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TSN1_SCHPO
ID   TSN1_SCHPO              Reviewed;         220 AA.
AC   Q9P7V3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Translin-1;
DE   AltName: Full=Meiotically up-regulated gene 90 protein;
DE   AltName: Full=Translin homolog;
GN   Name=tsn1; Synonyms=mug90; ORFNames=SPAC30.03c;
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   FUNCTION IN MEIOSIS.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [3]
RP   FUNCTION, SUBUNIT, AND DELETION MUTANT.
RX   PubMed=16043634; DOI=10.1093/nar/gki727;
RA   Laufman O., Ben Yosef R., Adir N., Manor H.;
RT   "Cloning and characterization of the Schizosaccharomyces pombe homologs of
RT   the human protein translin and the translin-associated protein TRAX.";
RL   Nucleic Acids Res. 33:4128-4139(2005).
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).
CC   -!- FUNCTION: DNA-binding protein that specifically recognizes consensus
CC       sequences at the breakpoint junctions in chromosomal translocations.
CC       Selectively binds single-stranded d(GT)n and d(GTT)n microsatellite
CC       repeats. Has much higher affinities for the homologous RNA sequences
CC       (GU)n and (GUU)n. Does not bind double-stranded DNA. Has a role in
CC       meiosis. {ECO:0000269|PubMed:16043634, ECO:0000269|PubMed:16303567}.
CC   -!- SUBUNIT: Forms an octameric ring-shaped structure, which is capable of
CC       binding DNA or RNA. {ECO:0000269|PubMed:16043634}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- MISCELLANEOUS: Deletion of both tsn1 and trax results in slightly
CC       stimulated cell proliferation.
CC   -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB66462.2; -; Genomic_DNA.
DR   PIR; T50209; T50209.
DR   RefSeq; NP_594557.2; NM_001019986.3.
DR   AlphaFoldDB; Q9P7V3; -.
DR   SMR; Q9P7V3; -.
DR   BioGRID; 278209; 5.
DR   STRING; 4896.SPAC30.03c.1; -.
DR   MaxQB; Q9P7V3; -.
DR   PaxDb; Q9P7V3; -.
DR   EnsemblFungi; SPAC30.03c.1; SPAC30.03c.1:pep; SPAC30.03c.
DR   GeneID; 2541714; -.
DR   KEGG; spo:SPAC30.03c; -.
DR   PomBase; SPAC30.03c; tsn1.
DR   VEuPathDB; FungiDB:SPAC30.03c; -.
DR   eggNOG; KOG3067; Eukaryota.
DR   HOGENOM; CLU_079179_0_0_1; -.
DR   InParanoid; Q9P7V3; -.
DR   OMA; LHAGFQI; -.
DR   PhylomeDB; Q9P7V3; -.
DR   Reactome; R-SPO-426486; Small interfering RNA (siRNA) biogenesis.
DR   PRO; PR:Q9P7V3; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:1990605; F:GU repeat RNA binding; IDA:PomBase.
DR   GO; GO:0035939; F:microsatellite binding; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; TAS:PomBase.
DR   CDD; cd14819; Translin; 1.
DR   Gene3D; 1.20.58.190; -; 1.
DR   Gene3D; 1.20.58.200; -; 1.
DR   InterPro; IPR033956; Translin.
DR   InterPro; IPR016069; Translin_C.
DR   InterPro; IPR002848; Translin_fam.
DR   InterPro; IPR016068; Translin_N.
DR   InterPro; IPR036081; Translin_sf.
DR   PANTHER; PTHR10741; PTHR10741; 1.
DR   PANTHER; PTHR10741:SF2; PTHR10741:SF2; 1.
DR   Pfam; PF01997; Translin; 1.
DR   SUPFAM; SSF74784; SSF74784; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Meiosis; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..220
FT                   /note="Translin-1"
FT                   /id="PRO_0000278571"
SQ   SEQUENCE   220 AA;  25493 MW;  B6CE14CFC230C567 CRC64;
     MNKSIFIQLQ DQIDKEHSIR EKLTAEVDLL DEKLRVLQLL LANCEQNLEN QEEILEALEI
     IKSKTRGLAE LASNFPYYKY NGVWDRSIQK VVYLYLLASW TGRLDKSLRP TYSLLSLSEV
     GQILQVPVFP EESTFHLSIE QYLHAVLSLC SELARQSVNS VISGNYHIPF EALNTIQKVH
     SSFQVLSLKN DSLRRHFDGL KYDLKRSEDV VYDLRIHKLV
 
 
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