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NAT2_YEAST
ID   NAT2_YEAST              Reviewed;         288 AA.
AC   P37293; D6VUS8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Putative N-terminal acetyltransferase 2;
DE            EC=2.3.1.-;
DE   AltName: Full=Amino-terminal, alpha-amino, acetyltransferase 2;
GN   Name=NAT2; OrderedLocusNames=YGR147C; ORFNames=G6630;
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=8175741; DOI=10.1016/s0021-9258(17)36810-2;
RA   Sherman F., Kulkarni M.S.;
RT   "NAT2, an essential gene encoding methionine N alpha-acetyltransferase in
RT   the yeast Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 269:13141-13147(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8585325; DOI=10.1002/yea.320111410;
RA   Skala J., Nawrocki A., Goffeau A.;
RT   "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT   Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT   NSR1 genes and ten new open reading frames.";
RL   Yeast 11:1421-1427(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [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).
CC   -!- FUNCTION: Maybe involved in N-terminal acetylation of proteins. N-
CC       acetylation plays a role in normal eukaryotic translation and
CC       processing, protect against proteolytic degradation and protein
CC       turnover.
CC   -!- SUBUNIT: Heterooligomeric. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L25608; AAA34812.1; -; Genomic_DNA.
DR   EMBL; X85807; CAA59805.1; -; Genomic_DNA.
DR   EMBL; Z72932; CAA97161.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08239.1; -; Genomic_DNA.
DR   PIR; S60438; S60438.
DR   RefSeq; NP_011663.3; NM_001181276.3.
DR   AlphaFoldDB; P37293; -.
DR   BioGRID; 33395; 35.
DR   STRING; 4932.YGR147C; -.
DR   MaxQB; P37293; -.
DR   PaxDb; P37293; -.
DR   PRIDE; P37293; -.
DR   EnsemblFungi; YGR147C_mRNA; YGR147C; YGR147C.
DR   GeneID; 853050; -.
DR   KEGG; sce:YGR147C; -.
DR   SGD; S000003379; NAT2.
DR   VEuPathDB; FungiDB:YGR147C; -.
DR   eggNOG; KOG4526; Eukaryota.
DR   GeneTree; ENSGT00940000156134; -.
DR   HOGENOM; CLU_059211_2_0_1; -.
DR   InParanoid; P37293; -.
DR   OMA; KWFNGLM; -.
DR   BioCyc; YEAST:YGR147C-MON; -.
DR   PRO; PR:P37293; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P37293; protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IMP:SGD.
DR   InterPro; IPR045866; FAM210A/B-like.
DR   InterPro; IPR009688; FAM210A/B-like_dom.
DR   PANTHER; PTHR21377; PTHR21377; 1.
DR   Pfam; PF06916; DUF1279; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..288
FT                   /note="Putative N-terminal acetyltransferase 2"
FT                   /id="PRO_0000096740"
FT   REGION          68..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        61
FT                   /note="Q -> K (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="R -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="V -> L (in Ref. 1; AAA34812)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  32804 MW;  C259310FD2D2B080 CRC64;
     MMVPRISASP VFKRIFLRWG FVTLPIQKTV SHTLRRDFSA PCRSMVKCLL LRPGISVHSA
     QDRKFYSTEE KSSQFDENKS KSNNGKKNEP HGIKGLMAKY GYSALIVYIL LTCVDLPLCF
     LGVHSLGEEK IKIYLNRGKQ LIGMGEPDES KVIQDVRRKQ AHREAVQAEN ADKVEDASRK
     TFNERWQEMK DSTLLAELLI AYGIHKSLII VRVPLTAVLT PSFVKLLQRF GIDLMKKQKK
     VFQTMASGAK IRYKGNNPSD FIKNEGTALD ITKRKPRTKG QKWFDGLM
 
 
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