ID F1SAQ3_PIG Unreviewed; 605 AA.
AC F1SAQ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Cyclin K {ECO:0000313|Ensembl:ENSSSCP00000002716.4};
GN Name=CCNK {ECO:0000313|Ensembl:ENSSSCP00000002716.4,
GN ECO:0000313|VGNC:VGNC:86362};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000002716.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000002716.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000002716.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000002716.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR AlphaFoldDB; F1SAQ3; -.
DR SMR; F1SAQ3; -.
DR STRING; 9823.ENSSSCP00000002716; -.
DR PaxDb; 9823-ENSSSCP00000002716; -.
DR Ensembl; ENSSSCT00000002787.4; ENSSSCP00000002716.4; ENSSSCG00000002509.4.
DR VGNC; VGNC:86362; CCNK.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000156384; -.
DR HOGENOM; CLU_022000_0_2_1; -.
DR InParanoid; F1SAQ3; -.
DR TreeFam; TF101010; -.
DR Reactome; R-SSC-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-SSC-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-SSC-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SSC-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SSC-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SSC-75955; RNA Polymerase II Transcription Elongation.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000002509; Expressed in oocyte and 45 other cell types or tissues.
DR GO; GO:0002944; C:cyclin K-CDK12 complex; IEA:Ensembl.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; IEA:Ensembl.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd20530; CYCLIN_CCNK_rpt1; 1.
DR CDD; cd20531; CYCLIN_CCNK_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF51; CYCLIN-K; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF21797; CycT2-like_C; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 55..149
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 158..283
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 162..256
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 262..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..499
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 67160 MW; 2504E82D64C8B7B5 CRC64;
MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR REGARFIFDV
GTRLGLHYDT LATGIIYFHR FYMFHSFKQF PRYVTGACCL FLAGKVEETP KKCKDIIKTA
RSLLNDVQFG QFGDDPKEEV MVLERILLQT IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK
LVQMAWTFVN DSLCTTLSLQ WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ
DVPVDVLEDI CHQILDLYSQ GKQQMPHHTP HQLQQPPSLH PAPQVPQVPQ SQSSQGSEAP
QPPQKDPQQP AQPQPPPPAQ PPKKPSPQPS PPRQAKRAVV VSPKEENKTA EPPPPKIAKI
ETTHPPLPPA HPPPDRKPPL AAALGEAEPP GAVEAGDLPK VQIPPPAHPA PVHQPPPLPH
RPPPPPPSSY ITGMSTTSSY MSGEGYQSLQ SMMKTEGPSY GALPPAYGPP AHLPYHPHVY
PPTRPRRPCR RRPPPSRRPP SRPRRPATPA PAHLQPQLPA PSPAPAPHSR SPAAPAPGPG
TAAGQLPTPC RPPGRTAPRA AAHPPTRHAA RRGAGAGRLD EITRRLPPPL PCFLKTKVFS
NEPEK
//
