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SSRP1_MAIZE
ID   SSRP1_MAIZE             Reviewed;         639 AA.
AC   Q9LEF5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=FACT complex subunit SSRP1;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE   AltName: Full=Recombination signal sequence recognition protein 1;
DE   AltName: Full=Zm-SSRP1;
GN   Name=SSRP1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DNA-BINDING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10929132; DOI=10.1046/j.1365-313x.2000.00801.x;
RA   Roettgers K., Krohn N.M., Lichota J., Stemmer C., Merkle T., Grasser K.D.;
RT   "DNA-interactions and nuclear localisation of the chromosomal HMG domain
RT   protein SSRP1 from maize.";
RL   Plant J. 23:395-405(2000).
RN   [2]
RP   DNA-BINDING.
RX   PubMed=11425313; DOI=10.1021/bi010548y;
RA   Lichota J., Grasser K.D.;
RT   "Differential chromatin association and nucleosome binding of the maize
RT   HMGA, HMGB, and SSRP1 proteins.";
RL   Biochemistry 40:7860-7867(2001).
RN   [3]
RP   PHOSPHORYLATION AT SER-634 AND SER-638.
RX   PubMed=12571244; DOI=10.1074/jbc.m300250200;
RA   Krohn N.M., Stemmer C., Fojan P., Grimm R., Grasser K.D.;
RT   "Protein kinase CK2 phosphorylates the high mobility group domain protein
RT   SSRP1, inducing the recognition of UV-damaged DNA.";
RL   J. Biol. Chem. 278:12710-12715(2003).
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 (By similarity). Binds specifically to
CC       double-stranded DNA. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC       and SSRP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:10929132}. Chromosome {ECO:0000269|PubMed:10929132}.
CC   -!- TISSUE SPECIFICITY: Present in leaves and kernels, but not in roots.
CC       {ECO:0000269|PubMed:10929132}.
CC   -!- PTM: Phosphorylated by CK2 following UV but not gamma irradiation.
CC       {ECO:0000269|PubMed:12571244}.
CC   -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR   EMBL; AJ244017; CAB96421.1; -; mRNA.
DR   AlphaFoldDB; Q9LEF5; -.
DR   SMR; Q9LEF5; -.
DR   STRING; 4577.GRMZM2G032252_P02; -.
DR   iPTMnet; Q9LEF5; -.
DR   PaxDb; Q9LEF5; -.
DR   MaizeGDB; 411236; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9LEF5; baseline and differential.
DR   GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
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   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 2.30.29.220; -; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR013719; DUF1747.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR035417; POB3_N.
DR   InterPro; IPR000969; SSrcognition.
DR   InterPro; IPR024954; SSRP1_dom.
DR   InterPro; IPR038167; SSRP1_sf.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF17292; POB3_N; 1.
DR   Pfam; PF08512; Rtt106; 1.
DR   Pfam; PF03531; SSrecog; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..639
FT                   /note="FACT complex subunit SSRP1"
FT                   /id="PRO_0000245195"
FT   DNA_BIND        557..625
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          460..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         634
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000305|PubMed:12571244"
FT   MOD_RES         638
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000305|PubMed:12571244"
SQ   SEQUENCE   639 AA;  71418 MW;  963AA72507A450EA CRC64;
     MTDGHHFNNI LLGGRGGTNP GQFKVHSGGL AWKRQGGGKT IEIDKADVTA VTWMKVPRAY
     QLGVRIKAGL FYRFIGFREQ DVSNLTNFIQ KNMGVTPDEK QLSVSGQNWG GIDIDGNMLT
     FMVGSKQAFE VSLPDVAQTQ MQGKTDVLLE LHVDDTTGAN EKDSLMDLSF HVPTSNTQFV
     GDESRPPAHI LWETILKFAD VGSSEEPVVT FEGIAILTPR GRYSVELHLS FLRLQGQAND
     FKIQYSSIVR LFLLPKSNNP HTFVVITLDP PIRKGQTLYP HIVIQFETEA VVERDLALSK
     ELLVEKYKDR LEESYKGLIH EVFTKVLRGL SGAKVTRPGS FRSCQDGYAV KSSLKAEDGL
     LYPLEKGFFF LPKPPTLILH EEIEFVEFER HGAGGASISS HYFDLLVKLK NDQEHLFRNI
     QRNEYHNLFN FINGKNIKIM NLGGDGQGAS GVVTDVLRDT DDDAVDPHLE RIKNQAGDEE
     SDEEDEDFVA DKDDSGSPTD DSGDEESDAS DSGGEKEKSS KKEASSSKPV QKRKHKARDD
     EGQEKKKPKK KKDPNAPKRA MTPFMYFSMA ERGNMKSSNP DLPTTEIAKK LGEMWQKMSG
     EEKQPYIQQA QVDKKRYEKE SAVYRGEATV DVDSGNESD
 
 
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