NAB6_YEAST
ID NAB6_YEAST Reviewed; 1134 AA.
AC Q03735; D6W0G7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=RNA-binding protein NAB6;
DE AltName: Full=Nucleic acid-binding protein 6;
GN Name=NAB6; OrderedLocusNames=YML117W; ORFNames=YM8339.02;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14570984; DOI=10.1152/physiolgenomics.00139.2003;
RA Jones D.L., Petty J., Hoyle D.C., Hayes A., Ragni E., Popolo L.,
RA Oliver S.G., Stateva L.I.;
RT "Transcriptome profiling of a Saccharomyces cerevisiae mutant with a
RT constitutively activated Ras/cAMP pathway.";
RL Physiol. Genomics 16:107-118(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP FUNCTION.
RX PubMed=18959479; DOI=10.1371/journal.pbio.0060255;
RA Hogan D.J., Riordan D.P., Gerber A.P., Herschlag D., Brown P.O.;
RT "Diverse RNA-binding proteins interact with functionally related sets of
RT RNAs, suggesting an extensive regulatory system.";
RL PLoS Biol. 6:E255-E255(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: RNA-binding protein that associates with mRNAs encoding cell
CC wall proteins. {ECO:0000269|PubMed:18959479}.
CC -!- INTERACTION:
CC Q03735; P29468: PAP1; NbExp=2; IntAct=EBI-27955, EBI-12917;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression down-regulated by cAMP.
CC {ECO:0000269|PubMed:14570984}.
CC -!- DISRUPTION PHENOTYPE: Displays increased sensitivity to some cell wall
CC disrupting agents including sodium dodecyl sulfate (SDS) and calcofluor
CC white (CFW). {ECO:0000269|PubMed:14570984}.
CC -!- MISCELLANEOUS: Present with 1540 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49210; CAA89101.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09781.1; -; Genomic_DNA.
DR PIR; S53955; S53955.
DR RefSeq; NP_013589.1; NM_001182479.1.
DR AlphaFoldDB; Q03735; -.
DR SMR; Q03735; -.
DR BioGRID; 35087; 159.
DR DIP; DIP-2976N; -.
DR IntAct; Q03735; 21.
DR MINT; Q03735; -.
DR STRING; 4932.YML117W; -.
DR iPTMnet; Q03735; -.
DR MaxQB; Q03735; -.
DR PaxDb; Q03735; -.
DR PRIDE; Q03735; -.
DR EnsemblFungi; YML117W_mRNA; YML117W; YML117W.
DR GeneID; 854922; -.
DR KEGG; sce:YML117W; -.
DR SGD; S000004585; NAB6.
DR VEuPathDB; FungiDB:YML117W; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00390000002792; -.
DR HOGENOM; CLU_276472_0_0_1; -.
DR InParanoid; Q03735; -.
DR OMA; SDVMAQY; -.
DR BioCyc; YEAST:G3O-32698-MON; -.
DR PRO; PR:Q03735; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03735; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR018885; mRNA-bd_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR018835; RNA-binding_domain_put.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR Pfam; PF10567; Nab6_mRNP_bdg; 1.
DR Pfam; PF10378; RRM; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1134
FT /note="RNA-binding protein NAB6"
FT /id="PRO_0000082034"
FT DOMAIN 653..726
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 112..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1134 AA; 126139 MW; 47B0FF7C5B98A053 CRC64;
MSNSNSKKPV ANYAYRQQQD YNGMNAMVGN PMMYHPVDFV NGAGQYGPSQ HPAYYTNSPL
PNIPPTPFDT AYGASLFPSH LLMGSPFVSS PNMQSGYNSA RSSNLKRKAY SRPVSNHNGY
NGNSNSNQNN TNNGMVTPSN YYRMGRNSFS RNNNSTRNVT HNNNKGCDTR NNSGRRTFAR
NNIFDDILPE MLLQRPFCIN YKVLPTGDDA YRTRSLLIEN VDHSIDLHSI VKNFVKSNTL
ESAYLIEGGK SDDSKDVETK NLSILISFLT KGDCLNFYNN ILQRLSEFKT FLKSEALNLK
FVCLNYDPKC LPTFIESEAL TENAEEADIT NGSTMISASL HHNIANKDAT RSIIIEFKSP
VEKSDLFKKK LQFLDRSKNK RYILESIDLV NTDVPSNQFP ENYAVLTFLN ISMAIEVLDY
LKKYSKNLGI SKCFYVSLAP LVVSSARSSV ANIYEGKTST HRLSVPSVTA GNNNDSNNNG
NNNKSNMSGI TTLNNNSSIG VSVYGHSNMS LTSLSSSVSL NEEIDMLATK LQGVELDGTY
LEINYRDYQT PTIEEHSTHL SNVKISKTTE NSRQFSQDIP SPLPLNEHMF MNDSNQSNGA
IIPQQLIATP SPVSPNLQMN QRVLPNPITQ SLEQNFNVSA KVASSMGSDI GNRTIYIGNI
NPRSKAEDIC NVVRGGILQS IKYIPEKKIC FVTFIEAPSA VQFYANSFID PIVLHGNMLR
VGWGHYSGPL PKLISLAVTI GASRNVYVSL PEFAFKEKFI HDPQYKKLHE TLSLPDAEQL
REDFSTYGDI EQINYLSDSH CCWINFMNIS SAISLVEEMN KESTVQNESG EVTLKRATEE
KFGGRYKGLL INYGKDRCGN INKNLIAGKN SRFYKKVKRP SYNIRLSKLE EKRRQNEIDE
KEKAFDKPLN LESLGISLDA HKDNGGGETG TANNTGHENE SELEAENENG NETGSFGGLG
LAVASSDVKR ATSDETDYED IFNKSSGSSD SSSDVEVIMH SPSDPEYALK SQTLRSSSQT
VINSKRPVKI EDEEEAVGMS QLNYRSSLRQ APPRAPSTLS YNHSKNNETP MQDIFTNGET
ANNRKKKRGS FARHRTIPGS DVMAQYLAQV QHSTFMYAAN ILGASAEDNT HPDE
