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ASF1A_ARATH
ID   ASF1A_ARATH             Reviewed;         196 AA.
AC   Q9C9M6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable histone chaperone ASF1A;
DE   AltName: Full=Anti-silencing function protein 1-like protein a;
DE            Short=Anti-silencing function 1a protein;
DE   AltName: Full=S-locus protein 7;
DE            Short=AtSP7;
DE   AltName: Full=Silencing group A protein 2;
GN   Name=ASF1A; Synonyms=SGA2, SP7; OrderedLocusNames=At1g66740;
GN   ORFNames=F4N21.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Kaya H., Lee J., Araki T., Shibahara K.;
RT   "Arabidopsis thaliana ASF1 genes.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11759841; DOI=10.1093/dnares/8.5.215;
RA   Takada Y., Ito A., Ninomiya C., Kakizaki T., Takahata Y., Suzuki G.,
RA   Hatakeyama K., Hinata K., Shiba H., Takayama S., Isogai A., Watanabe M.;
RT   "Characterization of expressed genes in the SLL2 region of self-compatible
RT   Arabidopsis thaliana.";
RL   DNA Res. 8:215-219(2001).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HIRA.
RC   STRAIN=cv. Columbia;
RX   PubMed=25086063; DOI=10.1242/bio.20148680;
RA   Nie X., Wang H., Li J., Holec S., Berger F.;
RT   "The HIRA complex that deposits the histone H3.3 is conserved in
RT   Arabidopsis and facilitates transcriptional dynamics.";
RL   Biol. Open 3:794-802(2014).
CC   -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC       histone exchange and removal during nucleosome assembly and disassembly
CC       (By similarity). While encoded by a region of the Arabidopsis thaliana
CC       genome that is homologous to the Brassica S-locus for self
CC       incompatibility, this protein may not play the same role in Arabidopsis
CC       thaliana. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with histone H3 and histone H4 (By similarity).
CC       Component of the HIRA complex made of UBN1, UBN2, ASF1A, CABIN1 and
CC       HIRA. Interacts with HIRA (PubMed:25086063). {ECO:0000250,
CC       ECO:0000269|PubMed:25086063}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25086063}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:25086063}. Note=Localized at rDNA loci in
CC       the nucleolus. {ECO:0000269|PubMed:25086063}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and flower buds.
CC       {ECO:0000269|PubMed:11759841}.
CC   -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR   EMBL; AB078339; BAC54103.1; -; mRNA.
DR   EMBL; AC013288; AAG60078.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34550.1; -; Genomic_DNA.
DR   EMBL; AY096540; AAM20190.1; -; mRNA.
DR   EMBL; AY065298; AAL38774.1; -; mRNA.
DR   RefSeq; NP_176846.1; NM_105344.4.
DR   AlphaFoldDB; Q9C9M6; -.
DR   SMR; Q9C9M6; -.
DR   BioGRID; 28213; 1.
DR   STRING; 3702.AT1G66740.1; -.
DR   PaxDb; Q9C9M6; -.
DR   PRIDE; Q9C9M6; -.
DR   ProteomicsDB; 246677; -.
DR   EnsemblPlants; AT1G66740.1; AT1G66740.1; AT1G66740.
DR   GeneID; 842992; -.
DR   Gramene; AT1G66740.1; AT1G66740.1; AT1G66740.
DR   KEGG; ath:AT1G66740; -.
DR   Araport; AT1G66740; -.
DR   TAIR; locus:2033359; AT1G66740.
DR   eggNOG; KOG3265; Eukaryota.
DR   HOGENOM; CLU_060354_1_2_1; -.
DR   InParanoid; Q9C9M6; -.
DR   OMA; FYVNNDY; -.
DR   OrthoDB; 1334998at2759; -.
DR   PhylomeDB; Q9C9M6; -.
DR   PRO; PR:Q9C9M6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9M6; baseline and differential.
DR   Genevisible; Q9C9M6; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030875; C:rDNA protrusion; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IMP:TAIR.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR   GO; GO:0031567; P:mitotic cell size control checkpoint signaling; IMP:TAIR.
DR   GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR   GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR   Gene3D; 2.60.40.1490; -; 1.
DR   InterPro; IPR006818; ASF1-like.
DR   InterPro; IPR036747; ASF1-like_sf.
DR   PANTHER; PTHR12040; PTHR12040; 1.
DR   Pfam; PF04729; ASF1_hist_chap; 1.
DR   SUPFAM; SSF101546; SSF101546; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..196
FT                   /note="Probable histone chaperone ASF1A"
FT                   /id="PRO_0000270797"
FT   REGION          146..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   196 AA;  22133 MW;  259D9842EA77F115 CRC64;
     MSAIKITNVA VLHNPAPFVS PFQFEISYEC LNSLKDDLEW KLIYVGSAED ETYDQLLESV
     LVGPVNVGNY RFVFQADPPD PSKIQEEDII GVTVLLLTCS YMGQEFLRVG YYVNNDYEDE
     QLKEEPPTKV LIDKVQRNIL SDKPRVTKFP IDFHPEEEQT AATAAPPEQS DEQQPNVNGE
     AQVLPDQSVE PKPEES
 
 
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