SPT2_XENLA
ID SPT2_XENLA Reviewed; 800 AA.
AC Q6NU13; Q8UW69;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Protein SPT2 homolog;
DE AltName: Full=Protein P16H6;
DE AltName: Full=SPT2 domain-containing protein 1;
GN Name=spty2d1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 714-800, AND DEVELOPMENTAL STAGE.
RX PubMed=11784032; DOI=10.1006/dbio.2001.0428;
RA Shibata M., Itoh M., Ohmori S.Y., Shinga J., Taira M.;
RT "Systematic screening and expression analysis of the head organizer genes
RT in Xenopus embryos.";
RL Dev. Biol. 239:241-256(2001).
CC -!- FUNCTION: Histone chaperone that stabilizes pre-existing histone
CC tetramers and regulates replication-independent histone exchange on
CC chromatin. Required for normal chromatin refolding in the coding region
CC of transcribed genes, and for the suppression of spurious
CC transcription. Binds DNA and histones and promotes nucleosome assembly
CC (in vitro). Facilitates formation of tetrameric histone complexes
CC containing histone H3 and H4 (By similarity). Modulates RNA polymerase
CC 1-mediated transcription (By similarity). Binds DNA, with a preference
CC for branched DNA species, such as Y-form DNA and Holliday junction DNA
CC (By similarity). {ECO:0000250|UniProtKB:E1BUG7,
CC ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBUNIT: Interacts with histones. Interacts with a heterotetrameric
CC complex formed by histone H3 and H4, especially when the histone
CC tetramer is not bound to DNA. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:E1BUG7}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at stage 9, then gradually
CC decrease. {ECO:0000269|PubMed:11784032}.
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
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DR EMBL; BC068789; AAH68789.1; -; mRNA.
DR EMBL; AB072003; BAB79594.1; -; mRNA.
DR RefSeq; NP_001131040.1; NM_001137568.1.
DR AlphaFoldDB; Q6NU13; -.
DR PRIDE; Q6NU13; -.
DR DNASU; 398281; -.
DR GeneID; 398281; -.
DR KEGG; xla:398281; -.
DR CTD; 398281; -.
DR Xenbase; XB-GENE-5940059; spty2d1.S.
DR OrthoDB; 1092455at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 398281; Expressed in blastula and 19 other tissues.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..800
FT /note="Protein SPT2 homolog"
FT /id="PRO_0000315739"
FT REGION 1..687
FT /note="Important for interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 70..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..800
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT COILED 53..82
FT /evidence="ECO:0000255"
FT COILED 196..224
FT /evidence="ECO:0000255"
FT COILED 756..800
FT /evidence="ECO:0000255"
FT COMPBIAS 70..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 83745 MW; 23F04EA1D6929865 CRC64;
MDFHSVLRMA AAKPGPDGVM KRYSLAVGPP RKDPKVKGVN SAAVQAFLRK KDQEIQNKEV
EAKRKKEGLL AKRKELKHDR KARAMASRTK DNFRGYNGIP VEEKPKKHKG SGLEEGPNES
MQSTEEDEEY MTEEELYEYS QSESEREEEQ EEMPPQKVAK AAPGKKPPPP ALNFTELLRL
AERKQHEPVE VIRPLKKEER LRTAEELKEL EFLERKAQKA DRKDPMRNGQ VVKISKGSGD
KYYSLKGSHS VEKRSHENSK SSSTEQNGTF RKSSSDNRSR EEKSGSVFHT KDSKFPTKSS
SAKDCGAKGF RPSATGDCKN RNDSTRASGS TSLRPSSGGS SSVSGRPSGS SEKPGSSSGK
PMGGSGSSSA RSSSGSGKPT GATGSGKPTG ASGSGSARSV GESGSRSGKP TGASGSGLAR
SVGASGSGSG KPTGATDSGR PTGVSGSGSA RSVGASGSGK PTGASVSGSA RSVGASGSGK
PTGASGSGSA RSVGASRSVS GKPTGASGSG KPTGAPGASS GKPAGVSGSV SSFARPRSNS
SMAPAKPAAS SGSARPSSSG TPRASSTGNS SSNYSRQASS SGAVRPSSGP PTGGTPKGPS
PRPGTGPNSV RHNTTSISVS ARSSLGSGPG RPVAASATGQ SAMAKPKCTV VAETISSKNF
VPKSINGHMN GMRSAVPPGH RPNMQPPGRP LPPITSSYKR RIDDDEYDSE MDDFIDDGGE
CQDEISKHIR EIFGYDRNRY RDESDYALRY MESSFREQQK EEARSLRLGI QEDLEELRRE
EEELKQKAKQ LKSAKKMKSR
