CCNB1_SOYBN
ID CCNB1_SOYBN Reviewed; 454 AA.
AC P25011;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=G2/mitotic-specific cyclin S13-6;
DE AltName: Full=B-like cyclin;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Akisengoku; TISSUE=Root;
RX PubMed=1831125; DOI=10.1002/j.1460-2075.1991.tb07811.x;
RA Hata S., Kouchi H., Suzuka I., Ishii T.;
RT "Isolation and characterization of cDNA clones for plant cyclins.";
RL EMBO J. 10:2681-2688(1991).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition.
CC -!- SUBUNIT: Interacts with the CDC2 protein kinase to form a
CC serine/threonine kinase holoenzyme complex also known as maturation
CC promoting factor (MPF). The cyclin subunit imparts substrate
CC specificity to the complex.
CC -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC destroyed at mitosis.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; X62820; CAA44632.1; -; mRNA.
DR PIR; S16522; S16522.
DR RefSeq; NP_001236113.1; NM_001249184.2.
DR AlphaFoldDB; P25011; -.
DR SMR; P25011; -.
DR STRING; 3847.GLYMA03G27910.1; -.
DR PRIDE; P25011; -.
DR GeneID; 547920; -.
DR KEGG; gmx:547920; -.
DR eggNOG; KOG0653; Eukaryota.
DR OrthoDB; 993640at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cyclin; Mitosis; Reference proteome.
FT CHAIN 1..454
FT /note="G2/mitotic-specific cyclin S13-6"
FT /id="PRO_0000080397"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50095 MW; 54EB4596586A7C10 CRC64;
MASRIVQQQQ ARGEAVVGGG KQQKKNGVAD GRNRKALGDI GNLANVRGVV DAKPNRPITR
SFGAQLLANA QAAAAADNSK RQACANVAGP PAVANEGVAV AKRAAPKPVS KKVIVKPKPS
EKVTDIDASP DKKEVLKDKK KEGDANPKKK SQHTLTSVLT ARSKAACGIT NKPKEQIIDI
DASDVDNELA AVEYIDDIYK FYKLVENESR PHDYIGSQPE INERMRAILV DWLIDVHTKF
ELSLETLYLT INIIDRFLAV KTVPRRELQL VGISAMLMAS KYEEIWPPEV NDFVCLSDRA
YTHEHILTME KTILNKLEWT LTVPTPLVFL VRFIKASVPD QELDNMAHFL SELGMMNYAT
LMYCPSMVAA SAVLAARCTL NKAPFWNETL KLHTGYSQEQ LMDCARLLVG FYSTLENGKL
RVVYRKYSDP QKGAVAVLPP AKFLLPEGSA SQHS