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SPT5_SCHPO
ID   SPT5_SCHPO              Reviewed;         990 AA.
AC   O13936; Q9US64;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Transcription elongation factor spt5;
DE   AltName: Full=Chromatin elongation factor spt5;
GN   Name=spt5; ORFNames=SPAC23C4.19;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 240-350, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH SPT4.
RX   PubMed=11893740; DOI=10.1074/jbc.m200015200;
RA   Pei Y., Shuman S.;
RT   "Interactions between fission yeast mRNA capping enzymes and elongation
RT   factor Spt5.";
RL   J. Biol. Chem. 277:19639-19648(2002).
RN   [4]
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: The spt4-spt5 complex mediates both activation and inhibition
CC       of transcription elongation, and plays a role in pre-mRNA processing.
CC       This complex seems to be important for the stability of the RNA
CC       polymerase II elongation machinery on the chromatin template but not
CC       for the inherent ability of this machinery to translocate down the gene
CC       (By similarity). {ECO:0000250, ECO:0000269|PubMed:11893740}.
CC   -!- SUBUNIT: Component of the spt4-spt5 complex. Interacts with RNA
CC       polymerase II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16890.1; -; Genomic_DNA.
DR   EMBL; AB028017; BAA87321.1; -; Genomic_DNA.
DR   PIR; T38274; T38274.
DR   RefSeq; NP_593191.1; NM_001018587.2.
DR   PDB; 4PZ8; X-ray; 3.10 A; B=827-844.
DR   PDBsum; 4PZ8; -.
DR   AlphaFoldDB; O13936; -.
DR   SMR; O13936; -.
DR   BioGRID; 278406; 17.
DR   STRING; 4896.SPAC23C4.19.1; -.
DR   iPTMnet; O13936; -.
DR   SwissPalm; O13936; -.
DR   MaxQB; O13936; -.
DR   PaxDb; O13936; -.
DR   PRIDE; O13936; -.
DR   EnsemblFungi; SPAC23C4.19.1; SPAC23C4.19.1:pep; SPAC23C4.19.
DR   GeneID; 2541916; -.
DR   KEGG; spo:SPAC23C4.19; -.
DR   PomBase; SPAC23C4.19; spt5.
DR   VEuPathDB; FungiDB:SPAC23C4.19; -.
DR   eggNOG; KOG1999; Eukaryota.
DR   HOGENOM; CLU_003537_1_1_1; -.
DR   InParanoid; O13936; -.
DR   OMA; VGYMNTP; -.
DR   PhylomeDB; O13936; -.
DR   Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SPO-72086; mRNA Capping.
DR   Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   PRO; PR:O13936; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IC:PomBase.
DR   GO; GO:0032044; C:DSIF complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003711; F:transcription elongation regulator activity; EXP:PomBase.
DR   GO; GO:0140673; P:co-transcriptional chromatin reassembly; TAS:PomBase.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0060195; P:negative regulation of antisense RNA transcription; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:PomBase.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   CDD; cd06081; KOW_Spt5_1; 1.
DR   CDD; cd06082; KOW_Spt5_2; 1.
DR   CDD; cd06083; KOW_Spt5_3; 1.
DR   CDD; cd06084; KOW_Spt5_4; 1.
DR   CDD; cd06085; KOW_Spt5_5; 1.
DR   CDD; cd09888; NGN_Euk; 1.
DR   Gene3D; 2.30.30.30; -; 3.
DR   Gene3D; 3.30.70.940; -; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR041973; KOW_Spt5_1.
DR   InterPro; IPR041975; KOW_Spt5_2.
DR   InterPro; IPR041976; KOW_Spt5_3.
DR   InterPro; IPR041977; KOW_Spt5_4.
DR   InterPro; IPR041978; KOW_Spt5_5.
DR   InterPro; IPR005100; NGN-domain.
DR   InterPro; IPR006645; NGN_dom.
DR   InterPro; IPR036735; NGN_dom_sf.
DR   InterPro; IPR039385; NGN_Euk.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR039659; SPT5.
DR   InterPro; IPR024945; Spt5_C_dom.
DR   InterPro; IPR022581; Spt5_N.
DR   InterPro; IPR017071; TF_Spt5_eukaryote.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11125; PTHR11125; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF03439; Spt5-NGN; 1.
DR   Pfam; PF11942; Spt5_N; 1.
DR   PIRSF; PIRSF036945; Spt5; 1.
DR   SMART; SM01104; CTD; 1.
DR   SMART; SM00739; KOW; 5.
DR   SMART; SM00738; NGN; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription.
FT   CHAIN           1..990
FT                   /note="Transcription elongation factor spt5"
FT                   /id="PRO_0000238565"
FT   DOMAIN          471..498
FT                   /note="KOW 1"
FT   DOMAIN          520..547
FT                   /note="KOW 2"
FT   DOMAIN          727..754
FT                   /note="KOW 3"
FT   REPEAT          818..826
FT                   /note="1"
FT   REPEAT          827..835
FT                   /note="2"
FT   REPEAT          836..844
FT                   /note="3"
FT   REPEAT          845..853
FT                   /note="4"
FT   REPEAT          854..862
FT                   /note="5"
FT   REPEAT          863..871
FT                   /note="6"
FT   REPEAT          872..880
FT                   /note="7"
FT   REPEAT          881..889
FT                   /note="8"
FT   REPEAT          890..898
FT                   /note="9"
FT   REPEAT          899..907
FT                   /note="10"
FT   REPEAT          908..916
FT                   /note="11"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..916
FT                   /note="11 X 9 AA tandem repeats of T-P-A-W-N-X-G-[NS]-[KR]"
FT   REGION          818..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..128
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..172
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   990 AA;  109014 MW;  6FF52652D1C8EE89 CRC64;
     MDTNSPKSID KDANSTEVDA AEQDAASVKI NSTRASPNGS DLLNDDSEAA KITTNEKQSS
     PVDSHNESPN DTTINKGEDG NENEVDNVNN NDKKEDEDNV EENEEEADAN EEEEEDEEDD
     EEDEEDEDES GGGRRKRARH DRRNQFLDIE AEVDEDEEEL EDEEDEIGRE DGFIEEEVGA
     DYVGDDRRHR ELDRQRQELQ SVDAERLAEE YREKYGRSQT VVGDTSNVPQ RLLLPSVNDP
     NIWAVRCKIG KEKDIVFTIM RKAMDLQYTS SPLEIISAFQ RDSLVGYIYV EARKQSHVLD
     ALNGVLNVYT NNMILVPIKE MPDLLKVQKQ VVELLPGAYV RIRRGKYAGD LAQVDNLSEN
     GLTARVRIVP RIDYSDGLKR KNSATRPQAR LFNESEAFKS NPSKFSKRGP RLFLFNNEEF
     EDGFLVKDIR ISSLITEGVN PTLDEVSKFN PNNEDLDLSS LALSVKGGHA EFQPGDHVEV
     YVGEQTGVSG VVENVRGSVI TMVSSDGLRL DVPSRGLRKR FRHGDYVKVI AGKYKDDTGM
     VVRISKDEVT FLSDTLMTEL TVFSRDLGEA SSAQAVNSAY ELHDLVQLDV NTVACIFSVD
     RDTYKVIDQN GGVRTVLASQ ITMRHSNRRG VATDRNGAEI RIGDKVKEVG GEGKQGTILH
     IYRAFVFLHN RDIAENNGVF SARSRNVATI AAKGARISAD LTKMNPALSN GPALPPVANL
     KRTIGRDKAI GATVRIRRGP MKGLLGVIKD TTDANARVEL HTGNKMVTIP KENLLYTTKT
     GELISYTEFI ERSRGIRPGS ISTADGPNVP NWAQGARTPA VANGSRTPAW NTGSRTPAWN
     SGSKTPAWNS GSRTPAWNSG NKTPAWNAGS RTPAWNSGNK TPAWNVGNKT PAWNSGAKTP
     AWNAGNKTPS WNNGTKTPAW NANQTPMVAN GTNTSWGQTP AYGGFSETNW DTEDNSKPYT
     APTPGAWAAP TPGGWDDEEG DSPKYVPPSP
 
 
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