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MIS12_SCHPO
ID   MIS12_SCHPO             Reviewed;         259 AA.
AC   Q9Y738;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Centromere protein mis12;
DE   AltName: Full=NMS complex subunit mis12;
GN   Name=mis12; ORFNames=SPBC409.04c;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10398680; DOI=10.1101/gad.13.13.1664;
RA   Goshima G., Saitoh S., Yanagida M.;
RT   "Proper metaphase spindle length is determined by centromere proteins Mis12
RT   and Mis6 required for faithful chromosome segregation.";
RL   Genes Dev. 13:1664-1677(1999).
RN   [2]
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   [3]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-190;
RP   THR-192 AND SER-213.
RX   PubMed=12773390; DOI=10.1093/emboj/cdg266;
RA   Goshima G., Iwasaki O., Obuse C., Yanagida M.;
RT   "The role of Ppe1/PP6 phosphatase for equal chromosome segregation in
RT   fission yeast kinetochore.";
RL   EMBO J. 22:2752-2763(2003).
RN   [4]
RP   INTERACTION WITH MAL2.
RX   PubMed=12242294; DOI=10.1128/mcb.22.20.7168-7183.2002;
RA   Jin Q.-W., Pidoux A.L., Decker C., Allshire R.C., Fleig U.;
RT   "The mal2p protein is an essential component of the fission yeast
RT   centromere.";
RL   Mol. Cell. Biol. 22:7168-7183(2002).
RN   [5]
RP   INTERACTION WITH MIS14.
RX   PubMed=15369671; DOI=10.1016/j.cell.2004.09.002;
RA   Hayashi T., Fujita Y., Iwasaki O., Adachi Y., Takahashi K., Yanagida M.;
RT   "Mis16 and Mis18 are required for CENP-A loading and histone deacetylation
RT   at centromeres.";
RL   Cell 118:715-729(2004).
RN   [6]
RP   IDENTIFICATION IN THE NMS COMPLEX.
RX   PubMed=16079914; DOI=10.1038/sj.emboj.7600762;
RA   Liu X., McLeod I., Anderson S., Yates J.R. III, He X.;
RT   "Molecular analysis of kinetochore architecture in fission yeast.";
RL   EMBO J. 24:2919-2930(2005).
RN   [7]
RP   IDENTIFICATION IN THE NMS COMPLEX.
RX   PubMed=17035632; DOI=10.1091/mbc.e06-05-0388;
RA   Hayashi A., Asakawa H., Haraguchi T., Hiraoka Y.;
RT   "Reconstruction of the kinetochore during meiosis in fission yeast
RT   Schizosaccharomyces pombe.";
RL   Mol. Biol. Cell 17:5173-5184(2006).
RN   [8]
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: Acts as a component of the NMS (Ndc80-MIND-Spc7) super
CC       complex which has a role in kinetochore function during late meiotic
CC       prophase and throughout the mitotic cell cycle. Required for correct
CC       segregation of chromosomes and for maintaining the inner centromere
CC       structure. {ECO:0000269|PubMed:12773390}.
CC   -!- SUBUNIT: Component of the NMS super complex which consists of mis12,
CC       mis13, mis14, ndc80, nnf1, nuf2, sos7, spc7, spc24 and spc25. Interacts
CC       with dis1, mal2, mis14, ppe1 and ekc1. {ECO:0000269|PubMed:12242294,
CC       ECO:0000269|PubMed:12773390, ECO:0000269|PubMed:15369671,
CC       ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:17035632}.
CC   -!- INTERACTION:
CC       Q9Y738; Q9Y812: cnp1; NbExp=3; IntAct=EBI-1002822, EBI-1153281;
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC       {ECO:0000269|PubMed:12773390}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:12773390}.
CC   -!- SIMILARITY: Belongs to the mis12 family. {ECO:0000305}.
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DR   EMBL; AB027472; BAA77791.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB52606.1; -; Genomic_DNA.
DR   PIR; T40432; T40432.
DR   RefSeq; NP_595454.1; NM_001021364.2.
DR   PDB; 5WWL; X-ray; 2.40 A; M=1-215.
DR   PDBsum; 5WWL; -.
DR   AlphaFoldDB; Q9Y738; -.
DR   SMR; Q9Y738; -.
DR   BioGRID; 277022; 42.
DR   IntAct; Q9Y738; 3.
DR   STRING; 4896.SPBC409.04c.1; -.
DR   iPTMnet; Q9Y738; -.
DR   MaxQB; Q9Y738; -.
DR   PaxDb; Q9Y738; -.
DR   EnsemblFungi; SPBC409.04c.1; SPBC409.04c.1:pep; SPBC409.04c.
DR   GeneID; 2540494; -.
DR   KEGG; spo:SPBC409.04c; -.
DR   PomBase; SPBC409.04c; mis12.
DR   VEuPathDB; FungiDB:SPBC409.04c; -.
DR   eggNOG; ENOG502S72R; Eukaryota.
DR   HOGENOM; CLU_046437_0_0_1; -.
DR   InParanoid; Q9Y738; -.
DR   OMA; EGLHKFE; -.
DR   PhylomeDB; Q9Y738; -.
DR   PRO; PR:Q9Y738; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0034506; C:chromosome, centromeric core domain; IDA:PomBase.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR   GO; GO:0000939; C:inner kinetochore; IDA:PomBase.
DR   GO; GO:0031617; C:NMS complex; IDA:PomBase.
DR   GO; GO:0000818; C:nuclear MIS12/MIND complex; IDA:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051382; P:kinetochore assembly; IBA:GO_Central.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR   GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IC:PomBase.
DR   GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
DR   InterPro; IPR008685; Centromere_Mis12.
DR   PANTHER; PTHR14527; PTHR14527; 1.
DR   Pfam; PF05859; Mis12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Kinetochore; Meiosis; Mitosis; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..259
FT                   /note="Centromere protein mis12"
FT                   /id="PRO_0000096492"
FT   COILED          123..156
FT                   /evidence="ECO:0000255"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:12773390"
FT   MOD_RES         192
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:12773390"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:12773390"
FT   HELIX           3..7
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           9..36
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           46..77
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           84..89
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   TURN            95..98
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           103..155
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           166..187
FT                   /evidence="ECO:0007829|PDB:5WWL"
FT   HELIX           196..212
FT                   /evidence="ECO:0007829|PDB:5WWL"
SQ   SEQUENCE   259 AA;  30195 MW;  B4D0B64BB9EB9007 CRC64;
     MLVELLEFTP LSFIDDVINI TNQLLYKGVN GVDKAFSQTR FAKKAPQEIE EGLHKFEVLF
     ESVVDRYYDG FEVYTLRNIF SYPPELKGYM RTFGKDVDYS ITTEQDAAMD QAIQEAAEKL
     VVKMQLRRDL RMRLSRKREK KTEIEKHLER ISFLNKVPEN WQVTLPETTD FLLDQLGNLQ
     HAVKRVVEAS PTVHSREVDE RITYLEKGYE RLSNPIDQQK DFWSHHLSKL ESTANTETAN
     NIHKLLLSSE KDVGHTDEP
 
 
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