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ABF2_YEAST
ID   ABF2_YEAST              Reviewed;         183 AA.
AC   Q02486; D6VZP6; Q712M5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=ARS-binding factor 2, mitochondrial;
DE   Flags: Precursor;
GN   Name=ABF2; Synonyms=HIM1; OrderedLocusNames=YMR072W; ORFNames=YM9916.11;
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], AND PROTEIN SEQUENCE OF 27-56.
RX   PubMed=1881919; DOI=10.1073/pnas.88.17.7864;
RA   Diffley J.F.X., Stillman B.;
RT   "A close relative of the nuclear, chromosomal high-mobility group protein
RT   HMG1 in yeast mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7864-7868(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sun C.L., Lee F.J., Lin-Chao S., Chao C.K.;
RT   "Molecular cloning and characterization of yeast CDRP1: an HMG protein
RT   which recognizes cisplatin-damaged DNA and confers drug sensitivity.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9742088; DOI=10.1128/mcb.18.10.5712;
RA   Cho J.H., Ha S.J., Kao L.R., Megraw T.L., Chae C.-B.;
RT   "A novel DNA-binding protein bound to the mitochondrial inner membrane
RT   restores the null mutation of mitochondrial histone Abf2p in Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 18:5712-5723(1998).
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   -!- FUNCTION: Specific binding to the autonomously replicating sequence 1
CC       (ARS1). Interaction with regulatory regions: probably involved in
CC       compacting the mitochondrial genome. It might play a positive role in
CC       gene expression and replication.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Has a temperature-sensitive growth defect in
CC       glucose-rich medium, with slower growth and smaller colonies at 37
CC       degrees Celsius but not 30 degrees Celsius; the phenotype is suppressed
CC       by overexpression of YHM2. {ECO:0000269|PubMed:9742088}.
CC   -!- MISCELLANEOUS: Present with 3810 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M73753; AAA73079.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AJ223169; CAA11146.1; -; mRNA.
DR   EMBL; Z48952; CAA88797.1; -; Genomic_DNA.
DR   EMBL; AY557967; AAS56293.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09970.1; -; Genomic_DNA.
DR   PIR; A41302; A41302.
DR   RefSeq; NP_013788.1; NM_001182570.1.
DR   PDB; 5JGH; X-ray; 2.60 A; A/D/G/J=27-183.
DR   PDB; 5JH0; X-ray; 2.18 A; A/D=27-183.
DR   PDBsum; 5JGH; -.
DR   PDBsum; 5JH0; -.
DR   AlphaFoldDB; Q02486; -.
DR   SMR; Q02486; -.
DR   BioGRID; 35247; 164.
DR   DIP; DIP-5492N; -.
DR   IntAct; Q02486; 30.
DR   MINT; Q02486; -.
DR   STRING; 4932.YMR072W; -.
DR   MaxQB; Q02486; -.
DR   PaxDb; Q02486; -.
DR   PRIDE; Q02486; -.
DR   EnsemblFungi; YMR072W_mRNA; YMR072W; YMR072W.
DR   GeneID; 855094; -.
DR   KEGG; sce:YMR072W; -.
DR   SGD; S000004676; ABF2.
DR   VEuPathDB; FungiDB:YMR072W; -.
DR   eggNOG; KOG0381; Eukaryota.
DR   HOGENOM; CLU_082854_2_0_1; -.
DR   InParanoid; Q02486; -.
DR   OMA; DMKNTEL; -.
DR   BioCyc; YEAST:G3O-32774-MON; -.
DR   Reactome; R-SCE-140342; Apoptosis induced DNA fragmentation.
DR   Reactome; R-SCE-163282; Mitochondrial transcription initiation.
DR   ChiTaRS; ABF2; yeast.
DR   PRO; PR:Q02486; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q02486; protein.
DR   GO; GO:0000262; C:mitochondrial chromosome; IDA:SGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:SGD.
DR   GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR   GO; GO:0090139; P:mitochondrial chromosome packaging; IMP:SGD.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR   GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR   Gene3D; 1.10.30.10; -; 2.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR033311; Ixr1/Abf2.
DR   PANTHER; PTHR48112:SF17; PTHR48112:SF17; 1.
DR   Pfam; PF00505; HMG_box; 2.
DR   SMART; SM00398; HMG; 2.
DR   SUPFAM; SSF47095; SSF47095; 2.
DR   PROSITE; PS50118; HMG_BOX_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-binding; Mitochondrion;
KW   Nucleus; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1881919"
FT   CHAIN           27..183
FT                   /note="ARS-binding factor 2, mitochondrial"
FT                   /id="PRO_0000013477"
FT   DNA_BIND        43..111
FT                   /note="HMG box 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   DNA_BIND        116..183
FT                   /note="HMG box 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:5JH0"
FT   HELIX           49..64
FT                   /evidence="ECO:0007829|PDB:5JH0"
FT   HELIX           70..83
FT                   /evidence="ECO:0007829|PDB:5JH0"
FT   HELIX           86..113
FT                   /evidence="ECO:0007829|PDB:5JH0"
FT   HELIX           122..137
FT                   /evidence="ECO:0007829|PDB:5JH0"
FT   HELIX           143..156
FT                   /evidence="ECO:0007829|PDB:5JH0"
FT   HELIX           159..179
FT                   /evidence="ECO:0007829|PDB:5JH0"
SQ   SEQUENCE   183 AA;  21562 MW;  D280A7D2B675B5B1 CRC64;
     MNSYSLLTRS FHESSKPLFN LASTLLKASK RTQLRNELIK QGPKRPTSAY FLYLQDHRSQ
     FVKENPTLRP AEISKIAGEK WQNLEADIKE KYISERKKLY SEYQKAKKEF DEKLPPKKPA
     GPFIKYANEV RSQVFAQHPD KSQLDLMKII GDKWQSLDQS IKDKYIQEYK KAIQEYNARY
     PLN
 
 
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