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PCS1_SCHPO
ID   PCS1_SCHPO              Reviewed;         261 AA.
AC   O13684; Q870L5; Q9UTP7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 4.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Monopolin complex subunit pcs1;
DE   AltName: Full=Chromosome segregation protein 1;
GN   Name=pcs1; ORFNames=SPAC11E3.03;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12689592; DOI=10.1016/s1534-5807(03)00086-8;
RA   Rabitsch K.P., Petronczki M., Javerzat J.-P., Genier S., Chwalla B.,
RA   Schleiffer A., Tanaka T.U., Nasmyth K.;
RT   "Kinetochore recruitment of two nucleolar proteins is required for homolog
RT   segregation in meiosis I.";
RL   Dev. Cell 4:535-548(2003).
RN   [4]
RP   FUNCTION, INTERACTION WITH MDE4, AND SUBCELLULAR LOCATION.
RX   PubMed=17627824; DOI=10.1016/j.cub.2007.06.044;
RA   Gregan J., Riedel C.G., Pidoux A.L., Katou Y., Rumpf C., Schleiffer A.,
RA   Kearsey S.E., Shirahige K., Allshire R.C., Nasmyth K.;
RT   "The kinetochore proteins Pcs1 and Mde4 and heterochromatin are required to
RT   prevent merotelic orientation.";
RL   Curr. Biol. 17:1190-1200(2007).
CC   -!- FUNCTION: The monopolin-like pcs1/mde4 complex is essential for
CC       accurate chromosome segregation during mitosis and meiosis II. May
CC       clamp together microtubule binding sites on the same kinetochore,
CC       preventing merotelic attachment of microtubules. In contrast to its
CC       S.cerevisiae ortholog CSM1, is not required ofr mono-orientation during
CC       meiosis I. {ECO:0000269|PubMed:12689592, ECO:0000269|PubMed:17627824}.
CC   -!- SUBUNIT: Component of a monopolin-like complex composed of pcs1 and
CC       mde4. The complex associates with the kinetochore.
CC   -!- INTERACTION:
CC       O13684; O43068: mde4; NbExp=3; IntAct=EBI-2211100, EBI-2211118;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12689592}.
CC       Chromosome, centromere {ECO:0000269|PubMed:12689592}. Note=Nucleolar
CC       during G2 (PubMed:12689592). Localizes to the centromeres throughout
CC       most stages of vegetative growth and meiotic development apart from the
CC       horse tail stage of prophase I (PubMed:12689592). Localizes to the
CC       central core of the centromere (PubMed:17627824).
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DR   EMBL; CU329670; CAD88639.2; -; Genomic_DNA.
DR   PIR; T37530; T37530.
DR   PIR; T37531; T37531.
DR   RefSeq; NP_001018298.2; NM_001020359.2.
DR   AlphaFoldDB; O13684; -.
DR   SMR; O13684; -.
DR   BioGRID; 280638; 10.
DR   DIP; DIP-47341N; -.
DR   IntAct; O13684; 7.
DR   STRING; 4896.SPAC11E3.03.1; -.
DR   MaxQB; O13684; -.
DR   PaxDb; O13684; -.
DR   EnsemblFungi; SPAC11E3.03.1; SPAC11E3.03.1:pep; SPAC11E3.03.
DR   GeneID; 3361562; -.
DR   KEGG; spo:SPAC11E3.03; -.
DR   PomBase; SPAC11E3.03; -.
DR   VEuPathDB; FungiDB:SPAC11E3.03; -.
DR   eggNOG; ENOG502R6WM; Eukaryota.
DR   HOGENOM; CLU_093249_0_0_1; -.
DR   InParanoid; O13684; -.
DR   OMA; SARIMKA; -.
DR   PRO; PR:O13684; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0034506; C:chromosome, centromeric core domain; IDA:PomBase.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR   GO; GO:0033551; C:monopolin complex; IDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:1990644; F:microtubule site clamp; IPI:PomBase.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR   GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:PomBase.
DR   GO; GO:1990893; P:mitotic chromosome centromere condensation; IMP:PomBase.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR   Gene3D; 3.90.1150.80; -; 1.
DR   InterPro; IPR040349; Csm1/Pcs1.
DR   InterPro; IPR020981; Csm1/Pcs1_C.
DR   InterPro; IPR038608; Csm1/Pcs1_C_sf.
DR   PANTHER; PTHR28006; PTHR28006; 1.
DR   Pfam; PF12539; Csm1; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Meiosis;
KW   Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Monopolin complex subunit pcs1"
FT                   /id="PRO_0000058266"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          91..170
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   261 AA;  30418 MW;  788A079D2920CE35 CRC64;
     MRKNNMQTSK DSELKEQAKG KSSKLIHKLP KQRTRISQGQ MHSTQDFVNN EDQDAYSVRE
     NENELHINNS GMSELNKKLQ LPNVELSTLS HTQEQEFNEL NKLIRKINEL QEFYLLEDLA
     KPVTNAGADA DDTIVKDLKK ELENEKKANH SLKNELLKTR EQIKNYSKIN ILIKELFGLE
     VADCIEDEDG YRFNCKNTGR RGTLEYQLLL DDQNFTFTPR LNVQTDEELM KHLPDYLLEE
     IIFTKEQGKL FSARLMKALQ D
 
 
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