NAF1_HUMAN
ID NAF1_HUMAN Reviewed; 494 AA.
AC Q96HR8; D3DP28; E9PAZ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=H/ACA ribonucleoprotein complex non-core subunit NAF1;
DE Short=hNAF1;
GN Name=NAF1;
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] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-162.
RC TISSUE=Placenta;
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-315, AND IDENTIFICATION BY
RP 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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DKC1.
RX PubMed=16618814; DOI=10.1083/jcb.200601105;
RA Darzacq X., Kittur N., Roy S., Shav-Tal Y., Singer R.H., Meier U.T.;
RT "Stepwise RNP assembly at the site of H/ACA RNA transcription in human
RT cells.";
RL J. Cell Biol. 173:207-218(2006).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DKC1 AND NOLA3.
RX PubMed=16601202; DOI=10.1261/rna.2344106;
RA Hoareau-Aveilla C., Bonoli M., Caizergues-Ferrer M., Henry Y.;
RT "hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs,
RT and telomerase.";
RL RNA 12:832-840(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17135485; DOI=10.1261/rna.249306;
RA Kittur N., Darzacq X., Roy S., Singer R.H., Meier U.T.;
RT "Dynamic association and localization of human H/ACA RNP proteins.";
RL RNA 12:2057-2062(2006).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP STRUCTURE BY NMR OF 181-276.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the NAF1 domain of hypothetical protein BC008207
RT [Homo sapiens].";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein required for the maturation of box H/ACA
CC snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA
CC snoRNPs complex, it associates with the complex and disappears during
CC maturation of the complex and is replaced by NOLA1/GAR1 to yield mature
CC H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding
CC with DKC1/NOLA4. {ECO:0000269|PubMed:16618814}.
CC -!- SUBUNIT: During assembly of the complex, component of the small
CC nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs
CC (H/ACA snoRNPs) which contains NOLA2/NHP2, NOLA3/NOP10, NAF1 and
CC DKC1/NOLA4. Interacts directly with DKC1/NOLA4.
CC {ECO:0000269|PubMed:16601202, ECO:0000269|PubMed:16618814}.
CC -!- INTERACTION:
CC Q96HR8; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-2515597, EBI-11983447;
CC Q96HR8; O75553: DAB1; NbExp=3; IntAct=EBI-2515597, EBI-7875264;
CC Q96HR8; Q15038: DAZAP2; NbExp=3; IntAct=EBI-2515597, EBI-724310;
CC Q96HR8; O60832: DKC1; NbExp=8; IntAct=EBI-2515597, EBI-713091;
CC Q96HR8; Q14241: ELOA; NbExp=3; IntAct=EBI-2515597, EBI-742350;
CC Q96HR8; Q92567: FAM168A; NbExp=3; IntAct=EBI-2515597, EBI-7957930;
CC Q96HR8; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-2515597, EBI-11978259;
CC Q96HR8; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-2515597, EBI-12121668;
CC Q96HR8; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-2515597, EBI-2868124;
CC Q96HR8; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-2515597, EBI-12020132;
CC Q96HR8; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-2515597, EBI-10241353;
CC Q96HR8; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-2515597, EBI-12111050;
CC Q96HR8; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-2515597, EBI-11962084;
CC Q96HR8; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-2515597, EBI-716006;
CC Q96HR8; Q9Y3C7: MED31; NbExp=3; IntAct=EBI-2515597, EBI-394707;
CC Q96HR8; P35548: MSX2; NbExp=3; IntAct=EBI-2515597, EBI-6447480;
CC Q96HR8; Q96HR8: NAF1; NbExp=3; IntAct=EBI-2515597, EBI-2515597;
CC Q96HR8; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-2515597, EBI-744023;
CC Q96HR8; O43251: RBFOX2; NbExp=3; IntAct=EBI-2515597, EBI-746056;
CC Q96HR8; Q8WV41: SNX33; NbExp=4; IntAct=EBI-2515597, EBI-2481535;
CC Q96HR8; O60504: SORBS3; NbExp=3; IntAct=EBI-2515597, EBI-741237;
CC Q96HR8; O75177-5: SS18L1; NbExp=3; IntAct=EBI-2515597, EBI-12035119;
CC Q96HR8; Q96A09: TENT5B; NbExp=3; IntAct=EBI-2515597, EBI-752030;
CC Q96HR8; Q08117-2: TLE5; NbExp=5; IntAct=EBI-2515597, EBI-11741437;
CC Q96HR8; Q7KZS0: UBE2I; NbExp=5; IntAct=EBI-2515597, EBI-10180829;
CC Q96HR8; P40615: Dkc1; Xeno; NbExp=3; IntAct=EBI-2515597, EBI-5746997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC cytoplasm and the nucleus. Absent from the nucleolus (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96HR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HR8-2; Sequence=VSP_046217, VSP_046218;
CC -!- SIMILARITY: Belongs to the NAF1 family. {ECO:0000305}.
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DR EMBL; AK308601; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04843.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04844.1; -; Genomic_DNA.
DR EMBL; BC008207; AAH08207.1; -; mRNA.
DR CCDS; CCDS3803.1; -. [Q96HR8-1]
DR CCDS; CCDS47159.1; -. [Q96HR8-2]
DR RefSeq; NP_001122403.1; NM_001128931.1. [Q96HR8-2]
DR RefSeq; NP_612395.2; NM_138386.2. [Q96HR8-1]
DR RefSeq; XP_011530712.1; XM_011532410.2. [Q96HR8-1]
DR PDB; 2EQN; NMR; -; A=181-276.
DR PDBsum; 2EQN; -.
DR AlphaFoldDB; Q96HR8; -.
DR SMR; Q96HR8; -.
DR BioGRID; 124938; 120.
DR IntAct; Q96HR8; 84.
DR MINT; Q96HR8; -.
DR STRING; 9606.ENSP00000274054; -.
DR GlyGen; Q96HR8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96HR8; -.
DR PhosphoSitePlus; Q96HR8; -.
DR BioMuta; NAF1; -.
DR DMDM; 296439238; -.
DR EPD; Q96HR8; -.
DR jPOST; Q96HR8; -.
DR MassIVE; Q96HR8; -.
DR MaxQB; Q96HR8; -.
DR PaxDb; Q96HR8; -.
DR PeptideAtlas; Q96HR8; -.
DR PRIDE; Q96HR8; -.
DR ProteomicsDB; 19109; -.
DR ProteomicsDB; 76779; -. [Q96HR8-1]
DR Antibodypedia; 48823; 43 antibodies from 14 providers.
DR DNASU; 92345; -.
DR Ensembl; ENST00000274054.3; ENSP00000274054.2; ENSG00000145414.9. [Q96HR8-1]
DR Ensembl; ENST00000422287.6; ENSP00000408963.2; ENSG00000145414.9. [Q96HR8-2]
DR GeneID; 92345; -.
DR KEGG; hsa:92345; -.
DR MANE-Select; ENST00000274054.3; ENSP00000274054.2; NM_138386.3; NP_612395.2.
DR UCSC; uc003iqj.4; human. [Q96HR8-1]
DR CTD; 92345; -.
DR DisGeNET; 92345; -.
DR GeneCards; NAF1; -.
DR GeneReviews; NAF1; -.
DR HGNC; HGNC:25126; NAF1.
DR HPA; ENSG00000145414; Low tissue specificity.
DR MIM; 617868; gene.
DR neXtProt; NX_Q96HR8; -.
DR OpenTargets; ENSG00000145414; -.
DR PharmGKB; PA162396775; -.
DR VEuPathDB; HostDB:ENSG00000145414; -.
DR eggNOG; KOG2236; Eukaryota.
DR GeneTree; ENSGT00390000004697; -.
DR HOGENOM; CLU_032218_0_0_1; -.
DR InParanoid; Q96HR8; -.
DR OMA; PSVNMGW; -.
DR OrthoDB; 1453365at2759; -.
DR PhylomeDB; Q96HR8; -.
DR TreeFam; TF313273; -.
DR PathwayCommons; Q96HR8; -.
DR SignaLink; Q96HR8; -.
DR BioGRID-ORCS; 92345; 338 hits in 1078 CRISPR screens.
DR ChiTaRS; NAF1; human.
DR EvolutionaryTrace; Q96HR8; -.
DR GenomeRNAi; 92345; -.
DR Pharos; Q96HR8; Tbio.
DR PRO; PR:Q96HR8; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96HR8; protein.
DR Bgee; ENSG00000145414; Expressed in tibial artery and 174 other tissues.
DR ExpressionAtlas; Q96HR8; baseline and differential.
DR Genevisible; Q96HR8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; ISS:BHF-UCL.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; TAS:BHF-UCL.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
DR GO; GO:0042254; P:ribosome biogenesis; IDA:UniProtKB.
DR GO; GO:0043489; P:RNA stabilization; ISS:BHF-UCL.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; ISS:BHF-UCL.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; IMP:BHF-UCL.
DR GO; GO:0090669; P:telomerase RNA stabilization; IMP:BHF-UCL.
DR Gene3D; 2.40.10.230; -; 1.
DR InterPro; IPR038664; Gar1/Naf1_Cbf5-bd_sf.
DR InterPro; IPR007504; H/ACA_rnp_Gar1/Naf1.
DR InterPro; IPR040309; Naf1.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR31633; PTHR31633; 1.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..494
FT /note="H/ACA ribonucleoprotein complex non-core subunit
FT NAF1"
FT /id="PRO_0000315637"
FT REGION 18..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 346..389
FT /note="EDFTEVHQNWNAHSSASEHAKGYRNREFTRGFSRARYPRSCHGR -> TGIS
FT HRYCGLGSRPLQSSESHKLFGFQMHIKVTFTCYFSLLSMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046217"
FT VAR_SEQ 390..494
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046218"
FT VARIANT 43
FT /note="P -> S (in dbSNP:rs12331663)"
FT /id="VAR_057795"
FT VARIANT 162
FT /note="I -> V (in dbSNP:rs4691896)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_063101"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:2EQN"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2EQN"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2EQN"
FT STRAND 234..245
FT /evidence="ECO:0007829|PDB:2EQN"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2EQN"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2EQN"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:2EQN"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2EQN"
SQ SEQUENCE 494 AA; 53717 MW; 5A0C9B635A982A62 CRC64;
MEVVEAAAAQ LETLKFNGTD FGVGEGPAAP SPGSAPVPGT QPPLQSFEGS PDAGQTVEVK
PAGEQPLQPV LNAVAAGTPA PQPQPPAESP ACGDCVTSPG AAEPARAPDS LETSDSDSDS
DSETDSDSSS SSSSSSSSSS SSSSSCISLP PVLSDGDDDL QIEKENKNFP LKTKDELLLN
ELPSVEELTI ILPEDIELKP LGMVSSIIEQ LVIIESMTNL PPVNEETVIF KSDRQAAGKI
FEIFGPVAHP FYVLRFNSSD HIESKGIKIK ETMYFAPSMK DFTQYIFTEK LKQDKGSDAS
WKNDQEPPPE ALDFSDDEKE KEAKQRKKSQ IQGRKKLKSE FNEPGEDFTE VHQNWNAHSS
ASEHAKGYRN REFTRGFSRA RYPRSCHGRP PPQHFYNSEH MVSQETSGFP SQRQNNPIMP
QYPFPLPVFD MHNFPLRPPP PPPPPPVNMG WATPNMAAHP LLNLPYSLPP PPPPPPLPPP
PSSGDSNSHF GPYY
