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SPT16_ARATH
ID   SPT16_ARATH             Reviewed;        1074 AA.
AC   O82491; C0SVH5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=SPT16; OrderedLocusNames=At4g10710; ORFNames=T12H20.3;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15546350; DOI=10.1111/j.1365-313x.2004.02242.x;
RA   Duroux M., Houben A., Ruzicka K., Friml J., Grasser K.D.;
RT   "The chromatin remodelling complex FACT associates with actively
RT   transcribed regions of the Arabidopsis genome.";
RL   Plant J. 40:660-671(2004).
CC   -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC       that acts to reorganize nucleosomes. The FACT complex is involved in
CC       multiple processes that require DNA as a template such as mRNA
CC       elongation, DNA replication and DNA repair. During transcription
CC       elongation the FACT complex acts as a histone chaperone that both
CC       destabilizes and restores nucleosomal structure. It facilitates the
CC       passage of RNA polymerase II and transcription by promoting the
CC       dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC       subsequently promotes the reestablishment of the nucleosome following
CC       the passage of RNA polymerase II (Probable).
CC       {ECO:0000305|PubMed:15546350}.
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC       and SSRP.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15546350}. Chromosome
CC       {ECO:0000269|PubMed:15546350}. Note=Colocalizes with RNA polymerase II
CC       on chromatin. Recruited to actively transcribed loci.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Present in embryos, shoots and
CC       roots, whereas it is not present in terminally differentiated cells
CC       such as mature trichoblasts or cells of the root cap (at protein
CC       level). {ECO:0000269|PubMed:15546350}.
CC   -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although related to the peptidase M24 family, this protein
CC       lacks conserved active site residues suggesting that it may lack
CC       peptidase activity. {ECO:0000305}.
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DR   EMBL; AF080119; AAC35521.1; -; Genomic_DNA.
DR   EMBL; AL161518; CAB81172.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82919.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67190.1; -; Genomic_DNA.
DR   EMBL; AB493678; BAH30516.1; -; mRNA.
DR   PIR; T01906; T01906.
DR   RefSeq; NP_001329034.1; NM_001340681.1.
DR   RefSeq; NP_192809.1; NM_117139.3.
DR   AlphaFoldDB; O82491; -.
DR   SMR; O82491; -.
DR   BioGRID; 11964; 27.
DR   STRING; 3702.AT4G10710.1; -.
DR   iPTMnet; O82491; -.
DR   PaxDb; O82491; -.
DR   PRIDE; O82491; -.
DR   ProteomicsDB; 234097; -.
DR   EnsemblPlants; AT4G10710.1; AT4G10710.1; AT4G10710.
DR   EnsemblPlants; AT4G10710.2; AT4G10710.2; AT4G10710.
DR   GeneID; 826665; -.
DR   Gramene; AT4G10710.1; AT4G10710.1; AT4G10710.
DR   Gramene; AT4G10710.2; AT4G10710.2; AT4G10710.
DR   KEGG; ath:AT4G10710; -.
DR   Araport; AT4G10710; -.
DR   TAIR; locus:2132756; AT4G10710.
DR   eggNOG; KOG1189; Eukaryota.
DR   HOGENOM; CLU_004627_1_0_1; -.
DR   InParanoid; O82491; -.
DR   OMA; HQFFLDG; -.
DR   OrthoDB; 145488at2759; -.
DR   PhylomeDB; O82491; -.
DR   PRO; PR:O82491; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O82491; baseline and differential.
DR   Genevisible; O82491; AT.
DR   GO; GO:0000791; C:euchromatin; IDA:TAIR.
DR   GO; GO:0035101; C:FACT complex; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   CDD; cd01091; CDC68-like; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR013719; DUF1747.
DR   InterPro; IPR029148; FACT-Spt16_Nlobe.
DR   InterPro; IPR013953; FACT_Spt16.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR040258; Spt16.
DR   InterPro; IPR033825; Spt16_M24.
DR   PANTHER; PTHR13980; PTHR13980; 1.
DR   Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF08512; Rtt106; 1.
DR   Pfam; PF08644; SPT16; 1.
DR   SMART; SM01285; FACT-Spt16_Nlob; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SMART; SM01286; SPT16; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..1074
FT                   /note="FACT complex subunit SPT16"
FT                   /id="PRO_0000245175"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          493..520
FT                   /evidence="ECO:0000255"
FT   COILED          637..658
FT                   /evidence="ECO:0000255"
FT   COILED          782..802
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        962..976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..1007
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1074 AA;  120586 MW;  1AA6FA6475DDBB25 CRC64;
     MADSRNGNAR APPSGVPPKA GNTYSIDVKN FISRARALYE HWKKHSADLW GSADALAIAT
     PPASDDLRYL KSSALNIWLL GYEFPDTIMV FTKKQIHFLC SRNKASLLEV VKKPAHDELK
     LDVIMHVKPK GDDGTGLMDA IFRAIRDLSR GDGNDSQVVG HIAREAPEGK LLETWTERLK
     NANFQFVDIT GGLSDLFAVK DDTEVMSVKK AAYLAYSVMK NVVVPNLESA IDEEKDVTHS
     ALMDLTEKAI LEPTKASVKL KPENVDICYP PIFQSGGKFD LKPSAASNDE LLTYDPASII
     ICAVGARYNS YCSNVARTYL IDATSLQSKA YEVLLKAHEA AIDALRSGRK INTVYQAALS
     VVEKNAPEFV DKLTKSAGTG IGLEFRESGL NINAKNDKVL RPKMAFNVSL GFQNLECESE
     SRSKNKKFSL LLADTVLVTD QKPELLTKCS KSVKDVAYSF KEDEEEEKPR KKARTSGSEN
     YITKTALRSD DHVVSKEELR KQHQAELARQ KNEETARRLA GDSSGAGDSR STAKTSADVV
     AYKNVNDMPH KELMIQVDTR NEAVLLPIYG SLVPFHVATI RTVSGNQDTN RNCYIRIIFN
     VPGTPFNPHD SNSLKNQGAI YLKEVSFRTK DSRHSSEVTQ QIKTLRRQVM ARESERAERA
     TLVTQEKLQL AGNKFKPLRL SELWIRPPFS GRKKIPGTLE AHANGFRYST TRPDERVDVL
     FANIKHAFFQ PAEKEMITLL HFHLHNHIMV GTKKTKDVQF YVEVMDVVQS LGGGRRSAYD
     PDEIDEEQRE RDRKNKINMD FNHFANRVND MWQLPQFASL DLEFDQPLRE LGFHGVPHKT
     SAFIIPTSSC LVELIEYPFL VVSLSEIEIV NLERVGFGQK NFDMAIIFKD FKKDVLRVDS
     VPTSSLEGIK EWLDTTDIKY YESKLNLNWR QILKTITDDP QSFIDDGGWE FLNLDGSDSE
     SGGSEESDKG YEPSDVEVES ESEDEASESE SLVESDDDEE EDSEQESEEE KGKTWDELER
     EATNADREHG VESDSEEERK RRKMKAFGKS RPGTSGGGGS SSMKNMPPSK RKHR
 
 
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