ID   JJJ1_YEAST              Reviewed;         590 AA.
AC   P53863; D6W0W4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=J protein JJJ1;
GN   Name=JJJ1; OrderedLocusNames=YNL227C; ORFNames=N1254;
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].
RX   PubMed=8896273;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA   Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT   "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT   reading frames including a novel gene encoding a globin-like domain.";
RL   Yeast 12:1071-1076(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504, AND IDENTIFICATION BY
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND THR-504, AND
RP   IDENTIFICATION BY 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).
CC   -!- INTERACTION:
CC       P53863; P38344: REI1; NbExp=6; IntAct=EBI-29183, EBI-21136;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 2310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z69381; CAA93371.1; -; Genomic_DNA.
DR   EMBL; Z71504; CAA96132.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10330.1; -; Genomic_DNA.
DR   PIR; S63193; S63193.
DR   RefSeq; NP_014172.1; NM_001183065.1.
DR   AlphaFoldDB; P53863; -.
DR   SMR; P53863; -.
DR   BioGRID; 35610; 243.
DR   DIP; DIP-972N; -.
DR   IntAct; P53863; 25.
DR   MINT; P53863; -.
DR   STRING; 4932.YNL227C; -.
DR   iPTMnet; P53863; -.
DR   MaxQB; P53863; -.
DR   PaxDb; 4932-YNL227C; -.
DR   PeptideAtlas; P53863; -.
DR   EnsemblFungi; YNL227C_mRNA; YNL227C; YNL227C.
DR   GeneID; 855495; -.
DR   KEGG; sce:YNL227C; -.
DR   AGR; SGD:S000005171; -.
DR   SGD; S000005171; JJJ1.
DR   VEuPathDB; FungiDB:YNL227C; -.
DR   eggNOG; KOG0717; Eukaryota.
DR   HOGENOM; CLU_009539_2_1_1; -.
DR   InParanoid; P53863; -.
DR   OMA; RANHEES; -.
DR   OrthoDB; 5491419at2759; -.
DR   BioCyc; YEAST:G3O-33229-MONOMER; -.
DR   BioGRID-ORCS; 855495; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53863; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53863; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IMP:SGD.
DR   GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IMP:SGD.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR44029; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR   PANTHER; PTHR44029:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Chaperone; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..590
FT                   /note="J protein JJJ1"
FT                   /id="PRO_0000071162"
FT   DOMAIN          3..72
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   ZN_FING         338..362
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         549..573
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          269..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         504
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   590 AA;  68783 MW;  0D184EF861105C95 CRC64;
     MKTCYYELLG VETHASDLEL KKAYRKKALQ YHPDKNPDNV EEATQKFAVI RAAYEVLSDP
     QERAWYDSHK EQILNDTPPS TDDYYDYEVD ATVTGVTTDE LLLFFNSALY TKIDNSAAGI
     YQIAGKIFAK LAKDEILSGK RLGKFSEYQD DVFEQDINSI GYLKACDNFI NKTDKLLYPL
     FGYSPTDYEY LKHFYKTWSA FNTLKSFSWK DEYMYSKNYD RRTKREVNRR NEKARQQARN
     EYNKTVKRFV VFIKKLDKRM KEGAKIAEEQ RKLKEQQRKN ELNNRRKFGN DNNDEEKFHL
     QSWQTVKEEN WDELEKVYDN FGEFENSKND KEGEVLIYEC FICNKTFKSE KQLKNHINTK
     LHKKNMEEIR KEMEEENITL GLDNLSDLEK FDSADESVKE KEDIDLQALQ AELAEIERKL
     AESSSEDESE DDNLNIEMDI EVEDVSSDEN VHVNTKNKKK RKKKKKAKVD TETEESESFD
     DTKDKRSNEL DDLLASLGDK GLQTDDDEDW STKAKKKKGK QPKKNSKSTK STPSLSTLPS
     SMSPTSAIEV CTTCGESFDS RNKLFNHVKI AGHAAVKNVV KRKKVKTKRI
//