SPT2_SCHPO
ID SPT2_SCHPO Reviewed; 406 AA.
AC O94714;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein spt2;
GN Name=spt2; ORFNames=SPCC1393.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. Global regulatory protein that plays positive as well as
CC negative regulatory roles in transcription.
CC {ECO:0000250|UniProtKB:P06843}.
CC -!- SUBUNIT: Interacts with tetramers formed by histone H3 and H4.
CC {ECO:0000250|UniProtKB:P06843}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000250|UniProtKB:P06843}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
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DR EMBL; CU329672; CAB38158.1; -; Genomic_DNA.
DR PIR; T40950; T40950.
DR RefSeq; NP_587960.1; NM_001022951.2.
DR AlphaFoldDB; O94714; -.
DR SMR; O94714; -.
DR BioGRID; 275468; 23.
DR STRING; 4896.SPCC1393.02c.1; -.
DR iPTMnet; O94714; -.
DR MaxQB; O94714; -.
DR PaxDb; O94714; -.
DR PRIDE; O94714; -.
DR EnsemblFungi; SPCC1393.02c.1; SPCC1393.02c.1:pep; SPCC1393.02c.
DR GeneID; 2538890; -.
DR KEGG; spo:SPCC1393.02c; -.
DR PomBase; SPCC1393.02c; spt2.
DR VEuPathDB; FungiDB:SPCC1393.02c; -.
DR eggNOG; ENOG502QRJX; Eukaryota.
DR HOGENOM; CLU_767599_0_0_1; -.
DR InParanoid; O94714; -.
DR OMA; HEPPGLI; -.
DR PhylomeDB; O94714; -.
DR PRO; PR:O94714; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000792; C:heterochromatin; ISM:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISO:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISS:PomBase.
DR GO; GO:0010847; P:regulation of chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:PomBase.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 3: Inferred from homology;
KW Activator; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..406
FT /note="Protein spt2"
FT /id="PRO_0000339143"
FT REGION 38..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..406
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:P06843"
FT REGION 383..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..111
FT /evidence="ECO:0000255"
FT COILED 370..406
FT /evidence="ECO:0000255"
FT COMPBIAS 38..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45636 MW; 59E62CBDDDD8ECA5 CRC64;
MAGTPSFQKL MALADSQSAQ AAVQIEQLRK AQIREKAREI TEERNRQRKL QRERELRQKY
EEEQRRQQAM EAKRIAASTR QTSERPPLSA EEAKRIREVK EKDRLESKKN ERQGKPRSYN
ELLRQASSAP AVNETSSSGL LQSKDKRSQS PHSPKKPVKN SSSRDQPVRN SGATSTASLP
PAGLRAGRGS QISASLAWLK TGGASAAPSN PRQPPPTSNF SNRKARYASN GLVQLQTGPK
RDKRSAGEVQ DEIMKRRQNS SISQAATPRT VSNSETSYVG SPALKQSKPN SLKSNNTSRK
TSASSAITKP KARPHTSRHD EFVVSDDDEL NDRVPDVSSE IWKIFGKRKQ DYVSRDVFSD
EDDMEATGHD VWREEQAAAR AARLEDELEE QRERERELAK KRRKNK
