HGH1_YEAST
ID HGH1_YEAST Reviewed; 394 AA.
AC P48362; D6VUX0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein HGH1;
DE AltName: Full=HMG1/2 protein homolog;
GN Name=HGH1; OrderedLocusNames=YGR187C; ORFNames=G7538;
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].
RA Sun Z., Liang J., Hampsey M.;
RT "The HGH1 gene encodes a protein with structural similarity to mammalian
RT HMG1/2 proteins.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133739;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA Nombela C.;
RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:357-363(1997).
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- MISCELLANEOUS: Present with 20800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HGH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA77038.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U27358; AAA77038.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X99074; CAA67531.1; -; Genomic_DNA.
DR EMBL; Z72972; CAA97213.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08281.1; -; Genomic_DNA.
DR PIR; S64505; S64505.
DR RefSeq; NP_011703.3; NM_001181316.3.
DR PDB; 6HB1; X-ray; 2.33 A; A/B/C/D=1-363.
DR PDB; 6HB2; X-ray; 2.70 A; A/B/C/D=2-363.
DR PDB; 6HB3; X-ray; 3.00 A; A/B/C/D=1-363.
DR PDBsum; 6HB1; -.
DR PDBsum; 6HB2; -.
DR PDBsum; 6HB3; -.
DR AlphaFoldDB; P48362; -.
DR SMR; P48362; -.
DR BioGRID; 33439; 189.
DR DIP; DIP-4721N; -.
DR IntAct; P48362; 9.
DR MINT; P48362; -.
DR STRING; 4932.YGR187C; -.
DR iPTMnet; P48362; -.
DR MaxQB; P48362; -.
DR PaxDb; P48362; -.
DR PRIDE; P48362; -.
DR DNASU; 853099; -.
DR EnsemblFungi; YGR187C_mRNA; YGR187C; YGR187C.
DR GeneID; 853099; -.
DR KEGG; sce:YGR187C; -.
DR SGD; S000003419; HGH1.
DR VEuPathDB; FungiDB:YGR187C; -.
DR eggNOG; KOG2973; Eukaryota.
DR GeneTree; ENSGT00390000016546; -.
DR HOGENOM; CLU_037769_2_1_1; -.
DR InParanoid; P48362; -.
DR OMA; HRWEKDV; -.
DR BioCyc; YEAST:G3O-30877-MON; -.
DR PRO; PR:P48362; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P48362; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0061770; F:translation elongation factor binding; IDA:SGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039717; Hgh1.
DR InterPro; IPR007206; Protein_HGH1_C.
DR InterPro; IPR007205; Protein_HGH1_N.
DR PANTHER; PTHR13387; PTHR13387; 1.
DR Pfam; PF04063; DUF383; 1.
DR Pfam; PF04064; DUF384; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..394
FT /note="Protein HGH1"
FT /id="PRO_0000083966"
FT REGION 357..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..394
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:6HB1"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:6HB1"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6HB1"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6HB1"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:6HB1"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:6HB1"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6HB1"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:6HB1"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:6HB1"
SQ SEQUENCE 394 AA; 44951 MW; 24D4EFAEBD5D7A48 CRC64;
MTSQLNELVE FLHSPQPAVR QIAIDNLVGF SAGPTSKVFK NDSYRPIKDI IKMIMDPEHG
TRVIIQQGVT ILVNLSEDKL VRNIILSDDK KFLKFLVWKI VDLTNPNADI MCILLSNLAK
DDGILAVLNI KRNSSGEEVD DGLKLAALNK EVFKSLRAMD CLMDCFVKGY DKKLTKYASF
NYLAFFFADI SRFKLGRMYF IEEQEYDGVV PISKLLVFTE KYDAKVRREG VASTIKNSLF
DSETHERLLK DEKINLLPYI LLPIASAKDS EIDEEDMFNL PDELQLLPED KERDPIPAII
CCHLESILLL CTTHAGREYL RDKSVYPLVR ELHKNVENED IGELCYRIVN MLMRGEPGAG
AVEEMPSKNA EEEEEEESEE EEDDDEEDEI VEVA
