CCNL1_MOUSE
ID CCNL1_MOUSE Reviewed; 532 AA.
AC Q52KE7; Q8BQ75; Q8R5H9; Q922K0; Q9CSZ3; Q9WV44;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cyclin-L1;
DE Short=Cyclin-L;
DE AltName: Full=Cyclin Ania-6a;
GN Name=Ccnl1; Synonyms=Ania6a, Ccn1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Testis;
RX PubMed=11683997; DOI=10.1016/s0896-6273(01)00465-2;
RA Berke J.D., Sgambato V., Zhu P.-P., Lavoie B., Vincent M., Krause M.,
RA Hyman S.E.;
RT "Dopamine and glutamate induce distinct striatal splice forms of Ania-6, an
RT RNA polymerase II-associated cyclin.";
RL Neuron 32:277-287(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-309 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH CDK13.
RX PubMed=17261272; DOI=10.1016/j.bbrc.2007.01.049;
RA Chen H.H., Wong Y.H., Geneviere A.M., Fann M.J.;
RT "CDK13/CDC2L5 interacts with L-type cyclins and regulates alternative
RT splicing.";
RL Biochem. Biophys. Res. Commun. 354:735-740(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18216018; DOI=10.1074/jbc.m708188200;
RA Loyer P., Trembley J.H., Grenet J.A., Busson A., Corlu A., Zhao W.,
RA Kocak M., Kidd V.J., Lahti J.M.;
RT "Characterization of cyclin L1 and L2 interactions with CDK11 and splicing
RT factors: influence of cyclin L isoforms on splice site selection.";
RL J. Biol. Chem. 283:7721-7732(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-344 AND SER-358, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Functions in association with
CC cyclin-dependent kinases (CDKs). May play a role in the regulation of
CC RNA polymerase II (pol II). Inhibited by the CDK-specific inhibitor
CC CDKN1A/p21. {ECO:0000250|UniProtKB:Q9UK58}.
CC -!- SUBUNIT: Interacts with POLR2A via its hyperphosphorylated C-terminal
CC domain (CTD) (By similarity). Interacts with CDK11A, CDK11B, CDK12 and
CC CDK13. May form a ternary complex with CDK11B and casein kinase II
CC (CKII). Interacts with pre-mRNA-splicing factors, including at least
CC SRSF1, SRSF2 AND SRSF7/SLU7 (By similarity) (PubMed:17261272).
CC {ECO:0000250|UniProtKB:Q9R1Q2, ECO:0000250|UniProtKB:Q9UK58,
CC ECO:0000269|PubMed:17261272}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus speckle
CC {ECO:0000269|PubMed:11683997}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in nuclear intrachromatin
CC granules clusters (IGC), also called nuclear speckles, which are
CC storage compartments for nuclear proteins involved in mRNA processing.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:11683997}. Cytoplasm {ECO:0000269|PubMed:11683997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Cyclin L alpha;
CC IsoId=Q52KE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q52KE7-2; Sequence=VSP_016126, VSP_016127;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:18216018}.
CC -!- DOMAIN: Contains a RS region (arginine-serine dipeptide repeat) within
CC the C-terminal domain which is the hallmark of the SR family of
CC splicing factors. This region probably plays a role in protein-protein
CC interactions (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Found in the nucleus, with a speckled
CC pattern of expression.
CC -!- MISCELLANEOUS: [Isoform 2]: Found both in the nucleus and cytoplasm.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43568.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF159159; AAD43568.1; ALT_FRAME; mRNA.
DR EMBL; AF467251; AAL75565.1; -; mRNA.
DR EMBL; AK051380; BAC34619.1; -; mRNA.
DR EMBL; AK011629; BAB27744.3; -; mRNA.
DR EMBL; BC094383; AAH94383.1; -; mRNA.
DR CCDS; CCDS17390.1; -. [Q52KE7-1]
DR RefSeq; NP_064321.2; NM_019937.3. [Q52KE7-1]
DR AlphaFoldDB; Q52KE7; -.
DR SMR; Q52KE7; -.
DR BioGRID; 208134; 8.
DR ComplexPortal; CPX-351; Cyclin L1-CDK11B(p110) complex.
DR ComplexPortal; CPX-352; Cyclin L1-CDK11B(p58) complex.
DR IntAct; Q52KE7; 1.
DR MINT; Q52KE7; -.
DR STRING; 10090.ENSMUSP00000029416; -.
DR iPTMnet; Q52KE7; -.
DR PhosphoSitePlus; Q52KE7; -.
DR EPD; Q52KE7; -.
DR jPOST; Q52KE7; -.
DR MaxQB; Q52KE7; -.
DR PaxDb; Q52KE7; -.
DR PeptideAtlas; Q52KE7; -.
DR PRIDE; Q52KE7; -.
DR ProteomicsDB; 281339; -. [Q52KE7-1]
DR ProteomicsDB; 281340; -. [Q52KE7-2]
DR Antibodypedia; 18411; 233 antibodies from 34 providers.
DR DNASU; 56706; -.
DR Ensembl; ENSMUST00000029416; ENSMUSP00000029416; ENSMUSG00000027829. [Q52KE7-1]
DR GeneID; 56706; -.
DR KEGG; mmu:56706; -.
DR UCSC; uc008pku.1; mouse. [Q52KE7-1]
DR UCSC; uc008pkx.1; mouse. [Q52KE7-2]
DR CTD; 57018; -.
DR MGI; MGI:1922664; Ccnl1.
DR VEuPathDB; HostDB:ENSMUSG00000027829; -.
DR eggNOG; KOG0835; Eukaryota.
DR GeneTree; ENSGT00940000159135; -.
DR HOGENOM; CLU_022000_6_1_1; -.
DR InParanoid; Q52KE7; -.
DR OMA; RCHMVQE; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q52KE7; -.
DR TreeFam; TF101011; -.
DR BioGRID-ORCS; 56706; 8 hits in 70 CRISPR screens.
DR ChiTaRS; Ccnl1; mouse.
DR PRO; PR:Q52KE7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q52KE7; protein.
DR Bgee; ENSMUSG00000027829; Expressed in granulocyte and 256 other tissues.
DR ExpressionAtlas; Q52KE7; baseline and differential.
DR Genevisible; Q52KE7; MM.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008023; C:transcription elongation factor complex; ISO:MGI.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0046605; P:regulation of centrosome cycle; IC:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR015431; Cyclin_L1.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF64; PTHR10026:SF64; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cyclin; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..532
FT /note="Cyclin-L1"
FT /id="PRO_0000080481"
FT REGION 94..196
FT /note="Cyclin-like 1"
FT REGION 209..293
FT /note="Cyclin-like 2"
FT REGION 332..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..438
FT /note="RS"
FT COMPBIAS 349..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..422
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..454
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK58"
FT VAR_SEQ 210..252
FT /note="IIVMYLQVLECERNQTLVQTAWNYMNDSLRTNVFVRFQPETIA -> VSCKV
FT QTLQFVSIRAFSEILNSVWRVKLTGVFKSFLLDVDICF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016126"
FT VAR_SEQ 253..532
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016127"
FT CONFLICT 93..94
FT /note="CE -> WQ (in Ref. 1; AAL75565)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="E -> G (in Ref. 2; BAB27744)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> G (in Ref. 2; BAB27744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 60133 MW; ECBE41C070D0CA18 CRC64;
MASGPHPTST AAAAAAAAAS ASSAAPSAGG SSSGTTTTTT TTTGGILIGD RLYSEVSLTI
DHSLIPEERL SPTPSMQDGL DLPSETDLRI LGCELIQAAG ILLRLPQVAM ATGQVLFHRF
FYSKSFVKHS FEIVAMACIN LASKIEEAPR RIRDVINVFH HLRQLRGKRT PSPLILDQNY
INTKNQVIKA ERRVLKELGF CVHVKHPHKI IVMYLQVLEC ERNQTLVQTA WNYMNDSLRT
NVFVRFQPET IACACIYLAA RALQIPLPTR PHWFLLFGTT EEEIQEICIE TLRLYTRKKP
NYELLEKEVE KRKVALQEAK LKAKGLNLDG TPALSTLGGF SPASKPSSPR EVKAEEKSPV
SINVKTVKKE PEDRQQASKS PYNGVRKDSK RSRTSRSASR SRSRTRSRSR SHSPRRHYNN
RRSRSGTYSS RSRSRSRSHS ESPRRHHNHG SPHLKAKHTR EDLKSSNRHG HKRKKSRSRS
QSKTRDHSDV TKKHRHERGH HRDRRERSRS FERSHKGKHH GGSRSGHGRH RR
