CCNL2_MOUSE
ID CCNL2_MOUSE Reviewed; 518 AA.
AC Q9JJA7; A2AD95; A2RSY2; Q5XK66; Q60995; Q8C136; Q8CIJ8; Q99L73; Q9QXH5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cyclin-L2;
DE AltName: Full=Cyclin Ania-6b;
DE AltName: Full=Paneth cell-enhanced expression protein;
DE Short=PCEE;
GN Name=Ccnl2; Synonyms=Ania6b; ORFNames=MNCb-5160;
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 2).
RC STRAIN=C57BL/6J;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=14684736; DOI=10.1074/jbc.m312895200;
RA Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.;
RT "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in
RT pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma
RT cells.";
RL J. Biol. Chem. 279:11639-11648(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Pancreas, Skin, and Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 321-518.
RC STRAIN=BALB/cJ; TISSUE=Jejunal epithelium;
RX PubMed=8838426;
RX DOI=10.1002/(sici)1097-0185(199601)244:1<78::aid-ar8>3.0.co;2-b;
RA Cheng H., Bjerknes M.;
RT "Patterns of gene expression along the crypt-villus axis in mouse jejunal
RT epithelium.";
RL Anat. Rec. 244:78-94(1996).
RN [9]
RP INTERACTION 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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. May induce cell death,
CC possibly by acting on the transcription and RNA processing of
CC apoptosis-related factors. {ECO:0000250|UniProtKB:Q96S94}.
CC -!- SUBUNIT: Interacts with CDK11A, CDK11B, CDK12, CDK13 and POLR2A, the
CC hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. May
CC form a ternary complex with CDK11B and casein kinase II (CKII).
CC Interacts with pre-mRNA-splicing factors, including at least SRSF1,
CC SRSF2 AND SRSF7/SLU7. {ECO:0000250|UniProtKB:Q96S94,
CC ECO:0000269|PubMed:17261272}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96S94}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96S94}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JJA7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJA7-2; Sequence=VSP_016134, VSP_016135;
CC Name=3;
CC IsoId=Q9JJA7-3; Sequence=VSP_016133;
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 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52504.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC52504.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF211859; AAF23011.1; -; mRNA.
DR EMBL; AY337018; AAQ01205.1; -; mRNA.
DR EMBL; AB041605; BAA95088.1; -; mRNA.
DR EMBL; AK007552; BAB25103.1; -; mRNA.
DR EMBL; AK029033; BAC26255.1; -; mRNA.
DR EMBL; AK048244; BAE43334.1; -; mRNA.
DR EMBL; AK156037; BAE33556.1; -; mRNA.
DR EMBL; AK169857; BAE41413.1; -; mRNA.
DR EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15040.1; -; Genomic_DNA.
DR EMBL; BC003773; AAH03773.2; -; mRNA.
DR EMBL; BC023747; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC083055; AAH83055.1; -; mRNA.
DR EMBL; BC132295; AAI32296.1; -; mRNA.
DR EMBL; U37351; AAC52504.1; ALT_SEQ; mRNA.
DR CCDS; CCDS19042.1; -. [Q9JJA7-1]
DR RefSeq; NP_997561.1; NM_207678.1. [Q9JJA7-1]
DR AlphaFoldDB; Q9JJA7; -.
DR SMR; Q9JJA7; -.
DR BioGRID; 207786; 17.
DR ComplexPortal; CPX-350; Cyclin L2-CDK11B(p110) complex.
DR ComplexPortal; CPX-353; Cyclin L2-CDK11B(p58) complex.
DR STRING; 10090.ENSMUSP00000030944; -.
DR iPTMnet; Q9JJA7; -.
DR PhosphoSitePlus; Q9JJA7; -.
DR EPD; Q9JJA7; -.
DR jPOST; Q9JJA7; -.
DR MaxQB; Q9JJA7; -.
DR PaxDb; Q9JJA7; -.
DR PeptideAtlas; Q9JJA7; -.
DR PRIDE; Q9JJA7; -.
DR ProteomicsDB; 281426; -. [Q9JJA7-1]
DR ProteomicsDB; 281427; -. [Q9JJA7-2]
DR ProteomicsDB; 281428; -. [Q9JJA7-3]
DR Antibodypedia; 26320; 132 antibodies from 26 providers.
DR DNASU; 56036; -.
DR Ensembl; ENSMUST00000030944; ENSMUSP00000030944; ENSMUSG00000029068. [Q9JJA7-1]
DR GeneID; 56036; -.
DR KEGG; mmu:56036; -.
DR UCSC; uc008wev.1; mouse. [Q9JJA7-3]
DR UCSC; uc008wew.1; mouse. [Q9JJA7-1]
DR CTD; 81669; -.
DR MGI; MGI:1927119; Ccnl2.
DR VEuPathDB; HostDB:ENSMUSG00000029068; -.
DR eggNOG; KOG0835; Eukaryota.
DR GeneTree; ENSGT00940000159239; -.
DR HOGENOM; CLU_022000_6_1_1; -.
DR InParanoid; Q9JJA7; -.
DR OMA; KYPAQKP; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q9JJA7; -.
DR TreeFam; TF101011; -.
DR BioGRID-ORCS; 56036; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Ccnl2; mouse.
DR PRO; PR:Q9JJA7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JJA7; protein.
DR Bgee; ENSMUSG00000029068; Expressed in secondary palatal shelf and 273 other tissues.
DR ExpressionAtlas; Q9JJA7; baseline and differential.
DR Genevisible; Q9JJA7; MM.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; 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:0043484; P:regulation of RNA splicing; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 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; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..518
FT /note="Cyclin-L2"
FT /id="PRO_0000080488"
FT REGION 81..183
FT /note="Cyclin-like 1"
FT REGION 196..280
FT /note="Cyclin-like 2"
FT REGION 310..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..420
FT /note="RS"
FT COMPBIAS 370..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 219..518
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016133"
FT VAR_SEQ 219..224
FT /note="NYMNDS -> VASEGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11683997,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_016134"
FT VAR_SEQ 225..518
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11683997,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_016135"
FT CONFLICT 16
FT /note="S -> A (in Ref. 4; BAE41413/BAE33556, 6; EDL15040
FT and 7; AAI32296)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="K -> R (in Ref. 4; BAC26255)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="Y -> F (in Ref. 7; AAH03773)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="T -> S (in Ref. 6; EDL15040 and 7; AAH03773/
FT AAI32296)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="E -> VE (in Ref. 7; AAH03773/AAH83055 and 8;
FT AAC52504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 58005 MW; C93AEE68682CDBA5 CRC64;
MAAAAAGAAG LMAPASAACS SGSAGAAPGS QGVLIGDRLY SGVLITLENC LLPDDKLRFT
PSMSSGLDVD TETGLRVVGC ELIQAAGILL RLPQVAMATG QVLFQRFFYT KSFVKHSMEH
VSMACVHLAS KIEEAPRRIR DVINVFHRLR HLREKKKPVP LVLDQEYVNL KNQIIKAERR
VLKELGFCVH VKHPHKIIVM YLQVLECERN QHLVQTAWNY MNDSLRTDVF VRFQPESIAC
ACIYLAARTL EIPLPNRPHW FLLFGATEEE IQEICFKILQ LYTRKKVDLT HLESEVEKRK
HAIEEAKARA KGLLPGTAPG LDSAAGFSPA PKLESPKEGK GGKPSPPSGK SAKRKMEGPK
KAQGHSPVNG LLKGQESRSQ SRSREQSYSR SPSRSASPKR RKSDSGSTSG GSKSQSRSRS
RSDSPPRQVH RGAPYKGSEV RGSRKSKDCK YLTQKPHKSR SRSSSRSRSR SRERTDNSGK
YKKKSHYYRD QRRERSRSYE RTGHRYERDH PGHSRHRR
