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   27-MAR-2024, entry version 142.
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,
RC   Pancreas, 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; 10090-ENSMUSP00000029416; -.
DR   PeptideAtlas; Q52KE7; -.
DR   ProteomicsDB; 281339; -. [Q52KE7-1]
DR   ProteomicsDB; 281340; -. [Q52KE7-2]
DR   Pumba; Q52KE7; -.
DR   Antibodypedia; 18411; 255 antibodies from 34 providers.
DR   DNASU; 56706; -.
DR   Ensembl; ENSMUST00000029416.14; ENSMUSP00000029416.8; ENSMUSG00000027829.16. [Q52KE7-1]
DR   GeneID; 56706; -.
DR   KEGG; mmu:56706; -.
DR   UCSC; uc008pku.1; mouse. [Q52KE7-1]
DR   UCSC; uc008pkx.1; mouse. [Q52KE7-2]
DR   AGR; MGI:1922664; -.
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; GHKHRDG; -.
DR   OrthoDB; 4848076at2759; -.
DR   PhylomeDB; Q52KE7; -.
DR   TreeFam; TF101011; -.
DR   BioGRID-ORCS; 56706; 8 hits in 75 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 259 other cell types or tissues.
DR   ExpressionAtlas; Q52KE7; baseline and differential.
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; NAS:ComplexPortal.
DR   GO; GO:0051726; P:regulation of cell cycle; NAS:ComplexPortal.
DR   GO; GO:0046605; P:regulation of centrosome cycle; NAS: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   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:SF64; CYCLIN-L1; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF036580; Cyclin_L; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   Genevisible; Q52KE7; MM.
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
//