; 4.60 A; UB=1-810.
DR PDB; 7AJU; EM; 3.80 A; UB=1-810.
DR PDB; 7D4I; EM; 4.00 A; RN=1-810.
DR PDB; 7D5S; EM; 4.60 A; RN=1-810.
DR PDB; 7D5T; EM; 6.00 A; RN=1-810.
DR PDB; 7D63; EM; 12.30 A; RN=1-810.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q99207; -.
DR SMR; Q99207; -.
DR BioGRID; 31913; 337.
DR ComplexPortal; CPX-1735; NOP14-NOC4 complex.
DR DIP; DIP-4733N; -.
DR IntAct; Q99207; 54.
DR MINT; Q99207; -.
DR STRING; 4932.YDL148C; -.
DR iPTMnet; Q99207; -.
DR MaxQB; Q99207; -.
DR PaxDb; Q99207; -.
DR PRIDE; Q99207; -.
DR EnsemblFungi; YDL148C_mRNA; YDL148C; YDL148C.
DR GeneID; 851407; -.
DR KEGG; sce:YDL148C; -.
DR SGD; S000002307; NOP14.
DR VEuPathDB; FungiDB:YDL148C; -.
DR eggNOG; KOG2147; Eukaryota.
DR GeneTree; ENSGT00390000017459; -.
DR HOGENOM; CLU_008874_0_0_1; -.
DR InParanoid; Q99207; -.
DR OMA; KSKMHKY; -.
DR BioCyc; YEAST:G3O-29545-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q99207; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q99207; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030692; C:Noc4p-Nop14p complex; IPI:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
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); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
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); IMP:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IC:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR InterPro; IPR007276; Nop14.
DR PANTHER; PTHR23183; PTHR23183; 1.
DR Pfam; PF04147; Nop14; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..810
FT /note="Nucleolar complex protein 14"
FT /id="PRO_0000137163"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..354
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 94302 MW; F7615D96B02E15DE CRC64;
MAGSQLKNLK AALKARGLTG QTNVKSKNKK NSKRQAKEYD REEKKKAIAE IREEFNPFEI
KAARNKRRDG LPSKTADRIA VGKPGISKQI GEEQRKRAFE ARKMMKNKRG GVIDKRFGER
DKLLTEEEKM LERFTRERQS QSKRNANLFN LEDDEDDGDM FGDGLTHLGQ SLSLEDELAN
DEEDFLASKR FNEDDAELQQ PQRKKTKAEV MKEVIAKSKF YKQERQKAQG IMEDQIDNLD
DNFEDVMSEL MMTQPKKNPM EPKTDLDKEY DIKVKELQLD KRAAPSDRTK TEEEKNAEAE
EKKRELEQQR LDRMNGMIEL EEGEERGVED LDDGFWENEE DYEDDNDGIA DSDDDIKFED
QGRDEGFSQI LKKKNISISC PRTHDALLDQ VKKLDLDDHP KIVKNIIKAY QPKLAEGNKE
KLGKFTAVLL RHIIFLSNQN YLKNVQSFKR TQNALISILK SLSEKYNREL SEECRDYINE
MQARYKKNHF DALSNGDLVF FSIIGILFST SDQYHLVITP ALILMSQFLE QIKFNSLKRI
AFGAVLVRIV SQYQRISKRY IPEVVYFFQK ILLTFIVEKE NQEKPLDFEN IRLDSYELGL
PLDVDFTKKR STIIPLHTLS TMDTEAHPVD QCVSVLLNVM ESLDATISTV WKSLPAFNEI
ILPIQQLLSA YTSKYSDFEK PRNILNKVEK LTKFTEHIPL ALQNHKPVSI PTHAPKYEEN
FNPDKKSYDP DRTRSEINKM KAQLKKERKF TMKEIRKDAK FEARQRIEEK NKESSDYHAK
MAHIVNTINT EEGAEKNKYE RERKLRGGKK
