CKS1_SCHPO
ID CKS1_SCHPO Reviewed; 113 AA.
AC P08463;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 174.
DE RecName: Full=Cyclin-dependent kinases regulatory subunit;
DE AltName: Full=P13;
GN Name=suc1; ORFNames=SPBC1734.14c;
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].
RX PubMed=3031478; DOI=10.1128/mcb.7.1.504-511.1987;
RA Hindley J., Phear G., Stein M., Beach D.;
RT "Sucl+ encodes a predicted 13-kilodalton protein that is essential for cell
RT viability and is directly involved in the division cycle of
RT Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 7:504-511(1987).
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 ASSOCIATION WITH CDC2.
RX PubMed=3322810; DOI=10.1002/j.1460-2075.1987.tb02676.x;
RA Brizuela L., Draetta G., Beach D.;
RT "p13suc1 acts in the fission yeast cell division cycle as a component of
RT the p34cdc2 protein kinase.";
RL EMBO J. 6:3507-3515(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7889931; DOI=10.1002/j.1460-2075.1995.tb07081.x;
RA Endicott J.A., Noble M.E.M., Garman E.F., Brown N., Rasmussen B., Nurse P.,
RA Johnson L.N.;
RT "The crystal structure of p13suc1, a p34cdc2-interacting cell cycle control
RT protein.";
RL EMBO J. 14:1004-1014(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7479758; DOI=10.1073/pnas.92.22.10232;
RA Bourne Y., Arvai A.S., Bernstein S.L., Watson M.H., Reed S.I.,
RA Endicott J.E., Noble M.E.M., Johnson L.N., Tainer J.A.;
RT "Crystal structure of the cell cycle-regulatory protein suc1 reveals a
RT beta-hinge conformational switch.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10232-10236(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=8805536; DOI=10.1016/s0969-2126(96)00034-2;
RA Khazanovich N., Bateman K.S., Chernaia M., Michalak M., James M.N.G.;
RT "Crystal structure of the yeast cell-cycle control protein, p13suc1, in a
RT strand-exchanged dimer.";
RL Structure 4:299-309(1996).
CC -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinase
CC (cdc2) and is essential for its biological function.
CC -!- SUBUNIT: Homodimer (in presence of zinc).
CC -!- SIMILARITY: Belongs to the CKS family. {ECO:0000305}.
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DR EMBL; M16032; AAA35346.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21308.1; -; Genomic_DNA.
DR PIR; A26722; A26722.
DR RefSeq; NP_595431.1; NM_001021339.2.
DR PDB; 1PUC; X-ray; 1.95 A; A=2-106.
DR PDB; 1SCE; X-ray; 2.20 A; A/B/C/D=1-112.
DR PDBsum; 1PUC; -.
DR PDBsum; 1SCE; -.
DR AlphaFoldDB; P08463; -.
DR BMRB; P08463; -.
DR SMR; P08463; -.
DR BioGRID; 276571; 12.
DR IntAct; P08463; 5.
DR STRING; 4896.SPBC1734.14c.1; -.
DR PaxDb; P08463; -.
DR EnsemblFungi; SPBC1734.14c.1; SPBC1734.14c.1:pep; SPBC1734.14c.
DR GeneID; 2540027; -.
DR KEGG; spo:SPBC1734.14c; -.
DR PomBase; SPBC1734.14c; suc1.
DR VEuPathDB; FungiDB:SPBC1734.14c; -.
DR eggNOG; KOG3484; Eukaryota.
DR HOGENOM; CLU_140546_0_0_1; -.
DR InParanoid; P08463; -.
DR OMA; RPINYGQ; -.
DR PhylomeDB; P08463; -.
DR EvolutionaryTrace; P08463; -.
DR PRO; PR:P08463; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:PomBase.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR Gene3D; 3.30.170.10; -; 1.
DR InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR Pfam; PF01111; CKS; 1.
DR PRINTS; PR00296; CYCLINKINASE.
DR SMART; SM01084; CKS; 1.
DR SUPFAM; SSF55637; SSF55637; 1.
DR PROSITE; PS00944; CKS_1; 1.
DR PROSITE; PS00945; CKS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..113
FT /note="Cyclin-dependent kinases regulatory subunit"
FT /id="PRO_0000206246"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:1PUC"
FT TURN 17..21
FT /evidence="ECO:0007829|PDB:1PUC"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1PUC"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1SCE"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1PUC"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1PUC"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1PUC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1PUC"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:1PUC"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1SCE"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1SCE"
SQ SEQUENCE 113 AA; 13446 MW; 1CE50666AAD8264F CRC64;
MSKSGVPRLL TASERERLEP FIDQIHYSPR YADDEYEYRH VMLPKAMLKA IPTDYFNPET
GTLRILQEEE WRGLGITQSL GWEMYEVHVP EPHILLFKRE KDYQMKFSQQ RGG
