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SIM3_SCHPO
ID   SIM3_SCHPO              Reviewed;         396 AA.
AC   Q9USQ4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=NASP-related protein sim3;
DE   AltName: Full=CENP-A escort protein sim3;
DE   AltName: Full=Silencing in the middle of the centromere protein 3;
GN   Name=sim3; ORFNames=SPBC577.15c;
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, SUBCELLULAR LOCATION, INTERACTION WITH CNP1 AND HHT1; HHT2 AND
RP   HHT3, AND MUTAGENESIS OF GLY-81 AND GLU-207.
RX   PubMed=18158900; DOI=10.1016/j.molcel.2007.10.010;
RA   Dunleavy E.M., Pidoux A.L., Monet M., Bonilla C., Richardson W.,
RA   Hamilton G.L., Ekwall K., McLaughlin P.J., Allshire R.C.;
RT   "A NASP (N1/N2)-related protein, Sim3, binds CENP-A and is required for its
RT   deposition at fission yeast centromeres.";
RL   Mol. Cell 28:1029-1044(2007).
CC   -!- FUNCTION: Histone H3 and H3-like CENP-A-specific chaperone. Promotes
CC       delivery and incorporation of CENP-A in centromeric chromatin, probably
CC       by escorting nascent CENP-A to CENP-A chromatin assembly factors.
CC       Required for central core silencing and normal chromosome segregation.
CC       {ECO:0000269|PubMed:18158900}.
CC   -!- SUBUNIT: Interacts with cnp1, hht1, hht2 and hht3; has a preference for
CC       CENP-A (cnp1) over histone H3 (hht1/2/3).
CC       {ECO:0000269|PubMed:18158900}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18158900}.
CC   -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB54823.1; -; Genomic_DNA.
DR   PIR; T40559; T40559.
DR   RefSeq; NP_595313.1; NM_001021220.2.
DR   AlphaFoldDB; Q9USQ4; -.
DR   SMR; Q9USQ4; -.
DR   BioGRID; 277411; 16.
DR   STRING; 4896.SPBC577.15c.1; -.
DR   iPTMnet; Q9USQ4; -.
DR   MaxQB; Q9USQ4; -.
DR   PaxDb; Q9USQ4; -.
DR   PRIDE; Q9USQ4; -.
DR   EnsemblFungi; SPBC577.15c.1; SPBC577.15c.1:pep; SPBC577.15c.
DR   GeneID; 2540895; -.
DR   KEGG; spo:SPBC577.15c; -.
DR   PomBase; SPBC577.15c; sim3.
DR   VEuPathDB; FungiDB:SPBC577.15c; -.
DR   eggNOG; KOG4563; Eukaryota.
DR   HOGENOM; CLU_028900_1_0_1; -.
DR   InParanoid; Q9USQ4; -.
DR   OMA; IKPMSSG; -.
DR   PhylomeDB; Q9USQ4; -.
DR   PRO; PR:Q9USQ4; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; NAS:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR   GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF10516; SHNi-TPR; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..396
FT                   /note="NASP-related protein sim3"
FT                   /id="PRO_0000363381"
FT   REPEAT          32..65
FT                   /note="TPR 1"
FT   REPEAT          89..122
FT                   /note="TPR 2"
FT   REPEAT          199..232
FT                   /note="TPR 3"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          267..329
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        140..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         81
FT                   /note="G->E: In sim3-143; Reduces interaction with CENP-A
FT                   and causes abnormal mitotic phenotypes, including
FT                   hypercondensed chromatin, lagging chromosomes in anaphase,
FT                   and unequal segregation of chromosomes."
FT                   /evidence="ECO:0000269|PubMed:18158900"
FT   MUTAGEN         207
FT                   /note="E->K: In sim3-205; Reduces interaction with CENP-A
FT                   and causes abnormal mitotic phenotypes, including
FT                   hypercondensed chromatin, lagging chromosomes in anaphase,
FT                   and unequal segregation of chromosomes."
FT                   /evidence="ECO:0000269|PubMed:18158900"
SQ   SEQUENCE   396 AA;  43903 MW;  2077DFC3449FC270 CRC64;
     MSSDTKTLEN SKGNSATDAD TKNPSSSDSR AIEQLVTQGN MAYAQKNYEE AVDKYGQALM
     QSESIHGSES LENRNVLWLY GKSLFQIAIE NSQVLGNALG AKESVSQATE SFEEPEAIGS
     FTFSGQKIEN KYTVNEENSS IAHPEKESEE KETNEASPAS EEDEDDFNVA WEVLDLTRVM
     QSKAVDAYPD SKDEKIRLAD IYDLLGELSL EIENFSQASQ DLKTALEWKE KVYNVSNNTL
     LSEAHYKLAL ALEFTNPEDP SNKSRACEHV EKAAEILKNV LNERENEVTD KKGKGKQKAE
     ESTLTSDLEN LREMLSELEQ KTLDLKHGAP SLEEAVMSKM HESSLLSKDS SSLAQAVAEA
     VKNANDLGGL VKRKRTKQEV TSSSQKEGPK DKKKKD
 
 
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