ID FAP1_YEAST Reviewed; 965 AA.
AC P53971; D6W1F6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=FKBP12-associated protein 1;
GN Name=FAP1; OrderedLocusNames=YNL023C; ORFNames=N2812;
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 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 [4]
RP FUNCTION, INTERACTION WITH FPR1, AND SUBCELLULAR LOCATION.
RX PubMed=10998178; DOI=10.1046/j.1365-2958.2000.02105.x;
RA Kunz J., Loeschmann A., Deuter-Reinhard M., Hall M.N.;
RT "FAP1, a homologue of human transcription factor NF-X1, competes with
RT rapamycin for binding to FKBP12 in yeast.";
RL Mol. Microbiol. 37:1480-1493(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-951, 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).
CC -!- FUNCTION: May play a role in transcription regulation. {ECO:0000250,
CC ECO:0000269|PubMed:10998178}.
CC -!- SUBUNIT: Interacts with FPR1. {ECO:0000269|PubMed:10998178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10998178}. Nucleus
CC {ECO:0000269|PubMed:10998178}. Note=Translocates to the nucleus in
CC response to rapamycin.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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DR EMBL; Z71299; CAA95885.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10522.1; -; Genomic_DNA.
DR PIR; S62935; S62935.
DR RefSeq; NP_014375.1; NM_001182862.1.
DR AlphaFoldDB; P53971; -.
DR SMR; P53971; -.
DR BioGRID; 35803; 149.
DR DIP; DIP-967N; -.
DR IntAct; P53971; 14.
DR MINT; P53971; -.
DR STRING; 4932.YNL023C; -.
DR iPTMnet; P53971; -.
DR MaxQB; P53971; -.
DR PaxDb; 4932-YNL023C; -.
DR PeptideAtlas; P53971; -.
DR EnsemblFungi; YNL023C_mRNA; YNL023C; YNL023C.
DR GeneID; 855708; -.
DR KEGG; sce:YNL023C; -.
DR AGR; SGD:S000004968; -.
DR SGD; S000004968; FAP1.
DR VEuPathDB; FungiDB:YNL023C; -.
DR eggNOG; KOG1952; Eukaryota.
DR GeneTree; ENSGT00940000156325; -.
DR HOGENOM; CLU_005714_2_2_1; -.
DR InParanoid; P53971; -.
DR OMA; KCQSVCH; -.
DR OrthoDB; 1412at2759; -.
DR BioCyc; YEAST:G3O-33061-MONOMER; -.
DR BioGRID-ORCS; 855708; 0 hits in 10 CRISPR screens.
DR PRO; PR:P53971; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53971; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd06008; NF-X1-zinc-finger; 4.
DR CDD; cd06006; R3H_unknown_2; 1.
DR CDD; cd16492; RING-CH-C4HC3_NFX1-like; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034077; R3H_FAP1.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 5.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00438; ZnF_NFX; 7.
DR SUPFAM; SSF82708; R3H domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..965
FT /note="FKBP12-associated protein 1"
FT /id="PRO_0000056343"
FT DOMAIN 733..796
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 68..118
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 159..177
FT /note="NF-X1-type 1"
FT ZN_FING 216..235
FT /note="NF-X1-type 2"
FT ZN_FING 362..382
FT /note="NF-X1-type 3"
FT ZN_FING 468..487
FT /note="NF-X1-type 4"
FT ZN_FING 586..606
FT /note="NF-X1-type 5"
FT MOD_RES 951
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 965 AA; 108495 MW; 121C57BB07C6FA9D CRC64;
MTEHESLGLE QNQDGGDTYR HHNLSDGCIS SVEDANEQPS SYEEESDDDM QYYERAIQEI
SSGDSYVCMI CTVEMDYTCQ MFACKRCYRV FDYGCIREWA LKSTEKTVDR IWKCPNCYYV
SKRVPVKNRP TCWCGKVVNP DPNPLDPNSC GQTCNASTCM HGCSKICHLG PHPECTRMVE
IMCHCGKHSK SIFCYQSKVM KKNFNCQEVC GLPLSCSIHT CKKKCHPGLC GPCPEMIISK
DSPKKQIKCY CGNHTRANIK CSETKFPKSG KSSKDENGNR WIGVFACADN RVVDYSCRKH
SFIESCISPP TINGEKACPF LPSSLKTCPC GRTALEELTK PRKHCDDPIP TCDSRCGKPL
KCGKHSCPFT CHDKACMEPC LQIDSVKCAC EQSTFSVPCG FQGRPRCNIK CESLMSCRRH
RCTDRCCSGR PSAIRRKKNL FRTQDLLDES LVEAKHICLK PCNLTLSCGI HKCQRKCHPG
KCPPCLESDS NDLVCPCGNT VVPAPVRCGT KLPTCNHPCI KVVRGESTCG HKPMPHTCHS
LDVSCPPCTE TVFKPCKCGK KTKVRTVCFQ TDVSCGIKCG IPLSYCYHTC QKTCHLPGNC
QKVCKQTCGQ KRLNCNHECP KPCHGKTECP DLPCATLVKI YCKCGRIKKS VTCGAKSDRV
SVTESSVLDC NEECEALKRL KELKEAFGIK EETNNFTSNE LDALKKLVSV ATTFEELQLP
FTEAALSVYS KQERWCSQIE AILNKLMDDK TRSSLHFKPM RPPQRHFIRE LAKAYGLYSE
SQDREPMRSV FIKKEDNGAS NKPVLSLAEA YPLYESFKQL QKERKAQEFQ ARTTAKLINF
EVQDTEPKVE VAKKNGFLVQ NLVAGNTAED LRRFFEPHLK HTLVVNPQYL ILDDGKTALV
YPENYETASV NTERDMELLV GHFDFMAKEA FLADSISLCS TEEELERRLD TPVIQEDSPV
MDNNT
//
