ID CA120_YEAST Reviewed; 1060 AA.
AC P53836; D6W0R6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=CCR4-NOT transcriptional complex subunit CAF120;
DE AltName: Full=120 kDa CCR4-associated factor;
GN Name=CAF120; OrderedLocusNames=YNL278W; ORFNames=N0610;
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=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 [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 IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX.
RX PubMed=11733989; DOI=10.1006/jmbi.2001.5162;
RA Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L.;
RT "Purification and characterization of the 1.0 MDa CCR4-NOT complex
RT identifies two novel components of the complex.";
RL J. Mol. Biol. 314:683-694(2001).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510; SER-518; SER-538 AND
RP SER-556, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-556; SER-871 AND
RP SER-885, AND 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 -!- FUNCTION: Acts as a component of the CCR4-NOT core complex, which in
CC the nucleus seems to be a general transcription factor, and in the
CC cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT
CC protein subcomplex negatively regulates the basal and activated
CC transcription of many genes. Preferentially affects TC-type TATA
CC element-dependent transcription. Could directly or indirectly inhibit
CC component(s) of the general transcription machinery.
CC -!- SUBUNIT: Subunit of the 1.0 MDa CCR4-NOT core complex that contains
CC CCR4, CAF1, CAF120, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In
CC the complex interacts with NOT1. The core complex probably is part of a
CC less characterized 1.9 MDa CCR4-NOT complex.
CC {ECO:0000269|PubMed:11733989}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Bud neck {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CAF120 family. {ECO:0000305}.
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DR EMBL; Z71554; CAA96190.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10282.1; -; Genomic_DNA.
DR PIR; S63252; S63252.
DR RefSeq; NP_014121.1; NM_001183116.1.
DR AlphaFoldDB; P53836; -.
DR BioGRID; 35563; 126.
DR DIP; DIP-6489N; -.
DR IntAct; P53836; 3.
DR STRING; 4932.YNL278W; -.
DR GlyGen; P53836; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P53836; -.
DR MaxQB; P53836; -.
DR PaxDb; 4932-YNL278W; -.
DR PeptideAtlas; P53836; -.
DR EnsemblFungi; YNL278W_mRNA; YNL278W; YNL278W.
DR GeneID; 855443; -.
DR KEGG; sce:YNL278W; -.
DR AGR; SGD:S000005222; -.
DR SGD; S000005222; CAF120.
DR VEuPathDB; FungiDB:YNL278W; -.
DR eggNOG; ENOG502QPV9; Eukaryota.
DR GeneTree; ENSGT00940000176380; -.
DR HOGENOM; CLU_006977_1_0_1; -.
DR InParanoid; P53836; -.
DR OMA; EWKEHIS; -.
DR OrthoDB; 1440555at2759; -.
DR BioCyc; YEAST:G3O-33270-MONOMER; -.
DR BioGRID-ORCS; 855443; 0 hits in 10 CRISPR screens.
DR PRO; PR:P53836; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53836; Protein.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1060
FT /note="CCR4-NOT transcriptional complex subunit CAF120"
FT /id="PRO_0000203378"
FT DOMAIN 75..204
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 465..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1060 AA; 118280 MW; CFB3F2D0B268E15B CRC64;
MRIFSGDNKV VDSLASNPGL MSPSNFGGDF GSRLKVNVTS KKKLNDSSPT SPMESSPVSP
ELVPILTLLN AHTHRRYHEG VFLILQDLNN NGTHAARKWK DVYGVLLGTQ LALWDAKELA
EFTDPSCPVS EKKLKEVASK PTYINLTDAT LRTLDNSDNI VMECGKNLTN ALVVSTTLKN
RYFLQFGNKE SFNAWNSAIR LCLYECSSLQ EAYTGAFISS RGAKLGDIRI LLTNRKYDYK
DWVSVRFGAG MPWKRCYAVI SQSSSKKKGH FGEINLYEND KKVKKNHAMA TIVEAKALYA
VYPSSPKLID SSTIIKVVGS VKFEKKESAQ EKDVFIMPEK HQAVPSYDTI IRFLIPAMDT
FKLYGRPEKL LSSKNDPHSL LFGLPVLPHI YYLEVEDLLP LTNSVSSLHW SNNEWKEHIS
DILQRKIAQG YCGCNSTSNI TSPLPSPFLG SADLFERADG VLSPKLSYGS KSSSNNSSKN
SLPKRERVKL SSSSEQDLNN SDSPSIKRKS PPLVISESPH KVHTPTDASF RTRVTEGSPY
AKQRHPKPFA SSVNDSPSDR AKSRTVPYNN NDRKATTPEK FERGETSCGK NVDESLEKVR
NMKLEIPESN FDKFMTDKNL LSVDSKCSNE KKLSVESDLS AIYEKYSNGP FGHTEGLNGS
SDETYLRFQR ASVHSESNYN SRKSFTPSDF SNGNEEEHAV LQELNSLTQR INELGMESIN
SNSDSDRING SYSQVDFGNN NDEDDMNLFD PDFMAQDQLR AEERDYNKDD RTPLAKVPAA
FQSTGLGITP DDDIERQYIT EHRSRHEVPK RSPEKPSNPL EIGNPYAKPG TRLNTTHTHS
KTDRSITPQR GQPVPSGQQI SSYVQPANIN SPNKMYGANN SAMGSPRNPK TRAPPGPYNQ
GWNNRPSPSN IYQRPHPSDT QPQAYHLPGN PYSTGNRPNM QAQYHPQQVP MPILQQPNRP
YQPYAMNTHM GSPGGYAGAA PPFQPANVNY NTRPQQPWPT PNSPSAHYRP PPNLNQPQNG
SAGYYRPPAP QLQNSQARPQ KKDGFSQFMP SATTKNPYAQ
//
