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FAP1_YEAST
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   03-AUG-2022, entry version 175.
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; 105.
DR   DIP; DIP-967N; -.
DR   IntAct; P53971; 14.
DR   MINT; P53971; -.
DR   STRING; 4932.YNL023C; -.
DR   iPTMnet; P53971; -.
DR   MaxQB; P53971; -.
DR   PaxDb; P53971; -.
DR   PRIDE; P53971; -.
DR   EnsemblFungi; YNL023C_mRNA; YNL023C; YNL023C.
DR   GeneID; 855708; -.
DR   KEGG; sce:YNL023C; -.
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; WCEKEVD; -.
DR   BioCyc; YEAST:G3O-33061-MON; -.
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:0003700; F:DNA-binding transcription factor activity; ISS:SGD.
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   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd06006; R3H_unknown_2; 1.
DR   Gene3D; 3.30.1370.50; -; 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; PTHR12360; 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; SSF82708; 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
 
 
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